<?xml version="1.0" encoding="UTF-8" standalone="yes"?>
<keywordList>
    <keyword id="KW-0001">
        <name>2Fe-2S</name>
        <name>[Fe2S2] cluster</name>
        <name>Fe2/S2 (inorganic) cluster</name>
        <name>[2Fe-2S] cluster</name>
        <name>Di-mu-sulfido-diiron</name>
        <name>2 iron, 2 sulfur cluster binding</name>
        <name>Fe2S2</name>
        <description>Protein which contains at least one 2Fe-2S iron-sulfur cluster: 2 iron
atoms complexed to 2 inorganic sulfides and 4 sulfur atoms of
cysteines from the protein</description>
        <go id="GO:0051537"/>
    </keyword>
    <keyword id="KW-0002">
        <name>3D-structure</name>
        <description>Protein, or part of a protein, whose three-dimensional structure has
been resolved experimentally (for example by X-ray crystallography or
NMR spectroscopy) and whose coordinates are available in the PDB
database. Can also be used for theoretical models</description>
    </keyword>
    <keyword id="KW-0003">
        <name>3Fe-4S</name>
        <description>Protein which contains at least one 3Fe-4S iron-sulfur cluster: 3 iron
atoms complexed to 4 inorganic sulfides and 3 sulfur atoms of
cysteines from the protein. In a number of iron-sulfur proteins, the
4Fe-4S cluster can be reversibly converted by oxidation and loss of
one iron ion to a 3Fe-4S cluster</description>
        <go id="GO:0051538"/>
    </keyword>
    <keyword id="KW-0004">
        <name>4Fe-4S</name>
        <description>Protein which contains at least one 4Fe-4S iron-sulfur cluster: 4 iron
atoms complexed to 4 inorganic sulfides and 4 sulfur atoms of
cysteines from the protein. In a number of iron-sulfur proteins, the
4Fe-4S cluster can be reversibly converted by oxidation and loss of
one iron ion to a 3Fe-4S cluster</description>
        <go id="GO:0051539"/>
    </keyword>
    <keyword id="KW-0937">
        <name>Abscisic acid biosynthesis</name>
        <name>Abscisic acid synthesis</name>
        <name>ABA synthesis</name>
        <name>Abscisic acid biosynthetic process</name>
        <name>ABA formation</name>
        <name>ABA biosynthesis</name>
        <name>Abscisic acid formation</name>
        <name>Abscisic acid anabolism</name>
        <name>ABA anabolism</name>
        <description>Protein involved in the synthesis of abscisic acid (ABA) (5-(1-
hydroxy-2,6,6,trimethyl-4-oxocyclohex-2-en-1-y1)-3-methylpenta-2,4-
dienoic acid). ABA is a plant hormone which play a role in many
aspects of plant growth, development and cellular signaling (e.g. seed
dormancy, seed maturation, vegetative growth and responses to various
environmental stimuli such as stomatal closure during drought). This
phytohormone can be synthesized from farnesyl diphosphate (direct C15
pathway) or from 9-cis-violaxanthine (indirect C40 pathway)</description>
        <go id="GO:0009688"/>
    </keyword>
    <keyword id="KW-0938">
        <name>Abscisic acid signaling pathway</name>
        <name>ABA mediated signaling</name>
        <name>Abscisic acid mediated signaling</name>
        <name>ABA signaling pathway</name>
        <description>Protein involved in the abscisic acid (ABA) (5-(1-hydroxy-
2,6,6,trimethyl-4-oxocyclohex-2-en-1-y1)-3-methylpenta-2,4-dienoic
acid) signaling pathway (e.g. transport and signal transduction) that
regulates many aspects of plant growth, development and cellular
signaling (e.g. seed dormancy, seed maturation, vegetative growth and
responses to various environmental stimuli such as stomatal closure
during drought). This phytohormone can be synthesized from farnesyl
diphosphate (direct C15 pathway) or from 9-cis-violaxanthine (indirect
C40 pathway)</description>
        <go id="GO:0009738"/>
    </keyword>
    <keyword id="KW-0005">
        <name>Acetoin biosynthesis</name>
        <name>Acetoin formation</name>
        <name>3-hydroxy-2-butanone biosynthesis</name>
        <name>3-hydroxy-2-butanone biosynthetic process</name>
        <name>3-hydroxy-2-butanone synthesis</name>
        <name>Acetoin anabolism</name>
        <name>3-hydroxy-2-butanone formation</name>
        <name>Acetoin biosynthetic process</name>
        <name>Acetoin synthesis</name>
        <name>3-hydroxy-2-butanone anabolism</name>
        <description>Protein involved in the synthesis of acetoin (3-hydroxy-2-butanone)
Acetoin is a component of the butanediol cycle (butanediol
fermentation) in microorganisms</description>
        <go id="GO:0045151"/>
    </keyword>
    <keyword id="KW-0006">
        <name>Acetoin catabolism</name>
        <name>3-hydroxy-2-butanone catabolic process</name>
        <name>Acetoin breakdown</name>
        <name>3-hydroxy-2-butanone catabolism</name>
        <name>3-hydroxy-2-butanone breakdown</name>
        <name>Acetoin degradation</name>
        <name>Acetoin catabolic process</name>
        <name>3-hydroxy-2-butanone degradation</name>
        <description>Protein involved in the degradation of acetoin (3-hydroxy-2-butanone)
Acetoin is a component of the butanediol cycle (butanediol
fermentation) in microorganisms</description>
        <go id="GO:0045150"/>
    </keyword>
    <keyword id="KW-0007">
        <name>Acetylation</name>
        <name>Acetylated</name>
        <name>N-acetylated</name>
        <description>Protein which is posttranslationally modified by the attachment of at
least one acetyl group; generally at the N-terminus</description>
    </keyword>
    <keyword id="KW-0008">
        <name>Acetylcholine receptor inhibiting toxin</name>
        <name>Nicotinic AChR inhibitor</name>
        <name>nAChR inhibitor</name>
        <description>Toxin which interferes with the function of the nicotinic
acetylcholine receptor (nAChR). The nAChR is a postsynaptic membrane
protein that undergoes an extensive conformational change upon binding
to acetylcholine, leading to opening of an ion-conducting channel
across the plasma membrane. These toxins are mostly found in snake and
cone snail venoms</description>
        <go id="GO:0030550"/>
    </keyword>
    <keyword id="KW-0117">
        <name>Actin capping</name>
        <name>Actin filament capping</name>
        <name>F-actin capping</name>
        <description>Protein that binds to the free end of the actin filament and thereby
blocks further addition of subunits</description>
        <go id="GO:0051693"/>
    </keyword>
    <keyword id="KW-0009">
        <name>Actin-binding</name>
        <name>Actin filament binding</name>
        <description>Protein which binds to actin, and thereby can modulate the properties
and/or functions of the actin filament</description>
        <go id="GO:0003779"/>
    </keyword>
    <keyword id="KW-1178">
        <name>Actin-dependent inwards viral transport</name>
        <description>Viral protein that allows the active transport of viral material along
actin filaments toward the intracellular replication sites during
virus entry. This transport probably involves motor proteins like
myosins or polymerization/depolymerization reactions as a driving
force. Viruses such as poliovirus may utilize this type of
intracellular transport</description>
        <go id="GO:0039680"/>
    </keyword>
    <keyword id="KW-1072">
        <name>Activation of host autophagy by virus</name>
        <description>Viral protein involved in the activation of host autophagy. Autophagy
is a major intracellular pathway in the delivery of cytoplasmic
material to lysosomes for degradation. It is also essential for the
removal of pathogenic protein aggregates from the cell during
infection. Although autophagy is clearly important for antiviral
immune response, it can also be activated by viruses and serves as
platform for viral replication. Some viruses such as poliovirus, use
the autophagic pathway as a nonlytic mechanism for viral release</description>
        <go id="GO:0039520"/>
    </keyword>
    <keyword id="KW-1073">
        <name>Activation of host caspases by virus</name>
        <description>Viral protein involved in the activation of host cell apoptosis by
acting on host caspases. While many viruses encode protein that
inhibit apoptosis, viruses can also use apoptosis to their advantage
to suppress immune response or to disseminate. Therefore, some viral
proteins are able to cleave or activate caspases in order to promote
apoptosis</description>
        <go id="GO:0052151"/>
    </keyword>
    <keyword id="KW-1074">
        <name>Activation of host NF-kappa-B by virus</name>
        <description>Viral protein involved in the activation of host NF-kappa-B. This
protein is a pleiotropic transcription factor which is present in
almost all cell types and is involved in many biological processed
such as inflammation, immunity, differentiation, cell growth,
tumorigenesis and apoptosis. Several viruses have developed strategies
to activate the NF-kappa-B pathway in order to promote viral
replication and prevent virus-induced apoptosis</description>
        <go id="GO:0085033"/>
    </keyword>
    <keyword id="KW-0010">
        <name>Activator</name>
        <name>Positive activator</name>
        <description>Protein that positively regulates either the transcription of one or
more genes, or the translation of mRNA</description>
    </keyword>
    <keyword id="KW-0011">
        <name>Acute phase</name>
        <name>Acute-phase response</name>
        <name>Acute-phase reaction</name>
        <description>Protein involved in acute phase, a response of the vertebrate body to
insults, infections, immunological reactions or inflammatory
processes; characterised by redness (rubor), heat (calor), swelling
(tumor), pain (dolor) and sometimes loss of function</description>
        <go id="GO:0006953"/>
    </keyword>
    <keyword id="KW-0012">
        <name>Acyltransferase</name>
        <description>Enzyme catalyzing the transfer of acyl- (RCO-) groups</description>
        <go id="GO:0016746"/>
    </keyword>
    <keyword id="KW-1064">
        <name>Adaptive immunity</name>
        <name>Acquired immunity</name>
        <description>Protein involved in adaptive immunity. Vertebrates can develop a broad
and almost infinite repertoire of antigen-specific receptors, which
allows vertebrates to recognize almost any potential pathogen or toxin
and to mount antigen-specific responses to it. Two types of adaptive
immunity systems have evolved in vertebrates in order to generate
immune receptor diversity. The jawed vertebrates strategy uses the
V(D)JC recombination to achieve combinatorial diversity of
immunoglobulin-based B cell receptors and T cell receptors. The
jawless vertebrate strategy uses the somatic rearrangements of
variable leucine-rich cassettes in the variable lymphocyte receptors
(VLRs). The hallmarks of an adaptive immune system is the production
of antigen-specific recognition receptor by somatic gene
rearrangement. The long life of some antigen-primed cytotoxic
lymphocytes and plasma cells provide protective memory to prevent
reinvasion</description>
        <go id="GO:0002250"/>
    </keyword>
    <keyword id="KW-0013">
        <name>ADP-ribosylation</name>
        <name>ADP-ribosylated</name>
        <name>Adenosinediphospho-ribosylation</name>
        <description>Protein which is posttranslationally modified by the attachment of at
least one ADP-ribosyl group</description>
    </keyword>
    <keyword id="KW-0913">
        <name>Age-related macular degeneration</name>
        <name>ARMD</name>
        <description>Protein which, if defective, causes age-related macular degeneration
(ARMD), the most common cause of irreversible vision loss in the
developed world. In most patients, the disease is manifest as
ophthalmoscopically visible yellowish accumulations of protein and
lipid (known as drusen) that lie beneath the retinal pigment
epithelium and within an elastin-containing structure known as Bruch's
membrane. ARMD is likely to be a mechanistically heterogeneous group
of disorders, and the specific disease mechanisms that underlie the
vast majority of cases are currently unknown. However, a number of
studies have suggested that both genetic and environmental factors are
likely to play a role</description>
    </keyword>
    <keyword id="KW-0948">
        <name>Aicardi-Goutieres syndrome</name>
        <name>Pseudo-torch syndrome</name>
        <name>Cree encephalitis</name>
        <name>Pseudotoxoplasmosis syndrome</name>
        <name>AGS</name>
        <description>Protein which, if defective, causes Aicardi-Goutieres syndrome, a
genetic disorder that is phenotypically similar to in utero viral
infection. The disease is characterized by severe neurological
dysfunction in infancy, leading to progressive microcephaly,
spasticity, dystonic posturing, profound psychomotor retardation and
often death in early childhood</description>
    </keyword>
    <keyword id="KW-0014">
        <name>AIDS</name>
        <name>Acquired immunodeficiency syndrome</name>
        <description>Protein encoded by the human immunodeficiency viruses HIV-1 or HIV-2,
which are the cause of acquired immunodeficiency syndrome (AIDS). This
disease is characterized by a severe defect of cell-mediated immunity
which is often accompanied by cancers such as Kaposi's sarcoma, as
well as secondary infections such as tuberculosis</description>
    </keyword>
    <keyword id="KW-0015">
        <name>Albinism</name>
        <description>Protein which, if defective, causes albinism, a genetically determined
or environmentally induced absence of pigmentation in animals normally
pigmented. This can lead for example to lack of pigmentation in hair,
skin and eyes</description>
    </keyword>
    <keyword id="KW-0016">
        <name>Alginate biosynthesis</name>
        <name>Alginic acid synthesis</name>
        <name>Alginic acid biosynthesis</name>
        <name>Alginate synthesis</name>
        <name>Alginate formation</name>
        <name>Alginate anabolism</name>
        <name>Alginic acid anabolism</name>
        <name>Alginic acid formation</name>
        <description>Protein involved in the synthesis of alginate. Alginate is an
exopolysaccharide in the cell walls of brown algae and in the capsular
material of certain strains of Pseudomonas and Azotobacter, in which
it provides a protective barrier against host immune defenses and
antibiotics</description>
        <go id="GO:0042121"/>
    </keyword>
    <keyword id="KW-0017">
        <name>Alkaloid metabolism</name>
        <name>Alkaloid metabolic process</name>
        <description>Protein involved in a biochemical reaction with alkaloids, a group of
nitrogenous organic molecules (mostly heterocyclic) usually found in
plants. Various alkaloids have toxic or medical properties, such as
caffeine, morphine and nicotine</description>
        <go id="GO:0009820"/>
    </keyword>
    <keyword id="KW-0019">
        <name>Alkylphosphonate uptake</name>
        <description>Protein involved in alkylphosphonate uptake. Certain bacteria such as
Escherichia coli can use alkylphosphonates as a phosphorus source</description>
        <go id="GO:0015716"/>
    </keyword>
    <keyword id="KW-0020">
        <name>Allergen</name>
        <description>Protein that stimulates the production of, and reacts with, antibodies
(IgE) thus creating an allergic reaction (immediate-type
hypersensitivity). Examples are pollen allergens from plants, venom
allergens from insects, dust-mite allergens, and animal hair
allergens</description>
    </keyword>
    <keyword id="KW-0021">
        <name>Allosteric enzyme</name>
        <description>Enzyme whose activity is modified by the noncovalent binding of an
allosteric effector at a site other than the active site. This binding
mediates conformational changes, altering its catalytic or binding
properties</description>
        <go id="GO:0008152"/>
        <go id="GO:0003824"/>
    </keyword>
    <keyword id="KW-0022">
        <name>Alpha-amylase inhibitor</name>
        <description>Protein that inhibits alpha-amylase, an enzyme that catalyzes the
endohydrolysis of 1,4-alpha-glucosidic linkages in oligosaccharides
and polysaccharides</description>
        <go id="GO:0015066"/>
    </keyword>
    <keyword id="KW-0023">
        <name>Alport syndrome</name>
        <description>Protein which, if defective, causes Alport syndrome, an hereditary
disorder characterized by a progressive glomerulonephritis leading to
end-stage renal disease, often associated with sensorineural hearing
loss and ocular abnormalities</description>
    </keyword>
    <keyword id="KW-0024">
        <name>Alternative initiation</name>
        <description>Protein for which at least two isoforms exist due to the usage of
alternative initiation codons in the same mRNA (the resulting isoforms
differ in their N-terminus if they are in frame)</description>
    </keyword>
    <keyword id="KW-0877">
        <name>Alternative promoter usage</name>
        <description>Protein for which at least two isoforms exist due to the alternative
usage of promoters</description>
    </keyword>
    <keyword id="KW-0025">
        <name>Alternative splicing</name>
        <description>Protein for which at least two isoforms exist due to distinct pre-mRNA
splicing events</description>
    </keyword>
    <keyword id="KW-0026">
        <name>Alzheimer disease</name>
        <name>Alzheimer's disease</name>
        <description>Protein which, if defective, causes Alzheimer disease, a
neurodegenerative disorder characterized by progressive dementia and
global loss of cognitive abilities. The condition primarily occurs
after age 60, and is marked pathologically by severe cortical atrophy,
senile plaques, neurofibrillary tangles, and neuropil threads. Early-
onset forms also occurr</description>
    </keyword>
    <keyword id="KW-0986">
        <name>Amelogenesis imperfecta</name>
        <description>Protein which, if defective, causes amelogenesis imperfecta, a
clinically and genetically heterogeneous group of disorders affecting
the dental enamel. The enamel may be hypoplastic, hypomineralized or
both, and affected teeth may be discoloured, sensitive or prone to
disintegration either pre-eruption or post-eruption. In the
hypoplastic type of amelogenesis imperfecta, the enamel is of normal
hardness but does not develop to normal thickness. In the
hypomineralized type, the enamel is of normal thickness but opaque or
yellowish white without lustre on newly erupted teeth; it is so soft
that it is lost soon after eruption. Amelogenesis imperfecta
occasionally occurs in conjunction with other dental, oral and extra-
oral features</description>
    </keyword>
    <keyword id="KW-0027">
        <name>Amidation</name>
        <name>Amidated</name>
        <description>Peptide which is posttranslationally modified by C-terminal amidation
The amino acid to be modified is almost always followed by a glycine,
which provides the amide group. In a first reaction step the glycine
is oxidized to form alpha-hydroxy-glycine. The oxidized glycine
cleaves into the C-terminally amidated peptide and an N-glyoxylated
peptide. C-terminal amidation is essential to the biological activity
of many neuropeptides and hormones. In a few cases alpha-oxidative
cleavage of an amino acid other than glycine has been observed. All
such cases are additionally annotated with the word "atypical" in the
feature description</description>
    </keyword>
    <keyword id="KW-0028">
        <name>Amino-acid biosynthesis</name>
        <name>Amino-acid synthesis</name>
        <name>Amino-acid anabolism</name>
        <name>Amino-acid formation</name>
        <description>Protein involved in the synthesis of naturally-occuring amino acids
In addition to their use for protein biosynthesis, they are the
precursors of many molecules such as purines, pyrimidines, histamines,
adrenaline and melanin</description>
        <go id="GO:0008652"/>
    </keyword>
    <keyword id="KW-0029">
        <name>Amino-acid transport</name>
        <name>Amino acid transport</name>
        <description>Protein involved in the transport of amino acids</description>
        <go id="GO:0006865"/>
    </keyword>
    <keyword id="KW-0030">
        <name>Aminoacyl-tRNA synthetase</name>
        <name>Aminoacyl-tRNA synthase</name>
        <name>Amino acid translase</name>
        <name>Aminoacyl-tRNA ligase</name>
        <description>Enzyme that activates an amino acid for translation by forming an
aminoacyladenylate intermediate and then links this activated amino
acid to the corresponding tRNA molecule (amino acid-tRNA, aminoacyl-
tRNA). In general, a specific aminoacyl-tRNA synthase is available for
each amino acid</description>
        <go id="GO:0004812"/>
    </keyword>
    <keyword id="KW-0031">
        <name>Aminopeptidase</name>
        <description>Enzyme that catalyzes the removal of amino acids from the N-terminus
of peptides and proteins</description>
        <go id="GO:0004177"/>
    </keyword>
    <keyword id="KW-0032">
        <name>Aminotransferase</name>
        <name>Transaminase</name>
        <description>Enzyme that catalyzes the transfer of an alpha-amino group from an
amino acid to an alpha-keto acid. The amino group is usually
covalently bound by the prosthetic group pyridoxal phosphate</description>
        <go id="GO:0008483"/>
    </keyword>
    <keyword id="KW-0924">
        <name>Ammonia transport</name>
        <name>Ammonium transport</name>
        <description>Protein involved in the transport of ammonia/ammonium. Ammonia is an
excellent nitrogen source for many bacteria, fungi, and plants, but it
can be cytotoxic, especially for animal cells at high concentration
Its transport across cellular membranes is thus of high biological
relevance. Ammonia (NH3) is a weak base and exists predominantly as
the ammonium ion (NH4+) in biological fluids</description>
        <go id="GO:0072488"/>
    </keyword>
    <keyword id="KW-0878">
        <name>Amphibian defense peptide</name>
        <description>Protein specifically found in the skin of animals belonging to the
vertebrate class amphibia, that includes frogs, toads, newts,
salamanders and worm-like apoda. The skins of anuran amphibians, in
addition to mucous glands, contain highly specialized poison glands,
which, in reaction to stress or attack, exude a complex noxious
species-specific cocktail of biologically active molecules. These
secretions often contain a plethora of peptides such as neuropeptides
and hormones. The frog dermatous glands also synthesize and store an
extraordinarily rich variety of wide-spectrum antimicrobial peptides
that are released onto the outer layer of the skin to provide an
effective and fast-acting defense against harmful microorganisms</description>
        <go id="GO:0006952"/>
    </keyword>
    <keyword id="KW-0034">
        <name>Amyloid</name>
        <name>Amyloid filament-forming</name>
        <name>Amyloid-forming</name>
        <name>Amyloid-like fibril-forming</name>
        <name>Amyloid-like filament-forming</name>
        <name>Amyloid-like fibre-forming</name>
        <name>Functional amyloid</name>
        <name>Amyloid fibre-forming</name>
        <name>Amyloid fibril-forming</name>
        <description>Proteins which may form wide, insoluble, unbranched filaments
possessing a cross-beta sheet quaternary structure, where the beta
sheets are oriented perpendicular to the fibre axis. Amyloid fibrils
may be involved in abnormal protein depositions, or amyloidosis, such
as Alzheimer's or Parkinson's diseases. Functional amyloids, found in
a wide range of organism, from bacteria to mammals are involved in
diverse functions such as biofilm formation, formation of aerial
hyphae, long-term memory or regulation of melanin biosynthesis</description>
    </keyword>
    <keyword id="KW-1008">
        <name>Amyloidosis</name>
        <description>Protein which, if defective, causes amyloidosis, a vast group of
diseases defined by the accumulation of amyloid in tissues
Amyloidoses are classified according to clinical signs, biochemical
type of amyloid protein involved, and the extent of amyloid deposition
(generalized or localized). Most amyloidoses are multisystemic
diseases affecting several organs or systems. Mainly affected organs
are the kidneys, heart, gastrointestinal tract, liver, skin,
peripheral nerves and eyes, but any organ can be affected. The most
frequent forms are primary amyloidosis, also known as light-chain
immunoglobulin amyloidosis (AL), reactive or inflammatory amyloidosis,
also known as acquired amyloidosis (AA), and transthyretin amyloidosis
(ATTR). Localized amyloidosis affecting the brain is characteristic of
Alzheimer's disease, trisomy 21, and prion diseases (transmissible
spongiform encephalitis, Creutzfeldt-Jakob disease, Gerstmann-
Straussler-Scheinker syndrome, fatal familial insomnia). In prion
diseases the amyloid precursor is the prion protein</description>
    </keyword>
    <keyword id="KW-0035">
        <name>Amyloplast</name>
        <description>Protein found in the amyloplast, a colorless plant plastid that forms
and stores starch. Amyloplasts are found in many tissues, particularly
in storage tissues</description>
    </keyword>
    <keyword id="KW-0036">
        <name>Amyotrophic lateral sclerosis</name>
        <name>ALS</name>
        <description>Protein which, if defective, causes amyotrophic lateral sclerosis
(ALS), a degenerative disorder of motor neurons in the cortex, brain
stem and spinal cord. ALS is characterized by muscular weakness and
atrophy</description>
    </keyword>
    <keyword id="KW-0037">
        <name>Angiogenesis</name>
        <name>Vascularization</name>
        <description>Protein involved in angiogenesis, the sprouting or splitting of
capillaries from pre-existing vasculature. Angiogenesis plays an
important role for example during embryonic development, normal growth
of tissues and maintenance of the normal vasculature, wound healing,
tumor growth and metastasis</description>
        <go id="GO:0001525"/>
    </keyword>
    <keyword id="KW-0039">
        <name>Anion exchange</name>
        <name>Anion exchanger activity</name>
        <description>Protein involved in the exchange of anions across a membrane. Anion
exchange is a cellular transport function which contributes to the
regulation of cell pH and volume by a functionally related anion
exchanger protein family</description>
        <go id="GO:0015297"/>
    </keyword>
    <keyword id="KW-0040">
        <name>ANK repeat</name>
        <name>ANK motif</name>
        <name>Ankyrin repeat</name>
        <description>Protein containing at least one ANK repeat, a conserved domain of
approximately 33 amino acids, that was originally identified in
ankyrin. It has been described as an L-shaped structure consisting of
a beta-hairpin and two alpha-helices. Many ankyrin repeat regions are
known to function as protein-protein interaction domains</description>
    </keyword>
    <keyword id="KW-0041">
        <name>Annexin</name>
        <name>Annexin repeat</name>
        <description>Protein containing at least one annexin repeat, a conserved domain of
61 residues, which is present in proteins of the annexin family in
either four or eight copies. The annexin calcium binding sites are
found within the repeated domains</description>
    </keyword>
    <keyword id="KW-0042">
        <name>Antenna complex</name>
        <name>Light-harvesting antenna</name>
        <name>Light-harvesting complex</name>
        <description>Component of an antenna complex or protein regulating the expression
of such components. Antenna complexes are light-harvesting systems
(LHC) which are protein-pigment complexes in or on photosynthetic
membranes. LHCs receive radiant energy and transfer it to the reaction
centers; an array of LHCs is often referred to as an "antenna". LHCs
typically include one or more associated pigments (phycobilins,
chlorophylls, bacteriochlorophylls and carotenoids)</description>
        <go id="GO:0030076"/>
    </keyword>
    <keyword id="KW-0044">
        <name>Antibiotic</name>
        <name>Antibacterial</name>
        <name>Bactericide</name>
        <description>Protein with antibacterial activity</description>
        <go id="GO:0042742"/>
    </keyword>
    <keyword id="KW-0045">
        <name>Antibiotic biosynthesis</name>
        <name>Antibiotic formation</name>
        <name>Antibiotic anabolism</name>
        <name>Antibiotic synthesis</name>
        <description>Protein involved in the synthesis of antibiotics. Antibiotics are
organic compounds produced by living organims that can selectively
inhibit the growth of, or kill bacteria</description>
        <go id="GO:0017000"/>
    </keyword>
    <keyword id="KW-0046">
        <name>Antibiotic resistance</name>
        <name>Resistance to antibiotic</name>
        <description>Protein that confers, on bacteria, the ability to withstand
antibiotics. The resistance is often due either to mutations that
prevent antibiotic binding to the protein or to amplification of the
gene encoding the protein</description>
        <go id="GO:0046677"/>
    </keyword>
    <keyword id="KW-0047">
        <name>Antifreeze protein</name>
        <name>Ice structuring protein</name>
        <name>ISP</name>
        <name>AFP</name>
        <description>Protein that lowers the freezing point of blood or other biological
fluids by inhibiting the formation of water ice crystals</description>
    </keyword>
    <keyword id="KW-0929">
        <name>Antimicrobial</name>
        <description>Protein which has deleterious effects on any type of microbe. Microbe
is a general term for microscopic unicellular organisms, such as
bacteria, archaea, fungi and protista. While the term microbe is often
also used for viruses, we do not apply the keyword antimicrobial to
antiviral proteins</description>
    </keyword>
    <keyword id="KW-0049">
        <name>Antioxidant</name>
        <description>Protein capable of counteracting the damaging effects of oxidation,
e.g. by trapping free radicals generated during the metabolic burst
and possibly inhibiting ageing. Scavengers of highly reactive and
harmful oxygen species</description>
        <go id="GO:0016209"/>
    </keyword>
    <keyword id="KW-0050">
        <name>Antiport</name>
        <name>Exchange transporter</name>
        <name>Antiporter</name>
        <name>Exchanger</name>
        <name>Countertransporter</name>
        <description>Protein involved in the transport of a solute across a biological
membrane coupled, directly, to the transport of a different solute in
the opposite direction</description>
        <go id="GO:0015297"/>
    </keyword>
    <keyword id="KW-0051">
        <name>Antiviral defense</name>
        <description>Protein synthesized or activated in the cell in response to viral
infection, or protein with specific antiviral activity within the
cell. Eukaryotic cells have an innate immune mechanism to fight viral
infection, which is activated through the interferon signaling pathway
or through dsRNA detection in the cytoplasm. It leads to the
establishment of an antiviral cell state, which prevents virus
replication or induces apoptosis. Most viruses have developed specific
proteins to prevent the establishment of an antiviral state. About
half of all bacteria and most archaea have a CRISPR (clustered
regularly interspersed short plaindromic repeats) system of adaptive
immunity to exogenous DNA. CRISPRs clusters are tandem arrays of
alternating repeats and spacers, where the spacers in some cases are
homologous to sequences from virus and plasmid genomes. The CRISPR
arrays are transcribed, processed and in some way aid in detection and
resistance to foreign DNA. In at least a few bacteria (E.coli,
S.epidermidis) it seems DNA is the target, whereas in Pyrococcus
furiosis it seems the CRISPR system targets RNA</description>
        <go id="GO:0051607"/>
    </keyword>
    <keyword id="KW-0930">
        <name>Antiviral protein</name>
        <description>Protein with antiviral activity. Often this activity is fortuitous
(e.g. a bacterial protein displaying anti-HIV activity)</description>
        <go id="GO:0050688"/>
    </keyword>
    <keyword id="KW-0993">
        <name>Aortic aneurysm</name>
        <description>Protein which, if defective, causes aortic aneurysm. Aortic aneurysm
is the dilation of the wall of the aorta. It forms a sac that is
filled with fluid or clotted blood, often resulting in a pulsating
tumor. Aortic aneurysms are classified by their location on the aorta</description>
    </keyword>
    <keyword id="KW-0933">
        <name>Apicoplast</name>
        <name>Thick-walled organelle</name>
        <name>Golgi-adjunct organelle</name>
        <description>Protein encoded by the apicoplast genome or protein located in the
apicoplast, a plastid found in some apicomplexan parasites which is a
non-photosynthetic plastid relict. This organelle contains ring-like
DNA of about 35 Kb as a third type of cell genome. Apicoplasts do not
contain thylakoids; it is not yet clear if they contain internal
membranes</description>
    </keyword>
    <keyword id="KW-0052">
        <name>Apoplast</name>
        <description>Protein which is found in the part of the plant which is external to
the living protoplast, ie the cell wall, the intercellular space and
the lumina of dead cells such as xylem vessels and tracheids</description>
    </keyword>
    <keyword id="KW-0053">
        <name>Apoptosis</name>
        <name>Active cell death</name>
        <name>Apoptotic programmed cell death</name>
        <name>Type I programmed cell death</name>
        <description>Protein involved in apoptotic programmed cell death. Apoptosis is
characterized by cell morphological changes, including blebbing, cell
shrinkage, nuclear fragmentation, chromatin condensation and
chromosomal DNA fragmentation, and eventually death. Unlike necrosis,
apoptosis produces cell fragments, called apoptotic bodies, that
phagocytic cells are able to engulf and quickly remove before the
contents of the cell can spill out onto surrounding cells and cause
damage. In general, apoptosis confers advantages during an organism's
life cycle</description>
        <go id="GO:0006915"/>
    </keyword>
    <keyword id="KW-0054">
        <name>Arabinose catabolism</name>
        <name>Arabinose degradation</name>
        <name>Arabinose breakdown</name>
        <name>Arabinose catabolic process</name>
        <description>Protein involved in arabinose breakdown. Arabinose is a 5-carbon
aldose sugar found in plant gums, pectins and bacterial cell wall
polysaccharides</description>
        <go id="GO:0019568"/>
    </keyword>
    <keyword id="KW-0974">
        <name>Archaeal flagellum</name>
        <name>Archaellum</name>
        <name>Archaeal flagella</name>
        <name>Archaeal flagellar apparatus</name>
        <description>The archaellum (archaeal flagellum) is the motility apparatus of
archaea which propels the cell through liquid medium. The archaellum
is the functional equivalent of the bacterial flagellum but its
architecture, composition and mode of assembly is completely
unrelated. The archaellum is thinner (10-15 nm) compared to the
bacterial flagellum (18-24 nm). Its filament is assembled from
archaellin subunits, which are N-glycosylated proteins. The archaellum
is considered to be a type IV pilus-like structure and accordingly is
assembled from the base into a 3-start helix. Archaellins have a type
III signal sequence which is removed by the pre-archaellin peptidase
Core components of the assembly machinery are ArlI and ArlJ
(previously FlaI, FlaJ) which are distantly related to PilB and PilC
from type II secretion systems and type IV pills assembly systems
ArlI is a dual function ATPase which first assembles the filament and
then rotates it by using the energy from ATP hydrolysis. Ion gradients
are not used for archaellum rotation</description>
    </keyword>
    <keyword id="KW-1209">
        <name>Archaeal flagellum biogenesis</name>
        <name>Archaeal flagellar apparatus biogenesis</name>
        <name>Archaeal flagella biogenesis</name>
        <description>Protein which is involved in the formation, organization or
maintenance of the archaellum (archaeal flagellum) the motility
apparatus of archaea which propels the cell through liquid medium. The
archaellum is the functional equivalent of the bacterial flagellum but
its architecture, composition and mode of assembly is completely
unrelated. The archaellum is thinner (10-15 nm) compared to the
bacterial flagellum (18-24 nm). Its filament is assembled from
archaellin subunits (archaeal flagellin), N-glycosylated proteins. The
archaellum is considered to be a type IV pilus-like structure and
accordingly is assembled from the base into a 3-start helix
Archaellins have a type III signal sequence which is removed by the
pre-archaellin peptidase. Core components of the assembly machinery
are ArlI and ArlJ (previously FlaI, FlaJ) which are distantly related
to PilB and PilC from type II secretion systems and type IV pills
assembly systems. ArlI is a dual function ATPase which first assembles
the filament and then rotates it by using the energy from ATP
hydrolysis</description>
    </keyword>
    <keyword id="KW-0055">
        <name>Arginine biosynthesis</name>
        <name>Arginine synthesis</name>
        <name>Arginine anabolism</name>
        <name>Arginine formation</name>
        <name>Arginine biosynthetic process</name>
        <description>Protein involved in the synthesis of the basic amino acid arginine
(Arg)</description>
        <go id="GO:0006526"/>
    </keyword>
    <keyword id="KW-0056">
        <name>Arginine metabolism</name>
        <name>Arginine metabolic process</name>
        <description>Protein involved in biochemical reactions with the basic amino acid
arginine (Arg)</description>
        <go id="GO:0006525"/>
    </keyword>
    <keyword id="KW-0057">
        <name>Aromatic amino acid biosynthesis</name>
        <name>Aromatic amino acid synthesis</name>
        <name>Aromatic amino acid anabolism</name>
        <name>Aromatic amino acid formation</name>
        <name>Aromatic amino acid family biosynthetic process</name>
        <description>Protein involved in the synthesis of an amino acid with an aromatic
side-chain: phenylalanine (Phe), tyrosine (Tyr) and tryptophan (Trp)</description>
        <go id="GO:0009073"/>
    </keyword>
    <keyword id="KW-0058">
        <name>Aromatic hydrocarbons catabolism</name>
        <name>Aromatic hydrocarbons degradation</name>
        <name>Aromatic hydrocarbons breakdown</name>
        <name>Aromatic compound catabolic process</name>
        <description>Protein involved in the breakdown of aromatic hydrocarbons. Aromatic
hydrocarbons are compounds which only contain carbon and hydrogen,
examples include the common pollutants benzene and naphthalene</description>
        <go id="GO:0009056"/>
    </keyword>
    <keyword id="KW-0059">
        <name>Arsenical resistance</name>
        <name>Arsenic resistance</name>
        <name>Resistance to arsenic</name>
        <description>Protein that confers, on bacteria and other microorganisms, the
ability to withstand aromatic compounds of arsenic</description>
        <go id="GO:0046685"/>
    </keyword>
    <keyword id="KW-0060">
        <name>Ascorbate biosynthesis</name>
        <name>Ascorbate synthesis</name>
        <name>Ascorbate anabolism</name>
        <name>Ascorbate formation</name>
        <name>Ascorbic acid biosynthesis</name>
        <name>Ascorbic acid synthesis</name>
        <name>Ascorbic acid anabolism</name>
        <name>Ascorbic acid formation</name>
        <name>Vitamin C biosynthesis</name>
        <name>Ascorbate biosynthetic process</name>
        <name>Vitamin C biosynthetic process</name>
        <name>Ascorbic acid biosynthetic process</name>
        <name>Vitamin C anabolism</name>
        <name>Vitamin C synthesis</name>
        <name>Vitamin C formation</name>
        <description>Protein involved in the synthesis of ascorbate, the ionized form of
ascorbic acid (vitamin C). Ascorbic acid is derived from glucose via
the uronic acid pathway. This water-soluble vitamin is essential for
the synthesis of bone, cartilage and dentine. It is required in the
diet of primates and some other species that cannot synthesize L-
ascorbic acid because of their deficiency in L-gulono-gamma-lactone
oxidase, a key enzyme for the biosynthesis of this vitamin</description>
        <go id="GO:0019853"/>
    </keyword>
    <keyword id="KW-0061">
        <name>Asparagine biosynthesis</name>
        <name>Asparagine biosynthetic process</name>
        <name>Asparagine anabolism</name>
        <name>Asparagine formation</name>
        <name>Asparagine synthesis</name>
        <description>Protein involved in the synthesis of the polar amino acid asparagine
(Asn)</description>
        <go id="GO:0006529"/>
    </keyword>
    <keyword id="KW-0062">
        <name>Aspartic protease inhibitor</name>
        <name>Aspartic-type endopeptidase inhibitor</name>
        <name>Aspartic proteinase inhibitor</name>
        <name>Aspartyl protease inhibitor</name>
        <description>Protein which inhibits the catalytic activity of an aspartyl protease,
a class of proteases that contains an active site aspartate residue
(Asp), e.g. pepsin, HIV retropepsin, renin, etc</description>
        <go id="GO:0019828"/>
    </keyword>
    <keyword id="KW-0063">
        <name>Aspartyl esterase</name>
        <description>Enzyme which catalyzes the hydrolysis of esters and is characterized
by a catalytically active aspartic acid residue in its active site</description>
        <go id="GO:0045330"/>
    </keyword>
    <keyword id="KW-0064">
        <name>Aspartyl protease</name>
        <name>Acid protease</name>
        <name>Aspartic-type endopeptidase</name>
        <name>Aspartic proteinase</name>
        <name>Aspartate protease</name>
        <name>Aspartic protease</name>
        <name>Aspartyl proteinase</name>
        <description>Proteolytic enzyme with an aspartate residue (Asp) in its active site
There are many families of aspartyl proteases. The most well known one
is the pepsin family (A1 in MEROPS classification) which is known to
exist in vertebrates, fungi, plants, retroviruses and some plant
viruses</description>
        <go id="GO:0004190"/>
    </keyword>
    <keyword id="KW-1270">
        <name>Asperger syndrome</name>
        <description>Protein which, if defective, is involved in Asperger syndrome, a
complex, multifactorial disorder. It is characterized by clinically
significant impairment of social interaction, and restricted
repetitive and stereotyped patterns of behavior. Asperger syndrome is
primarily distinguished from autism by the higher cognitive abilities
and a more normal and timely development of language and communicative
phrases</description>
    </keyword>
    <keyword id="KW-1058">
        <name>Asthma</name>
        <description>Protein which, if defective, is associated with asthma, a bronchial
disorder associated with airway inflammation, swelling and
obstruction. It is marked by recurrent attacks of paroxysmal dyspnea,
with wheezing due to spasmodic contraction of the bronchi</description>
    </keyword>
    <keyword id="KW-0065">
        <name>Atherosclerosis</name>
        <name>Arteriosclerosis</name>
        <description>Protein which, if defective, causes atherosclerosis, which is
characterized by deposits of plaques (atheromas) in the blood vessels,
thus narrowing the vessel lumen and restricting blood flow. Atheromas
consist of lipids (cholesterol), carbohydrates, blood products,
fibrous tissue and calcium deposits</description>
    </keyword>
    <keyword id="KW-0066">
        <name>ATP synthesis</name>
        <name>ATP biosynthetic process</name>
        <name>ATP formation</name>
        <name>Adenosine 5'-triphosphate formation</name>
        <name>Adenosine triphosphate biosynthetic process</name>
        <name>Adenosine triphosphate formation</name>
        <name>Adenosine 5'-triphosphate biosynthetic process</name>
        <name>Adenosine 5'-triphosphate biosynthesis</name>
        <name>Adenosine triphosphate anabolism</name>
        <name>Adenosine triphosphate biosynthesis</name>
        <name>ATP biosynthesis</name>
        <name>Adenosine 5'-triphosphate anabolism</name>
        <name>ATP anabolism</name>
        <description>Protein involved in the synthesis of adenosine 5'-triphosphate (ATP)
ATP is a ribonucleotide adenosine (a purine base adenine linked to the
sugar D-ribofuranose) which carries 3 phosphate groups esterified to
the sugar moiety. It is the cell's source for energy and phosphate</description>
        <go id="GO:0006754"/>
    </keyword>
    <keyword id="KW-0067">
        <name>ATP-binding</name>
        <name>Adenosine triphosphate binding</name>
        <name>Adenosine 5'-triphosphate binding</name>
        <description>Protein which binds adenosine 5'-triphosphate (ATP), a ribonucleotide
adenosine (a purine base adenine linked to the sugar D-ribofuranose)
that carries three phosphate groups esterified to the sugar moiety. It
is the cell's source for energy and phosphate</description>
        <go id="GO:0005524"/>
    </keyword>
    <keyword id="KW-1020">
        <name>Atrial fibrillation</name>
        <name>ATFB</name>
        <name>AF</name>
        <description>Protein which, if defective, causes atrial fibrillation, a common
cardiac arrhythmia marked by disorganized atrial electrical activity
and rapid randomized contractions of small areas of the atrial
myocardium, causing a totally irregular, and rapid, ventricular rate</description>
    </keyword>
    <keyword id="KW-0976">
        <name>Atrial septal defect</name>
        <name>Atrioseptal defect</name>
        <description>Protein which, if defective, causes atrial septal defect, a congenital
cardiac anomaly characterized by persistent patency of the atrial
septum that results in blood flow between the atria. It is due to
failure of fusion between either the septum secundum or the septum
primum and the endocardial cushions</description>
    </keyword>
    <keyword id="KW-1269">
        <name>Autism</name>
        <name>Autistic disorder</name>
        <description>Protein which, if defective, is involved in autism, a pervasive
developmental disorder. It is a complex, multifactorial disease
characterized by impairments in reciprocal social interaction and
communication, restricted and stereotyped patterns of interests and
activities, and the presence of developmental abnormalities by 3 years
of age. Most individuals with autism manifest moderate mental
retardation</description>
    </keyword>
    <keyword id="KW-1268">
        <name>Autism spectrum disorder</name>
        <name>ASD</name>
        <description>Protein which, if defective, is involved in autism spectrum disorder,
a clinically heterogeneous group of disorders that share common
features of impaired social relationships, impaired language and
communication, repetitive behaviors, and a restricted range of
interests. The spectrum includes diverse phenotypic manifestations,
such as classic autism, Asperger syndrome, childhood disintegrative
disorder, Rett syndrome, and pervasive developmental disorder not
otherwise specified</description>
    </keyword>
    <keyword id="KW-0068">
        <name>Autocatalytic cleavage</name>
        <name>Autocatalytic peptide cleavage</name>
        <description>Protein catalyzing its own cleavage</description>
    </keyword>
    <keyword id="KW-0069">
        <name>Autoimmune encephalomyelitis</name>
        <name>Autoimmune encephalitis</name>
        <description>Protein which, if defective, causes autoimmune encephalomyelitis. This
form of autoimmune inflammation of the brain and spinal cord causes
demyelination</description>
    </keyword>
    <keyword id="KW-0070">
        <name>Autoimmune uveitis</name>
        <description>Protein which, if defective, causes autoimmune inflammation of the
uvea, which is the vascular middle coat of the eye, comprising the
iris, ciliary body and choroid</description>
    </keyword>
    <keyword id="KW-0071">
        <name>Autoinducer synthesis</name>
        <name>Autoinducer anabolism</name>
        <name>Autoinducer biosynthesis</name>
        <name>Autoinducer formation</name>
        <name>Autoinducer biosynthetic process</name>
        <description>Protein involved in the synthesis of an autoinducer, a molecule which
triggers the regulators of biosynthetic genes</description>
    </keyword>
    <keyword id="KW-0072">
        <name>Autophagy</name>
        <description>Protein participating in autophagy, a process of intracellular bulk
degradation in which cytoplasmic components including organelles are
sequestered within double-membrane vesicles that deliver the contents
to the lysosome/vacuole for degradation. There are three primary forms
of autophagy: chaperone-mediated autophagy, microautophagy and
macroautophagy. During macroautophagy, the sequestering vesicles,
termed autophagosomes, fuse with the lysosome or vacuole resulting in
the delivery of an inner vesicle (autophagic body) into the lumen of
the degradative compartment</description>
        <go id="GO:0006914"/>
    </keyword>
    <keyword id="KW-0073">
        <name>Auxin biosynthesis</name>
        <name>Auxin biosynthetic process</name>
        <name>Auxin anabolism</name>
        <name>Auxin formation</name>
        <name>Auxin synthesis</name>
        <description>Protein involved in the synthesis of auxins. Auxins are plant hormones
which play a role in many aspects of plant growth and development</description>
        <go id="GO:0009851"/>
    </keyword>
    <keyword id="KW-0927">
        <name>Auxin signaling pathway</name>
        <name>Auxin mediated signaling pathway</name>
        <description>Protein involved in the auxin signaling pathway (e.g. transport and
signal transduction) that regulates many aspects of plant growth and
development (e.g. caulogenesis, rhizogenesis, tropisms, nodulation)
The major form of this phytohormone is indole-3-acetic acid (IAA) that
can be synthesized both from tryptophan (Trp) using Trp-dependent
pathways and from an indolic Trp precursor via Trp-independent
pathways. Plants can also obtain IAA by b-oxidation of indole-3-
butyric acid (IBA), a second endogenous auxin, or by hydrolysing IAA
conjugates, in which IAA is linked to amino acids, sugars or peptides</description>
        <go id="GO:0009734"/>
    </keyword>
    <keyword id="KW-0075">
        <name>B-cell activation</name>
        <description>Protein involved in the activation and proliferation of B-cells. B-
cells are activated by the binding of antigen to receptors on its cell
surface which causes the cell to divide and proliferate. Some
stimulated B-cells become plasma cells, which secrete antibodies
Others become long-lived memory B-cells which can be stimulated at a
later time to differentiate into plasma cells</description>
        <go id="GO:0042113"/>
    </keyword>
    <keyword id="KW-0975">
        <name>Bacterial flagellum</name>
        <name>Bacterial flagellar apparatus</name>
        <name>Bacterial flagella</name>
        <description>Bacterial protein present in a flagellum, a long hair-like cell
surface appendage. The flagellar apparatus consists of the flagellar
filament made of polymerized flagellin, the hook-like structure near
the cell surface and a system of rings embedded in the cell enveloppe
(the basal body or flagellar motor). The basal body and the hook
anchor the whip-like filament to the cell surface. The flagellum is a
rotating structure with switches propels the cell through a liquid
medium</description>
    </keyword>
    <keyword id="KW-1005">
        <name>Bacterial flagellum biogenesis</name>
        <name>Bacterial flagellar apparatus biogenesis</name>
        <name>Bacterial flagella biogenesis</name>
        <description>Protein which is involved in the formation, organization or
maintenance of the bacterial flagellum, a long hair-like cell surface
appendage. The flagellar apparatus consists of the flagellar filament
made of polymerized flagellin, the hook-like structure near the cell
surface and a system of rings embedded in the cell enveloppe (the
basal body or flagellar motor). The basal body and the hook anchor the
whip-like filament to the cell surface. The flagellum is a rotating
structure whose switches propels the cell through a liquid medium</description>
        <go id="GO:0044781"/>
    </keyword>
    <keyword id="KW-1006">
        <name>Bacterial flagellum protein export</name>
        <name>Bacterial flagellar apparatus protein export</name>
        <name>Bacterial flagella protein export</name>
        <name>Bacterial flagellar protein export</name>
        <description>Protein which is involved in the export of bacterial flagellar
proteins. The bacterial flagellum export apparatus consists of six
integral membrane proteins (FlhA, FlhB, FliO, FliP, FliQ and FliR) and
three soluble proteins (FliH, FliI and FliJ), and is located at the
base of the flagellum. This system is characterized by ATP hydrolysis
and a lack of substrate signal peptide cleavage</description>
    </keyword>
    <keyword id="KW-1261">
        <name>Bacterial host gene expression shutoff by virus</name>
        <description>Viral protein which prevents host gene expression by blocking host
transcription or inducing the degradation of the bacterial chromosome
This gives viral transcripts a competitive edge to use the hijacked
host translation machinery. Preventing the expression of host proteins
is also a strategy to counteract the antiviral response</description>
    </keyword>
    <keyword id="KW-1263">
        <name>Bacterial host transcription shutoff by virus</name>
        <description>Viral protein involved in inhibiting transcription of bacterial genes
to ensure the shutoff of host proteins expression and give viral
transcripts a competitive edge for access to the cellular translation
machinery. Preventing the expression of host proteins is also a
strategy to counteract the antiviral response. Some bacterial viruses
inhibit the host RNAP: bacteriophage SPO1 for example is known to shut
off host RNA synthesis</description>
    </keyword>
    <keyword id="KW-1283">
        <name>Bacterial microcompartment</name>
        <description>Protein located in or on a bacterial microcompartment (BMC),
proteinaceous polyhedral shells that encapsulate enzymes. The
selectively permeable organelles protect their contents from the
cytoplasm and/or the cytoplasm from reactants in their interior
Examples of BMCs include carboxysomes, which enhance autotrophic CO(2)
fixation by encapsulating RuBisCO and carbonic anhydrase, as well as
BMCs involved in ethanolamine or propanediol degradation; both
pathways make toxic intermediates. Artifical BMCs can be expressed and
filled with cargo proteins for biotechnological uses. BMCs are found
in many bacterial phyla; in most cases their cargo is unknown</description>
    </keyword>
    <keyword id="KW-0076">
        <name>Bacteriochlorophyll</name>
        <description>Protein interacting with bacteriochlorophyll, a photosynthetic pigment
found in non-oxygenic photosynthetic bacteria. It is a magnesium-
porphyrin complex esterified to a long hydrophobic terpenoid side
chain (the alcohol phytol). It differs from chlorophyll of oxygenic
organisms in the substituents around the tetrapyrrole nucleus of the
molecule, and in the absorption spectra. Different bacteria have
different species of bacteriochlorophyll</description>
        <go id="GO:0042314"/>
    </keyword>
    <keyword id="KW-0077">
        <name>Bacteriochlorophyll biosynthesis</name>
        <name>Bacteriochlorophyll anabolism</name>
        <name>Bacteriochlorophyll formation</name>
        <name>Bacteriochlorophyll synthesis</name>
        <name>Bacteriochlorophyll biosynthetic process</name>
        <description>Protein involved in the synthesis of bacteriochlorophylls. These
photosynthetic pigments are magnesium-porphyrin complexes with a long
hydrophobic terpenoid side chain (the alcohol phytol). Biosynthesis of
bacteriochlorophyll is a light-independent reaction</description>
        <go id="GO:0030494"/>
    </keyword>
    <keyword id="KW-0078">
        <name>Bacteriocin</name>
        <description>Peptidic antibiotic, often plasmid encoded, produced by specific
strains of bacteria that is lethal against other strains of the same
or related species. E.g. bacteriocin, colicin, lantibiotic</description>
        <go id="GO:0031640"/>
    </keyword>
    <keyword id="KW-0871">
        <name>Bacteriocin biosynthesis</name>
        <name>Bacteriocin biosynthetic process</name>
        <name>Bacteriocin synthesis</name>
        <name>Bacteriocin anabolism</name>
        <name>Bacteriocin formation</name>
        <description>Protein involved in the synthesis of a bacteriocin</description>
        <go id="GO:0030152"/>
    </keyword>
    <keyword id="KW-0079">
        <name>Bacteriocin immunity</name>
        <description>Protein that confers to a bacteria immunity against a specific
bacteriocin that it synthesizes</description>
        <go id="GO:0030153"/>
    </keyword>
    <keyword id="KW-0080">
        <name>Bacteriocin transport</name>
        <description>Protein involved in the export of a bacteriocin (bacterial
antibiotic)</description>
        <go id="GO:0043213"/>
    </keyword>
    <keyword id="KW-0081">
        <name>Bacteriolytic enzyme</name>
        <description>Enzyme, e.g. lysozyme or endopeptidase, essential for lysis of
bacterial cell walls</description>
        <go id="GO:0008152"/>
        <go id="GO:0031640"/>
        <go id="GO:0042742"/>
        <go id="GO:0003824"/>
    </keyword>
    <keyword id="KW-0082">
        <name>Bait region</name>
        <description>Protein having a peptide stretch which contains specific cleavage
sites for different proteinases, and which enables inhibition of all
four classes of proteinases</description>
        <go id="GO:0030414"/>
        <go id="GO:0010466"/>
    </keyword>
    <keyword id="KW-0083">
        <name>Bardet-Biedl syndrome</name>
        <name>BBS</name>
        <description>Protein which, if defective, causes Bardet-Biedl syndrome (BBS), a
genetically heterogeneous, autosomal recessive disorder. It is
characterized by pigmentary retinopathy, obesity, polydactyly,
hypogenitalism, renal malformation and intellectual disability
Secondary features include diabetes mellitus, hypertension and
congenital heart disease</description>
    </keyword>
    <keyword id="KW-0910">
        <name>Bartter syndrome</name>
        <description>Protein which, if defective, causes Bartter syndrome (BS). In general,
Bartter syndrome refers to a group of autosomal recessive disorders
characterized by often severe intravascular volume depletion due to
renal salt-wasting associated with low blood pressure, hypokalemic
alkalosis, hypercalciuria, and normal serum magnesium levels. Patients
with Bartter syndrome are often critically ill from birth onwards, and
their long-term clinical course may be complicated by
nephrocalcinosis, leading to renal failure. Clinical disease results
from defective renal reabsorption of sodium chloride in the thick
ascending limb (TAL) of the Henle loop, where only 30% of filtered
salt is normally reabsorbed</description>
    </keyword>
    <keyword id="KW-0084">
        <name>Basement membrane</name>
        <description>Protein which is a component of the basement membrane, an
extracellular matrix found under epithelial cells and around smooth
and striated muscle cells. This matrix contains intrinsic
macromolecular components such as collagen, laminin, and sulfated
proteoglycans</description>
    </keyword>
    <keyword id="KW-0085">
        <name>Behavior</name>
        <description>Protein which affects the behavior, the action or reaction, of an
organism to a stimulus or situation</description>
        <go id="GO:0007610"/>
    </keyword>
    <keyword id="KW-0086">
        <name>Bence-Jones protein</name>
        <description>Protein which is a dimer of immunoglobulin light chains synthesized in
large amounts by patients who have myeloma or bone marrow tumor
Bence-Jones protein is sufficiently small to be excreted by the kidney
into urine</description>
    </keyword>
    <keyword id="KW-0087">
        <name>Bernard Soulier syndrome</name>
        <name>BSS</name>
        <description>Protein which, if defective, causes Bernard Soulier syndrome (BSS), a
familial coagulation disorder characterized by a prolonged bleeding
time, unusually large platelets, and impaired prothrombin consumption
BSS is caused by a genetic deficiency in platelet membrane
glycoprotein Ib alpha chain and platelet glycoprotein IX, where
platelets aggregate normally but do not stick to collagen of the sub-
endothelial membrane</description>
    </keyword>
    <keyword id="KW-0088">
        <name>Bile acid catabolism</name>
        <name>Bile acid degradation</name>
        <name>Bile salt breakdown</name>
        <name>Bile salt catabolism</name>
        <name>Bile salt degradation</name>
        <name>Bile salt catabolic process</name>
        <name>Bile acid breakdown</name>
        <name>Bile acid catabolic process</name>
        <description>Protein involved in degradation of bile acids. Bile acids, which exist
mainly as bile salts, are a family of carboxylic acid derivatives of
cholesterol which play an important role in the digestion and
absorption of fat. They are made in the liver, stored in the
gallblader, and secreted as needed into the intestines</description>
        <go id="GO:0030573"/>
    </keyword>
    <keyword id="KW-0089">
        <name>Bile pigment</name>
        <name>Bilin chromophore</name>
        <description>Protein binding covalently at least one linear tetrapyrrole
chromophore, e.g. bilirubin, biliverdin, bilifuscin, biliprasin,
choleprasin, bilihumin, and bilicyanin. Bile pigments are produced by
breaking down protoporphyrin IX derived from hemoglobin and other heme
proteins</description>
    </keyword>
    <keyword id="KW-0090">
        <name>Biological rhythms</name>
        <name>Rhythmic process</name>
        <description>Protein involved in the generation of rhythmic pattern of behaviors or
activities, e.g. circadian rhythm which is a metabolic or behavioural
rhythm within a cycle of 24 hours</description>
        <go id="GO:0048511"/>
    </keyword>
    <keyword id="KW-0091">
        <name>Biomineralization</name>
        <description>Protein involved in the process by which mineral crystals are
deposited in an organized fashion in the matrix (either cellular or
extracellular) of living organisms. Such process give rise to
inorganic-based structures such as bone, tooth, ivory, shells,
cuticles, corals or bacterial magnetosomes</description>
        <go id="GO:0031214"/>
    </keyword>
    <keyword id="KW-0092">
        <name>Biotin</name>
        <name>Biopeiderm</name>
        <name>Vitamin B8</name>
        <name>Vitamin H</name>
        <name>Coenzyme R</name>
        <name>Vitamin B7</name>
        <description>Protein which contains at least one biotin as prosthetic group or
cofactor (e.g. some carboxylases and decarboxylases, and biotin
carboxyl carrier protein) or which binds biotin, like avidin. Biotin
is a water-soluble vitamin (member of the B complex vitamins)
essential for fatty acid biosynthesis, catabolism, and it acts as a
growth factor for many cells</description>
    </keyword>
    <keyword id="KW-0093">
        <name>Biotin biosynthesis</name>
        <name>Biopeiderm biosynthetic process</name>
        <name>Biotin synthesis</name>
        <name>Vitamin B7 formation</name>
        <name>Coenzyme R biosynthetic process</name>
        <name>Vitamin H synthesis</name>
        <name>Biopeiderm formation</name>
        <name>Vitamin B7 anabolism</name>
        <name>Coenzyme R synthesis</name>
        <name>Vitamin B7 biosynthetic process</name>
        <name>Vitamin B8 synthesis</name>
        <name>Biopeiderm biosynthesis</name>
        <name>Biotin anabolism</name>
        <name>Vitamin B8 biosynthetic process</name>
        <name>Vitamin B7 synthesis</name>
        <name>Vitamin B8 anabolism</name>
        <name>Biopeiderm anabolism</name>
        <name>Coenzyme R anabolism</name>
        <name>Biotin biosynthetic process</name>
        <name>Vitamin B8 formation</name>
        <name>Biotin formation</name>
        <name>Coenzyme R formation</name>
        <name>Vitamin H biosynthetic process</name>
        <name>Biopeiderm synthesis</name>
        <name>Vitamin H anabolism</name>
        <name>Coenzyme R biosynthesis</name>
        <name>Vitamin H formation</name>
        <name>Vitamin H biosynthesis</name>
        <description>Protein involved in the synthesis of biotin, a prosthetic group for
some carboxylase and decarboxylase enzymes. This water-soluble vitamin
is essential for fatty acid biosynthesis, catabolism, and it acts as a
growth factor for many cells</description>
        <go id="GO:0009102"/>
    </keyword>
    <keyword id="KW-0094">
        <name>Blood coagulation</name>
        <description>Protein involved in blood clotting, a complex enzymatic cascade in
which the activated form of one factor catalyzes the activation of the
next factor. Both the extrinsic clotting pathway, induced by a damaged
surface, and the intrinsic pathway, induced by a trauma, converge in a
final common pathway to form cross-linked fibrin clots</description>
        <go id="GO:0007596"/>
    </keyword>
    <keyword id="KW-1204">
        <name>Blood coagulation cascade activating toxin</name>
        <description>Toxin which activates the blood coagulation cascade, which leads to
the production of fibrin clots. Blood coagulation activating toxins
include a variety of snake venom proteases</description>
    </keyword>
    <keyword id="KW-1203">
        <name>Blood coagulation cascade inhibiting toxin</name>
        <description>Toxin which inhibits the blood coagulation cascade, which leads to the
production of fibrin clots. Blood coagulation inhibiting toxins
include a variety of snake venom proteases</description>
    </keyword>
    <keyword id="KW-0095">
        <name>Blood group antigen</name>
        <name>Agglutinogen</name>
        <description>Protein belonging to the set of cell surface antigens found chiefly,
but not solely, on blood cells. More than fifteen different blood
group systems are recognised in humans. In most cases the antigenic
determinant resides in the carbohydrate chains of membrane
glycoproteins or glycolipids</description>
    </keyword>
    <keyword id="KW-1222">
        <name>Bradykinin receptor impairing toxin</name>
        <description>Toxin which interferes with the function of the bradykinin receptor
(BDKR). BDKRs are G-protein coupled receptors whose principal ligand
is the 9-amino acid peptide bradykinin</description>
    </keyword>
    <keyword id="KW-1136">
        <name>Bradyzoite</name>
        <description>Protein expressed in the bradyzoite stage, a latent, slowly growing
and cyst-forming stage in the life cycle of coccidians (e.g
Toxoplasmy). Encysted bradyzoites promote chronic infection and
widespread dissemination of the parasite</description>
    </keyword>
    <keyword id="KW-0100">
        <name>Branched-chain amino acid biosynthesis</name>
        <name>Branched-chain amino acid biosynthetic process</name>
        <name>Branched-chain amino acid synthesis</name>
        <name>Branched-chain amino acid formation</name>
        <name>Branched-chain amino acid anabolism</name>
        <description>Protein involved in the synthesis of the essential aliphatic branched-
chain amino acids leucine (Leu), isoleucine (Ile) and valine (Val)</description>
        <go id="GO:0009082"/>
    </keyword>
    <keyword id="KW-0101">
        <name>Branched-chain amino acid catabolism</name>
        <name>Branched-chain amino acid catabolic process</name>
        <name>Branched-chain amino acid degradation</name>
        <name>Branched-chain amino acid breakdown</name>
        <description>Protein involved in the degradation of the branched-chain amino acids
leucine (Leu), isoleucine (Ile) and valine (Val)</description>
        <go id="GO:0009083"/>
    </keyword>
    <keyword id="KW-1069">
        <name>Brassinosteroid biosynthesis</name>
        <name>Brassinosteroid biosynthetic process</name>
        <name>Brassinosteroid synthesis</name>
        <name>Brassinosteroid anabolism</name>
        <name>Brassinosteroid formation</name>
        <description>Protein involved in the synthesis of brassinosteroids, a class of
steroid plant hormones. Brassinosteroids are involved in numerous
plant processes, such as cell expansion and elongation (in association
with auxin), vascular differentiation, pollen elongation and pollen
tube formation and protection to plants during chilling and drought
stress. Brassinolide is the first isolated brassinosteroid</description>
        <go id="GO:0016132"/>
    </keyword>
    <keyword id="KW-1070">
        <name>Brassinosteroid signaling pathway</name>
        <name>BR-signalling pathway</name>
        <name>BR signalling pathway</name>
        <description>Protein involved in the brassinosteroid (BR) signaling pathway (e.g
transport and signal transduction) that regulates many aspects of
plant growth and development including cell expansion and elongation
(in association with auxin), vascular differentiation and pollen
elongation and pollen tube formation. Also involved in plants
protection during chilling and drought stress. BRs are
polyhydroxysteroid phytohormones and over 70 BR compounds have been
isolated in plants. Brassinolide was the first BR isolated from
Brassica napus and remains one of the most active BR</description>
        <go id="GO:0009742"/>
    </keyword>
    <keyword id="KW-0102">
        <name>Bromination</name>
        <name>Bromated</name>
        <name>Brominated</name>
        <description>Protein which is posttranslationally modified by the attachment of at
least one bromine</description>
    </keyword>
    <keyword id="KW-0103">
        <name>Bromodomain</name>
        <description>Protein containing at least one bromodomain. The bromodomain is a
conserved region, approximately 70 amino acids, characteristic for a
class of regulatory proteins. It mediates interactions with proteins
that are necessary for transcriptional activation</description>
    </keyword>
    <keyword id="KW-0992">
        <name>Brugada syndrome</name>
        <name>BRS</name>
        <description>Protein which, if defective, causes Brugada syndrome, a heart disease
characterized by an electrocardiogram pattern showing ST segment
elevation in right precordial leads (V1 to V3), incomplete or complete
right bundle branch block, and ventricular tachyarrhythmia. In some
cases, tachycardia does not terminate spontaneously and it may
degenerate into ventricular fibrillation and lead to sudden death</description>
    </keyword>
    <keyword id="KW-0973">
        <name>c-di-GMP</name>
        <name>cGpGp</name>
        <name>c-(Gpgp)</name>
        <name>Cyclic-bis(3',5')diguanylic acid</name>
        <name>Cyclic dinucleotide di-GMP</name>
        <name>Bis-(3'-5')-cyclic dimeric guanosine monophosphate</name>
        <name>Guanosine 3',5'-cyclic monophosphate</name>
        <name>Cyclic diguanylate</name>
        <name>Bis-(3'-5') cyclic diguanylic acid</name>
        <name>3',5'-cyclic di-GMP</name>
        <name>Cyclic diguanylic acid</name>
        <name>3'-5'-cyclic diguanylic acid</name>
        <description>Protein whose function is c-di-GMP-dependent or which catalyzes its
hydrolysis. c-di-GMP is the abbreviation for cyclic di-GMP, bis-(3'-
5') cyclic diguanylic acid. It acts as a bacterial second messenger</description>
    </keyword>
    <keyword id="KW-0104">
        <name>Cadmium</name>
        <name>Cd</name>
        <name>Cadmium ion</name>
        <description>Protein which binds at least one cadmium atom, or protein whose
function is cadmium-dependent. Cadmium is a heavy metal, chemical
symbol Cd</description>
    </keyword>
    <keyword id="KW-0105">
        <name>Cadmium resistance</name>
        <name>Resistance to cadmium ion</name>
        <name>Resistance to Cd</name>
        <name>Cadmium ion resistance</name>
        <name>Cd resistance</name>
        <name>Resistance to cadmium</name>
        <description>Protein that confers, on bacteria and other microorganisms, the
ability to withstand the transition metal cadmium (Cd)</description>
        <go id="GO:0046686"/>
    </keyword>
    <keyword id="KW-0106">
        <name>Calcium</name>
        <name>Calcium ion</name>
        <name>Ca</name>
        <description>Protein which binds at least one calcium atom, or protein whose
function is calcium-dependent. Calcium is a metal, chemical symbol Ca
Calcium is essential for a variety of bodily functions, such as
neurotransmission, muscle contraction and proper heart function</description>
    </keyword>
    <keyword id="KW-0107">
        <name>Calcium channel</name>
        <name>Ca channel</name>
        <name>Calcium ion channel</name>
        <description>Cell membrane glycoprotein forming a channel in a biological membrane
selectively permeable to calcium ions. Calcium is essential for a
variety of bodily functions, such as neurotransmission, muscle
contraction and proper heart function</description>
        <go id="GO:0070588"/>
        <go id="GO:0005262"/>
    </keyword>
    <keyword id="KW-0108">
        <name>Calcium channel impairing toxin</name>
        <name>Ca channel inhibitor</name>
        <name>Calcium ion channel inhibitor</name>
        <description>Protein which interferes with the function of calcium channels which
are membrane proteins forming a channel in a biological membrane
selectively permeable to calcium ions. They are found in various
venoms from snakes, scorpions and spiders</description>
        <go id="GO:0005246"/>
    </keyword>
    <keyword id="KW-0109">
        <name>Calcium transport</name>
        <name>Ca transport</name>
        <name>Calcium ion transport</name>
        <description>Protein involved in the transport of calcium ions. Calcium is
essential for a variety of bodily functions, such as
neurotransmission, muscle contraction and proper heart function</description>
        <go id="GO:0006816"/>
    </keyword>
    <keyword id="KW-1221">
        <name>Calcium-activated potassium channel impairing toxin</name>
        <description>Protein which interferes with the function of calcium-activated
potassium channels (KCa) which are membrane proteins forming a channel
in a biological membrane selectively permeable to potassium ions and
gated by intracellular calcium. They are mostly found in snake and
scorpion venoms</description>
    </keyword>
    <keyword id="KW-0111">
        <name>Calcium/phospholipid-binding</name>
        <name>Calcium-dependent phospholipid binding</name>
        <description>Protein which contains at least one binding site for calcium and
phospholipid. For example, proteins with annexin repeats, of which a
pair may form one binding site for calcium and phospholipid, or some
proteins with C2 domains</description>
        <go id="GO:0005544"/>
    </keyword>
    <keyword id="KW-0112">
        <name>Calmodulin-binding</name>
        <description>Protein which binds at least one calmodulin, an ubiquitous small
calcium-binding protein. Its binding to proteins may cause a
conformational change which either activates or inactivates their
function</description>
        <go id="GO:0005516"/>
    </keyword>
    <keyword id="KW-0113">
        <name>Calvin cycle</name>
        <name>Reductive pentose phosphate cycle</name>
        <name>Calvin-Benson cycle</name>
        <description>Protein involved in the cycle of biochemical reactions responsible for
photosynthetic CO(2) fixation in many photosynthetic bacteria and in
the stroma of plant chloroplasts. The energy and reducing power for
this reaction are provided by the ATP and NADPH produced during the
light reactions of photosynthesis. The Calvin cycle is the only
photosynthetic pathway in C3 plants. In C4 and CAM plants CO(2) is
initially fixed into other organic acids that are subsequently
decarboxylated to release CO(2) to the Calvin cycle. Non-
photosynthetic organism (e.g. Rhizobium) also use the cycle to fix
CO(2)</description>
        <go id="GO:0019253"/>
    </keyword>
    <keyword id="KW-0114">
        <name>cAMP</name>
        <name>3',5'-cyclic AMP</name>
        <name>Adenosine-3',5'-cyclic-monophosphate</name>
        <name>Cyclic AMP</name>
        <name>Adenosine 3',5'-phosphate</name>
        <name>Cyclic adenylic acid</name>
        <description>Protein whose function is cAMP-dependent or which catalyzes its
hydrolysis. cAMP is the abbreviation for cyclic AMP, adenosine 3',5'-
cyclic monophosphate, the first second messenger hormone signaling
system to be characterised. It is generated from ATP by the action of
adenyl cyclase that is coupled to hormone receptors by G proteins
cAMP activates a specific protein kinase and is inactivated by
phosphodiesterase action giving 5'AMP</description>
    </keyword>
    <keyword id="KW-0115">
        <name>cAMP biosynthesis</name>
        <name>3',5'-cyclic AMP anabolism</name>
        <name>cAMP synthesis</name>
        <name>Adenosine 3',5'-phosphate anabolism</name>
        <name>Adenosine-3',5'-cyclic-monophosphate synthesis</name>
        <name>Adenosine 3',5'-phosphate synthesis</name>
        <name>3',5'-cyclic AMP biosynthesis</name>
        <name>Cyclic AMP biosynthesis</name>
        <name>Cyclic AMP anabolism</name>
        <name>Adenosine-3',5'-cyclic-monophosphate biosynthetic process</name>
        <name>Cyclic AMP formation</name>
        <name>Cyclic adenylic acid anabolism</name>
        <name>Cyclic adenylic acid formation</name>
        <name>Cyclic adenylic acid biosynthetic process</name>
        <name>Adenosine 3',5'-phosphate biosynthesis</name>
        <name>Adenosine-3',5'-cyclic-monophosphate biosynthesis</name>
        <name>Adenosine-3',5'-cyclic-monophosphate formation</name>
        <name>Adenosine 3',5'-phosphate formation</name>
        <name>cAMP anabolism</name>
        <name>cAMP formation</name>
        <name>Cyclic AMP biosynthetic process</name>
        <name>cAMP biosynthetic process</name>
        <name>Cyclic adenylic acid biosynthesis</name>
        <name>3',5'-cyclic AMP synthesis</name>
        <name>3',5'-cyclic AMP biosynthetic process</name>
        <name>Adenosine 3',5'-phosphate biosynthetic process</name>
        <name>3',5'-cyclic AMP formation</name>
        <name>Adenosine-3',5'-cyclic-monophosphate anabolism</name>
        <name>Cyclic adenylic acid synthesis</name>
        <name>Cyclic AMP synthesis</name>
        <description>Protein involved in the synthesis of cAMP. cAMP is the abbreviation
for cyclic AMP, adenosine 3',5'-cyclic monophosphate</description>
        <go id="GO:0006171"/>
    </keyword>
    <keyword id="KW-0116">
        <name>cAMP-binding</name>
        <name>Cyclic adenylic acid-binding</name>
        <name>Adenosine 3',5'-phosphate-binding</name>
        <name>Cyclic AMP-binding</name>
        <name>3',5'-cyclic AMP-binding</name>
        <name>Adenosine-3',5'-cyclic-monophosphate-binding</name>
        <description>Protein which binds at least one cAMP. cAMP is the abbreviation for
cyclic AMP, adenosine 3',5'-cyclic monophosphate</description>
        <go id="GO:0030552"/>
    </keyword>
    <keyword id="KW-1157">
        <name>Cap snatching</name>
        <description>Protein involved in cap snatching, a process in which a cellular mRNA
is cleaved few nucleotides after the 5'cap. The resulting 10- to 13-
nucleotides long capped fragment serve as primer for the initiation of
viral mRNA synthesis. Cap snatching is used by negative stranded RNA
virus which do not encode a guanylyl transferase, like influenza or
hantaviruses</description>
        <go id="GO:0075526"/>
    </keyword>
    <keyword id="KW-1232">
        <name>Capsid decoration protein</name>
        <description>Viral decoration protein attached to the capsid of some prokaryotic
viruses. Decoration proteins are located on the outermost surface of
the capsid and are involved in stabilizing the head structure</description>
        <go id="GO:0098021"/>
    </keyword>
    <keyword id="KW-1231">
        <name>Capsid inner membrane protein</name>
        <description>Viral protein part of the inner membrane of the capsid, a lipid
bilayer contained inside the virion capsid</description>
        <go id="GO:0039641"/>
    </keyword>
    <keyword id="KW-0167">
        <name>Capsid protein</name>
        <name>Head protein</name>
        <name>Coat protein</name>
        <description>Structural protein which is part of the complex forming the protective
shell around the nucleic acids of the virus. In prokaryotic viruses,
this closed shell is also referred to as the head</description>
        <go id="GO:0019028"/>
    </keyword>
    <keyword id="KW-0875">
        <name>Capsule</name>
        <description>Protein which is part of a capsule, the protective structure
surrounding some bacteria or fungi. The bacterial capsule is a layer
of material, usually polysaccharide, attached to the cell wall
possibly via covalent attachments to either phospholipid or lipid-A
molecules. It has several functions: promote bacterial adhesion to
surfaces or interaction with other organisms; act as a permeability
barrier, as a defense mechanism against phagocytosis and/or as a
nutrient reserve. Among pathogens, capsule formation often correlates
with pathogenicity. The fungal capsule is an extracellular layer which
lies outside the cell wall and it is usually composed of
polysaccharides. It protects the cell from different environmental
dangers such as phagocytosis, dessication, etc</description>
    </keyword>
    <keyword id="KW-0972">
        <name>Capsule biogenesis/degradation</name>
        <description>Protein which is involved in the formation, organization, maintenance
or degradation of the capsule. The capsule is a protective structure
surrounding some bacteria or fungi. The bacterial capsule is a layer
of material, usually polysaccharide, attached to the cell wall
possibly via covalent attachments to either phospholipid or lipid-A
molecules. The fungal capsule is an extracellular layer which lies
outside the cell wall and it is usually composed of polysaccharides</description>
    </keyword>
    <keyword id="KW-0119">
        <name>Carbohydrate metabolism</name>
        <name>Carbohydrate metabolic process</name>
        <name>Sugar metabolism</name>
        <name>Sugar metabolic process</name>
        <description>Protein participating in biochemical reactions in which carbohydrates
are involved. Carbohydrate is a general term for sugars and related
compounds with the general formula Cn(H2O)n. The smallest are
monosaccharides (e.g. glucose); polysaccharides (e.g. starch,
cellulose, glycogen) can be large and vary in length</description>
    </keyword>
    <keyword id="KW-0120">
        <name>Carbon dioxide fixation</name>
        <name>Carbon utilization by fixation of CO(2)</name>
        <name>CO2 fixation</name>
        <name>Carbon utilization by fixation of carbon dioxide</name>
        <name>Carbon utilization by fixation of CO2</name>
        <name>CO(2) fixation</name>
        <description>Protein involved in the process of carbon dioxide fixation, e.g
incorporation of carbon dioxide into carbohydrates by photosynthetic
organisms or formation of oxaloacetate from pyruvate</description>
        <go id="GO:0015977"/>
    </keyword>
    <keyword id="KW-0121">
        <name>Carboxypeptidase</name>
        <description>Protein that hydrolyzes a C-terminal peptide bond in polypeptide
chains</description>
        <go id="GO:0004180"/>
    </keyword>
    <keyword id="KW-1282">
        <name>Carboxysome</name>
        <description>Protein located in or on the carboxysome, bacterial microcompartments
in which ribulose bisphosphate carboxylase (RuBisCO)-mediated CO(2)
fixation occurs. The cytoplasmic polyhedral inclusion bodies are
surrounded by a thin protein coat. Found in cyanobacteria and some
chemoautotrophs, they enhance autotrophic CO(2) fixation in air by
increasing the CO(2) concentration around RuBisCO, thus reducing its
reaction with O(2), a competing substrate. They contain carbonic
anhydrase as part of the CO(2) concentration mechanism</description>
    </keyword>
    <keyword id="KW-0122">
        <name>Cardiomyopathy</name>
        <description>Protein which, if defective, causes cardiomyopathy, a chronic disorder
which affects the heart muscle causing a reduced pumping function. It
is a major cause of morbidity and mortality</description>
    </keyword>
    <keyword id="KW-0123">
        <name>Cardiotoxin</name>
        <description>Protein which has a poisonous or deleterious effect upon the heart or
other parts of the cardiovascular system</description>
    </keyword>
    <keyword id="KW-0124">
        <name>Carnitine biosynthesis</name>
        <name>Carnitine biosynthetic process</name>
        <name>Gamma-trimethyl-hydroxybutyrobetaine synthesis</name>
        <name>Gamma-trimethyl-hydroxybutyrobetaine biosynthesis</name>
        <name>Carnitine formation</name>
        <name>Gamma-trimethyl-hydroxybutyrobetaine anabolism</name>
        <name>3-hydroxy-4-(trimethylammonio)butanoate biosynthesis</name>
        <name>3-hydroxy-4-(trimethylammonio)butanoate synthesis</name>
        <name>Carnitine anabolism</name>
        <name>Gamma-trimethyl-hydroxybutyrobetaine formation</name>
        <name>3-hydroxy-4-(trimethylammonio)butanoate anabolism</name>
        <name>3-hydroxy-4-(trimethylammonio)butanoate biosynthetic process</name>
        <name>3-hydroxy-4-(trimethylammonio)butanoate formation</name>
        <name>Carnitine synthesis</name>
        <name>Gamma-trimethyl-hydroxybutyrobetaine biosynthetic process</name>
        <description>Protein involved in the biosynthesis of carnitine (L-3-hydroxy-4,
N,N,N-trimethylaminobutyrate), an essential metabolite with a number
of indispensable roles in intermediary metabolism</description>
        <go id="GO:0045329"/>
    </keyword>
    <keyword id="KW-0125">
        <name>Carotenoid biosynthesis</name>
        <name>Carotenoid biosynthetic process</name>
        <name>Carotenoid formation</name>
        <name>Carotenoid anabolism</name>
        <name>Carotenoid synthesis</name>
        <description>Protein involved in the synthesis of carotenoids, a group of orange,
yellow, red, purple or brown pigments in plants, bacteria and some
fungi. Carotenoids, which comprise the carotenes and the xanthophylls,
are long polyisoprenoid molecules having conjugated double bonds
enabling light absorbtion</description>
        <go id="GO:0016117"/>
    </keyword>
    <keyword id="KW-0898">
        <name>Cataract</name>
        <description>Protein which, if defective, causes cataract, a partial or complete
ocular opacity that affects the crystalline lens or its capsule,
leading to impaired vision or blindness. The many types of cataract
are classified by their morphology (size, shape, location) or etiology
(cause and time of occurrence). Cataracts may occur as an isolated
anomaly, as part of generalized ocular developmental defects, or as a
component of a multisystem disorder</description>
    </keyword>
    <keyword id="KW-0127">
        <name>Catecholamine biosynthesis</name>
        <name>Catecholamine anabolism</name>
        <name>Catecholamine biosynthetic process</name>
        <name>Catecholamine formation</name>
        <name>Catecholamine synthesis</name>
        <description>Protein involved in the synthesis of catecholamines, which are amine
derivatives of catechol (2-hydroxyphenol). They are synthesized from
the amino acid tyrosine (Tyr) in sympathetic-nerve terminals and in
the adrenal gland. Catecholamines act as hormones or neuro-
transmitters, e.g. adrenaline, noradrenaline and dopamine</description>
        <go id="GO:0042423"/>
    </keyword>
    <keyword id="KW-0128">
        <name>Catecholamine metabolism</name>
        <name>Catecholamine metabolic process</name>
        <description>Protein participating the biochemical reactions in which
catecholamines are involved. Catecholamines are amine derivatives of
catechol (2-hydroxyphenol). They are synthesized from the amino acid
tyrosine (Tyr) in sympathetic-nerve terminals and in the adrenal
gland. Catecholamines act as hormones or neuro-transmitters, e.g
adrenaline, noradrenaline and dopamine</description>
        <go id="GO:0006584"/>
    </keyword>
    <keyword id="KW-1166">
        <name>Caveolin-mediated endocytosis of virus by host</name>
        <name>Virion endocytosis by caveolin-coated vesicle</name>
        <description>Viral protein involved in virus internalization by the host cell via
caveolae, which are specialized lipid rafts that form 50-70 nm flask-
shaped invaginations of the cell membrane. Caveolins form the
structural backbone of caveolae. Internalization via caveolae is not a
constitutive process but only occurs upon cell stimulation.Endocytic
caveolae deliver their viral content to early endosomes. Caveolae
represent a low capacity but highly regulated pathway. This pathway is
used by viruses including HPV-31, BK virus, NDV, RSV, Coxsackie B
virus, SV40, murine polyomavirus, and Echovirus 1</description>
        <go id="GO:0075513"/>
    </keyword>
    <keyword id="KW-0129">
        <name>CBS domain</name>
        <description>Protein containing at least one CBS domain, a conserved domain found
in a wide range of proteins, which is named after cystathionine beta-
synthase (CBS), an enzyme that contains 2 copies of this domain</description>
    </keyword>
    <keyword id="KW-0130">
        <name>Cell adhesion</name>
        <description>Protein involved in the adherence of cells to other cells or to a
matrix. Cell adhesion is mediated by cell surface proteins</description>
        <go id="GO:0007155"/>
    </keyword>
    <keyword id="KW-1217">
        <name>Cell adhesion impairing toxin</name>
        <description>Toxin which interferes with the adherence of cells to other cells or
to a matrix. Cell adhesion impairing toxins are mostly found in venom
of snakes</description>
    </keyword>
    <keyword id="KW-0131">
        <name>Cell cycle</name>
        <description>Protein involved in the complex series of events by which the cell
duplicates its contents and divides into two. The eukaryotic cell
cycle can be divided in four phases termed G1 (first gap period), S
(synthesis, phase during which the DNA is replicated), G2 (second gap
period) and M (mitosis). The prokaryotic cell cycle typically involves
a period of growth followed by DNA replication, partition of
chromosomes, formation of septum and division into two similar or
identical daughter cells</description>
        <go id="GO:0007049"/>
    </keyword>
    <keyword id="KW-0132">
        <name>Cell division</name>
        <description>Protein involved in the separation of one cell into two daughter
cells. In eukaryotic cells, cell division includes the nuclear
division (mitosis) and the subsequent cytoplasmic division
(cytokinesis)</description>
        <go id="GO:0051301"/>
    </keyword>
    <keyword id="KW-0997">
        <name>Cell inner membrane</name>
        <name>Inner membrane</name>
        <description>Protein found in or associated with the prokaryotic cell inner
membrane, a selectively permeable membrane which separates the
cytoplasm from the periplasm in prokaryotes with 2 membranes</description>
    </keyword>
    <keyword id="KW-0965">
        <name>Cell junction</name>
        <description>Protein found in or associated with a cell junction, a cell-cell or
cell-extracellular matrix contact within a tissue of a multicellular
organism, especially abundant in epithelia. In vertebrates, there are
three major types of cell junctions: anchoring junctions (e.g
adherens junctions), communicating junctions (e.g. gap junctions) and
occluding junctions (e.g. tight junctions)</description>
    </keyword>
    <keyword id="KW-1003">
        <name>Cell membrane</name>
        <name>Plasmalemma</name>
        <name>Plasma membrane</name>
        <name>Cytoplasmic membrane</name>
        <description>Protein found in or associated with the cytoplasmic membrane, a
selectively permeable membrane which separates the cytoplasm from its
surroundings. Known as the cell inner membrane in prokaryotes with 2
membranes</description>
    </keyword>
    <keyword id="KW-0998">
        <name>Cell outer membrane</name>
        <name>Outer membrane</name>
        <description>Protein found in or associated with the prokaryotic cell outer
membrane, a selectively permeable membrane which separates the
prokaryotic periplasm from its surroundings. Traditionally only Gram-
negative bacteria were thought of as having an outer membrane, but
recent work has shown some Actinobacteria, including Mycobacterium
tuberculosis, as well as at least 1 archaea (Ignicoccus hospitalis)
have a cell outer membrane</description>
    </keyword>
    <keyword id="KW-0966">
        <name>Cell projection</name>
        <name>Cell protrusion</name>
        <description>Protein found in or associated with a cell protrusion such as
pseudopodium, filopodium, lamellipodium, growth cone, flagellum,
acrosome or axon, or bacterial comet tail. These membrane-
cytoskeleton-coupled processes are involved in many biological
functions, such as cell motility, cancer-cell invasion, endocytosis,
phagocytosis, exocytosis, pathogen infection, neurite extension and
cytokinesis</description>
    </keyword>
    <keyword id="KW-0133">
        <name>Cell shape</name>
        <description>Protein involved in the formation and maintenance of the cell shape,
the physical dimensions of a cell. In most plants, algae, bacteria and
fungi the cell wall is responsible for the shape of the cells</description>
        <go id="GO:0008360"/>
    </keyword>
    <keyword id="KW-0134">
        <name>Cell wall</name>
        <description>Protein found in or associated with a complex and rigid layer
surrounding the cell. Cell walls are found in bacteria, archaea,
fungi, plants, and algae. The cell wall envelopes the inner or plasma
membrane in all bacteria and is surrounded by the outer membrane in
bacteria with 2 membranes (Gram-negative). Bacterial cell walls
contain peptidoglycan whereas those of archaea do not. Some archaea
may contain pseudopeptidoglycan, which is composed of N-
acetyltalosaminuronic acid, instead of N-acetyl muramic acid in
peptidoglycan. The plant cell wall is made of fibrils of cellulose
embedded in a matrix of several other kinds of polymers such as pectin
and lignin. Algal cell walls are usually composed of cellulose,
glycoproteins, sporopollenin, calcium and various polysaccharides such
as manosyl, xylanes, alginic acid. Diatom cell walls (or frustules)
contain silica. The cell wall plays a role in cell shape, cell
stability and development, and protection against environmental
dangers</description>
    </keyword>
    <keyword id="KW-0961">
        <name>Cell wall biogenesis/degradation</name>
        <description>Protein which is involved in the formation, organization, maintenance
or degradation of the cell wall. The cell wall is an extracellular
layer outside the cell membrane which protects the cell against
mechanical damage, osmotic strength and which determines the cell
shape. It is prominent in most plants, algae, bacteria and fungi</description>
        <go id="GO:0071555"/>
    </keyword>
    <keyword id="KW-0135">
        <name>Cellulose biosynthesis</name>
        <name>Cellulose synthesis</name>
        <name>Cellulose formation</name>
        <name>Cellulose anabolism</name>
        <name>Cellulose biosynthetic process</name>
        <description>Protein involved in the synthesis of cellulose, a linear polymer of
(1-4)-beta-linked D-glucose subunits. It is the most abundant cell-
wall and structural polysaccharide in plants and it is also found in
some lower invertebrates. Cellulose is the major component of wood and
thus of paper. Cotton is the purest natural form of cellulose. As a
raw material, it forms the basis for many derivatives used in
chromatography, ion exchange materials, explosives manufacturing and
pharmaceutical preparations</description>
        <go id="GO:0030244"/>
    </keyword>
    <keyword id="KW-0136">
        <name>Cellulose degradation</name>
        <name>Cellulose breakdown</name>
        <name>Cellulose catabolic process</name>
        <name>Cellulose catabolism</name>
        <description>Protein involved in the conversion of cellulose into D-glucose
Cellulose is the most abundant cell-wall and structural polysaccharide
in plants and it is also found in some lower invertebrates. Cellulose
is the major component of wood and thus of paper. Cotton is the purest
natural form of cellulose. As a raw material, it forms the basis for
many derivatives used in chromatography, ion exchange materials,
explosives manufacturing and pharmaceutical preparations</description>
        <go id="GO:0030245"/>
    </keyword>
    <keyword id="KW-0137">
        <name>Centromere</name>
        <name>Chromosome pericentric region</name>
        <description>Protein which binds centromeres or which is required for the assembly
and movement of centromeres. Centromeres are the regions of replicated
eukaryotic chromosomes where the two chromatids are joined together</description>
    </keyword>
    <keyword id="KW-0138">
        <name>CF(0)</name>
        <name>ATPase membrane proton channel</name>
        <name>Proton-transporting ATP synthase complex coupling factor F(0)</name>
        <description>Protein component of the F-type ATP synthase complex CF(0) or protein
involved in its assembly. F-type ATPases consist of the two complex
components CF(0), the membrane proton channel, and CF(1), the
catalytic core</description>
        <go id="GO:0045259"/>
    </keyword>
    <keyword id="KW-0139">
        <name>CF(1)</name>
        <name>ATPase catalytic core</name>
        <name>Proton-transporting ATP synthase complex catalytic core F(1)</name>
        <description>Protein component of the F-type ATP synthase complex CF(1) or protein
involved in its assembly. F-type ATPases consist of the two complex
components CF(0), the membrane proton channel, and CF(1), the
catalytic core</description>
        <go id="GO:0045259"/>
    </keyword>
    <keyword id="KW-0140">
        <name>cGMP</name>
        <name>3',5'-cyclic GMP</name>
        <name>Guanosine 3',5'-cyclic monophosphate</name>
        <name>Cyclic GMP</name>
        <name>Guanosine 3',5'-phosphate</name>
        <name>Cyclic guanylic acid</name>
        <description>Protein whose function is cGMP-dependent or which catalyzes its
hydrolysis. cGMP is the abbreviation for cyclic GMP, guanosine 3',5'-
cyclic monophosphate. It acts as a second messenger</description>
    </keyword>
    <keyword id="KW-0141">
        <name>cGMP biosynthesis</name>
        <name>3',5'-cyclic GMP biosynthetic process</name>
        <name>Cyclic GMP anabolism</name>
        <name>Cyclic GMP biosynthesis</name>
        <name>3',5'-cyclic GMP biosynthesis</name>
        <name>Guanosine 3',5'-phosphate synthesis</name>
        <name>cGMP formation</name>
        <name>Cyclic guanylic acid anabolism</name>
        <name>3',5'-cyclic GMP synthesis</name>
        <name>cGMP anabolism</name>
        <name>Guanosine-3',5'-cyclic-monophosphate anabolism</name>
        <name>Guanosine-3',5'-cyclic-monophosphate formation</name>
        <name>3',5'-cyclic GMP formation</name>
        <name>Cyclic GMP biosynthetic process</name>
        <name>Cyclic GMP synthesis</name>
        <name>Cyclic guanylic acid formation</name>
        <name>Guanosine 3',5'-phosphate biosynthetic process</name>
        <name>Guanosine 3',5'-phosphate biosynthesis</name>
        <name>Guanosine 3',5'-phosphate formation</name>
        <name>cGMP biosynthetic process</name>
        <name>Cyclic GMP formation</name>
        <name>Guanosine-3',5'-cyclic-monophosphate biosynthesis</name>
        <name>3',5'-cyclic GMP anabolism</name>
        <name>Cyclic guanylic acid synthesis</name>
        <name>Cyclic guanylic acid biosynthesis</name>
        <name>Guanosine 3',5'-phosphate anabolism</name>
        <name>Guanosine-3',5'-cyclic-monophosphate biosynthetic process</name>
        <name>Guanosine-3',5'-cyclic-monophosphate synthesis</name>
        <name>cGMP synthesis</name>
        <name>Cyclic guanylic acid biosynthetic process</name>
        <description>Protein involved in the synthesis of cGMP. cGMP is the abbreviation
for cyclic GMP, guanosine 3',5'-cyclic monophosphate</description>
        <go id="GO:0006182"/>
    </keyword>
    <keyword id="KW-0142">
        <name>cGMP-binding</name>
        <name>3',5'-cyclic GMP-binding</name>
        <name>Guanosine 3',5'-phosphate-binding</name>
        <name>Cyclic GMP-binding</name>
        <name>Cyclic guanylic acid-binding</name>
        <name>Guanosine 3',5'-cyclic monophosphate-binding</name>
        <description>Protein which binds at least one cGMP. cGMP is the abbreviation for
cyclic GMP, guanosine 3',5'-cyclic monophosphate</description>
        <go id="GO:0030553"/>
    </keyword>
    <keyword id="KW-0143">
        <name>Chaperone</name>
        <description>Protein which is transiently involved in the noncovalent folding,
assembly and/or disassembly of other polypeptides or RNA molecules,
including any transport and oligomerisation processes they may
undergo, and the refolding and reassembly of protein and RNA molecules
denatured by stress. Though involved in these processes, chaperones
are not an integral part of these functioning molecules. Also used for
metallochaperones, which function to provide a metal directly to
target proteins while protecting this metal from scavengers</description>
    </keyword>
    <keyword id="KW-0144">
        <name>Charcot-Marie-Tooth disease</name>
        <description>Protein which, if defective, causes Charcot-Marie-Tooth disease (CMT),
a heterogeneous group of hereditary motor and sensory neuropathies
(HMSN) characterized by distal muscular atrophy and weakness, hollow
feet, absent or diminished deep-tendon reflexes and impaired
sensation. CMT is classified into two major classes. CMT type 1
includes demyelinating neuropathies that are characterized by nerve
conductance velocities (NCVs) less than 38m/s and segmental
demyelination and remyelination; CMT type 2 includes axonal
neuropathies that are characterized by normal or mildly reduced NCVs
and chronic axonal degeneration and regeneration</description>
    </keyword>
    <keyword id="KW-0145">
        <name>Chemotaxis</name>
        <description>Protein involved in the movement of a cell, or organism, along a
concentration gradient of a chemotactic agent, such as a protein which
causes, mediates or responds to chemotaxis. Chemotactic molecules such
as sugars, peptides, cell metabolites, cell-wall or membrane lipids
bind to cell surface receptors and trigger activation of intracellular
signaling pathways, as well as remodeling of the cytoskeleton through
the activation or inhibition of various actin-binding proteins</description>
        <go id="GO:0006935"/>
    </keyword>
    <keyword id="KW-0146">
        <name>Chitin degradation</name>
        <name>Chitin breakdown</name>
        <name>Chitin catabolic process</name>
        <name>Chitin catabolism</name>
        <description>Protein involved in the breakdown of chitin, a linear polysaccharide
consisting of (1-&gt;4)-beta-linked D-glucosamine residues, most of which
are N-acetylated</description>
        <go id="GO:0006032"/>
    </keyword>
    <keyword id="KW-0147">
        <name>Chitin-binding</name>
        <description>Protein which binds chitin, a linear polysaccharide consisting of
(1-&gt;4)-beta-linked D-glucosamine residues, most of which are N-
acetylated. The 30-43 amino acids long chitin-binding domain contains
several conserved glycine and cysteines residues. The conserved
cysteines form disulfide bonds. Chitin-binding domains have been found
in plant, fungal and bacterial proteins</description>
        <go id="GO:0008061"/>
    </keyword>
    <keyword id="KW-0868">
        <name>Chloride</name>
        <name>Chloride anion</name>
        <name>Cl-</name>
        <name>Chloride ion</name>
        <description>Protein which binds at least one chloride, or protein whose function
is chloride-dependent. Chloride is a negatively-charged ion, which is
abbreviated Cl(-)</description>
    </keyword>
    <keyword id="KW-0869">
        <name>Chloride channel</name>
        <name>Chloride anion channel</name>
        <name>Cl- channel</name>
        <name>Chloride ion channel</name>
        <description>Protein which is part of an anion channel found in the plasma membrane
and in intracellular membranes. These channels are permeable for
various anions, such as iodide, bromide, but also for nitrates,
phosphates and even negatively charged amino acids. They are called
chloride channels, because chloride is the most abundant anion and the
predominant permeating species in all organisms. They have been
classified according to their gating mechanisms, which may depend on
changes in the transmembrane electric field (voltage-dependent/gated
chloride channels, e.g. ClC family), on a protein kinase/nucleotide
mediated mechanism (CFTR), an increase in intracellular calcium
(calcium activated chloride channels, e.g. CaCC), cell swelling
(volume-regulated anion channels, e.g. VRAC) or binding of a ligand,
e.g. glycine or - aminobutyric acid (GABA) activated channels. In
contrast with cation channels, they are not involved in the initiation
or spread of excitation, but in the regulation of excitability in
nerve and muscle. They also participate in many housekeeping
processes, such as volume regulation, pH regulation in organelles,
electrogenesis and control of synaptic activity. The chloride channels
are crucial for transepithelial transport and the control of water
flow, and often provide unexpected permeation pathways for a large
variety of anions</description>
        <go id="GO:0006821"/>
        <go id="GO:0034707"/>
        <go id="GO:0005254"/>
    </keyword>
    <keyword id="KW-1265">
        <name>Chloride channel impairing toxin</name>
        <name>Chloride anion channel inhibitor</name>
        <name>Cl- channel inhibitor</name>
        <name>Chloride ion channel inhibitor</name>
        <description>Protein which interferes with the function of chloride channels which
are membrane proteins forming a channel in a biological membrane
selectively permeable to chloride ions. Chloride channels include
voltage-gated chloride channels (ClC), ionotropic GABA receptors
(ligand-gated ion channels activated by GABA) and CFTR ion channels
(ABC transporter-class ion channels). Toxins that target these
channels are found in venom of several species including scorpions and
snakes</description>
    </keyword>
    <keyword id="KW-0148">
        <name>Chlorophyll</name>
        <description>Protein which interacts with chlorophyll, the major light-absorbing
pigment in most oygenic green organisms. Higher plants contain
chlorophyll a and chlorophyll b which are magnesium-porphyrin
complexes esterified to a long hydrophobic terpenoid side chain (the
alcohol phytol)</description>
        <go id="GO:0016168"/>
    </keyword>
    <keyword id="KW-0149">
        <name>Chlorophyll biosynthesis</name>
        <name>Chlorophyll anabolism</name>
        <name>Chlorophyll synthesis</name>
        <name>Chlorophyll formation</name>
        <name>Chlorophyll biosynthetic process</name>
        <description>Protein involved in the synthesis of chlorophylls. These
photosynthetic pigments are magnesium-porphyrin complexes with a long
hydrophobic terpenoid side chain (the alcohol phytol). Angiosperms
have only a light-dependent pathway for chlorophyll biosynthesis,
other oxygenic organisms seem to have both the light-dependent and the
light-independent pathways. Non-oxygenic organisms, which make
bacteriochlorophyll, only have a light-independent pathway</description>
        <go id="GO:0015995"/>
    </keyword>
    <keyword id="KW-0881">
        <name>Chlorophyll catabolism</name>
        <name>Chlorophyll degradation</name>
        <name>Chlorophyll breakdown</name>
        <name>Chlorophyll catabolic process</name>
        <description>Protein involved in the degradation of chlorophylls. These
photosynthetic pigments are magnesium-porphyrin complexes with a long
hydrophobic terpenoid side chain (the alcohol phytol)</description>
        <go id="GO:0015996"/>
    </keyword>
    <keyword id="KW-0150">
        <name>Chloroplast</name>
        <description>Protein encoded by or localized in the chloroplast, the most common
form of plastid, found in all photosynthetic organisms except
glaucophyte algae. In green (photosynthesizing) tissue they house the
machinery necessary for photosynthesis and CO(2) fixation. They are
surrounded by between 2 and 4 membranes and contain thylakoids in
green tissue</description>
    </keyword>
    <keyword id="KW-0151">
        <name>Chlorosome</name>
        <description>Photosynthetic light-harvesting complexes found in green bacteria
Chlorosomes are sac-like organelles appressed to the cytoplasmic
membrane of the cell membrane</description>
    </keyword>
    <keyword id="KW-0152">
        <name>Cholesterol biosynthesis</name>
        <name>Cholesterol formation</name>
        <name>Cholesterol biosynthetic process</name>
        <name>Cholesterol synthesis</name>
        <name>Cholesterol anabolism</name>
        <description>Protein involved in the synthesis of cholesterol, the major sterol of
higher animals. It is a component of cell membranes, especially of the
plasma membrane</description>
        <go id="GO:0006695"/>
    </keyword>
    <keyword id="KW-0153">
        <name>Cholesterol metabolism</name>
        <name>Cholesterol metabolic process</name>
        <description>Protein which participates in the biochemical reactions where
cholesterol is involved, including transport. Cholesterol is the major
sterol of higher animals and an important component of cell membranes,
especially of the plasma membrane</description>
        <go id="GO:0008203"/>
    </keyword>
    <keyword id="KW-0891">
        <name>Chondrogenesis</name>
        <name>Cartilage formation</name>
        <name>Cartilage biogenesis</name>
        <name>Cartilage biosynthesis</name>
        <name>Cartilage development</name>
        <description>Protein involved in chondrogenesis, the mechanism of cartilage
formation. Chondrogenesis proceeds through determination of cells and
their aggregation into prechondrogenic condensations, differentiation
into chondrocytes, and later maturation. The formation of the long
bones requires a cartilage template</description>
        <go id="GO:0051216"/>
    </keyword>
    <keyword id="KW-0155">
        <name>Chromate resistance</name>
        <name>Resistance to chromate</name>
        <description>Protein that enables bacteria and other microorganisms to withstand
chromate, a salt of chromic acid (H2CrO4)</description>
        <go id="GO:0046687"/>
    </keyword>
    <keyword id="KW-0156">
        <name>Chromatin regulator</name>
        <description>Protein controlling the opening or closing of chromatin</description>
        <go id="GO:0006325"/>
    </keyword>
    <keyword id="KW-0157">
        <name>Chromophore</name>
        <description>Protein which interacts with one or more chromophores. A chromophore
absorbs and transmits light energy. Originally it was used for visibly
colored molecules, but it applies also to UV- and IR-absorbing
molecules</description>
    </keyword>
    <keyword id="KW-0957">
        <name>Chromoplast</name>
        <description>Protein found in or associated with a chromoplast, a plastid
containing pigments other than chlorophyll. Found in flower, petals
and fruit</description>
    </keyword>
    <keyword id="KW-0160">
        <name>Chromosomal rearrangement</name>
        <description>Protein which can be altered by a structural chromosomal
rearrangement. Structural rearrangements result from chromosome
breakage, followed by reconstitution in an abnormal combination
Classes of chromosomal rearrangements include: deletions,
duplications, insertions, inversions, translocations and
transpositions</description>
    </keyword>
    <keyword id="KW-0158">
        <name>Chromosome</name>
        <name>Chromosomal protein</name>
        <description>Protein which is associated with chromosomal DNA, including histones,
protamines and high mobility group proteins</description>
    </keyword>
    <keyword id="KW-0159">
        <name>Chromosome partition</name>
        <name>Chromosome segregation</name>
        <description>Protein involved in chromosome partition, the process by which newly
replicated plasmids and chromosomes are actively segregated prior to
cell division. E.g., par and soj which contribute to efficient
chromosome partitioning by serving functions analogous to centromeres
(i.e. pairing or positioning of sister chromosomes)</description>
        <go id="GO:0007059"/>
    </keyword>
    <keyword id="KW-0161">
        <name>Chronic granulomatous disease</name>
        <name>CGD</name>
        <description>Protein which, if defective, causes chronic granulomatous disease
(CGD), a disease characterized by the failure of activated phagocytes
to generate superoxide</description>
    </keyword>
    <keyword id="KW-0162">
        <name>Chylomicron</name>
        <description>Protein component of the chylomicrons or involved in their catabolism
Chylomicrons are the largest lipoprotein complexes with the lowest
protein-to-lipid ratio. They are present in the blood or lymph and
transport exogenous (dietary) cholesterol, triacylglycerols and other
lipids from the intestine to the liver or to the adipose tissue</description>
        <go id="GO:0042627"/>
    </keyword>
    <keyword id="KW-1186">
        <name>Ciliopathy</name>
        <description>Protein which, if defective, causes any one of a group of diseases
associated with either abnormal formation or function of cilia
Ciliopathies cover a large spectrum of often overlapping phenotypes
ranging from relatively mild, tissue-restricted pathologies to severe
defects in multiple organs. Although cilia play important roles in
many tissues, the predominantly affected organs are kidney, eye, liver
and brain. Clinical features typically include retinal degeneration,
renal disease and cerebral anomalies. Additional manifestations
include congenital fibrocystic diseases of the liver, diabetes,
obesity and skeletal dysplasias. Ciliary dysfunction in the embryo may
cause randomization of left-right body asymmetry or situs inversus, as
well as severe malformations leading to embryonic lethality</description>
    </keyword>
    <keyword id="KW-0969">
        <name>Cilium</name>
        <name>Cilia</name>
        <description>Protein found in or associated with a cilium, a cell surface
projection found at the surface of a large proportion of eukaryotic
cells. The two basic types of cilia, motile (alternatively named
flagella) and non-motile, collectively perform a wide variety of
functions broadly encompassing cell/fluid movement and sensory
perception. Their most prominent structural component is the axoneme
which consists of nine doublet microtubules, with all motile cilia
- except those at the embryonic node - containing an additional
central pair of microtubules. The axonemal microtubules of all cilia
nucleate and extend from a basal body, a centriolar structure most
often composed of a radial array of nine triplet microtubules. In most
cells, basal bodies associate with cell membranes and cilia are
assembled as 'extracellular' membrane-enclosed compartments</description>
    </keyword>
    <keyword id="KW-0970">
        <name>Cilium biogenesis/degradation</name>
        <description>Protein which is involved in the formation, organization, maintenance
and degradation of the cilium, a cell surface projection found at the
surface of a large proportion of eukaryotic. Their most prominent
structural component is the axoneme which consists of nine doublet
microtubules, with all motile cilia - except those at the embryonic
node - containing an additional central pair of microtubules</description>
        <go id="GO:0030030"/>
    </keyword>
    <keyword id="KW-0163">
        <name>Citrate utilization</name>
        <description>Protein which allows the utilization of the 6-carbon tricarboxylic
acid citrate as a sole source of carbon and energy</description>
        <go id="GO:0006101"/>
    </keyword>
    <keyword id="KW-0164">
        <name>Citrullination</name>
        <name>N5-carbamoylornithine</name>
        <name>Citrulline</name>
        <name>2-amino-5-(carbamoylamino)pentanoic acid</name>
        <description>Protein which is posttranslationally modified by the deimination of
one or more arginine residues</description>
    </keyword>
    <keyword id="KW-1167">
        <name>Clathrin- and caveolin-independent endocytosis of virus by host</name>
        <name>Non-clathrin/non caveolin-mediated endocytosis by host</name>
        <description>Viral protein involved in virus internalization into the host cell via
endocytic pathways that involve neither clathrin nor caveolins. These
pathways can be further defined by their dependency on various
molecules such as cholesterol, DNM2/Dynamin-2, small GTPases or
tyrosine kinase and possibly involve non-caveolar lipid rafts
Clathrin- and caveolin-independent pathways are used by viruses
including poliovirus, human rhinovirus 14, lymphocytic
choriomeningitis virus, murine norovirus-1 and SV40</description>
        <go id="GO:0019065"/>
    </keyword>
    <keyword id="KW-1165">
        <name>Clathrin-mediated endocytosis of virus by host</name>
        <name>Virion endocytosis by clathrin-coated vesicle</name>
        <description>Viral protein involved in virus internalization by the host cell via
clathrin-mediated endocytosis. In response to an internalization
signal, clathrin is assembled on the inside face of the cell membrane
to form characteristic invaginations or clathrin coated pits that
pinch off through the action of DNM1/Dynamin-1 or DNM2/Dynamin-2. The
virus bound to its host cell receptor is internalized into clathrin-
coated vesicles (CCV). Endocytic CCV deliver their viral content to
early endosomes. The endosomal acidic pH and/or receptor binding
usually induces structural modifications of the virus surface proteins
that lead to penetration of the endosomal membrane via fusion or
permeabilization mechanisms</description>
        <go id="GO:0075512"/>
    </keyword>
    <keyword id="KW-0165">
        <name>Cleavage on pair of basic residues</name>
        <description>Protein which is posttranslationally modified by the cleavage on at
least one pair of basic residues, in order to release one or more
mature active peptides (such as hormones)</description>
    </keyword>
    <keyword id="KW-0168">
        <name>Coated pit</name>
        <description>Protein which is a component of a coated pit. Coated pits are regions
of the donor membrane where the assembly of the vesicle coat take
place. The coat assembles from soluble protomers such as coat protein
complex-I and coat protein complex-II. The components of the coat
often define the intracellular sorting station, and contribute to both
membrane deformation and local movement of the resulting transport
intermediate following scission. During the first steps of the
vesicle-mediated membrane transport, coated pits are internalized to
form coated vesicles which transport proteins between distinct
membrane-bound organelles</description>
        <go id="GO:0005905"/>
    </keyword>
    <keyword id="KW-0846">
        <name>Cobalamin</name>
        <name>Vitamin B12</name>
        <description>Protein which contains at least one cobalamin as cofactor, e.g
methylmalonyl-CoA mutase, or which binds and/or transports cobalamin,
such as intrinsic factor or transcobalamins. Cobalamin, which is
synthesized by microorganisms, has equatorial sites occupied by a
tetrapyrrol ring structure (corrin ring) with a cobalt(III) ion in the
center, one axial site occupied by an intramolecularly-bound
dimethylbenzimidazole and the other axial site occupied by a number of
different ligands such as water (aquacobalamin), cyanide
(cyanocobalamin=vitamin B12), glutathione (glutathionylcobalamin),
5'deoxyadenosine (adenosylcobalamin=coenzyme B12) or a methyl group
(methylcobalamin). It is a prosthetic group of certain mammalian
enzymes, where it is essential for the normal maturation and
development of erythrocytes. A deficiency in the diet or more
frequently the failure to absorb the vitamin give rise to pernicious
anemia</description>
        <go id="GO:0031419"/>
    </keyword>
    <keyword id="KW-0169">
        <name>Cobalamin biosynthesis</name>
        <name>Vitamin B12 anabolism</name>
        <name>Cobalamin formation</name>
        <name>Cobalamin anabolism</name>
        <name>Vitamin B12 formation</name>
        <name>Vitamin B12 synthesis</name>
        <name>Cobalamin biosynthetic process</name>
        <name>Cobalamin synthesis</name>
        <name>Vitamin B12 biosynthetic process</name>
        <name>Vitamin B12 biosynthesis</name>
        <description>Protein involved in the synthesis of cobalamin. Cobalamin, which is
synthesized by microorganisms, has equatorial sites occupied by a
modified porphyrin ring system, with two of the four pyrrol rings
fused directly (without an intervening methine bridge). The modified
porphyrin system binds a cobalt(III) ion in the center, and this is
called a corrin ring system. One axial site is occupied usually by an
intramolecularly-bound dimethylbenzimidazole nucleotide and the other
axial site is occupied by a number of different ligands such as water
(aquacobalamin), cyanide (cyanocobalamine=vitamin B12), glutathione
(glutathionylcobalamine), 5'deoxyadenosine
(adenosylcobalamine=coenzyme B12) or a methyl group (methylcobalamin)
Vitamin B12, for instance, is a prosthetic group of certain mammalian
enzymes, where it is essential for the normal maturation and
development of erythrocytes. A deficiency in the diet or more
frequently the failure to absorb the vitamin B12 give rise to
pernicious anemia</description>
        <go id="GO:0009236"/>
    </keyword>
    <keyword id="KW-0170">
        <name>Cobalt</name>
        <name>Cobalt cation</name>
        <name>Co ion</name>
        <name>Cobalt ion</name>
        <name>Co cation</name>
        <name>Co</name>
        <description>Protein which binds at least one cobalt atom, or protein whose
function is cobalt-dependent. Cobalt is a metallic element, chemical
symbol Co</description>
    </keyword>
    <keyword id="KW-0171">
        <name>Cobalt transport</name>
        <name>Co cation transport</name>
        <name>Cobalt cation transport</name>
        <name>Co transport</name>
        <name>Cobalt ion transport</name>
        <name>Co ion transport</name>
        <description>Protein involved in the transport of the trace element cobalt, which
is a component of vitamin B12</description>
        <go id="GO:0006824"/>
    </keyword>
    <keyword id="KW-0172">
        <name>Cockayne syndrome</name>
        <name>CS</name>
        <name>Cockayne's syndrome</name>
        <description>Protein which, if defective, causes Cockayne's syndrome (CS), an
autosomal recessive disease characterized by UV-sensitive skin
(without pigmentation abnormalities), neurological dysfunction due to
demyelination of neurons and calcification of basal ganglia
(psychomotor retardation, deafness, optic atrophy, retinal
pigmentation and hyperreflexes) and dysmorphic dwarfism (immature
sexual development and microcephaly)</description>
    </keyword>
    <keyword id="KW-0173">
        <name>Coenzyme A biosynthesis</name>
        <name>CoA biosynthetic process</name>
        <name>CoASH biosynthetic process</name>
        <name>CoASH anabolism</name>
        <name>Coenzyme A synthesis</name>
        <name>CoA anabolism</name>
        <name>CoA biosynthesis</name>
        <name>CoA synthesis</name>
        <name>CoA formation</name>
        <name>Coenzyme A anabolism</name>
        <name>Coenzyme A formation</name>
        <name>CoASH formation</name>
        <name>Coenzyme A biosynthetic process</name>
        <name>CoASH synthesis</name>
        <name>CoASH biosynthesis</name>
        <description>Protein involved in the biosynthetic pathway leading from pantothenate
to coenzyme A (CoA). CoA has two halves in phosphodiester linkage: a
3',5'-ADP residue, and 4-phosphopantetheine. The phosphopantetheine
moiety is itself composed of three structural entities: a branched
chain dihydroxy acid in amide linkage to a beta-alanyl residue, which
is in turn linked to a cysteamide containing the reactive thiol
Coenzyme A functions as a carrier of acetyl and acyl groups and is
essential for numerous biosynthetic, energy-yielding, and degradative
metabolic pathways. Acetyl-CoA is the common cellular currency for
acetyl transfers</description>
        <go id="GO:0015937"/>
    </keyword>
    <keyword id="KW-0174">
        <name>Coenzyme M biosynthesis</name>
        <name>2-mercaptoethanesulfonic acid formation</name>
        <name>CoM anabolism</name>
        <name>CoM biosynthesis</name>
        <name>2-mercaptoethanesulfonic acid synthesis</name>
        <name>CoM synthesis</name>
        <name>Coenzyme M synthesis</name>
        <name>Coenzyme M formation</name>
        <name>CoM biosynthetic process</name>
        <name>CoM formation</name>
        <name>Coenzyme M anabolism</name>
        <name>2-mercaptoethanesulfonic acid anabolism</name>
        <name>2-mercaptoethanesulfonic acid biosynthesis</name>
        <name>2-mercaptoethanesulfonic acid biosynthetic process</name>
        <name>Coenzyme M biosynthetic process</name>
        <description>Protein involved in the biosynthesis of coenzyme M. Coenzyme M (2-
mercaptoethanesulfonic acid) is the smallest known organic cofactor
CoM serves as a methyl group carrier in key reactions within the
pathway of methane formation from C1 precursors. In the alkene
metabolism pathway, it is involved in aliphatic epoxyde carboxylation</description>
        <go id="GO:0019295"/>
    </keyword>
    <keyword id="KW-0175">
        <name>Coiled coil</name>
        <name>Heptad repeat pattern</name>
        <description>Protein which contains at least one coiled coil domain, a type of
secondary structure composed of two or more alpha helices which
entwine to form a cable structure. In proteins, the helical cables
serve a mechanical role in forming stiff bundles of fibres</description>
    </keyword>
    <keyword id="KW-0176">
        <name>Collagen</name>
        <description>Protein which contains one or more collagen-like domain. Collagen is a
fibrous protein found in vertebrates, the major element of skin, bone,
tendon, cartilage, blood vessels and teeth. It forms insoluble fibres
of high tensile strength and which contains the unusual amino acids
hyroxyproline and hydroxylysine. It is rich in glycine but lacks
cysteine and tryptophan, and has an unusually regular amino-acid
domain</description>
        <go id="GO:0005581"/>
    </keyword>
    <keyword id="KW-0177">
        <name>Collagen degradation</name>
        <name>Collagen catabolic process</name>
        <name>Collagen breakdown</name>
        <name>Collagen catabolism</name>
        <description>Protein involved in the degradation of collagen, a family of fibrous
proteins found in skin, bones, teeth, cartilage and other tissues of
vertebrates</description>
        <go id="GO:0030574"/>
    </keyword>
    <keyword id="KW-0178">
        <name>Competence</name>
        <description>Protein involved in competence, the state in which a cell or organism
is able to take up DNA and become genetically transformed</description>
        <go id="GO:0030420"/>
    </keyword>
    <keyword id="KW-1018">
        <name>Complement activation lectin pathway</name>
        <name>Lectin pathway</name>
        <name>Lectin complement pathway</name>
        <description>Protein involved in the complement activation lectin pathway which
activates the proteins of the complement system. This pathway can be
activated mainly by mannose-binding lectin (MBL) interacting with
carbohydrate structures on microbial surfaces and by ficolins with
different fine carbohydrate binding specificity</description>
        <go id="GO:0001867"/>
    </keyword>
    <keyword id="KW-0179">
        <name>Complement alternate pathway</name>
        <name>Alternate complement pathway</name>
        <name>Complement activation alternative pathway</name>
        <name>Properdin system</name>
        <description>Protein involved in the complement alternate pathway which activates
the proteins of the complement system. This pathway can be activated
by IgA immune complexes, but also by bacterial endotoxins,
polysaccharides and cell walls, without participation of an antigen-
antibody reaction</description>
        <go id="GO:0006957"/>
    </keyword>
    <keyword id="KW-0180">
        <name>Complement pathway</name>
        <name>Classical complement pathway</name>
        <name>Complement activation classical pathway</name>
        <description>Pathway which activates the proteins of the complement system, a group
of blood proteins of the globulin class involved in the lysis of
foreign cells after they have been coated with antibody, and which
also promote the removal of antibody-coated foreign particles by
phagocytic cells. The pathway proceeds by a cascade reaction of
successive binding and proteolytic cleavage of complement components
This pathway can be activated by either IgG or IgM binding to an
antigen</description>
        <go id="GO:0006958"/>
    </keyword>
    <keyword id="KW-1216">
        <name>Complement system impairing toxin</name>
        <description>Toxin which interferes with the complement system. These toxins act by
activating, inhibiting, or mimicking proteins of this system. They are
mostly found in snake and spider venoms</description>
    </keyword>
    <keyword id="KW-0182">
        <name>Cone-rod dystrophy</name>
        <description>Protein which, if defective, causes cone-rod dystrophy, a disease
where dystrophy of cone-rod cells is characterized by the initial
degeneration of cone photoreceptor cells, thus causing early loss of
visual acuity and color vision, followed by the degeneration of rod
photoreceptor cells and leading to progressive night blindness and
peripheral visual field loss</description>
    </keyword>
    <keyword id="KW-0954">
        <name>Congenital adrenal hyperplasia</name>
        <name>CAH</name>
        <description>Protein which, if defective, causes congenital adrenal hyperplasia, a
group of inherited disorders of cortisol biosynthesis. Defective
cortisol biosynthesis results in compensatory hypersecretion of
corticotropin with subsequent adrenal hyperplasia and excessive
androgen production. Various clinical types are recognized: "salt
wasting form" is the most severe type, "simple virilizing form" with
normal aldosterone biosynthesis, "non-classic form" or late onset, and
"cryptic form" or asymptomatic</description>
    </keyword>
    <keyword id="KW-0900">
        <name>Congenital disorder of glycosylation</name>
        <description>Protein which, if defective, causes a congenital disorder of
glycosylation. In the endoplasmic reticulum (ER) of eukaryotes, N-
linked glycans are first assembled on the lipid carrier dolichyl
pyrophosphate. The GlcNAc(2)Man(9)Glc(3) oligosaccharide is
transferred to selected asparagine residues of nascent polypeptides
Defects along the biosynthetic pathway of N-glycans are associated
with severe multisystemic syndromes called congenital disorders of
glycosylation (CDG). The characteristic biochemical feature of CDG is
defective glycosylation of glycoproteins due to mutations in genes
required for the biosynthesis of N-linked oligosaccharides. Defects of
the assembly of dolichyl-linked oligosaccharides or their transfer on
to nascent glycoproteins form type I forms of CDG, whereas CDG type II
comprises all defects of the trimming and elongation of N-linked
oligosaccharides</description>
    </keyword>
    <keyword id="KW-1055">
        <name>Congenital dyserythropoietic anemia</name>
        <name>CDA</name>
        <description>Protein which, if defective, causes congenital dyserythropoietic
anemia, a heterogeneous group of disorders characterized by the
occurrence of multinuclear erythroid precursors in the bone marrow,
ineffective erythropoiesis, iron overload and anemia. Various forms
are differentiated mainly by the morphological appearance of the
erythroid precursors</description>
    </keyword>
    <keyword id="KW-0985">
        <name>Congenital erythrocytosis</name>
        <name>Congenital polycythemia</name>
        <description>Protein which, if defective, causes congenital absolute
erythrocytosis, a disorder characterized by expansion of the
erythrocyte compartment in the peripheral blood. Total red cell mass
is increased in the absence of a reduction of plasma volume
Erythrocytoses are usually divided into primary and secondary forms
Primary erythrocytoses are due to defects in the erythroid progenitors
and are characterized by low erythropoietin levels. Secondary
erythrocytoses can be due to defects in hypoxia sensing, or to
conditions that cause low tissue oxygen tension with consequent
increase in erythropoietin secretion</description>
    </keyword>
    <keyword id="KW-1022">
        <name>Congenital generalized lipodystrophy</name>
        <name>Berardinelli-Seip syndrome</name>
        <name>Congenital generalized lipoatrophy</name>
        <description>Protein which, if defective, causes congenital generalized
lipodystrophy, a disorder characterized by near complete absence of
adipose tissue from birth. Affected patients manifest insulin
resistance, early onset diabetes mellitus, hypertriglyceridemia,
hepatic steatosis and acanthosis nigricans</description>
    </keyword>
    <keyword id="KW-0984">
        <name>Congenital hypothyroidism</name>
        <description>Protein which, if defective, causes congenital hypothyroidism, a
condition due to thyroid hormones deficiency, presenting at birth
Congenital hypothyroidism occurs when the thyroid gland fails to
develop or function properly. In most cases, the thyroid gland is
absent, abnormally located, or severely reduced in size. In the
remaining cases, a normal-sized or enlarged thyroid gland is present,
but production of thyroid hormones is decreased or absent. If
untreated, congenital hypothyroidism can lead to intellectual
disability and growth failure</description>
    </keyword>
    <keyword id="KW-0912">
        <name>Congenital muscular dystrophy</name>
        <description>The congenital muscular dystrophies (CMD) are a heterogeneous group of
disorders characterized by hypotonia, muscle weakness, dystrophic
changes on skeletal muscle biopsy, and joint contractures that present
at birth or during the first 6 months of life. Intellectual disability
with or without structural brain changes is an additional feature of
several CMD syndromes</description>
    </keyword>
    <keyword id="KW-1004">
        <name>Congenital myasthenic syndrome</name>
        <name>CMS</name>
        <description>Protein which, if defective, causes congenital myasthenic syndrome
Congenital myasthenic syndromes constitute a group of inherited
diseases characterized by a congenital defect in neuromuscular
transmission at the neuromuscular junction, including pre-synaptic,
synaptic, and post-synaptic disorders that are not of autoimmune
origin. Congenital myasthenic syndromes are characterized by muscle
weakness affecting the axial and limb muscles (with hypotonia in
early-onset forms), the ocular muscles (leading to ptosis and
ophthalmoplegia), and the facial and bulbar musculature (affecting
sucking and swallowing, and leading to dysphonia). The symptoms
fluctuate and worsen with physical effort</description>
    </keyword>
    <keyword id="KW-1014">
        <name>Congenital stationary night blindness</name>
        <name>CSNB</name>
        <description>Protein which, if defective, causes congenital stationary night
blindness that is the failure or imperfection of vision at night or in
dim light, with good vision only on bright days</description>
    </keyword>
    <keyword id="KW-0183">
        <name>Conidiation</name>
        <name>Conidia biosynthesis</name>
        <name>Conidia formation</name>
        <name>Conidium biosynthesis</name>
        <name>Conidium formation</name>
        <description>Protein involved in conidiation, the production of conidia which are
asexual fungal spores</description>
        <go id="GO:0048315"/>
    </keyword>
    <keyword id="KW-0184">
        <name>Conjugation</name>
        <description>Protein involved in the temporary fusion of two gametes or two cells
leading to the transfer of genetic material. This process is seen in
bacteria, ciliate protozoa and certain fungi</description>
    </keyword>
    <keyword id="KW-0186">
        <name>Copper</name>
        <name>Copper cation</name>
        <name>Cu</name>
        <name>Copper ion</name>
        <name>Cu cation</name>
        <name>Cu ion</name>
        <description>Protein which binds at least one copper atom, or protein whose
function is copper-dependent. Copper is a trace metallic element,
chemical symbol Cu</description>
    </keyword>
    <keyword id="KW-0187">
        <name>Copper transport</name>
        <name>Copper cation transport</name>
        <name>Copper ion transport</name>
        <name>Cu transport</name>
        <description>Protein involved in the transport of ions of the trace element copper</description>
        <go id="GO:0006825"/>
    </keyword>
    <keyword id="KW-0188">
        <name>Copulatory plug</name>
        <description>Protein involded in the formation of the copulatory plug, a plug
composed of a number of proteins which are secreted by the seminal
vesicle under the influence of testosterone. Found in rodents</description>
        <go id="GO:0042628"/>
    </keyword>
    <keyword id="KW-1212">
        <name>Corneal dystrophy</name>
        <description>Protein which, if defective, causes corneal dystrophy. The term
corneal dystrophy includes a heterogeneous group of bilateral, primary
alterations of the cornea that are not associated with prior
inflammation or secondary to systemic disease. Most corneal
dystrophies present with variable shaped corneal opacities in a clear
or cloudy cornea and they affect visual acuity to different degrees
Corneal dystrophies may be present at birth but more frequently
develop during adolescence and progress slowly throughout life</description>
    </keyword>
    <keyword id="KW-0190">
        <name>Covalent protein-DNA linkage</name>
        <name>DNA-protein covalent cross-linking</name>
        <description>Protein covalently attached to a DNA molecule. For example some
viruses contains proteins that are attached to the end of a viral
replicating DNA and which are necessary for DNA replication</description>
    </keyword>
    <keyword id="KW-0191">
        <name>Covalent protein-RNA linkage</name>
        <name>RNA-protein covalent cross-linking</name>
        <description>Protein covalently attached to a RNA molecule. For example some
viruses contains proteins that are attached to the end of a viral
replicating RNA and which are necessary for RNA replication</description>
        <go id="GO:0018144"/>
    </keyword>
    <keyword id="KW-0989">
        <name>Craniosynostosis</name>
        <name>Craniostosis</name>
        <description>Protein which, if defective, causes craniosynostosis, the premature
closure of one or more cranial sutures which results in an abnormal
head shape. Different types of craniosynostosis are known. All are
characterized by skull deformities, with face and often limb
involvement in the syndromic forms</description>
    </keyword>
    <keyword id="KW-1257">
        <name>CRISPR-cas system evasion by virus</name>
        <description>Viral protein that inhibits host defense CRISPR-cas system (Clustered
Regularly Interspaced Short Palindromic Repeats). The CRISPR-cas
system is composed of genomic sensors that allow prokaryotes to
acquire DNA fragments from invading viruses and plasmids into the
CRISPR locus. These stored fragments (called spacers) are transcribed
and processed into small crRNA which are used to destroy matching DNA
in future viral and plasmid invasion. Some prokaryotic viruses express
specific genes that allow them to evade CRISPR-cas system</description>
        <go id="GO:0098672"/>
    </keyword>
    <keyword id="KW-0192">
        <name>Crown gall tumor</name>
        <description>Protein involved in crown gall tumor formation, a plant tumor caused
by the bacterium Agrobacterium tumefaciens</description>
    </keyword>
    <keyword id="KW-0885">
        <name>CTQ</name>
        <name>Cysteine tryptophylquinone</name>
        <description>Protein which contains at least one cysteine tryptophylquinone (CTQ)
cross-link modification. CTQ is formed by oxidation of the indole ring
of a tryptophan to form tryptophylquinone followed by covalent cross-
linking with a cysteine residue. In the quinohemoprotein amine
dehydrogenase, CTQ mediates during the catalytic cycle electron
transfer from the substrate to either a copper protein, azurin, or
cytochrome c-550</description>
    </keyword>
    <keyword id="KW-1062">
        <name>Cushing syndrome</name>
        <name>Hypercortisolism</name>
        <name>Cushing's syndrome</name>
        <name>Hyperadrenocorticism</name>
        <description>Protein which, if defective, causes Cushing syndrome, a condition
caused by prolonged exposure to excess levels of cortisol from
endogenous or exogenous sources. Endogenous Cushing syndrome is due to
excess production of cortisol by the adrenal glands. It may be caused
by pituary hypersecretion of adrenocorticotropic hormone (ACTH),
ectopic ACTH secretion by non-pituary tumors, or may result from
cortisol hypersecretion by adrenal gland tumors (ACTH-independent
Cushing syndrome). Cushing syndrome is clinically characterized by
upper body obesity, osteoporosis, hypertension, diabetes mellitus,
hirsutism, amenorrhea, and excess body fluid</description>
    </keyword>
    <keyword id="KW-0193">
        <name>Cuticle</name>
        <description>Protein which is a component of the cuticle, the outer protective
layer produced by epidermal cells that covers the body of many
invertebrates</description>
        <go id="GO:0042302"/>
    </keyword>
    <keyword id="KW-0194">
        <name>Cyanelle</name>
        <name>Cyanoplast</name>
        <name>Muroplast</name>
        <description>Protein encoded by the cyanelle genome or protein located in the
cyanelle. Cyanelles are the plastids of glaucocystophyte algae. They
are surrounded by a double membrane and, in between, a peptidoglycan
wall. The cyanelle genome is of chloroplast size and contains genes
for tRNAs, rRNAs and approx. 150 proteins, which is more than found in
higher plant chloroplast genomes (this feature is also shared by other
primitive plastids). Thylakoid membrane architecture is cyanobacteria-
like. Historically, the term cyanelle is derived from a classification
as endosymbiotic cyanobacteria, and thus is not fully correct</description>
    </keyword>
    <keyword id="KW-0195">
        <name>Cyclin</name>
        <description>Protein that belongs to the cyclin family or that contains a cyclin
box-like domain. Cyclins are regulatory subunits of the cyclin-
dependent protein kinases. They form kinase holoenzymes, with distinct
biochemical characteristics and nonredundant biological functions,
which mediate phosphorylation of cellular proteins, including key cell
cycle regulatory molecules. In this way, the kinase holoenzymes
promote the transit of cells through the division cycle. Cyclins
accumulate during interphase of eukaryotic cell cycle and are
destroyed at the end of mitosis</description>
    </keyword>
    <keyword id="KW-0196">
        <name>Cycloheximide resistance</name>
        <name>Resistance to cycloheximide</name>
        <description>Protein that confers, on an organism, the ability to withstand
cycloheximide, an antibiotic produced by Streptomyces griseus, which
inhibits eukaryotic elongation during protein synthesis. The
resistance is often due to mutations that prevent antibiotic binding
to the protein</description>
        <go id="GO:0046898"/>
    </keyword>
    <keyword id="KW-0198">
        <name>Cysteine biosynthesis</name>
        <name>Cysteine formation</name>
        <name>Cysteine anabolism</name>
        <name>Cysteine biosynthetic process</name>
        <name>Cysteine synthesis</name>
        <description>Protein involved in the synthesis of cysteine, the amino acid with the
highly reactive sulfhydryl group (-SH). It is derived from the amino
acids methionine and serine. Cysteine plays a special role in shaping
some proteins by forming disulfide bonds. In enzymes the unique
reactivity of this group is frequently exploited at the catalytic
site</description>
        <go id="GO:0019344"/>
    </keyword>
    <keyword id="KW-0199">
        <name>Cystinuria</name>
        <name>CSNU</name>
        <description>Protein which, if defective, causes cystinuria (CSNU), an autosomal
recessive condition of persistent excessive urinary excretion of
cystine and three other dibasic amino acids: lysine, ornithine, and
arginine. CSNU arises from impaired reabsorption of these amino acids
through the epithelial cells of the renal tubule and gastrointestinal
tract. It is characterized by cystine stones in the kidney, ureter and
bladder. Three clinical types of cystinuria have been described:
cystinuria type-I (CSNU1), type-II (CSNU2) and type-III (CSNU3)</description>
    </keyword>
    <keyword id="KW-0200">
        <name>Cytadherence</name>
        <description>Protein involved in cytadherence, the attachment of mycoplasma to the
epithelium</description>
        <go id="GO:0020035"/>
    </keyword>
    <keyword id="KW-0201">
        <name>Cytochrome c-type biogenesis</name>
        <name>Cytochrome c-type synthesis</name>
        <name>Cytochrome c-type formation</name>
        <description>Protein involved in the biogenesis of c-type cytochromes. Cytochromes
c are electron-transfer proteins having one or several heme c groups,
bound to the protein by one or, more commonly two, thioether bonds
involving sulphydryl groups of cysteine residues</description>
        <go id="GO:0017004"/>
    </keyword>
    <keyword id="KW-0202">
        <name>Cytokine</name>
        <description>Small secreted proteins from higher eukaryotes which affect the
growth, division and functions of other cells, e.g. interleukins,
lymphokines, TNF and interferons. Generally, growth factors are not
classified as cytokines, though TGF is an exception. Chemokines are a
subset of cytokines. They differ from classical hormones in that they
are produced by a number of tissues or cell types rather than by
specialized glands. They generally act locally in a paracrine or
autocrine rather than endocrine manner</description>
        <go id="GO:0005125"/>
        <go id="GO:0005615"/>
    </keyword>
    <keyword id="KW-0203">
        <name>Cytokinin biosynthesis</name>
        <name>Cytokinin biosynthetic process</name>
        <name>Cytokinin formation</name>
        <name>Cytokinin synthesis</name>
        <name>Cytokinin anabolism</name>
        <description>Protein involved in the synthesis of cytokinins, a class of plant
hormones which promote cell division (e.g. kinetin, zeatin, benzyl
adenine). They are also involved in cell growth, cell differentiation
and in other physiological processes</description>
        <go id="GO:0009691"/>
    </keyword>
    <keyword id="KW-0932">
        <name>Cytokinin signaling pathway</name>
        <name>Cytokinin mediated signaling</name>
        <description>Protein involved in the cytokinin signaling pathway (i.e. transport or
signal transduction). Cytokinins (i.e. kinetin and zeatin) are defined
more by their biological activity (e.g. inducing cell division in
tissue culture) rather than by structure. These phytohormones are
synthesized in the root apical meristem and transported through the
plant in the xylem sap. Cytokinins are involved in several
physiological processes such as promoting cell division and
chloroplast maturation, regulating cell growth and differentiation,
and monitoring nutrient uptake and senescence. Together with auxin,
they also regulate the cell cycle and tissue morphogenesis</description>
        <go id="GO:0009736"/>
    </keyword>
    <keyword id="KW-0204">
        <name>Cytolysis</name>
        <name>Cell lysis</name>
        <description>Protein involved in the rupture of cell membranes and loss of
cytoplasm, e.g. exotoxin, cytolysin</description>
        <go id="GO:0031640"/>
    </keyword>
    <keyword id="KW-0963">
        <name>Cytoplasm</name>
        <description>Protein found in the cytoplasm, the content of a cell within the
plasma membrane and, in eukaryotics cells, surrounding the nucleus
This three-dimensional, jelly-like lattice interconnects and supports
the other solid structures. The cytosol (the soluble portion of the
cytoplasm outside the organelles) is mostly composed of water and many
low molecular weight compounds. In eukaryotes, the cytoplasm also
contains a network of cytoplasmic filaments (cytoskeleton)</description>
    </keyword>
    <keyword id="KW-1176">
        <name>Cytoplasmic inwards viral transport</name>
        <description>Viral protein that allows the active transport of viral components
along cytoskeletal filaments toward the intracellular replication
sites during virus entry. Viruses such as adenoviruses, adeno-
associated virus, vaccinia virus, poliovirus, canine parvovirus,
African swine fever virus, rabies virus, human herpes virus 1, foamy
virus are thought to use active intracellular transport of viral
components</description>
        <go id="GO:0075606"/>
    </keyword>
    <keyword id="KW-0968">
        <name>Cytoplasmic vesicle</name>
        <description>Protein found in or associated with cytoplasmic vesicles, which
mediate vesicular transport among the organelles of secretory and
endocytic systems. These transport vesicles are classified by the
identity of the protein coat used in their formation and also by the
cargo they contain, e.g. clathrin-, COPI-, and COPII-coated vesicles,
synaptic vesicles, secretory vesicles, phagosomes, etc</description>
        <go id="GO:0031410"/>
    </keyword>
    <keyword id="KW-0205">
        <name>Cytosine metabolism</name>
        <name>Cytosine metabolic process</name>
        <description>Protein involved in the biochemical reactions with the pyrimidine base
cytosine</description>
        <go id="GO:0019858"/>
    </keyword>
    <keyword id="KW-0206">
        <name>Cytoskeleton</name>
        <description>Protein which is a component or which is associated with the
cytoskeleton, a dynamic three-dimensional filamentous structure in the
cytoplasm. The cytoskeleton is both a muscle and a skeleton, and its
roles include maintenance of cell shape, cell movement (in
eukaryotes), cytokinesis, and the organization of the organelles
within the cell. This includes the major components of cytoskeleton;
microfilaments (actin-like proteins), microtubules (tubulin-like
proteins) and intermediate filaments (mostly in eukaryotes) and
prokaryotic MinD-ParA proteins. Originally not thought to exist in
prokaryotes, but now known to have the same functions as in
eukyaryotes</description>
    </keyword>
    <keyword id="KW-0208">
        <name>D-amino acid</name>
        <description>Protein which contains at least one D-amino acid. All of the amino
acids derived from natural proteins are of the L configuration. D-
amino acids are found in nature, especially as components of certain
peptide antibiotics and in walls of certain microorganisms</description>
    </keyword>
    <keyword id="KW-0209">
        <name>Deafness</name>
        <description>Protein which, if defective, causes a partial or total inability to
hear. The two principal types of deafness are conductive deafness that
results from changes in the middle ear, and nerve or sensorineural
deafness that is caused by damages to the inner ear, the nerve
pathways to the brain, or the area of the brain that receives sound
information</description>
    </keyword>
    <keyword id="KW-0210">
        <name>Decarboxylase</name>
        <description>Enzyme that belongs to the lyase family and which catalyzes the
spliting of CO(2) from the carboxylic group of amino acids, beta-keto
acids and alpha-keto acids</description>
        <go id="GO:0016831"/>
    </keyword>
    <keyword id="KW-1132">
        <name>Decay of host mRNAs by virus</name>
        <description>Viral protein involved in the degradation of host mRNAs. Viruses have
evolved ways of degrading host mRNAs to inhibit cellular translation
This global inhibition of cellular protein synthesis serves to ensure
maximal viral gene expression and to evade host immune response. Decay
of host mRNAs can be achieved by endonucleotic RNA cleavage or
associated with PABPC1 nuclear relocalization</description>
        <go id="GO:0039595"/>
    </keyword>
    <keyword id="KW-0211">
        <name>Defensin</name>
        <description>Families of microbicidal and cytotoxic peptides. Defensins have
antibacterial, antifungal and antiviral properties. Defensins kills
cells by forming voltage-regulated multimeric channels in the
susceptible cell's membrane</description>
        <go id="GO:0006952"/>
    </keyword>
    <keyword id="KW-1238">
        <name>Degradation of host capsule during virus entry</name>
        <description>Virion protein involved in breaking down host cell capsule to reach
the host cell wall, and finally the host cytoplasmic membrane. Many
prokaryotic viruses carry for example glycanase, polysaccharide lyase
or deacetylase activities to specifically digest host capsule</description>
        <go id="GO:0098996"/>
    </keyword>
    <keyword id="KW-1235">
        <name>Degradation of host cell envelope components during virus entry</name>
        <description>Virion protein involved in breaking down host cell surface components
to reach the host cytoplasmic membrane. Many prokaryotic viruses for
example carry enzymatic activities to degrade the host cell
lipopolysaccharide layer, cell wall, or capsule</description>
        <go id="GO:0098994"/>
    </keyword>
    <keyword id="KW-1247">
        <name>Degradation of host chromosome by virus</name>
        <description>Viral protein that rapidly degrades the host DNA at the onset of
infection. The breakdown products can be reused to synthesize viral
DNA or can be excreted from the host cell. Degrading host chromosome
provides an advantage during the virus life cycle by reducing or
eliminating competing host macromolecular synthesis. Bacteriophages
such as T4 or T5 for example are known to induce degradation of the
host chromosome and excretion of the host DNA degradation products</description>
        <go id="GO:0099015"/>
    </keyword>
    <keyword id="KW-1237">
        <name>Degradation of host lipopolysaccharides during virus entry</name>
        <description>Virion protein involved in breaking down host cell lipopolysaccharides
(LPS) to reach the cytoplasmic membrane of prokaryotes with 2
membranes. Many prokaryotic viruses carry glycanase or deacetylase
activities to digest host LPS</description>
        <go id="GO:0098995"/>
    </keyword>
    <keyword id="KW-1236">
        <name>Degradation of host peptidoglycans during virus entry</name>
        <description>Virion exolysin involved in breaking down host cell peptidoglycans
(e.g. murein, pseudomurein) to reach the host cytoplasmic membrane
during virus entry. Exolysins are usually part of the tail or the base
plate of prokaryotic viruses. Exolysins can display various enzymatic
activities such as lysozyme, transglycosylase, muramidase or even
protease activity. Murein hydrolases for example are widespread in
bacteriophages infecting Gram-positive or Gram-negative bacteria</description>
        <go id="GO:0098932"/>
    </keyword>
    <keyword id="KW-0213">
        <name>Dejerine-Sottas syndrome</name>
        <name>DSS</name>
        <description>Protein which, if defective, causes Dejerine-Sottas disease. DSS is a
hereditary motor and sensory neuropathy (HMSN) of the Charcot-Marie-
Tooth disease type 1 class. DSS is characterized by severe early
onset, very slow nerve conduction velocities (less than 12m/sec) and
raised cerebrospinal fluid protein concentrations (0.7 g/l). Clinical
signs are delayed age of walking as well as areflexia</description>
    </keyword>
    <keyword id="KW-0214">
        <name>Dental caries</name>
        <description>Protein involved in dental caries or important in the prevention of
dental caries. Dental caries are localized destruction of the tooth
surface, initiated by decalcification of the enamel and followed by
enzymatic lysis of organic structures, the result of which is cavity
formation. The cavity may penetrate the enamel and dentin, and reach
the pulp. The disease may be caused by acids produced by bacteria
which lead to decalcification, or by microorganisms that destroy the
enamel protein, or by keratolytic microorganisms producing chelates
that lead to decalcification</description>
    </keyword>
    <keyword id="KW-0215">
        <name>Deoxyribonucleotide synthesis</name>
        <name>Deoxyribonucleotide biosynthetic process</name>
        <name>Deoxyribonucleotide anabolism</name>
        <name>Deoxyribonucleotide biosynthesis</name>
        <name>Deoxyribonucleotide formation</name>
        <description>Protein involved in the synthesis of deoxyribonucleotides, the basic
repeating units in DNA. Deoxyribonucleotides consist of a purine or a
pyrimidine base bonded to deoxyribose, which in turn is bound to a
phosphate group. They are synthesised by reduction of ribonucleoside
diphosphates</description>
        <go id="GO:0009263"/>
    </keyword>
    <keyword id="KW-1061">
        <name>Dermonecrotic toxin</name>
        <description>Protein involved in the necrosis of the skin</description>
    </keyword>
    <keyword id="KW-0911">
        <name>Desmin-related myopathy</name>
        <description>Protein which, if defective, causes desmin-related myopathy (DRM), a
clinically and genetically heterogeneous group of muscular disorders
defined morphologically by intrasarcoplasmic aggregates of desmin,
usually accompanied by other protein aggregates. Both autosomal
dominant and autosomal recessive inheritance have been reported
Approximately one-third of DRMs are thought to be caused by mutations
in the desmin gene</description>
    </keyword>
    <keyword id="KW-0216">
        <name>Detoxification</name>
        <description>Protein involved in degrading toxic compounds. Detoxification
generally takes place in the liver or kidney and inactivates toxins,
either by degradation or by conjugation of residues to a hydrophilic
moiety in order to promote excretion</description>
        <go id="GO:0009636"/>
    </keyword>
    <keyword id="KW-0217">
        <name>Developmental protein</name>
        <description>Protein involved in development, the process whereby a multicellular
organism develops from its early immature forms, e.g., zygote, larva,
embryo, into an adult</description>
        <go id="GO:0007275"/>
    </keyword>
    <keyword id="KW-0218">
        <name>Diabetes insipidus</name>
        <description>Protein which, if defective, causes diabetes insipidus, a rare form of
diabetes in which the kidney tubules do not reabsorb enough water
resulting in excessive urine excretion (polyuria). Two types of
diabetes insipidus are recognized: central or neurohypophyseal
diabetes insipidus which is due to defects in the neurohypophyseal
system and results in a deficient quantity of anti-diuretic hormone
being produced or released; nephrogenic diabetes insipidus, a
vasopressin unresponsive condition of polyuria and hyposthenuria</description>
    </keyword>
    <keyword id="KW-0219">
        <name>Diabetes mellitus</name>
        <description>Protein which, if defective, causes diabetes mellitus, a disorder of
impaired carbohydrate, protein, and fat metabolism due to insufficient
secretion of insulin or to target tissue insulin resistance. Diabetes
mellitus can be divided into two main types, type I or insulin-
dependent diabetes mellitus (IDDM), and type II, or non insulin-
dependent diabetes mellitus (NIDDM). Type I diabetes mellitus normally
starts in childhood or adolescence and is caused by the body's own
immune system which destroys the insulin-producing beta cells in the
pancreas. Classical features are polydipsia, polyphagia and polyuria,
due to hyperglycemia-induced osmotic diuresis. Type II diabetes
mellitus normally starts in adulthood and is caused by a lack of
sensitivity to the body's own insulin. It is usually characterized by
a gradual onset with minimal or no symptoms of metabolic disturbance
Both forms of diabetes mellitus lead to secondary complications
(notably cardiovascular, nephropathy, retinopathy, neuropathy). Two
other major subcategories of diabetes mellitus are gestational
diabetes and diabetes secondary to other medical conditions. In common
usage, the term diabetes, when used alone, refers to diabetes mellitus
and not diabetes insipidus</description>
    </keyword>
    <keyword id="KW-0220">
        <name>Diaminopimelate biosynthesis</name>
        <name>Diaminopimelate anabolism</name>
        <name>Diaminopimelate synthesis</name>
        <name>Diaminopimelate biosynthetic process</name>
        <name>Diaminopimelate formation</name>
        <description>Protein involved in the synthesis of diaminopimelate, the ionic form
of the amino acid diaminopimelic acid (DAP) which is found in the
murein peptidoglycans of bacterial cell walls. Diaminopimelic acid is
synthesised from aspartate</description>
        <go id="GO:0019877"/>
    </keyword>
    <keyword id="KW-1024">
        <name>Diamond-Blackfan anemia</name>
        <name>BDS</name>
        <name>Blackfan-Diamond disease</name>
        <name>Congenital erythroid hypoplastic anemia</name>
        <name>Congenital hypoplastic anemia of Blackfan and Diamond</name>
        <name>Aase syndrome</name>
        <name>DBA</name>
        <name>Aase-Smith syndrome II</name>
        <name>Chronic congenital aregenerative anemia</name>
        <name>Erythrogenesis imperfecta</name>
        <name>Blackfan-Diamond syndrome</name>
        <name>Pure red cell aplasia</name>
        <description>Protein which, if defective, causes Diamond-Blackfan anemia, a rare
congenital non-regenerative hypoplastic anemia that usually presents
early in infancy. The disease is characterized by a moderate to severe
macrocytic anemia, erythroblastopenia, and an increased risk of
developing leukemia. 30 to 40% of Diamond-Blackfan anemia patients
present with short stature and congenital anomalies, the most frequent
being craniofacial (Pierre-Robin syndrome and cleft palate), thumb and
urogenital anomalies</description>
    </keyword>
    <keyword id="KW-0221">
        <name>Differentiation</name>
        <name>Cell differentiation</name>
        <description>Protein involved in differentiation, the developmental process of a
multicellular organism by which cells become specialized for
particular functions. Differentiation requires selective expression of
the genome; the fully differentiated state may be preceded by a stage
in which the cell is already programmed for differentiation but is not
yet expressing the characteristic phenotype determination. Also used
for fungal conidiation proteins, and for some bacteria that present
specialization of function in cell types, such as Caulobacter
crescentus</description>
        <go id="GO:0030154"/>
    </keyword>
    <keyword id="KW-0222">
        <name>Digestion</name>
        <description>Protein involved in the process whereby nutrients are rendered soluble
and capable of being absorbed by the organism or cell, by action of
various hydrolytic enzymes that break down proteins, carbohydrates,
fats, etc</description>
        <go id="GO:0007586"/>
    </keyword>
    <keyword id="KW-0223">
        <name>Dioxygenase</name>
        <description>Enzyme that reduces molecular oxygen by incorporating both atoms into
its substrate(s)</description>
        <go id="GO:0051213"/>
    </keyword>
    <keyword id="KW-0224">
        <name>Dipeptidase</name>
        <description>Enzyme that hydrolyzes a dipeptide into its constituent amino acids</description>
        <go id="GO:0016805"/>
    </keyword>
    <keyword id="KW-0903">
        <name>Direct protein sequencing</name>
        <description>Protein, whose amino acid sequence has been partially (more than one
residue) or completely determined experimentally by Edman degradation
or by mass spectrometry</description>
    </keyword>
    <keyword id="KW-0225">
        <name>Disease variant</name>
        <description>Protein for which at least one genetic variant involved in a disease
is reported in the feature table of the UniProtKB/Swiss-Prot entry</description>
    </keyword>
    <keyword id="KW-1015">
        <name>Disulfide bond</name>
        <description>Protein which is modified by the formation of a bond between the thiol
groups of two peptidyl-cysteine residues. The process of chemical
oxidation that forms interchain disulfide bonds can produce stable,
covalently linked protein dimers, multimers or complexes, whereas
intrachain disulfide bonds can contribute to protein folding and
stability. Depending on the protein environment, some disulfide bonds
are more labile, forming transient redox-active disulfide bonds that
are alternately reduced and oxidized in the course of an enzymatic
reaction</description>
    </keyword>
    <keyword id="KW-0226">
        <name>DNA condensation</name>
        <description>Protein involved in DNA condensation. In most eukaryotes, the
chromosomal packing involves the wrapping of DNA around a core of
histones to form nucleosomes. Adjacent nucleosomes are packaged
together via Histone 1 and nucleosomes are organised into a 30 nm
chromatin fibre. DNA condensation takes place as cells enter mitosis
or when germ cells enter meiosis</description>
        <go id="GO:0030261"/>
    </keyword>
    <keyword id="KW-0227">
        <name>DNA damage</name>
        <name>DNA damage response</name>
        <name>Response to DNA damage stimulus</name>
        <description>Protein induced by DNA damage or protein involved in the response to
DNA damage. Drug- or radiation-induced injuries in DNA introduce
deviations from its normal double-helical conformation. These changes
include structural distortions which interfere with replication and
transcription, as well as point mutations which disrupt base pairs and
exert damaging effects on future generations through changes in DNA
sequence. Response to DNA damage results in either repair or
tolerance</description>
        <go id="GO:0006974"/>
    </keyword>
    <keyword id="KW-1256">
        <name>DNA end degradation evasion by virus</name>
        <description>Viral protein that inhibits or counteracts prokaryotic host
helicase/nuclease proteins in order to escape the antiviral activity
of the latter. When functioning in their exonuclease mode,
helicase/nuclease proteins such as bacterial RecBCD or AddAB degrade
any free DNA end as well as the linear dsDNA products resulting from
restriction Type II cleavage. Any prokaryotic virus that exposes free
dsDNA ends as part of its life cycle must find the means to evade
destruction by these host enzymes. Prokaryotic viruses escape this
host defense by expressing inhibitors or by protecting the ends of
their linear genomes from digestion</description>
        <go id="GO:0099016"/>
    </keyword>
    <keyword id="KW-0228">
        <name>DNA excision</name>
        <description>Protein involved in the repair of damages to one strand of DNA (loss
of purines due to thermal fluctuations, formation of pyrimidine dimers
by UV irradiation, for instance). The site of damage is recognized,
excised by an endonuclease, the correct sequence is copied from the
complementary strand by a polymerase and the ends of this correct
sequence are joined to the rest of the strand by a ligase. In
bacterial systems, the polymerase also acts as endonuclease. Excisase
A and other proteins involved in recombination mediate DNA excision; a
process whereby abnormal or mismatched nucleotides are enzymatically
cut out of a strand of a DNA molecule</description>
        <go id="GO:0006281"/>
    </keyword>
    <keyword id="KW-0229">
        <name>DNA integration</name>
        <description>Protein involved in DNA integration, a process that mediates the
insertion of foreign genetic material, or other duplex DNA, into a
chromosome, or another replicon, in order to form a covalently linked
DNA continuous with the host DNA</description>
        <go id="GO:0015074"/>
    </keyword>
    <keyword id="KW-0230">
        <name>DNA invertase</name>
        <description>Specific recombinases which catalyze the inversion of a DNA segment
within a nucleoprotein structure termed invertasome</description>
        <go id="GO:0003677"/>
        <go id="GO:0006310"/>
        <go id="GO:0000150"/>
    </keyword>
    <keyword id="KW-0233">
        <name>DNA recombination</name>
        <description>Protein involved in DNA recombination, i.e. any process in which DNA
molecules are cleaved and the fragments are rejoined to give a new
combination</description>
        <go id="GO:0006310"/>
    </keyword>
    <keyword id="KW-0234">
        <name>DNA repair</name>
        <description>Protein involved in the repair of DNA, the various biochemical
processes by which damaged DNA can be restored. DNA repair embraces,
for instance, not only the direct reversal of some types of damage
(such as the enzymatic photoreactivation of thymine dimers), but also
multiple distinct mechanisms for excising damaged base; termed
nucleotide excision repair (NER), base excision repair (BER) and
mismatch repair (MMR); or mechanisms for repairing double-strand
breaks</description>
        <go id="GO:0006281"/>
    </keyword>
    <keyword id="KW-0235">
        <name>DNA replication</name>
        <description>Protein involved in DNA replication, i.e. the duplication of DNA by
making a new copy of an existing molecule. The parental double-
stranded DNA molecule is replicated semi conservatively, i.e. each
copy contains one of the original strands paired with a newly
synthesized strand that is complementary in terms of AT and GC base
pairing</description>
        <go id="GO:0006260"/>
    </keyword>
    <keyword id="KW-0236">
        <name>DNA replication inhibitor</name>
        <name>Negative regulation of DNA replication</name>
        <description>Protein involved in the inhibition of DNA replication</description>
        <go id="GO:0008156"/>
    </keyword>
    <keyword id="KW-0237">
        <name>DNA synthesis</name>
        <name>DNA biosynthesis</name>
        <name>DNA biosynthetic process</name>
        <description>Protein involved in the synthesis of DNA from deoxyribonucleic acid
monomers</description>
        <go id="GO:0071897"/>
    </keyword>
    <keyword id="KW-0238">
        <name>DNA-binding</name>
        <description>Protein which binds to DNA, typically to pack or modify the DNA, or to
regulate gene expression. Among those proteins that recognize specific
DNA sequences, there are a number of characteristic conserved motifs
believed to be essential for specificity. Many DNA-binding domains are
described in PROSITE</description>
        <go id="GO:0003677"/>
    </keyword>
    <keyword id="KW-0239">
        <name>DNA-directed DNA polymerase</name>
        <description>Enzyme that catalyzes DNA synthesis by addition of deoxyribonucleotide
units to a DNA chain using DNA as a template. They can also possess
exonuclease activity and therefore function in DNA repair</description>
        <go id="GO:0003887"/>
    </keyword>
    <keyword id="KW-0240">
        <name>DNA-directed RNA polymerase</name>
        <description>Protein of the DNA-directed RNA polymerase complexes, which catalyze
RNA synthesis the by addition of ribonucleotide units to a RNA chain
using DNA as a template. They can initiate a chain de novo
Prokaryotes have a single enzyme for the three RNA types that is
subject to stringent regulatory mechanisms. Eukaryotes have type I
that synthesizes all rRNA except the 5S component, type II that
synthesizes mRNA and hnRNA and type III that synthesizes tRNA and the
5S component of rRNA</description>
        <go id="GO:0000428"/>
    </keyword>
    <keyword id="KW-0241">
        <name>Down syndrome</name>
        <name>Down's syndrome</name>
        <description>Protein which, if defective, causes Down's syndrome, a condition due
to the presence of three copies of chromosome 21 (trisomy 21),
characterized by some degree of intellectual disability, short stature
and poor muscle tone. Common (1 in 700 live births); incidence
increases with maternal age. The cause is usually non-disjunction at
meiosis but occasionally a translocation of fused chromosomes 21 and
14</description>
    </keyword>
    <keyword id="KW-0242">
        <name>Dwarfism</name>
        <description>Protein which, if defective, causes dwarfism, a skeletal growth defect
resulting in the condition of being undersized</description>
    </keyword>
    <keyword id="KW-0243">
        <name>Dynein</name>
        <description>Large multimeric complex with ATPase activity, responsible for the
movement of eukaryotic cilia and flagella (axonemal dynein) and for
the intracellular retrograde motility of vesicles, organelles and
chromosomes along microtubules (cytosolic dynein). Constitutes the
side arms of the outer microtubule doublets in the ciliary axoneme and
is responsible for the sliding. Also used for the dynein-associated
microtubule-binding proteins (MTBs), e.g. dynactin</description>
        <go id="GO:0030286"/>
    </keyword>
    <keyword id="KW-1011">
        <name>Dyskeratosis congenita</name>
        <name>DKC</name>
        <description>Protein which, if defective, causes dyskeratosis congenita, a
clinically and genetically heterogeneous disorder characterized by
abnormal skin pigmentation, mucosal leukoplakia, nail dystrophy,
progressive bone marrow failure, and increased predisposition to
cancer</description>
    </keyword>
    <keyword id="KW-1023">
        <name>Dystonia</name>
        <description>Protein which, if defective, causes dystonia or dystonic conditions
that feature persistent or recurrent episodes of dystonia as a major
manifestation of disease. Dystonia is a movement disorder with a
neurological basis, due to disordered tonicity of muscle. It is
characterized by sustained involuntary muscle contractions that cause
abnormal postures, twisting, repetitive and patterned movements. It
may affect muscles throughout the body (generalized), in certain parts
of the body (segmental), or may be confined to particular muscles or
muscle groups (focal)</description>
    </keyword>
    <keyword id="KW-1215">
        <name>Dystroglycanopathy</name>
        <description>Protein which, if defective, causes any of the muscular disorders
caused by aberrant glycosylation of dystroglycan. These genetically
heterogeneous diseases include a range of conditions with different
degrees of severity. At the most severe end of the clinical spectrum,
Walker-Warburg syndrome (WWS), muscle-eye-brain disease (MEB) and
Fukuyama congenital muscular dystrophy (FCMD) are characterized by
congenital muscular dystrophy and severe structural brain and eye
abnormalities, which in WWS result in early infantile death. At the
mildest end of the clinical spectrum, affected individuals present
with limb girdle muscular dystrophy (LGMD), without brain and eye
involvement</description>
    </keyword>
    <keyword id="KW-0244">
        <name>Early protein</name>
        <description>Bacteriophage or viral protein expressed in the first phase of the
infectious cycle</description>
    </keyword>
    <keyword id="KW-0038">
        <name>Ectodermal dysplasia</name>
        <name>ED</name>
        <description>Protein which, if defective, causes ectodermal dysplasia, a
heterogeneous group of developmental disorders affecting tissues of
ectodermal origin. Ectodermal dysplasias are characterized by abnormal
development of two or more ectodermal structures such as hair, teeth,
nails and sweat glands, with or without any additional clinical sign
Each combination of clinical features represents a different type of
ectodermal dysplasia</description>
    </keyword>
    <keyword id="KW-0245">
        <name>EGF-like domain</name>
        <description>Protein containing at least one EGF-like domain, a sequence of about
thirty to forty amino-acid residues long found in the sequence of
epidermal growth factor (EGF). It has been shown to be present, in a
more or less conserved form, in a large number of proteins. The EGF-
like domain contains six cysteines which form disulfide bonds within
the domain (C1-C3, C2-C4, C5-C6)</description>
    </keyword>
    <keyword id="KW-0248">
        <name>Ehlers-Danlos syndrome</name>
        <name>EDS</name>
        <description>Protein which, if defective, causes Ehlers-Danlos syndrome (EDS), a
genetically and phenotypically heterogeneous group of connective-
tissue disorders. It affects primarily the skin, ligaments, joints,
and blood vessels. Typical features include skin hyperextensibility,
joint hypermobility, easy bruisability, friability of tissues with
bleeding and poor wound healing. Inheritance can be autosomal
dominant, autosomal recessive, or X-linked recessive</description>
    </keyword>
    <keyword id="KW-0249">
        <name>Electron transport</name>
        <description>Protein involved in the transport of electrons, a process by which
electrons are transported through a series of reactions from the
reductant, or electron donor, to the oxidant, or electron acceptor,
with concomitant energy conversion. Necessary for both photosynthesis
and aerobic respiration</description>
    </keyword>
    <keyword id="KW-0250">
        <name>Elliptocytosis</name>
        <description>Protein which, if defective, causes elliptocytosis, a disorder
characterized by variable haemolytic anaemia and elliptical red blood
cell shape. Caused by deficiency/dysfunction of red blood cell
membrane proteins</description>
    </keyword>
    <keyword id="KW-0251">
        <name>Elongation factor</name>
        <name>Translation elongation factor activity</name>
        <description>Protein that associates with ribosomes cyclically during the
elongation phase of protein synthesis, and catalyze formation of the
acyl bond between the incoming amino-acid residue and the peptide
chain</description>
        <go id="GO:0003746"/>
        <go id="GO:0006414"/>
    </keyword>
    <keyword id="KW-1067">
        <name>Emery-Dreifuss muscular dystrophy</name>
        <name>Scapuloperoneal muscular dystrophy</name>
        <description>Protein which, if defective, causes Emery-Dreifuss muscular dystrophy,
a heterogenous group of inherited muscular dystrophy without the
involvement of nervous system. The disease is characterized by slowly
progressive muscle weakness, contracture of the elbows, Achilles
tendon and posterior cervical muscles, and cardiac features</description>
    </keyword>
    <keyword id="KW-1284">
        <name>Encapsulin nanocompartment</name>
        <description>Protein located in or on an encapsulin nanocompartment, proteinaceous
shells that encapsulate enzymes. The selectively permeable, self-
assembling 25-42 nm shell is made of only 1 protein, unlike the larger
bacterial microcompartment. The shell protein has an HK97-like fold
and probably evolved from a viral protein. Artificial encapsulin
nanocompartments can be expressed and filled with cargo proteins for
biotechnological uses. They are found in many bacterial and a few
archaeal phyla</description>
    </keyword>
    <keyword id="KW-0254">
        <name>Endocytosis</name>
        <description>Protein involved in endocytosis, a process by which extracellular
materials are taken up into a cell by invagination of the plasma
membrane to form vesicles enclosing these materials</description>
        <go id="GO:0006897"/>
    </keyword>
    <keyword id="KW-0255">
        <name>Endonuclease</name>
        <description>Phosphodiesterase capable of cleaving at phosphodiester internal bonds
within a DNA or RNA substrate</description>
        <go id="GO:0004519"/>
    </keyword>
    <keyword id="KW-0256">
        <name>Endoplasmic reticulum</name>
        <description>Protein whose subcellular location is the endoplasmic reticulum, a
membrane system continuous with the outer nuclear membrane. It
consists of flattened, single-membrane vesicles whose inner
compartments, the cisternae, interconnect to form channels throughout
the cytoplasm. The rough-surface portion is studded with ribosomes</description>
    </keyword>
    <keyword id="KW-0257">
        <name>Endorphin</name>
        <description>Morphine-like peptides produced by the brain in response to
neurotransmitters. They bind to neuron receptors that mediate the
action of opiates and induce analgesia and sedation</description>
        <go id="GO:0007218"/>
    </keyword>
    <keyword id="KW-0967">
        <name>Endosome</name>
        <description>Protein found in or associated with endosomes. Endosomes are highly
dynamic membrane systems involved in transport within the cell, they
receive endocytosed cell membrane molecules and sort them for either
degradation or recycling back to the cell surface. They also receive
newly synthesised proteins destined for vacuolar/lysosomal
compartments. In certain cell types, endosomal multivesicular bodies
may fuse with the cell surface in an exocytic manner. These released
vesicles are called exosomes</description>
    </keyword>
    <keyword id="KW-0259">
        <name>Enterobactin biosynthesis</name>
        <name>Enterobactin synthesis</name>
        <name>Enterochelin synthesis</name>
        <name>Enterobactin formation</name>
        <name>Enterochelin biosynthetic process</name>
        <name>Enterochelin biosynthesis</name>
        <name>Enterobactin anabolism</name>
        <name>Enterochelin formation</name>
        <name>Enterochelin anabolism</name>
        <name>Enterobactin biosynthetic process</name>
        <description>Protein involved in the synthesis of enterobactin, a compound that
transports iron from the bacterial environment into the cell
cytoplasm</description>
        <go id="GO:0009239"/>
    </keyword>
    <keyword id="KW-0260">
        <name>Enterotoxin</name>
        <description>Toxin which, either when ingested or when produced by enterobacteria
within the intestine, acts on the intestinal mucosa and induces
diarrhea by perturbing ion and water transport systems</description>
    </keyword>
    <keyword id="KW-0263">
        <name>Epidermolysis bullosa</name>
        <description>Protein which, if defective, causes epidermolysis bullosa, any of a
group of mechano-bullous disorders characterized by blistering and/or
erosion of the skin and mucous membranes which occur spontaneously or
as a result of mild physical trauma. Traditionally, epidermolysis
bullosa is divided into three broad categories based on the level of
tissue separation: in epidermolysis bullosa simplex (EBS), tissue
separation is intraepidermal and occurs within the basal keratinocytes
at the bottom layer of epidermis; the junctional forms (JEB) display
tissue separation within the dermo-epidermal basement membrane
(basement membrane zone, BMZ), primarily within the lamina lucida; in
the dystrophic forms (DEB), tissue separation occurs below the lamina
densa within the upper papillary dermis. Some forms of epidermolysis
bullosa display tissue separation at the basal cell/lamina lucida
interface, at the level of the hemidesmosomes (hemidesmosomal
variants). The hemidesmosomal variants overlap with the traditional
subtypes, particularly the simplex and junctional forms. In addition
to skin involvement, various extracutaneous manifestations can be
associated with distinct subtypes of epidermolysis bullosa</description>
    </keyword>
    <keyword id="KW-0887">
        <name>Epilepsy</name>
        <description>Protein which, if defective, causes epilepsy, any of a group of
disorders characterized by paroxysmal transient disturbances of the
electrical activity of the brain that may be manifested as episodic
impairment or loss of consciousness, abnormal motor phenomena, psychic
or sensory disturbances, or perturbation of the autonomic nervous
system. Epilepsy is classified as either symptomatic or idiopathic
according to whether the cause is known or unknown. Both of these
types can be classified into partial and generalized epilepsy,
depending on whether the seizures are due to limited or to widespread
brain lesions, respectively</description>
    </keyword>
    <keyword id="KW-0931">
        <name>ER-Golgi transport</name>
        <name>ER to Golgi transport</name>
        <name>ER/Golgi transport</name>
        <name>Golgi-to-ER transport</name>
        <description>Protein involved in the 'ER-to-Golgi' transport, a bidirectional
membrane traffic between the endoplasmic reticulum and the Golgi
apparatus which mediates the transfer of cargo molecules by means of
small vesicles or tubular-saccular extensions</description>
        <go id="GO:0016192"/>
    </keyword>
    <keyword id="KW-0895">
        <name>ERV</name>
        <name>Endogenous retrovirus</name>
        <name>Fossil virus</name>
        <description>Protein encoded by proviral genes of endogenous retroviruses. When a
retrovirus infects a host cell, viral reverse transcriptase (RT) makes
a DNA copy of the RNA viral genome. The integrated DNA form of a
retrovirus is referred to as a provirus. Proviral genes are expressed
by cellular mechanisms. Retroviruses that enter the germline are
referred to as endogenous retroviruses (ERVs) to distinguish them from
horizontally transmitted, not passed on to host progeny, "exogenous"
retroviruses. Amplification of ERV copy number via retrotransposition
or reinfection has given rise to numerous ERV sequences in the
vertebrate genomes. As much as 8% of the human genome, and 10% of the
mouse genome, consists of sequences derived from ERV insertions</description>
    </keyword>
    <keyword id="KW-0265">
        <name>Erythrocyte maturation</name>
        <name>RBC maturation</name>
        <name>Red blood cell maturation</name>
        <name>Red blood corpuscle maturation</name>
        <description>Protein involved in the maturation of erythrocytes, the predominant
type of cells present in vertebrate blood and which contain the gas-
transporting protein, hemoglobin</description>
        <go id="GO:0043249"/>
    </keyword>
    <keyword id="KW-0266">
        <name>Ethylene biosynthesis</name>
        <name>Ethylene biosynthetic process</name>
        <name>Ethylene synthesis</name>
        <name>Ethylene formation</name>
        <name>Ethylene anabolism</name>
        <description>Protein involved in the synthesis of ethylene (C2H4), an unsaturated
hydrocarbon gas mainly produced in plants. It has developmental
effects as a hormone, including growth inhibition, regulation of fruit
development, leaf abscission and aging</description>
        <go id="GO:0009693"/>
    </keyword>
    <keyword id="KW-0936">
        <name>Ethylene signaling pathway</name>
        <name>Ethylene mediated signaling pathway</name>
        <description>Protein involved in the ethylene signaling pathway (e.g. transport and
signal transduction) that regulates many aspects of plant growth and
development (e.g. seed germination, root and shoot growth, flower
development, plant defense, senescence, abscission and ripening). This
phytohormone can be synthesized from methionin</description>
        <go id="GO:0009873"/>
    </keyword>
    <keyword id="KW-1262">
        <name>Eukaryotic host gene expression shutoff by virus</name>
        <description>Viral protein which prevents host gene expression by blocking host
transcription, mRNA export or translation. This gives viral
transcripts a competitive edge to use the hijacked translation
machinery. Preventing the expression of host proteins is also a
strategy to counteract the antiviral response</description>
    </keyword>
    <keyword id="KW-1191">
        <name>Eukaryotic host transcription shutoff by virus</name>
        <description>Viral protein involved in inhibiting host transcription to ensure the
shutoff of cellular proteins expression and give virus transcripts a
competitive edge for access to the cellular translation machinery
Preventing the expression of host proteins is also a strategy to
counteract the antiviral response. Inhibition of transcription can be
performed by interfering with host RNA pol-II function or interfering
with general transcription factors</description>
        <go id="GO:0039653"/>
    </keyword>
    <keyword id="KW-1193">
        <name>Eukaryotic host translation shutoff by virus</name>
        <description>Viral protein involved in inhibiting the host translational machinery
to shutoff cellular gene expression. This gives virus transcripts a
competitive edge to use the hijacked translation machinery. Preventing
the expression of host proteins is also a strategy to counteract the
antiviral response. Several virus are known to inhibit host
translation mostly by inactivating translation factors</description>
        <go id="GO:0039604"/>
    </keyword>
    <keyword id="KW-1259">
        <name>Evasion of bacteria-mediated translation shutoff by virus</name>
        <description>Viral protein that counteracts the translation shutoff set up by the
bacterial host in order to inhibit viral replication. This antiviral
defense system alters a crucial cellular process thereby blocking
virus multiplication and ending up with host dormancy or even cell
death. For example, some E.coli strains infected by bacteriophage T4
activate an anticodon nuclease which causes depletion of tRNA(Lys)
and, consequently, abolishes T4 protein synthesis and causes cell
death. However, this effect is counteracted by the repair of tRNA(Lys)
in consecutive reactions catalyzed by the viral enzymes polynucleotide
kinase and RNA ligase. The ToxIN system functions as a toxin-antitoxin
(TA) tandem which is used as a antiviral defense mechanism</description>
    </keyword>
    <keyword id="KW-1125">
        <name>Evasion of host immunity by viral interleukin-like protein</name>
        <description>Viral protein sharing sequence homology with host interleukins
Interleukins are produced by immune system cells such as lymphocytes,
macrophages and monocytes, and modulate inflammation and immunity by
regulating growth, mobility and differentiation of lymphoid and other
cells. Several viruses encode interleukin-like proteins playing a role
in immune evasion. Additionally, viral interleukins have been shown to
activate cellular signaling cascades that enhance virus replication</description>
        <go id="GO:0019049"/>
    </keyword>
    <keyword id="KW-0267">
        <name>Excision nuclease</name>
        <description>Enzyme which excises abnormal or mismatched nucleotides from a DNA
strand</description>
        <go id="GO:0004518"/>
    </keyword>
    <keyword id="KW-0268">
        <name>Exocytosis</name>
        <name>Vesicle exocytosis</name>
        <description>Protein involved in exocytosis, a process by which a material is
transported out of a cell using a vesicle that first engulfs the
material and then is extruded through an opening in the cell membrane
The exocyst protein complex plays an important role in exocytosis by
directing exocytic vesicles to their precise sites of fusion in the
plasma membrane</description>
        <go id="GO:0006887"/>
    </keyword>
    <keyword id="KW-0269">
        <name>Exonuclease</name>
        <description>Enzyme that degrades DNA or RNA by progressively splitting off single
nucleotides from one end of the chain</description>
        <go id="GO:0004527"/>
    </keyword>
    <keyword id="KW-0270">
        <name>Exopolysaccharide synthesis</name>
        <name>EPS synthesis</name>
        <name>EPS biosynthesis</name>
        <name>Exopolysaccharide biosynthetic process</name>
        <name>Exopolysaccharide formation</name>
        <name>Exopolysaccharide anabolism</name>
        <name>EPS formation</name>
        <name>EPS biosynthetic process</name>
        <name>Exopolysaccharide biosynthesis</name>
        <name>EPS anabolism</name>
        <description>Protein involved in the synthesis of exopolysaccharide (EPS), a high
molecular-weight polymer composed of saccharide subunits. An example
is succinoglycan (EPS I) of Rhizobium meliloti, that is important for
invasion of the nodules that it elicits on its host, Medicago sativa</description>
        <go id="GO:0000271"/>
    </keyword>
    <keyword id="KW-0271">
        <name>Exosome</name>
        <description>Protein which is a component of the exosome, a complex of proteins
that includes 3-&gt;5 exoribonucleases and that plays a major role in
diverse RNA processing and degradation pathways in eukaryotes and
archaea</description>
        <go id="GO:0000178"/>
    </keyword>
    <keyword id="KW-0952">
        <name>Extinct organism protein</name>
        <description>Protein originating from a species thought to be extinct, i.e. from a
species for which no known surviving specimens are known to exist. Eg
Dodo, Mammoth or Neanderthal</description>
    </keyword>
    <keyword id="KW-0272">
        <name>Extracellular matrix</name>
        <description>Protein found in the extracellular matrix. The extracellular matrix
consists of any material produced by cells and secreted into the
surrounding medium, but this term generally applies to the non-
cellular components of animal tissues. The extracellular matrix forms
a supportive meshwork around cells and is largely composed of
collagen, laminin, fibronectin and glycosaminoglycans. It can
influence the properties of the cells that it supports. In certain
tissues, specific modifications to the extracellular matrix occur. For
instance, the matrix of bone is mineralized to resist compression</description>
        <go id="GO:0031012"/>
    </keyword>
    <keyword id="KW-0273">
        <name>Eye lens protein</name>
        <description>Protein found in the lens, a transparent body at the front of the
vertebrate eye</description>
        <go id="GO:0005212"/>
    </keyword>
    <keyword id="KW-0274">
        <name>FAD</name>
        <name>Flavin adenine dinucleotide</name>
        <description>Protein involved in flavin adenine dinucleotide synthesis or protein
which contains at least one FAD as prosthetic group, cofactor
(flavoprotein) or cosubstrate such as many oxidation-reduction
enzymes. FAD is an electron carrier molecule that functions as a
hydrogen acceptor. The generic term "flavin" derives from the Latin
word flavius ("yellow") because of the brilliant yellow color they
exhibit as solids and in neutral aqueous solutions</description>
    </keyword>
    <keyword id="KW-0951">
        <name>Familial hemophagocytic lymphohistiocytosis</name>
        <name>Hemophagocytic lymphohistiocytosis</name>
        <name>HPLH</name>
        <name>FHL</name>
        <description>Protein which, if defective, causes familial hemophagocytic
lymphohistiocytosis. FHL is a genetically heterogeneous, autosomal
recessive disorder characterized by immune dysregulation with
hypercytokinemia and defective natural killer cell function. The
clinical features of the disease include fever, hepatosplenomegaly,
cytopenia, hypertriglyceridemia, hypofibrinogenemia, and neurological
abnormalities ranging from irritability and hypotonia to seizures,
cranial nerve deficits and ataxia. Hemophagocytosis is a prominent
feature of the disease, and non-malignant infiltration of macrophages
and activated T lymphocytes in lymph nodes, spleen and other organs is
also found</description>
    </keyword>
    <keyword id="KW-0923">
        <name>Fanconi anemia</name>
        <name>Fanconi pancytopenia</name>
        <description>Protein which, if defective, causes Fanconi anemia. Fanconi anemia is
a rare recessive disorder characterized by progressive pancytopenia,
hypoplasia of the bone marrow and patchy brown discoloration of the
skin, due to melanin deposition. It is associated with multiple
congenital anomalies of the musculoskeletal and genitourinary systems</description>
    </keyword>
    <keyword id="KW-0275">
        <name>Fatty acid biosynthesis</name>
        <name>Fatty acid formation</name>
        <name>Fatty acid biosynthetic process</name>
        <name>Fatty acid anabolism</name>
        <name>Fatty acid synthesis</name>
        <description>Protein involved in the synthesis of fatty acids, long chain organic
acids of the general formula CH3(CnHx)COOH. They are constituents of
lipids and can be saturated or unsaturated. The esterified forms are
important both as energy storage molecules and structural molecules</description>
        <go id="GO:0006633"/>
    </keyword>
    <keyword id="KW-0276">
        <name>Fatty acid metabolism</name>
        <name>Fatty acid metabolic process</name>
        <description>Protein involved in the biochemical reactions with fatty acids. Fatty
acids are long chain organic acids of the general formula
CH3(CnHx)COOH. They are constituents of lipids and can be saturated or
unsaturated. The esterified forms are important both as energy storage
molecules and structural molecules</description>
        <go id="GO:0006631"/>
    </keyword>
    <keyword id="KW-0278">
        <name>Fertilization</name>
        <description>Protein involved in fertilization, the union of two haploid cells, the
gametes, to form a diploid cell, the zygote</description>
        <go id="GO:0007338"/>
    </keyword>
    <keyword id="KW-1206">
        <name>Fibrinogenolytic toxin</name>
        <description>Toxin involved in fibrinogen degradation leading to a decrease of
plasma fibrinogen concentration. Fibrinogenolytic toxins are mostly
snake venom proteases</description>
    </keyword>
    <keyword id="KW-0280">
        <name>Fibrinolysis</name>
        <description>Protein involved in fibrin degradation leading to the dissolving of
blood clots</description>
        <go id="GO:0042730"/>
    </keyword>
    <keyword id="KW-1205">
        <name>Fibrinolytic toxin</name>
        <description>Toxin involved in fibrin degradation leading to the dissolution of
fibrin clots. Fibrinolytic toxins are mostly snake venom proteases</description>
    </keyword>
    <keyword id="KW-0281">
        <name>Fimbrium</name>
        <name>Pili</name>
        <name>Pilus</name>
        <name>Fimbria</name>
        <description>Protein found in a fimbrium or pilus. A fimbrium or pilus is a hair-
like, non-flagellar, polymeric filamentous appendage that extend from
the bacterial or archaeal cell surface, such as type 1 pili, P-pili,
type IV pili or curli. Pili perform a variety of functions, including
surface adhesion, motility, cell-cell interactions, biofilm formation,
conjugation, DNA uptake, and twitching motility</description>
    </keyword>
    <keyword id="KW-1029">
        <name>Fimbrium biogenesis</name>
        <name>Fimbria biogenesis</name>
        <name>Pili biogenesis</name>
        <name>Pilus biogenesis</name>
        <description>Protein which is involved in the formation, organization or
maintenance of the fimbrium, a long hair-like cell surface appendage
The flagellar apparatus consists of the flagellar filament made of
polymerized flagellin, the hook-like structure near the cell surface
and a system of rings embedded in the cell enveloppe (the basal body
or flagellar motor). The basal body and the hook anchor the whip-like
filament to the cell surface. The flagellum is a rotating structure
whose switches propels the cell through a liquid medium</description>
    </keyword>
    <keyword id="KW-0283">
        <name>Flagellar rotation</name>
        <name>Flagellar motility</name>
        <name>Flagella rotation</name>
        <name>Flagellum motility</name>
        <name>Flagellum rotation</name>
        <name>Flagella motility</name>
        <description>Protein involved in the movement of the flagella</description>
        <go id="GO:0097588"/>
    </keyword>
    <keyword id="KW-0282">
        <name>Flagellum</name>
        <name>Undulipodia</name>
        <name>Motile cilia</name>
        <name>Flagella</name>
        <name>Motile cilium</name>
        <name>Undulipodium</name>
        <description>Protein present in the flagellum, a long whip-like or feathery
structure which propels the cell through a liquid medium. This motile
cilium is produced by unicellular eukaryotes and by the motile male
gametes of many eukaryotic organisms. The flagella commonly have a
characteristic axial '9+2' microtubular array (axoneme) and bends are
generated along the length of the flagellum by restricted sliding of
the nine outer doublets</description>
    </keyword>
    <keyword id="KW-0284">
        <name>Flavonoid biosynthesis</name>
        <name>Flavonoid synthesis</name>
        <name>Flavonoid formation</name>
        <name>Flavonoid anabolism</name>
        <name>Flavonoid biosynthetic process</name>
        <description>Protein involved in the synthesis of flavonoids, polyphenolic
compounds possessing 15 carbon atoms; two benzene rings joined by a
linear three carbon chain, a C6-C3-C6 skeleton. C6 presents a benzene
ring, C3 often is part of of an oxygen-containing ring. Flavonoids are
coloured phenolic pigments originally considered vitamins (Vitamins P,
C2) but not shown to have any nutritional role. They are responsible
for the red/purple colours of many higher plants</description>
        <go id="GO:0009813"/>
    </keyword>
    <keyword id="KW-0285">
        <name>Flavoprotein</name>
        <description>Enzymes which contain one or more flavin nucleotides (FAD or FMN) as
redox cofactors or cosubstrates. Flavoproteins are involved, for
example, in the oxidative degradation of pyruvate, fatty acids and
amino acids, and in the process of electron transport</description>
    </keyword>
    <keyword id="KW-0286">
        <name>Flight</name>
        <name>Flight behavior</name>
        <description>Protein which stimulates or which is involved in flight, the act of
passing through the air by the use of wings</description>
        <go id="GO:0007629"/>
    </keyword>
    <keyword id="KW-0287">
        <name>Flowering</name>
        <name>Flower development</name>
        <description>Protein involved in the transition from vegetative to reproductive
development in plants</description>
        <go id="GO:0009908"/>
    </keyword>
    <keyword id="KW-0288">
        <name>FMN</name>
        <name>Flavin mononucleotide</name>
        <name>Riboflavin 5'-phosphate</name>
        <name>Flavin adenine mononucleotide</name>
        <description>Protein involved in flavin adenine mononucleotide synthesis or protein
which contains at least one FMN as prosthetic group/cofactor
(flavoproteins) or cosubstrate, such as many oxidation-reduction
enzymes. FMN is an electron carrier molecule that functions as a
hydrogen acceptor. The generic term "flavin" derives from the Latin
word flavius ("yellow") because of the brilliant yellow color they
exhibit as solids and in neutral aqueous solutions</description>
    </keyword>
    <keyword id="KW-0289">
        <name>Folate biosynthesis</name>
        <name>Folic acid anabolism</name>
        <name>Folacin synthesis</name>
        <name>Folic acid biosynthetic process</name>
        <name>Folacin biosynthetic process</name>
        <name>Folate biosynthetic process</name>
        <name>Folic acid synthesis</name>
        <name>Folic acid formation</name>
        <name>Pteroylglutamic acid biosynthetic process</name>
        <name>Pteroylglutamic acid anabolism</name>
        <name>Pteroylglutamic acid biosynthesis</name>
        <name>Folic acid biosynthesis</name>
        <name>Folacin formation</name>
        <name>Folacin biosynthesis</name>
        <name>Folate synthesis</name>
        <name>Folate anabolism</name>
        <name>Folate formation</name>
        <name>Pteroylglutamic acid formation</name>
        <name>Pteroylglutamic acid synthesis</name>
        <name>Folacin anabolism</name>
        <description>Protein involved in the synthesis of folate, the ionic form of folic
acid (Latin folium, 'leaf'), first found in spinach leaves. Folate is
converted in a two-step reduction into its coenzyme form
tetrahydrofolate, often abbreviated FH4 or THF, which acts as a
carrier of one-carbon units at several oxidation levels in a variety
of biosyntheses</description>
        <go id="GO:0046656"/>
    </keyword>
    <keyword id="KW-0290">
        <name>Folate-binding</name>
        <name>Pteroylglutamic acid-binding</name>
        <name>Folacin-binding</name>
        <name>Folic acid-binding</name>
        <description>Protein that binds folate, the ionic form of folic acid</description>
        <go id="GO:0005542"/>
    </keyword>
    <keyword id="KW-0291">
        <name>Formylation</name>
        <name>N-Formylated</name>
        <description>A protein in which either the N-terminal N-formylmethionine has not
been processed by the methionyl-tRNA formyltransferase or which is
posttranslationally modified by the attachment of at least one formyl
group</description>
    </keyword>
    <keyword id="KW-0292">
        <name>Fruit ripening</name>
        <description>Protein involved in fruit ripening. The fruit is the matured ovary of
a plant, enclosing the seed(s). The plant hormone ethylene stimulates
fruit ripening</description>
        <go id="GO:0009835"/>
    </keyword>
    <keyword id="KW-0293">
        <name>Fruiting body</name>
        <description>Protein involved in fruiting body formation or expressed in fruiting
bodies, any specialized reproductive structure that produces spores or
gametes in fungi, slime molds, algae, etc. Fruiting bodies are
distinct in size, shape and coloration for each species</description>
    </keyword>
    <keyword id="KW-0294">
        <name>Fucose metabolism</name>
        <name>Fucose metabolic process</name>
        <description>Protein involved in the biochemical reactions with fucose. L-fucose
(6-deoxy-L-galactose) is present in some algae and identified in the
chains of glycoproteins; it is the only polysaccharides of certain
bacterias</description>
        <go id="GO:0006004"/>
    </keyword>
    <keyword id="KW-0295">
        <name>Fungicide</name>
        <name>Anti-fungal</name>
        <description>Protein capable of killing or inhibiting growth of fungi</description>
        <go id="GO:0031640"/>
        <go id="GO:0050832"/>
    </keyword>
    <keyword id="KW-1169">
        <name>Fusion of virus membrane with host cell membrane</name>
        <name>Viral entry into host cell via plasma membrane fusion</name>
        <description>Viral protein involved in the merging of the virus envelope with host
cytoplasmic membrane during viral penetration into host cell. Virus
fusion proteins drive this fusion reaction by undergoing a major
conformational change that is triggered by interactions with the
target cell. This pathway is used by viruses whose fusion protein is
usually pH independent such as most paramyxoviruses, herpesviruses and
retroviruses. MHV-JHM coronavirus has been shown to fuse directly with
the host cytoplasmic membrane. Prokaryotic viruses such as
Tectiviridae fuse their inner membrane with the host cytoplasmic
membrane whereas Cystoviridae fuse their outer membrane with the host
cytoplasmic membrane</description>
        <go id="GO:0019064"/>
    </keyword>
    <keyword id="KW-1170">
        <name>Fusion of virus membrane with host endosomal membrane</name>
        <name>Viral entry into host cell via plasma membrane fusion</name>
        <description>Viral protein involved in the merging of the virus envelope with host
endosomal membrane during viral penetration into host cell. Viral
fusion proteins drive this fusion reaction by undergoing a major
conformational change that is triggered by interactions with the
target cell. The specific trigger is mainly endosome acidification
which induce activation of the fusion protein by conformational
change. This pathway is used by enveloped viruses which are
endocytosed and whose fusion protein is usually pH-dependent like
influenza A virus, rhabdoviruses, bornaviruses, filoviruses,
asfarviridae, flaviviridae, alphaviruses, HIV-1, avian leukosis virus,
SARS, 229E, and MHV-2 coronaviruses</description>
        <go id="GO:0039654"/>
    </keyword>
    <keyword id="KW-1168">
        <name>Fusion of virus membrane with host membrane</name>
        <name>Viral entry into host cell via membrane fusion</name>
        <description>Viral protein involved in the merging of the virion membrane with a
host membrane during viral penetration into host cell. Viral fusion
proteins drive this fusion reaction by undergoing a major
conformational change that is triggered by interactions with the
target cell. The specific trigger depends on the virus and can be
exposure to low pH in the endocytic pathway or interaction of the
virion with the host receptor(s). In prokaryotic viruses, host-virus
membrane fusion can occur either at the host outer membrane or plasma
membrane. Bacteriophages such as cystoviridae fuse their external
envelope with the host outer membrane, whereas others like
tectiviridae fuse their inner envelope with the host plasma membrane</description>
        <go id="GO:0039663"/>
    </keyword>
    <keyword id="KW-1239">
        <name>Fusion of virus membrane with host outer membrane</name>
        <name>Viral entry into host cell via outer membrane fusion</name>
        <description>Viral protein involved in the merging of the virion external lipidic
membrane (envelope) with the prokaryotic host outer membrane during
viral penetration into host cell. Bacteriophages such as Cystoviridae
for example fuse their membrane with the host outer membrane</description>
        <go id="GO:0098997"/>
    </keyword>
    <keyword id="KW-1214">
        <name>G-protein coupled acetylcholine receptor impairing toxin</name>
        <name>mAChR regulator</name>
        <name>Muscarinic acetylcholine receptor regulator</name>
        <description>Toxin which interferes with the function of the muscarinic
acetylcholine receptor (mAChR). The mAChR is a specific class of G-
protein coupled receptor (GPCR) that binds acetylcholine. These toxins
are mostly found in snake venoms</description>
    </keyword>
    <keyword id="KW-0297">
        <name>G-protein coupled receptor</name>
        <name>7TM receptor</name>
        <name>GPCR</name>
        <description>Receptors which transduce extracellular signals across the cell
membrane. At the external side they receive a ligand (a photon in case
of opsins), and at the cytosolic side they activate a guanine
nucleotide-binding (G) protein. These receptors are hydrophobic
proteins that cross the membrane seven times</description>
        <go id="GO:0007186"/>
        <go id="GO:0004930"/>
    </keyword>
    <keyword id="KW-1213">
        <name>G-protein coupled receptor impairing toxin</name>
        <name>GPCR regulator</name>
        <description>Toxin which interferes with the function of G-protein coupled
receptors (GPCRs). These toxins are mostly found in snake and scorpion
venoms</description>
    </keyword>
    <keyword id="KW-1077">
        <name>G0/G1 host cell cycle checkpoint dysregulation by virus</name>
        <description>Viral protein involved in the modulation of host cell cycle
progression by dysregulating the G0/G1 transition. Some viruses
benefit from keeping cells in resting state (G0), while others favor
entry through G1 and subsequent cell division to replicate more
efficiently</description>
        <go id="GO:0039646"/>
    </keyword>
    <keyword id="KW-1078">
        <name>G1/S host cell cycle checkpoint dysregulation by virus</name>
        <description>Viral protein involved in the modulation of host cell cycle
progression by dysregulating the G1/S transition. Some viruses benefit
from an arrest in G1 to S phase transition, while others force through
S phase to favor their own replication</description>
        <go id="GO:0039645"/>
    </keyword>
    <keyword id="KW-0298">
        <name>Galactitol metabolism</name>
        <name>Galactitol metabolic process</name>
        <name>Dulcitol metabolism</name>
        <name>Dulcitol metabolic process</name>
        <description>Protein involved in the biochemical reactions with galactitol. This
sugar alcohol is derived from galactose. It can be found in certain
bacteria, yeasts, fungi and plants. In humans, the congenital
galactosemic cataracts are due to an accumulation of galactitol within
the lens</description>
        <go id="GO:0019402"/>
    </keyword>
    <keyword id="KW-0299">
        <name>Galactose metabolism</name>
        <name>Galactose metabolic process</name>
        <description>Protein involved in the biochemical reactions with the monosaccharide
galactose. This optical isomer (epimer) of glucose is a constituent of
various oligosaccharides (e.g. lactose, raffinose), polysaccharides
(e.g. galactans, agar, gum arabic) and also of sphingolipids
(galactocerebrosides)</description>
        <go id="GO:0006012"/>
    </keyword>
    <keyword id="KW-0301">
        <name>Gamma-carboxyglutamic acid</name>
        <name>1-carboxyglutamic acid</name>
        <description>Protein which possesses at least one gamma-carboxyglutamic acid, a
vitamin K dependent post-translational modification of a glutamate
residue found in blood coagulation proteins and in the proteins of
calcified tissues. Gamma-carboxyglutamyl residues are good chelators
of calcium ions. There are two natural forms of vitamin K, which are
phylloquinone (vitamin K1 or phytylmenaquinone) in green vegetables
and menaquinone (vitamin K2 or menaquinone-n, depending of the number
of isoprene units of the side-chain or MK-n) in intestinal bacteria,
as well as one synthetic provitamin form, menadione (vitamin K3). In
infants, the primary symptom of a deficiency of this fat-soluble
vitamin is a hemorrhagic syndrome</description>
    </keyword>
    <keyword id="KW-0331">
        <name>Gangliosidosis</name>
        <description>Protein which, if defective, causes gangliosidosis. Gangliosidosis
defines any of a group of autosomal recessive lysosomal storage
diseases characterized by the accumulation of gangliosides GM1 or GM2
and related glycoconiugates, and by progressive psychomotor
deterioration. Subtypes include GM1-gangliosidoses and GM2-
gangliosidoses</description>
    </keyword>
    <keyword id="KW-0303">
        <name>Gap junction</name>
        <description>Protein component of gap junctions which are specialized regions of
the plasma membrane formed by a cluster of channels allowing small
molecules to diffuse from the cytosol of one cell to that of an
adjacent cell. A current model of the gap junction consists of a
cluster of gap-junction channels. Both membranes contain connexon
hemichannels, composed of a hexamer of an integral membrane protein
which is often referred to as connexin. The junction of two adjacent
connexons forms a gap-junction channel</description>
    </keyword>
    <keyword id="KW-0302">
        <name>Gap protein</name>
        <description>A group of insect proteins which are crucial for the development of
proper embryonic segmentation. These are the first proteins that
define the coarsest subdivisions. Generally, gap gene mutations are
lethal and eliminate a large block of contiguous segments from the
embryo</description>
        <go id="GO:0035282"/>
    </keyword>
    <keyword id="KW-0304">
        <name>Gas vesicle</name>
        <description>Protein of, or involved in synthesis of, gas vesicles. Gas vesicles
(GV) are hollow, watertight, gas-permeable proteinaceous
nanostructures found in some microorganisms. During planktonic growth
they allow positioning of the organism at a favorable depth for light
or nutrient acquisition. By regulating their relative GV content,
aquatic microbes can perform vertical migrations. The GV is
impermeable to liquid water but is highly permeable to gases and is
normally filled with air. As they scatter light, they may also protect
against UV light. Two main proteins are present in the gas vesicle:
GvpA, an extremely hydrophobic protein which makes the ribs that form
the structure, and GvpC, which binds to the outside of the ribs, helps
shape GVs and stiffens the structure against collapse</description>
    </keyword>
    <keyword id="KW-0305">
        <name>Gaseous exchange</name>
        <description>Protein involved in the exchange of gases</description>
        <go id="GO:0007585"/>
    </keyword>
    <keyword id="KW-0306">
        <name>Gastrulation</name>
        <description>Protein involved in gastrulation, a stage in early embryogenesis in
which cell movements result in a massive reorganization of the embryo
from an initially unstructured group of cells, the blastula, into a
multi-layered organism. During gastrulation, the primary germ layers
(endoderm, mesoderm, and ectoderm) are formed and organized in their
proper locations for further development</description>
        <go id="GO:0007369"/>
    </keyword>
    <keyword id="KW-0307">
        <name>Gaucher disease</name>
        <description>Protein which, if defective, causes Gaucher disease, the most
prevalent sphingolipid storage disorder caused by a recessively
inherited deficiency of the enzyme glucocerebrosidase. Most common in
Ashkenazi Jews, it is associated with hepatosplenomegaly (enlargement
of liver and spleen) and, in severe early onset forms of the disease,
with neurological dysfunction</description>
    </keyword>
    <keyword id="KW-0308">
        <name>Genetically modified food</name>
        <description>Any protein used in a biotechnological process that results in the
modification of a naturally occurring food (crop or livestock)
Examples include proteins introduced to enable herbicide or insect
resistance or proteins that act in fruit ripening</description>
    </keyword>
    <keyword id="KW-0309">
        <name>Germination</name>
        <description>Protein involved in germination, the physiological and developmental
changes by a seed, spore, pollen grain (microspore), or zygote that
occur after release from dormancy, and encompassing events prior to
and including the first visible indications of growth</description>
    </keyword>
    <keyword id="KW-0939">
        <name>Gibberellin signaling pathway</name>
        <name>GA signalling pathway</name>
        <name>Gibberellic acid signaling pathway</name>
        <name>GA-signalling pathway</name>
        <description>Protein involved in the gibberellin (GA) signaling pathway (e.g
transport and signal transduction) that regulates many aspects of
plant growth including seed germination, hypocotyl elongation, stem
elongation, leaf expansion, trichome development, pollen maturation
and flower and fruit development. GAs are tetracyclic diterpenoid
phytohormones found in plants, fungi and bacteria. They are named
GA1....GAn in order of discovery. The term "gibberellin" was first
given to a substance, produced by the fungus Gibberella fujikuroi,
which caused overgrowth symptoms in rice. This substance was later
proven to be a mixture of GAs, with GA1 and GA3 being the active
factors</description>
        <go id="GO:0009740"/>
    </keyword>
    <keyword id="KW-0955">
        <name>Glaucoma</name>
        <description>Protein which, if defective, causes glaucoma, a group of eye diseases
characterized by pathological changes in the optic disk, progressive
loss of optic nerve axons and visual field defects. Most of the
patients with glaucoma have an increased intraocular pressure. The
disease is painless and often diagnosed at a late stage, when visual
field defects are severe. Glaucoma is one of the leading causes of
blindness worldwide</description>
    </keyword>
    <keyword id="KW-0311">
        <name>Gluconate utilization</name>
        <description>Protein involved in the biochemical pathway(s) in which gluconate is
the carbon source</description>
        <go id="GO:0019521"/>
    </keyword>
    <keyword id="KW-0312">
        <name>Gluconeogenesis</name>
        <name>Glucose biosynthetic process</name>
        <name>Glucose biosynthesis</name>
        <description>Protein involved in the biosynthesis of "new" glucose from such
noncarbohydrate precursors as pyruvate, lactate, certain amino acids
and intermediates of the tricarboxylic acid cycle</description>
        <go id="GO:0006094"/>
    </keyword>
    <keyword id="KW-0313">
        <name>Glucose metabolism</name>
        <name>Glucose metabolic process</name>
        <description>Protein involved in the biochemical reactions with the 6-carbon aldose
sugar glucose</description>
        <go id="GO:0006006"/>
    </keyword>
    <keyword id="KW-0314">
        <name>Glutamate biosynthesis</name>
        <name>Glutamate formation</name>
        <name>Glutamic acid synthesis</name>
        <name>Glutamate anabolism</name>
        <name>Glutamic acid anabolism</name>
        <name>Glutamic acid biosynthetic process</name>
        <name>Glutamate biosynthetic process</name>
        <name>Glutamic acid formation</name>
        <name>Glutamate synthesis</name>
        <name>Glutamic acid biosynthesis</name>
        <description>Protein involved in the synthesis of the acidic amino acid glutamate
Glutamate is a component of proteins and can also act as a
neurotransmitter in the central nervous system</description>
        <go id="GO:0006537"/>
    </keyword>
    <keyword id="KW-0315">
        <name>Glutamine amidotransferase</name>
        <name>Glutamine metabolic process</name>
        <description>Enzyme that catalyzes the removal of the ammonia group from glutamine
and transfers it to a substrate to form a new carbon-nitrogen group
Glutamine amidotransferase (GATase) domains can occur either as single
polypeptides or as domains in larger multifunctional proteins. There
exist two classes of glutamine amidotransferases domains: I and II</description>
    </keyword>
    <keyword id="KW-0316">
        <name>Glutaricaciduria</name>
        <name>GA</name>
        <name>Glutaric aciduria</name>
        <description>Protein which, if defective, causes glutaricaciduria (GA), a metabolic
disorder characterized by the excretion of glutaric acid in the urine
Type I GA is caused by the deficiency of glutaryl-CoA dehydrogenase, a
mitochondrial enzyme involved in the metabolism of lysine,
hydroxylysine and tryptophan. Type II GA differs from type I in that
multiple acyl-CoA dehydrogenase deficiencies result in a large
excretion not only of glutaric acid but also of lactic, ethylmalonic,
butyric, isobutyric, 2-methyl-butyric, and isovaleric acids. GA II can
result from a deficiency of any one of 3 mitochondrial molecules: the
alpha and beta subunits of electron transfer flavoprotein and electron
transfer flavoprotein-ubiquinone oxidoreductase</description>
    </keyword>
    <keyword id="KW-0317">
        <name>Glutathione biosynthesis</name>
        <name>Glutathione anabolism</name>
        <name>Glutathione biosynthetic process</name>
        <name>Glutathione formation</name>
        <name>Glutathione synthesis</name>
        <description>Protein involved in the synthesis of the tripeptide glutathione
(Gamma-Glu-Cys-Gly). Glutathione sulphydryl group is kept largely in
the reduced state; this allows it to act as a sulphydryl buffer,
reducing any disulphide bonds formed within cytoplasmic proteins to
cysteines. Glutathione is also important as a cofactor for the enzyme
glutathione peroxidase, in the uptake of amino acids and participates
in leucotriene synthesis. Glutathione contains an unusual peptide
linkage between the carboxyl group of the glutamate side chain and the
amine group of cysteine</description>
        <go id="GO:0006750"/>
    </keyword>
    <keyword id="KW-0318">
        <name>Glutathionylation</name>
        <name>Glutathionylated</name>
        <description>Protein which is posttranslationally modified by the attachment of a
glutathione molecule by a disulfide bond</description>
    </keyword>
    <keyword id="KW-0971">
        <name>Glycation</name>
        <name>Glycated</name>
        <description>Protein containing one or more covalently linked glucose residues,
resulting from a non-enzymatic spontaneous reaction. The carbohydrate
is attached to an amino-acid nitrogen atom (e.g. from a lysine side
chain, or the amino-terminal group). This modification is a side
effect of diabetes and aging. Glycation is the first step toward the
formation of advanced glycation endproducts (AGEs). Some AGEs are
benign, but others are implicated in age-related chronic diseases such
as: type II diabetes mellitus, cardiovascular diseases, Alzheimer's
disease, etc</description>
    </keyword>
    <keyword id="KW-0319">
        <name>Glycerol metabolism</name>
        <name>Glycerol metabolic process</name>
        <description>Protein involved in the biochemical reactions with the 3-carbon sugar
alcohol glycerol. Glycerol is primarily of interest as the central
structural component of the major classes of biological lipids,
triglycerides and phosphatidyl phospholipids. It is also an important
intermediate in carbohydrate and lipid metabolism</description>
        <go id="GO:0006071"/>
    </keyword>
    <keyword id="KW-0320">
        <name>Glycogen biosynthesis</name>
        <name>Glycogen formation</name>
        <name>Glycogen anabolism</name>
        <name>Glycogen biosynthetic process</name>
        <name>Glycogen synthesis</name>
        <description>Protein involved in the synthesis of glycogen, a branched polymer of
D-glucose (mostly -(1-4) linked, but with some -(1-6) linked residues
at branch points). Glycogen is the major short term storage polymer of
animal cells and is particularly abundant in liver and to a lesser
extent in muscles</description>
        <go id="GO:0005978"/>
    </keyword>
    <keyword id="KW-0321">
        <name>Glycogen metabolism</name>
        <name>Glycogen metabolic process</name>
        <description>Protein involved in the biochemical reactions with glycogen, a
branched polymer of D-glucose (mostly -(1-4) linked, but with some
- (1-6) linked residues at branch points). Glycogen is the major short
term storage polymer of animal cells and is particularly abundant in
liver and to a lesser extent in muscles</description>
        <go id="GO:0005977"/>
    </keyword>
    <keyword id="KW-0322">
        <name>Glycogen storage disease</name>
        <description>Protein which, if defective, causes glycogen storage disease, a group
of inherited metabolic disorders involving the enzymes responsible for
the synthesis and degradation of glycogen. At least thirteen types of
this disease have been described</description>
    </keyword>
    <keyword id="KW-0323">
        <name>Glycolate pathway</name>
        <name>Photorespiration pathway</name>
        <name>Oxidative photosynthetic carbon pathway</name>
        <name>Photosynthetic carbon oxydation cycle</name>
        <name>C2 cycle</name>
        <description>Protein involved in the glycolate pathway, synthesis of the amino
acids serine and glycine from glycolate via a glyoxylate intermediate</description>
        <go id="GO:0009854"/>
    </keyword>
    <keyword id="KW-0324">
        <name>Glycolysis</name>
        <description>Protein involved in the anaerobic enzymatic conversion of glucose to
lactate or pyruvate, resulting in energy stored in the form of
adenosine triphosphate (ATP), as occurs in skeletal muscle and in
embryonic tissue</description>
        <go id="GO:0006096"/>
    </keyword>
    <keyword id="KW-0325">
        <name>Glycoprotein</name>
        <name>Glycosylated</name>
        <description>Protein containing one or more covalently linked carbohydrates of
various types, i.e. from monosaccharides to branched polysaccharides,
including glycosylphosphatidylinositol (GPI), glycosaminoglycans
(GAG)</description>
    </keyword>
    <keyword id="KW-0326">
        <name>Glycosidase</name>
        <description>Hydrolases which attack glycosidic bonds in carbohydrates,
glycoproteins and glycolipids. The glycosidases are not highly
specific. Usually they distinguish only the type of bond, e.g. O- or
N-glycosidic, and its configuration (alpha or beta)</description>
        <go id="GO:0008152"/>
        <go id="GO:0016798"/>
    </keyword>
    <keyword id="KW-0327">
        <name>Glycosome</name>
        <description>Protein present in the glycosome, a microbody-like organelle found in
all members of the protist order Kinetoplastida examined. Nine enzymes
involved in glucose and glycerol metabolism are associated with these
organelles. These enzymes are involved in pathways which, in other
organisms, are usually located in the cytosol</description>
    </keyword>
    <keyword id="KW-0328">
        <name>Glycosyltransferase</name>
        <description>Enzymes that catalyze the transfer of glycosyl (sugar) residues to an
acceptor, both during degradation (cosubstrates= water or inorganic
phosphate) and during biosynthesis of polysaccharides, glycoproteins
and glycolipids. In biosynthetic glycosyl transfers, the common
activated monomeric sugar intermediate is a nucleoside diphosphate
sugar</description>
        <go id="GO:0016757"/>
    </keyword>
    <keyword id="KW-0329">
        <name>Glyoxylate bypass</name>
        <name>Glyoxylate cycle</name>
        <description>Protein involved in the glyoxylate bypass, an alternate route in
bacteria, plants, and fungi which bypasses the CO2-evolving steps of
the tricarboxylic acid cycle, thus permiting the utilization of fatty
acids or acetate, in the form of acetyl-CoA, as sole carbon source,
particularly for the net biosynthesis of carbohydrate from fatty
acids. The glyoxylate bypass is especially prominent in plant seeds</description>
        <go id="GO:0006097"/>
    </keyword>
    <keyword id="KW-0330">
        <name>Glyoxysome</name>
        <description>Protein present in the glyoxysome, a membrane-surrounded plant cell
organelle, especially found in germinating seeds, and involved in the
breakdown and conversion of fatty acids to acetyl-CoA for the
glyoxylate bypass. Since it is also rich in catalase, the glyoxysome
may be related to the microbodies or peroxisomes or derived from them</description>
    </keyword>
    <keyword id="KW-0332">
        <name>GMP biosynthesis</name>
        <name>Guanylic acid anabolism</name>
        <name>Guanylic acid formation</name>
        <name>GMP anabolism</name>
        <name>Guanosine 5'-monophosphate biosynthetic process</name>
        <name>Guanylic acid synthesis</name>
        <name>Guanosine 5'-monophosphate synthesis</name>
        <name>Guanylic acid biosynthetic process</name>
        <name>GMP formation</name>
        <name>GMP biosynthetic process</name>
        <name>GMP synthesis</name>
        <name>Guanosine 5'-monophosphate anabolism</name>
        <name>Guanosine 5'-monophosphate formation</name>
        <description>Protein involved in the synthesis of GMP. GMP is the abbreviation for
the nucleotide guanosine 5'-monophosphate</description>
        <go id="GO:0006177"/>
    </keyword>
    <keyword id="KW-0333">
        <name>Golgi apparatus</name>
        <name>Golgi complex</name>
        <name>Golgi stack</name>
        <description>Protein found in the Golgi apparatus, an organelle present in
eukaryotic cells that appears as a stack of 6-8 plate-like membranous
compartments and associated vesicles and vacuoles, often located near
the centrosome. It has four functionally distinct compartments: cis,
medial and trans Golgi stacks, and the trans Golgi network (TGN). The
first three are involved in posttranslational modifications of
proteins (e.g., N- or O-glycosylation, sulfation, processing of acid
hydrolases), while the TGN is involved in sorting the proteins to
their final destination (e.g., to lysosomes, to secretory vesicles, or
to plasma membrane)</description>
    </keyword>
    <keyword id="KW-0334">
        <name>Gonadal differentiation</name>
        <description>Protein involved in gonadal differentiation, the progressive
restriction of the developmental potential and increasing
specialization of function which takes place during the embryonic
development and leads to the formation of gamete-producing glands,
such as ovary or testis</description>
        <go id="GO:0007506"/>
    </keyword>
    <keyword id="KW-0335">
        <name>Gout</name>
        <description>Protein which, if defective, causes gout, a recurrent acute arthritis
of peripheral joints caused by the precipitation of monosodium urate
crystals in articular cartilage. Gout is usually due to overproduction
of uric acid secondary to an inherited abnormality of purine
metabolism, but may be a result of urate under-excretion</description>
    </keyword>
    <keyword id="KW-0336">
        <name>GPI-anchor</name>
        <name>Glycosylsphingolipidinositol anchor</name>
        <name>Glycosylphosphatidylinositol anchor</name>
        <description>Protein bound to the lipid bilayer of a membrane through either a GPI-
anchor (glycosylphosphatidylinositol anchor), a complex oligoglycan
linked to a phosphatidylinositol group, or a GPI-like-anchor, a
similar complex oligoglycan linked to a sphingolipidinositol group,
resulting in the attachment of the C-terminus of the protein to the
membrane</description>
        <go id="GO:0098552"/>
    </keyword>
    <keyword id="KW-0337">
        <name>GPI-anchor biosynthesis</name>
        <name>GPI-anchor biosynthetic process</name>
        <name>GPI-anchor synthesis</name>
        <name>Glycosylphosphatidylinositol anchor formation</name>
        <name>Glycosylphosphatidylinositol anchor anabolism</name>
        <name>Glycosylphosphatidylinositol anchor biosynthesis</name>
        <name>Glycosylphosphatidylinositol anchor biosynthetic process</name>
        <name>GPI-anchor formation</name>
        <name>Glycosylphosphatidylinositol anchor synthesis</name>
        <name>GPI-anchor anabolism</name>
        <description>Protein involved in the synthesis or the attachment to a protein of a
GPI-anchor (glycosylphosphatidylinositol anchor) or a GPI-like-anchor
(glycosylsphingolipidinositol anchor), both of which have complex
oligoglycan linked to a phospholipidinositol molecule that serves to
attach the C-terminus of some extracellular membrane proteins to the
lipid bilayer of a membrane. The core glycolipid is composed of a
tetraglycan: three mannose units and one glucosamine linked to a
phospholipidinositol. The terminal mannose is linked to the protein
via an ethanolamine attached to the C-terminal of the mature protein
The core structure is conserved from protozoa to humans. There are,
however, marked differences in the glycosyl side chains attached to
the core glycolipid. The phospholipid component may be either a
phosphatide (two long chain fatty acids attached by ester linkage to
glycerol phosphate) or a sphingolipid (a long chain fatty acid
attached by amide linkage to a ceramide phosphate). Some yeast and
Dictyosteliida synthesize the GPI-like anchor de novo, whereas other
organisms may interconvert the lipid components by a "resculpting"
process after the anchor is attached to the protein</description>
        <go id="GO:0006506"/>
    </keyword>
    <keyword id="KW-0338">
        <name>Growth arrest</name>
        <name>Cell cycle arrest</name>
        <name>Cellular quiescence</name>
        <description>Protein involved in growth arrest, a phenomenon occurring when a cell
does not proceed through the cell cycle</description>
        <go id="GO:0051726"/>
    </keyword>
    <keyword id="KW-0339">
        <name>Growth factor</name>
        <description>Protein which, by binding to a cell-surface receptor, triggers an
intracellular signal-transduction pathway leading to differentiation,
proliferation, or other cellular response</description>
        <go id="GO:0008083"/>
    </keyword>
    <keyword id="KW-0340">
        <name>Growth factor binding</name>
        <description>Protein other than a receptor that binds to a cell's growth factor</description>
        <go id="GO:0019838"/>
    </keyword>
    <keyword id="KW-0341">
        <name>Growth regulation</name>
        <name>Regulation of cell growth</name>
        <description>Protein involved in growth regulation, which usually implies the
control of the rate of division rather than that of the size of an
individual cell</description>
    </keyword>
    <keyword id="KW-0342">
        <name>GTP-binding</name>
        <name>Guanosine triphosphate-binding</name>
        <name>Guanosine 5'-triphosphate-binding</name>
        <description>Protein which binds guanosine 5'-triphosphate (GTP), a ribonucleotide
guanosine (a purine base guanine linked to the sugar D-ribofuranose)
that carries three phosphate groups esterified to the sugar moiety</description>
        <go id="GO:0005525"/>
    </keyword>
    <keyword id="KW-0343">
        <name>GTPase activation</name>
        <description>GTPase-activating protein (GAP) by itself does not hydrolyze GTP but,
by binding to a GTPase, accelerates its intrinsic GTPase activity</description>
        <go id="GO:0005096"/>
    </keyword>
    <keyword id="KW-0344">
        <name>Guanine-nucleotide releasing factor</name>
        <description>Protein which catalyzes the release of GDP (guanosine 5'-diphosphate)</description>
        <go id="GO:0005085"/>
    </keyword>
    <keyword id="KW-0345">
        <name>HDL</name>
        <description>Protein or apolipoprotein associated with High-Density Lipoproteins
(HDL), a class of proteins involved in lipid (cholesterol,
phospholipids and triacylglycerol) metabolism in the body fluids. HDL
are formed in the liver and are involved in reverse cholesterol
transport, the transport of cholesterol from peripherical tissues to
the liver. Apolipoproteins are proteins which are specifically
associated with lipoproteins, which is not the case for all the
proteins associated with HDL or with the other lipoprotein classes</description>
        <go id="GO:0034364"/>
    </keyword>
    <keyword id="KW-1009">
        <name>Hearing</name>
        <description>Protein involved in hearing, the special sense by which an organism is
able to receive an auditory stimulus, convert it to a molecular
signal, and recognize and characterize the signal. Sonic stimuli are
detected in the form of vibrations and are processed to form a sound</description>
        <go id="GO:0007605"/>
    </keyword>
    <keyword id="KW-1139">
        <name>Helical capsid protein</name>
        <description>Viral protein that forms a helical capsid to protect the viral genome
Viral helical capsids are about 7-30 nm in diameter and 200-2000 nm
long</description>
        <go id="GO:0019029"/>
    </keyword>
    <keyword id="KW-0347">
        <name>Helicase</name>
        <description>Protein with an helicase activity. Helicases are ATPases that catalyze
the unwinding of double-stranded nucleic acids. They are tightly
integrated (or coupled) components of various macromolecular complexes
which are involved in processes such as DNA replication,
recombination, and nucleotide excision repair, as well as RNA
transcription and splicing</description>
        <go id="GO:0004386"/>
    </keyword>
    <keyword id="KW-0348">
        <name>Hemagglutinin</name>
        <description>Protein which causes agglutination of erythrocytes or other cell
types: In viruses, a protein which is responsible for attaching the
virus to cell receptors and for initiating infection</description>
    </keyword>
    <keyword id="KW-0349">
        <name>Heme</name>
        <name>Haeme</name>
        <description>Protein containing at least one heme, an iron atom coordinated to a
protoporphyrin IX. In myoglobin and hemoglobin, one of the
coordination positions of iron is occupied by oxygen or other ligands,
such as carbon monoxide. Hemes are also found in cytochromes of the
electron-transport chain where they bind electrons, in reducing
peroxides (catalases and peroxidases), and act as terminal components
in multienzyme systems involved in hydroxylation. Cytochrome c is the
only common heme protein in which the heme is covalently bound</description>
    </keyword>
    <keyword id="KW-0350">
        <name>Heme biosynthesis</name>
        <name>Haeme biosynthesis</name>
        <name>Haeme formation</name>
        <name>Haeme synthesis</name>
        <name>Heme synthesis</name>
        <name>Haeme biosynthetic process</name>
        <name>Heme biosynthetic process</name>
        <name>Haeme anabolism</name>
        <name>Heme anabolism</name>
        <name>Heme formation</name>
        <description>Protein involved in the synthesis of heme, an iron atom coordinated to
a protoporphyrin IX</description>
        <go id="GO:0006783"/>
    </keyword>
    <keyword id="KW-0351">
        <name>Hemoglobin-binding</name>
        <name>Haemoglobin-binding</name>
        <description>Protein which binds hemoglobin, a gas-carrying protein found in red
blood cells</description>
        <go id="GO:0030492"/>
    </keyword>
    <keyword id="KW-0353">
        <name>Hemolymph clotting</name>
        <name>Haemolymph clotting</name>
        <name>Hemolymph coagulation</name>
        <description>Protein involved in the coagulation of hemolymph, the circulatory
fluid of invertebrate animals which is functionally comparable to the
blood and lymph of vertebrates</description>
        <go id="GO:0042381"/>
    </keyword>
    <keyword id="KW-0354">
        <name>Hemolysis</name>
        <name>Haemolysis</name>
        <description>Protein involved in hemolysis, the disruption of the integrity of the
red cell membrane, thus causing the release of hemoglobin</description>
        <go id="GO:0031640"/>
    </keyword>
    <keyword id="KW-1068">
        <name>Hemolytic uremic syndrome</name>
        <name>HUS</name>
        <name>Hemolytic-uremic syndrome</name>
        <description>Protein which, if defective, causes hemolytic uremic syndrome, a
disorder characterized by non-immune hemolytic anemia,
thrombocytopenia and renal failure. The vast majority of cases are
sporadic, occur in young children and are associated with epidemics of
diarrhea due to bacterial infections. This typical form of the disease
has a good prognosis and death rate is very low. In contrast to
typical hemolytic uremic syndrome, atypical forms present without a
prodrome of enterocolitis and diarrhea and have a poor prognosis, with
frequent development of end-stage renal disease or death</description>
    </keyword>
    <keyword id="KW-0355">
        <name>Hemophilia</name>
        <name>Haemophilia</name>
        <description>Protein which, if defective, causes hemophilia, a genetic disease
characterized by uncontrollable bleeding due to a sex-linked recessive
deficiency of blood-clotting factor (usually of Factor VIII)</description>
    </keyword>
    <keyword id="KW-1200">
        <name>Hemorrhagic toxin</name>
        <name>Hemorrhagin</name>
        <description>Toxin which induces the leakage of blood components into tissues by
damaging endothelial cells or disturbing endothelial cell interactions
with the basement membrane. Hemorrhagic toxins are mostly found in
snake venoms</description>
    </keyword>
    <keyword id="KW-0356">
        <name>Hemostasis</name>
        <description>Protein involved in the arrest of bleeding through blood clotting and
contraction of blood vessels</description>
        <go id="GO:0007599"/>
    </keyword>
    <keyword id="KW-1199">
        <name>Hemostasis impairing toxin</name>
        <description>Toxin which interferes with hemostasis regrouping all mechanisms
implicated in the cessation of blood loss through damaged vessels
Hence, hemostasis impairing toxins not only interfere with platelet
aggregation, the coagulation cascade, fibrinogen depletion, and fibrin
clot degradation (fibrinolysis), but also provoke hemorrhage by
damaging endothelial cells or disturbing their interaction with the
basement membrane. Numerous snake venom families have the capacity to
interfere with hemostasis</description>
    </keyword>
    <keyword id="KW-0357">
        <name>Heparan sulfate</name>
        <description>Protein containing at least one heparan sulfate, a highly sulfated
glycosaminoglycan, closely related to heparin, which consists of
repeating units of disaccharides composed of iduronic acid,
glucosamine and N-acetylglucosamine</description>
    </keyword>
    <keyword id="KW-0358">
        <name>Heparin-binding</name>
        <description>Protein which binds heparin, a highly sulfated glycosaminoglycan which
consists of repeating units of disaccharides composed of D-
glucosamine, D-glucuronic acid or L-iduronic acid. This anticoagulant
is found in the granules of mast cells</description>
        <go id="GO:0008201"/>
    </keyword>
    <keyword id="KW-0359">
        <name>Herbicide resistance</name>
        <name>Resistance to herbicide</name>
        <description>Protein that confers, on plants, bacteria or other microorganisms, the
ability to withstand herbicide action. Herbicides are chemicals that
selectively kill plants. Herbicide resistance occurs usually as a
result of mutation or amplification of a gene, e.g. 3-phosphoshikimate
1-carboxyvinyltransferase</description>
        <go id="GO:0009635"/>
    </keyword>
    <keyword id="KW-0360">
        <name>Hereditary hemolytic anemia</name>
        <name>Hereditary haemolytic anemia</name>
        <description>Protein which, if defective, causes hereditary hemolytic anemia, a
hereditary disease characterized by the premature destruction of red
blood cells</description>
    </keyword>
    <keyword id="KW-0361">
        <name>Hereditary multiple exostoses</name>
        <description>Protein which, if defective, causes hereditary multiple exostoses
(EXT). It is an autosomal dominant disease characterized by the
formation of cartilage-capped benign tumors (exostoses), developing
from the juxtaepiphyseal regions of the long bones and often
accompanied by skeletal deformities and short stature</description>
    </keyword>
    <keyword id="KW-0362">
        <name>Hereditary nonpolyposis colorectal cancer</name>
        <name>HNPCC</name>
        <name>Lynch's syndrome</name>
        <description>Protein which, if defective, causes hereditary non-polyposis
colorectal cancer (HNPCC), also known as Lynch's syndrome. It is an
autosomal dominant syndrome which confers an increased risk for
colorectal and endometrial cancers as well as others tumors
Clinically, HNPCC is often divided into two subgroups: type I,
characterized by a hereditary predisposition to colorectal cancer, a
young age of onset, and carcinoma observed in the proximal colon; type
II, characterized by an increased risk for cancers in certain tissues
such as the uterus, ovary, breast, stomach, small intestine, skin, and
larynx in addition to the colon</description>
    </keyword>
    <keyword id="KW-0890">
        <name>Hereditary spastic paraplegia</name>
        <name>HSP</name>
        <description>Protein which, if defective, causes hereditary spastic paraplegias
(HSPs). HSPs are a diverse class of hereditary degenerative spinal
cord disorders characterized by a slow, gradual, progressive weakness
and spasticity (stiffness) of the legs. Initial symptoms may include
difficulty with balance, weakness and stiffness in the legs, muscle
spasms, and dragging the toes when walking. In some forms of the
disorder, bladder symptoms (such as incontinence) may appear, or the
weakness and stiffness may spread to other parts of the body. Rate of
progression and the severity of symptoms are quite variable</description>
    </keyword>
    <keyword id="KW-0363">
        <name>Hermansky-Pudlak syndrome</name>
        <name>HPS</name>
        <description>Protein which, if defective, causes Hermansky-Pudlak syndrome, a rare
autosomal recessive disorder characterized by oculocutaneous albinism
and storage pool deficiency due to an absence of platelet dense
bodies. Lysosomal ceroid lipofuscinosis, pulmonary fibrosis and
granulomatous colitis are occasional manifestations of the disease</description>
    </keyword>
    <keyword id="KW-0364">
        <name>Heterocyst</name>
        <description>Protein which is implicated in heterocyst formation. A heterocyst is a
differentiated cyanobacterial cell that carries out nitrogen fixation
The heterocysts function as the sites for nitrogen fixation under
aerobic conditions. They are formed in response to a lack of fixed
nitrogen (NH4 or NO3). The morphological differentiation is
accompanied by biochemical alterations. The mature heterocysts contain
no functional photosystem II and cannot produce oxygen. Instead, they
contain only photosystem I, which enables them to carry out cyclic
photophosphorylation and ATP regeneration. These changes provide the
appropriate conditions for the functioning of the oxygen-sensitive
nitrogenase</description>
        <go id="GO:0043158"/>
    </keyword>
    <keyword id="KW-1056">
        <name>Heterotaxy</name>
        <name>Situs ambiguus</name>
        <name>Visceral heterotaxy</name>
        <name>Heterotaxia</name>
        <name>Situs ambiguous</name>
        <description>Protein which, if defective, causes heterotaxy, a broad group of
disorders caused by failure to correctly establish left-right
patterning during embryogenesis with consequent abnormal segmental
arrangements of cardiac chambers, vessels, lungs, and/or abdominal
organs. Heterotaxy include complex cardiac malformations, situs
inversus, situs ambiguus, isomerism. Situs inversus indicates complete
left-right reversal of organ position and is not usually associated
with structural anomalies. Situs ambiguus is an abnormal arrangement
of viscera almost invariably associated with complex cardiovascular
malformations as well as anomalies of the spleen and the
gastrointestinal system. Isomerism is a defect in asymmetry of paired
organs that usually have distinct right and left forms, but in this
condition, are mirror images</description>
    </keyword>
    <keyword id="KW-0909">
        <name>Hibernation</name>
        <description>Protein involved in the process of hibernation. Hibernation is a state
of inactivity in an animal brought about by short day lengths, cold
temperatures and limitations of food</description>
        <go id="GO:0042750"/>
    </keyword>
    <keyword id="KW-0367">
        <name>Hirschsprung disease</name>
        <name>HSCR</name>
        <description>Hirschsprung's disease (HSCR); a genetic disorder of neural crest
development characterized by the absence of intramural ganglion cells
in the hindgut; often resulting in intestinal obstruction</description>
    </keyword>
    <keyword id="KW-0368">
        <name>Histidine biosynthesis</name>
        <name>Histidine anabolism</name>
        <name>Histidine formation</name>
        <name>Histidine synthesis</name>
        <name>Histidine biosynthetic process</name>
        <description>Protein involved in the synthesis of the weakly basic amino acid
histidine</description>
        <go id="GO:0000105"/>
    </keyword>
    <keyword id="KW-0369">
        <name>Histidine metabolism</name>
        <name>Histidine metabolic process</name>
        <description>Protein involved in the biochemical reactions with the weakly basic
amino acid histidine</description>
        <go id="GO:0006547"/>
    </keyword>
    <keyword id="KW-0370">
        <name>Holoprosencephaly</name>
        <description>A clinically variable and genetically heterogeneous malformation in
which the developing forebrain fails to correctly separate into right
and left hemispheres. In its most severe form (alobar
holoprosencephaly), the forebrain consists of a single ventricle, and
midbrain structures may be malformed as well. In the most extreme
cases, anophthalmia or cyclopia is evident along with a congenital
absence of the mature nose. In milder forms (semilobar or lobar
holoprosencephaly), rudimentary midline structures are present. The
less severe form features facial dysmorphia characterized by ocular
hypertelorism, defects of the upper lip and/or nose, and absence of
the olfactory nerves or corpus callosum. The majority of cases are
sporadic, although families with both autosomal dominant and autosomal
recessive holoprosencephaly have been described</description>
    </keyword>
    <keyword id="KW-0371">
        <name>Homeobox</name>
        <name>Homeodomain</name>
        <description>Protein which contains at least one homeobox, a conserved sequence
originally detected, on the nucleotide level, in many of the genes
which give rise to homeotic and segmentation mutants in Drosophila
The homeobox, also termed homeodomain, consists of about 60 amino
acids and is involved in DNA-binding</description>
        <go id="GO:0003677"/>
    </keyword>
    <keyword id="KW-0372">
        <name>Hormone</name>
        <description>Protein which functions as a hormone, a biochemical substance secreted
by specialized cells that affects the metabolism or behavior of other
cells which possess functional receptors for the hormone. Hormones may
be hydrophilic, like insulin, in which case the receptors are on the
cell surface, or lipophilic, like the steroids, where the receptor can
be intracellular</description>
        <go id="GO:0005179"/>
    </keyword>
    <keyword id="KW-1030">
        <name>Host cell inner membrane</name>
        <name>Host inner membrane</name>
        <description>Protein found in or associated with the prokaryotic host cell inner
membrane, a selectively permeable membrane which separates the host
cytoplasm from the host periplasm in prokaryotes with 2 membranes</description>
    </keyword>
    <keyword id="KW-1031">
        <name>Host cell junction</name>
        <description>Protein found in or associated with a host cell junction, a host cell-
host cell or host cell-host extracellular matrix contact within a
tissue of a host multicellular organism, especially abundant in host
epithelia. In vertebrates, there are three major types of cell
junctions: anchoring junctions (e.g. adherens junctions),
communicating junctions (e.g. gap junctions) and occluding junctions
(e.g. tight junctions)</description>
    </keyword>
    <keyword id="KW-0578">
        <name>Host cell lysis by virus</name>
        <description>Viral protein involved in the lysis of the host cell allowing the
release of mature, newly formed virions. Viruses use different way to
lyse their host cell. They can express viroporins as Adenoviridae or
Picornaviridae do in the late phase of infection. Phycodnaviridae for
their part seem to express lytic phospholipids. In dsDNA prokaryotic
viruses, lysis-specific proteins are expressed: a holin, which
permeabilizes the inner membrane and an endolysin which then gains
access to and degrades the host peptidoglycans. Some bacterioviruses
express a signal-containing endolysin and thus do not need the holin
function</description>
        <go id="GO:0044659"/>
    </keyword>
    <keyword id="KW-1032">
        <name>Host cell membrane</name>
        <name>Host plasmalemma</name>
        <name>Host plasma membrane</name>
        <name>Host cytoplasmic membrane</name>
        <description>Protein found in or associated with the host cytoplasmic membrane, a
selectively permeable membrane which separates the cytoplasm from its
surroundings. Known as the host cell inner membrane in prokaryotes
with 2 membranes</description>
    </keyword>
    <keyword id="KW-1033">
        <name>Host cell outer membrane</name>
        <name>Host outer membrane</name>
        <description>Protein found in or associated with the prokaryotic cell outer
membrane, a selectively permeable membrane which separates the
prokaryotic periplasm from its surroundings in prokaryotes with 2
membranes. Traditionally only Gram-negative bacteria were thought of
as having an outer membrane, but recent work has shown some
Actinobacteria, including Mycobacterium tuberculosis, as well as at
least 1 archaea (Ignicoccus hospitalis) have a cell outer membrane</description>
    </keyword>
    <keyword id="KW-1034">
        <name>Host cell projection</name>
        <name>Host cell protrusion</name>
        <description>Protein found in or associated with a host cell projection, a host
cell protrusion such as pseudopodium, filopodium, lamellipodium,
growth cone, flagellum, acrosome, axon, pili or bacterial comet tail
These membrane-cytoskeleton-coupled processes are involved in many
biological functions, such as host cell motility, cancer-cell
invasion, endocytosis, phagocytosis, exocytosis, pathogen infection,
neurite extension and cytokinesis</description>
    </keyword>
    <keyword id="KW-1183">
        <name>Host cell receptor for virus entry</name>
        <name>Viral receptor activity</name>
        <description>Cell surface protein used by a virus as an attachment and entry
receptor. In some cases, binding to a cellular receptor is not
sufficient for infection: an additional cell surface molecule, or
coreceptor, is required for entry. Some viruses are able to use
different receptors depending on the target cell type. In prokaryotic
viruses, cell receptor for virus entry can also be localized on host
outer membrane, pilus or flagellum</description>
        <go id="GO:0001618"/>
    </keyword>
    <keyword id="KW-1035">
        <name>Host cytoplasm</name>
        <description>Protein found in the host cytoplasm, the content of a host cell within
the plasma membrane and, in eukaryotics cells, surrounds the host
nucleus</description>
    </keyword>
    <keyword id="KW-1036">
        <name>Host cytoplasmic vesicle</name>
        <description>Protein found in or associated with host cytoplasmic vesicles, which
mediate vesicular transport among the organelles of host secretory and
endocytic systems</description>
    </keyword>
    <keyword id="KW-1037">
        <name>Host cytoskeleton</name>
        <description>Protein which is a component or which is associated with the host
cytoskeleton, a dynamic three-dimensional structure that fills the
host cytoplasm of eukaryotic cells. It is responsible for cell
movement, cytokinesis, and the organization of the organelles or
organelle-like structures within the host cell</description>
    </keyword>
    <keyword id="KW-1038">
        <name>Host endoplasmic reticulum</name>
        <description>Protein whose subcellular location is the host endoplasmic reticulum
(ER), which is an extensive network of membrane tubules, vesicles and
flattened cisternae (sac-like structures) found throughout the
eukaryotic host cell, especially those responsible for the production
of hormones and other secretory products</description>
    </keyword>
    <keyword id="KW-1039">
        <name>Host endosome</name>
        <description>Protein found in or associated with host endosomes, which are highly
dynamic membrane systems involved in transport within the host cell,
they receive endocytosed host cell membrane molecules and sort them
for either degradation or recycling back to the host cell surface
They also receive newly synthesised proteins destined for host
vacuolar/lysosomal compartments</description>
    </keyword>
    <keyword id="KW-1079">
        <name>Host G2/M cell cycle arrest by virus</name>
        <description>Viral protein involved in the modulation of host cell cycle by
inhibiting the G2/M transition. A variety of viruses have been
associated with G2/M arrest, including some DNA viruses, some RNA
viruses and retroviruses but the mechanisms by which arrest is
achieved greatly differs between those viruses</description>
        <go id="GO:0039592"/>
    </keyword>
    <keyword id="KW-1190">
        <name>Host gene expression shutoff by virus</name>
        <description>Viral protein which prevents host gene expression by blocking for
example host transcription, mRNA export or translation. This gives
virus transcripts a competitive edge to use the hijacked translation
machinery. Preventing the expression of host proteins is also a
strategy to counteract the antiviral response</description>
        <go id="GO:0039657"/>
    </keyword>
    <keyword id="KW-1040">
        <name>Host Golgi apparatus</name>
        <name>Host Golgi complex</name>
        <name>Host apparatus golgiensis</name>
        <name>Host Golgi</name>
        <name>Host complexus golgiensis</name>
        <description>Protein found in the host Golgi apparatus, a series of flattened,
cisternal membranes and similar vesicles usually arranged in close
apposition to each other to form stacks. In mammalian cells, the host
Golgi apparatus is juxtanuclear, often pericentriolar. The stacks are
connected laterally by tubules to create a perinuclear ribbon
structure, the 'Golgi ribbon'. In plants and lower animal cells, the
host Golgi exists as many copies of discrete stacks dispersed
throughout the host cytoplasm. It is a polarized structure with, in
most higher eukaryotic cells, a cis-face associated with a tubular
reticular network of membranes facing the endoplasmic reticulum, the
cis-Golgi network (CGN), a medial area of disk-shaped flattened
cisternae, and a trans-face associated with another tubular reticular
membrane network, the trans-Golgi network (TGN) directed toward the
host plasma membrane and compartments of the host endocytic pathway</description>
    </keyword>
    <keyword id="KW-1041">
        <name>Host lipid droplet</name>
        <name>Host lipid bodies</name>
        <name>Host oil bodies</name>
        <name>Host oleosome</name>
        <name>Host oil body</name>
        <name>Host spherosome</name>
        <name>Host lipid body</name>
        <name>Host adiposome</name>
        <name>Host monolayer-surrounded lipid storage body</name>
        <name>Host lipid particle</name>
        <description>Protein characteristic of host lipid droplet, a dynamic cytoplasmic
host organelle which consists of an heterogeneous macromolecular
assembly of lipids and proteins covered by a unique phospholipid
monolayer. They may play a role in host lipid metabolism and storage,
and they may be involved in the regulation of intracellular
trafficking and signal transduction</description>
    </keyword>
    <keyword id="KW-1042">
        <name>Host lysosome</name>
        <description>Protein found in the host lysosome, a membrane-limited organelle
present in all eukaryotic cells, which contains a large number of
hydrolytic enzymes that are used for degrading almost any kind of
cellular constituent, including entire organelles. The mechanisms
responsible for delivering cytoplasmic cargo to the host
lysosome/vacuole are known collectively as autophagy and play an
important role in the maintenance of homeostasis</description>
    </keyword>
    <keyword id="KW-1043">
        <name>Host membrane</name>
        <description>Protein which is membrane-bound or membrane-associated with the host
membrane, a lipid bilayer which surrounds host enclosed spaces and
compartments. This selectively permeable structure is essential for
effective separation of a host cell or organelle from its
surroundings</description>
    </keyword>
    <keyword id="KW-1044">
        <name>Host microsome</name>
        <description>Protein found in host microsomes, which are a heterogenous set of
vesicles 20-200 nm in diameter and formed from the host endoplasmic
reticulum when host cells are disrupted</description>
    </keyword>
    <keyword id="KW-1045">
        <name>Host mitochondrion</name>
        <description>Protein encoded by or localized in the host mitochondrion, a
semiautonomous, self-reproducing organelle that occurs in the
cytoplasm of all cells of most, but not all, host eukaryotes. Each
host mitochondrion is surrounded by a double limiting membrane. The
inner membrane is highly invaginated, and its projections are called
cristae. They are the sites of the reactions of oxidative
phosphorylation, which result in the formation of ATP</description>
    </keyword>
    <keyword id="KW-1046">
        <name>Host mitochondrion inner membrane</name>
        <name>Host inner mitochondrial membrane</name>
        <name>Host mitochondrial inner membrane</name>
        <description>Protein found in or associated with the host mitochondrion inner
membrane, the membrane which separates the host mitochondrial matrix
from the host mitochondrial intermembrane space</description>
    </keyword>
    <keyword id="KW-1047">
        <name>Host mitochondrion outer membrane</name>
        <name>Host outer mitochondrial membrane</name>
        <name>Host mitochondrial outer membrane</name>
        <description>Protein found in or associated with the host mitochondrion outer
membrane, the host mitochondrial membrane facing the host cytoplasm</description>
    </keyword>
    <keyword id="KW-1192">
        <name>Host mRNA suppression by virus</name>
        <description>Viral protein involved in suppressing host mRNAs expression to
maximize expression of viral mRNAs. Decimating cellular mRNAs
eventually leads to shutoff of host proteins expression and gives
virus transcripts a competitive edge for access to the cellular
translation machinery. Preventing the expression of host proteins is
also a strategy to counteract the antiviral response. Suppression of
host mRNA can be performed by interfering with host pre-mRNA
processing function (splicing or polyadenylation), by degrading mRNAs
or blocking their export from the nucleus to the cytoplasm</description>
    </keyword>
    <keyword id="KW-1048">
        <name>Host nucleus</name>
        <description>Protein located in the host nucleus, which is the most obvious
organelle in any host eukaryotic cell. It is a membrane-bound
organelle and is surrounded by double membranes. It communicates with
the surrounding cytosol via numerous nuclear pores</description>
    </keyword>
    <keyword id="KW-1049">
        <name>Host periplasm</name>
        <name>Host periplasmic space</name>
        <description>Protein located in the host periplasm, the space between the inner and
outer membrane in host Gram-negative bacteria. In Gram-positive
bacteria a smaller periplasmic space is found between the inner
membrane and the peptidoglycan layer. Also used for the host
intermembrane spaces of host fungi and host organelles</description>
    </keyword>
    <keyword id="KW-1051">
        <name>Host synapse</name>
        <description>Protein located in the host synapse, the communicating cell-cell
junctions that allow signals to pass from a host nerve cell to a host
target cell. In a chemical synapse, the signal is carried by a
neurotransmitter which diffuses across a narrow synaptic cleft and
activates a receptor on the postsynaptic membrane of the target cell</description>
    </keyword>
    <keyword id="KW-1050">
        <name>Host thylakoid</name>
        <description>Protein located in or on the host thylakoid, a membranous cellular
structure containing the photosynthetic pigments, reaction centers and
electron-transport chain. In host chloroplast, thylakoids stack up to
form the grana or stay as single cisternae and interconnect the grana
Thylakoid, where photosynthesis occurs, are found in chloroplasts,
cyanelles and in photosynthetic bacteria where they are the extensive
invaginations of the plasma membrane</description>
    </keyword>
    <keyword id="KW-0945">
        <name>Host-virus interaction</name>
        <description>Viral or cellular protein involved in a host-virus interaction
Viruses interact with many cellular pathways to achieve their
replication cycle. Entry into the host cell, transport to the viral
replication sites or viral exit from the host cell are all steps that
require specific interactions between the virus and its host
Additionally, the evasion from the host immune response requires a lot
of viral proteins to associate with and inhibit cellular proteins with
antiviral functions</description>
    </keyword>
    <keyword id="KW-0373">
        <name>Hyaluronic acid</name>
        <description>Protein which binds hyaluronic acic, an acidic glycosaminoglycan which
consists of repeating units of the disaccharide composed of D-
glucuronic acid and N-acetyl-D-glucosamine. This linear polymer is
present in cell coats and in the extracellular ground substance of the
connective tissues of vertebrates; it also occurs in the synovial
fluid in joints and in the vitreous humor of the eye</description>
        <go id="GO:0005540"/>
    </keyword>
    <keyword id="KW-0374">
        <name>Hybridoma</name>
        <description>Protein sequenced from a hybridoma, an artificially produced hybrid
cell line created by fusion of a lymphocyte and a myeloma cell. These
cells can multiply indefinitely in culture and produce monoclonal
antibodies</description>
    </keyword>
    <keyword id="KW-0375">
        <name>Hydrogen ion transport</name>
        <name>Hydrogen cation transport</name>
        <name>Proton transport</name>
        <description>Protein involved in the transport of hydrogen ions across a membrane
Used to power processes such as ATP synthesis and bacterial flagellar
rotation</description>
        <go id="GO:1902600"/>
    </keyword>
    <keyword id="KW-0376">
        <name>Hydrogen peroxide</name>
        <description>Protein involved in hydrogen peroxide (H(2)O(2)) decomposition, e.g.,
catalase. H(2)O(2) is generated by the body as a byproduct of aerobic
cellular respiration</description>
        <go id="GO:0042744"/>
    </keyword>
    <keyword id="KW-0377">
        <name>Hydrogenosome</name>
        <description>Protein characteristic of the hydrogenosome, a redox organelle of
anaerobic unicellular eukaryotes which contains hydrogenase and
produces hydrogen and ATP by glycolysis. They are found in various
unrelated eukaryotes, such as anaerobic flagellates, chytridiomycete
fungi and ciliates. Most hydrogenosomes lack a genome, but some like
that of the anaerobic ciliate Nyctotherus ovalis, have retained a
rudimentary genome</description>
    </keyword>
    <keyword id="KW-0378">
        <name>Hydrolase</name>
        <description>Enzyme which catalyzes hydrolysis reaction, i.e. the addition of the
hydrogen and hydroxyl ions of water to a molecule with its consequent
splitting into two or more simpler molecules</description>
        <go id="GO:0016787"/>
    </keyword>
    <keyword id="KW-0379">
        <name>Hydroxylation</name>
        <name>Hydroxylated</name>
        <description>Protein which is posttranslationally modified by the attachment of at
least one hydroxyl (-OH) group</description>
    </keyword>
    <keyword id="KW-0380">
        <name>Hyperlipidemia</name>
        <description>Protein which, if defective, causes hyperlipidemia, a condition
characterized by the elevation of lipids in the bloodstream. There are
different types of hyperlipidemias: type I (lipoprotein lipase
deficiency), IIa (hypercholesterolemia; LDL receptor deficiency), IIb
(combined hyperlipidemia), III (dysbetalipoproteinemia), IV
(hypertriglyceridemia) and V (mixed hyperlipidemia)</description>
    </keyword>
    <keyword id="KW-0381">
        <name>Hypersensitive response</name>
        <name>HR</name>
        <description>Protein involved in hypersensitive response, a complex and early
defense response that causes necrosis and cell death to restrict the
growth of a pathogen. Local and systemic biochemical changes include
generation of active oxygen species (oxidative burst), cell death,
overproduction of lignin-related materials, and the induction of
certain proteins such as pathogen related (PR) proteins</description>
        <go id="GO:0009626"/>
    </keyword>
    <keyword id="KW-0928">
        <name>Hypersensitive response elicitation</name>
        <description>Proteins involved in hypersensitive response (HR) elicitation. HR is a
rapid defense-associated programmed cell death of plant cells at the
site of invasion</description>
        <go id="GO:0052040"/>
    </keyword>
    <keyword id="KW-1016">
        <name>Hypogonadotropic hypogonadism</name>
        <name>HH</name>
        <name>IHH</name>
        <name>Isolated hypogonadotropic hypogonadism</name>
        <name>Idiopathic hypogonadotropic hypogonadism</name>
        <description>Protein which, if defective, causes hypogonadotropic hypogonadism, a
disorder characterized by a deficiency of the pituitary secretion of
follicle-stimulating hormone (FSH) and luteinizing hormone (LH)
Affected individuals present with absent or impaired sexual
development due to sex-steroid-hormone deficiency, low serum levels of
the pituitary gonadotropins FSH and LH, and infertility</description>
    </keyword>
    <keyword id="KW-0382">
        <name>Hypotensive agent</name>
        <name>Antihypertensive agents</name>
        <description>Protein which can cause hypotension, i.e. low blood pressure or a
sudden drop in blood pressure</description>
        <go id="GO:0008217"/>
    </keyword>
    <keyword id="KW-1063">
        <name>Hypotrichosis</name>
        <description>Protein which, if defective, causes hypotrichosis, a condition
characterized by reduced pilosity over the body and scalp (with
sparse, thin, and short hair)</description>
    </keyword>
    <keyword id="KW-0385">
        <name>Hypusine</name>
        <description>Protein which is posttranslationally modified on at least one lysine
residue to form hypusine (N-epsilon-(4-aminobutyl)lysine). This
spermidine-dependent reaction is catalyzed by deoxyhypusine synthase
and deoxyhypusine hydroxylase. eIF-5A is the only protein in
eukaryotes and archaebacteria known to contain hypusine</description>
    </keyword>
    <keyword id="KW-0386">
        <name>Hypusine biosynthesis</name>
        <name>Hypusine formation</name>
        <name>Hypusine anabolism</name>
        <name>Hypusine biosynthetic process</name>
        <name>Hypusine synthesis</name>
        <description>Protein involved in the synthesis of hypusine, an amino acid formed by
the two posttranslational steps in the modification of a lysine: (i)
deoxyhypusine synthase catalyzes the transfer of a 4-aminobutyl moiety
from spermidine to a specific lysine residue to form a deoxyhypusine
residue, N-epsilon-(4-aminobutyl)lysine, and (ii) deoxyhypusine
hydroxylase catalyzes the hydroxylation of the deoxyhypusine residue
to form hypusine (N-epsilon-(4-amino-2-hydroxybutyl)lysine)</description>
        <go id="GO:0008612"/>
    </keyword>
    <keyword id="KW-0387">
        <name>Ice nucleation</name>
        <description>Protein which promotes the nucleation of ice. The proteins catalyzes
the formation of ice crystals in extracellular fluid at relatively
high temperatures (up to -2 degrees Celsius) to protect the organism
from damage by intracellular ice formation</description>
        <go id="GO:0050825"/>
    </keyword>
    <keyword id="KW-0977">
        <name>Ichthyosis</name>
        <description>Protein which, if defective, causes ichthyosis, any of a group of
cutaneous disorders characterized by increased or aberrant
keratinization and resulting in non-inflammatory scaling of the skin
Most ichthyoses are genetically determined, while some may be acquired
and develop in association with various systemic diseases or be a
prominent feature in certain genetic syndromes</description>
    </keyword>
    <keyword id="KW-1196">
        <name>IFIT mRNA restriction evasion by virus</name>
        <description>Viral protein allowing host innate defense evasion by methylating the
first and second ribonucleotide of viral mRNAs (cap1 and cap2). These
methylations allow viral RNA to escape cellular antiviral process
mediated by host IFIT proteins which degrade non cap1-methylated
mRNAs. Also prevents IFIH1/MDA5 sensor activation by cap0 mRNAs, which
would trigger interferon beta synthesis</description>
        <go id="GO:0039699"/>
    </keyword>
    <keyword id="KW-0388">
        <name>IgA-binding protein</name>
        <description>Protein binding to immunoglobulin A, the major class of antibodies
found in external secretions such as saliva, tears, gastric fluid,
milk and mucosal secretions</description>
        <go id="GO:0019862"/>
    </keyword>
    <keyword id="KW-0389">
        <name>IgE-binding protein</name>
        <description>Protein binding to immunoglobulin E, the antibody class involved in
local inflammatory reactions, reactions to parasites, and also in
allergic responses</description>
        <go id="GO:0019863"/>
    </keyword>
    <keyword id="KW-0390">
        <name>IgG-binding protein</name>
        <description>Protein binding to immunoglobulin G, the main type of immunoglobulin
produced towards the end of a primary immune response and in a
secondary response</description>
        <go id="GO:0019864"/>
    </keyword>
    <keyword id="KW-0391">
        <name>Immunity</name>
        <name>Immune response</name>
        <description>Protein involved in immunity, any immune system process that functions
in the response of an organism to a potential internal or invasive
threat. The vertebrate immune system is formed by the innate immune
system (composed of phagocytes, complement, antimicrobial peptides,
etc) and by the adaptive immune system which consists of T- and B-
lymphocytes</description>
        <go id="GO:0002376"/>
    </keyword>
    <keyword id="KW-1280">
        <name>Immunoglobulin</name>
        <name>Antibody</name>
        <description>A glycoprotein produced in membrane-bound or secreted form by B
lymphocytes. The basic structural unit of an immunoglobulin (Ig) is
composed of two identical covalently linked heavy chains and two
identical light chains. Both the heavy chains and light chains contain
a series of repeating homologous structural units called Ig domains
The N-terminal variable regions of the heavy and light chains form the
antigen binding sites, whereas the C-terminal constant regions of the
heavy chains interact with other molecules in the immune system. The
membrane-bound antibodies serve as receptors that mediate the antigen-
triggered activation of B cells. Secreted antibodies function as
mediators of specific humoral immunity by engaging various effector
mechanisms that serve to eliminate the bound antigen</description>
        <go id="GO:0019814"/>
    </keyword>
    <keyword id="KW-0393">
        <name>Immunoglobulin domain</name>
        <name>Immunoglobulin fold</name>
        <description>A globular structural motif found in many proteins of the immune
system, including immunoglobulins (Igs), T cell receptors (TCRs) and
major histocompatibility complex (MHC) molecules. Ig domains are
approximately 110 amino acid residues in length, include an internal
disulfide bond, and contain two layers of beta-pleated sheets, each
layer composed of three to five strands of antiparallel polypeptide
chains. Ig domains are classified as V-like or C-like on the basis of
closest homology to either Ig V or C domains</description>
    </keyword>
    <keyword id="KW-1271">
        <name>Inflammasome</name>
        <name>ASC focus</name>
        <name>ASC speck</name>
        <description>Component of the inflammasome complex involved in innate immunity and
inflammation. Inflammasomes are supramolecular micron-sized complexes
that assemble in the cytosol adjacent to the nucleus in response to
pathogens and other damage-associated signals. The core of
inflammasomes consists of at least 2 components: a signal sensor and
an effector inflammatory caspase (mostly CASP1). However, most
inflammasomes contain a third element, an adaptor (often ASC/PYCARD)
In response to a danger signal, the sensor homooligomerizes and
interacts with the adaptor that polymerizes and forms a platform to
recruit caspase precursors. This results in increased local
concentration of the enzyme, leading to trans-autocleavage and
activation. Active caspases process proinflammatory IL1B and IL18
cytokine precursors, which are then secreted in the extracellular
milieu and induce inflammatory responses. In adaptor-independent
inflammasomes, the sensor directly recruits the caspase. Additional
proteins may interaction with the core complex. Inflammasomes also
induce pyroptosis, an inflammatory form of programmed cell death</description>
    </keyword>
    <keyword id="KW-0395">
        <name>Inflammatory response</name>
        <name>Response to inflammation</name>
        <description>Protein involved in the localized protective response to tissue
damage, microbial infection, or the presence of foreign matter. It is
characterized by swelling, redness, heat and pain and involves a
complex series of events including vascular changes and accumulation
of blood cells, such as neutrophil leucocytes and mononuclear
phagocytes, at the site of injury</description>
        <go id="GO:0006954"/>
    </keyword>
    <keyword id="KW-1111">
        <name>Inhibition of eukaryotic host transcription initiation by virus</name>
        <description>Viral protein involved in the disruption of the host transcriptional
machinery. Viruses have evolved ways of interacting with the cellular
preinitiation complex (PIC) to shutoff host transcription initiation
For example, the TATA binding protein and TFIIH are targeted by some
viral proteins and thus cannot assemble properly to form a functional
PIC</description>
        <go id="GO:0039602"/>
    </keyword>
    <keyword id="KW-1075">
        <name>Inhibition of eukaryotic host translation factors by virus</name>
        <description>Viral protein that inhibits or degrades host translation initiation
factor(s). Viruses have evolved ways of interacting with the cellular
translational machinery to shutoff host gene expression. This global
inhibition of cellular protein synthesis serves to ensure maximal
viral gene expression and to evade host immune response. Some viruses
are known to cleave host translation initiation factors like EIF3 or
EIF4G, while others achieve translation inhibition by promoting
dephosphorylation of some host translation initiation factors or their
binding partners</description>
        <go id="GO:0039606"/>
    </keyword>
    <keyword id="KW-1080">
        <name>Inhibition of host adaptive immune response by virus</name>
        <description>Viral protein involved in the evasion of host adaptive immune
response. Upon infection, the innate immune system provides mechanisms
for the rapid sensing and elimination of viruses. Adaptive immunity
has evolved to provide a broader and more finely tuned repertoire of
recognition for both self- and nonself-antigens. In vertebrates, the
adaptive immune response is mediated by T and B lymphocytes expressing
specific receptors. A lot of viruses escape the adaptive immune
response by different mechanisms including interference with the
presentation of antigenic peptides at the surface of infected cells
Bacteria and archaea have adaptive immunity, the CRISPR-Cas system</description>
        <go id="GO:0039504"/>
    </keyword>
    <keyword id="KW-1081">
        <name>Inhibition of host apoptosis by viral BCL2-like protein</name>
        <description>Viral protein sharing sequence similarity with host BCL2 protein
Cellular BCL2 family members are divided in two groups, some having
anti-apoptotic activity (such as BCL2 itself) while others have pro-
apoptotic function (such as BAX). If the level of proapoptotic members
are higher than inhibitors, then the cell undergoes apoptosis. So far,
all viral homologues display anti-apoptotic activity</description>
        <go id="GO:0033668"/>
    </keyword>
    <keyword id="KW-1082">
        <name>Inhibition of host apoptosis by viral FLIP-like protein</name>
        <description>Viral protein sharing sequence similarity with host FLIPs (FLICE-
inhibitory proteins). Cellular FLIPs play an essential role in
apoptosis functioning as a link between cell survival and cell death
pathways . Viral FLIPs inhibit apoptosis by interfering with death
receptor signaling</description>
        <go id="GO:0019050"/>
    </keyword>
    <keyword id="KW-1083">
        <name>Inhibition of host autophagy by virus</name>
        <description>Viral protein involved in the inhibition of host autophagy. Autophagy
is a major intracellular pathway in the delivery of cytoplasmic
material to lysosomes for degradation. It is also essential for the
removal of pathogenic protein aggregates from the cell during
infection. Several viruses including influenza and HIV-1 block
autophagosome maturation by interacting with and inhibiting host
Beclin-1, an essential protein playing a central role in autophagy</description>
        <go id="GO:0140321"/>
    </keyword>
    <keyword id="KW-1085">
        <name>Inhibition of host caspases by virus</name>
        <description>Viral protein involved in the evasion of host cell apoptosis by
inhibiting host caspases. Many viruses from diverse families have
evolved mechanisms to evade or delay cell death by suppressing the
activity of cytoplasmic proteases termed caspases which have a central
role in apoptosis induction</description>
        <go id="GO:0033668"/>
    </keyword>
    <keyword id="KW-1086">
        <name>Inhibition of host chemokines by virus</name>
        <description>Viral protein involved in the evasion of host immune response by
inhibiting chemokines. Chemokines have several roles including Th1/Th2
differentiation, T_cell costimulation, or promotion of leukocyte
migration. Due to the importance of chemokines in immunity, viruses
have evolved mechanisms to counter the chemokine network. They encode
chemokine-like proteins, chemokine receptors, or chemokine-binding
proteins to inhibit cellular chemokines</description>
        <go id="GO:0042785"/>
    </keyword>
    <keyword id="KW-1087">
        <name>Inhibition of host complement factors by virus</name>
        <description>Viral protein involved in the evasion of host humoral response by
inhibiting the complement factors. The activation of complement
involves the sequential proteolyis of proteins to generate enzymes
with catalytic activities. The biological functions of the complement
include opsonization, inflammation, lysis of immune complexes, or
enhancement of the humoral immune response. Some herpesviruses,
poxviruses and retroviruses mimic or interact with complement
regulatory proteins to block complement activation and neutralization
of virus particles</description>
        <go id="GO:0042784"/>
    </keyword>
    <keyword id="KW-1248">
        <name>Inhibition of host DNA replication by virus</name>
        <description>Viral protein that blocks host DNA replication without inhibiting host
transcription or translation. Inhibiting host replication provides an
advantage during the virus life cycle by reducing or eliminating
competing host macromolecular synthesis. Bacteriophage N4 for example
is known to shut off the host DNA replication while the host genome
remains structurally intact. Bacteriophage lambda prevents host DNA
replication initiation and Staphylococcus bacteriophages target the
replicative DNA polymerase processivity clamp and the helicase</description>
        <go id="GO:0098673"/>
    </keyword>
    <keyword id="KW-1224">
        <name>Inhibition of host IKBKE by virus</name>
        <description>Viral protein involved in the evasion of host innate defenses by
inhibiting the IKBKE/IKK-epsilon kinase. Upon viral infection, the
DDX58/RIG-I or IFIH1/MDA5 receptors recognize foreign material and
transmit the signal to downstream components MAVS and IKBKE. In turn,
the IKBKE kinase phosphorylates and activates IRF3 and/or IRF7. Once
phosphorylated, IRF3 and IRF7 translocate into the nucleus to drive
transcription of interferons. Several viruses including arenaviruses
or ebola virus interact directly with and inhibit IKBKE/IKK-epsilon to
prevent IRFs activation</description>
        <go id="GO:0039724"/>
    </keyword>
    <keyword id="KW-1090">
        <name>Inhibition of host innate immune response by virus</name>
        <description>Viral protein involved in the evasion of host innate immune response
Upon viral infection, the innate immune system initially defends the
host in a non-specific manner. Many viral proteins interact with and
inhibit components the host innate system to replicate more
efficiently. In metazoans and plants, the innate immune system
includes the intracellular pattern recognition receptors (PRRs) that
detect pathogen-associated molecular patterns (PAMPs). In plants and
invertebrates, it includes the RNA interference (RNAi) system. Plants
also have effector-triggered immunity (ETI). In metazoans, it includes
the cell-dependent mechanisms (e.g. phagocytes) or secreted factors
Bacteria and archaea have an innate immune system relying on various
systems (e.g. the restriction-modification system, Pycsar)</description>
        <go id="GO:0052170"/>
    </keyword>
    <keyword id="KW-1091">
        <name>Inhibition of host interferon receptors by virus</name>
        <description>Viral protein involved in the evasion of the interferon pathway by
inhibiting interferon receptors. Interferon signaling exerts antiviral
effects through cell surface receptors termed interferon receptors. In
response to binding of extracellular interferons, they activate the
JAK/STAT pathway causing transcriptional activation of IFN-regulated
genes. To avoid this antiviral response, several viruses target the
interferon receptors and send them to degradation via the proteasome</description>
        <go id="GO:0140886"/>
    </keyword>
    <keyword id="KW-1114">
        <name>Inhibition of host interferon signaling pathway by virus</name>
        <description>Viral protein involved in the evasion of host innate defense by
inhibiting the interferon signaling pathway leading to the production
of interferon-induced genes. Interferons bind to the IFN receptors
(IFNAR) on the cell surface and activate Jak/Tyk kinases. These
kinases phosphorylate STAT1 and STAT2 that translocate to the nucleus
and induce the expression of interferon stimulated genes (ISGs). Many
viruses interact with components of this pathway to prevent expression
of ISGs and inhibit the host immune response</description>
        <go id="GO:0039502"/>
    </keyword>
    <keyword id="KW-1092">
        <name>Inhibition of host IRF3 by virus</name>
        <description>Viral protein involved in the evasion of host innate defense by
inhibiting the interferon regulatory factor-3 (IRF3) protein. Viral
infection triggers the phosphorylation and activation of IRF3. The
activated IRF3 migrates to the nucleus, where it complexes with the
transcription coactivator CREBBP/EP300, leading to the transcriptional
activation of the IFN-alpha and IFN-beta genes. Several viral proteins
directly bind to IRF3 and inhibit its transcriptional activity while
others target it to the proteasome for degradation</description>
        <go id="GO:0039548"/>
    </keyword>
    <keyword id="KW-1093">
        <name>Inhibition of host IRF7 by virus</name>
        <description>Viral protein involved in the evasion of host innate defense by
inhibiting the interferon regulatory factor-7 (IRF7) protein. Viral
infection triggers the phosphorylation and activation of IRF7. The
activated IRF7 migrates to the nucleus leading to the transcriptional
activation of the IFN-alpha and IFN-beta genes. Some viral proteins
prevent IRF7 phosphorylation and nuclear activation. Ebola virus VP35
interacts with IRF7 and hijacks the cellular SUMOylation machinery for
its advantage to increase IRF7 SUMOylation thereby disabling its
activity</description>
        <go id="GO:0039557"/>
    </keyword>
    <keyword id="KW-1094">
        <name>Inhibition of host IRF9 by virus</name>
        <description>Viral protein involved in the evasion of the type I and III interferon
pathway by inhibiting the interferon regulatory factor-9 (IRF9)
protein. Viral infection triggers the phosphorylation and activation
of IRF9. The activated IRF9 migrates to the nucleus leading to the
transcriptional activation of several hundred IFN-responsive genes
Some viral proteins inhibit IRF9 activation by preventing its nuclear
localization upon infection or by sending it to the nucleus in an
inactive state</description>
        <go id="GO:0039560"/>
    </keyword>
    <keyword id="KW-1095">
        <name>Inhibition of host ISG15 by virus</name>
        <description>Viral protein involved in the evasion of host immune defense by
inhibiting the ISG15 protein, an ubiquitin-like modifier playing
important roles in the innate immune response. Like ubiquitin, ISG15
is conjugated to lysines on numerous target proteins through its
conserved C-terminal region. Viruses escape from the antiviral
activity of ISG15 by direct interaction or by cleavage of ISG15
derivatives</description>
        <go id="GO:0039579"/>
    </keyword>
    <keyword id="KW-1096">
        <name>Inhibition of host JAK1 by virus</name>
        <description>Viral protein involved in the evasion of the type I, II and III
interferon pathways by inhibiting the JAK1 protein. Upon viral
infection, JAK1 is activated by the interferon-alpha/beta, -gamma, and
-lambda signal transduction pathways. Several viral proteins can
directly interact with JAK1 to prevent its ability to phosphorylate
the downstream partners STAT1 or STAT2</description>
        <go id="GO:0039576"/>
    </keyword>
    <keyword id="KW-1097">
        <name>Inhibition of host MAVS by virus</name>
        <description>Viral protein involved in the evasion of host innate defense by
inhibiting the MAVS protein. During viral replication, dsRNA is
produced and detected by DDX58/RIG-I or IFIH1/MDA5 that will activate
MAVS to coordinate pathways leading to induction of antiviral
cytokines. Several viral proteins including NS3/4A from Hepatitis C,
or protease 3C from hepatitis A virus, cleave MAVS to abrogate its
activity</description>
        <go id="GO:0039545"/>
    </keyword>
    <keyword id="KW-1089">
        <name>Inhibition of host MDA5 by virus</name>
        <description>Viral protein involved in the evasion of host innate defense by
inhibiting the IFIH1/MDA5 protein. Upon recognition of long viral
dsRNAs, IFIH1/MDA5 initiates an antiviral signaling cascade by
interacting with downstream partners. Some viral proteins including
paramyxovirus V proteins interact with IFIH1/MDA5 and blocks its
binding with its downstream partner MAVS</description>
        <go id="GO:0039554"/>
    </keyword>
    <keyword id="KW-1115">
        <name>Inhibition of host MHC class I molecule presentation by virus</name>
        <description>Viral protein involved in the evasion of host adaptive immune response
by inhibiting the presentation of loaded MHC class I molecules at the
cell surface. Many viruses 'intercept' the loaded MHC class I
molecules and retain them in the endoplasmic reticulum or target them
to degradation in order to prevent presentation of the peptides at the
cell surface</description>
        <go id="GO:0046776"/>
    </keyword>
    <keyword id="KW-1116">
        <name>Inhibition of host MHC class II molecule presentation by virus</name>
        <description>Viral protein involved in the evasion of host adaptive immune response
by inhibiting the presentation of loaded MHC class II molecules at the
cell surface. MHC class II molecules are found only on a few
specialized cells termed professional antigen-presenting cells (APCs)
This group includes macrophages, dendritic cells and B-cells. Many
viruses 'intercept' the loaded MHC class II molecules and retain them
in the endoplasmic reticulum or target them to degradation in order to
prevent presentation of the peptides at the cell surface</description>
        <go id="GO:0039505"/>
    </keyword>
    <keyword id="KW-1098">
        <name>Inhibition of host mitotic exit by virus</name>
        <description>Viral protein involved in the inhibition of host cell cycle
progression by preventing cells to exit mitosis</description>
        <go id="GO:0039593"/>
    </keyword>
    <keyword id="KW-1099">
        <name>Inhibition of host mRNA nuclear export by virus</name>
        <description>Viral protein involved in the disruption of the mRNA nuclear export
machinery. Viruses have evolved ways of interacting with the nuclear
export machinery to inhibit cellular translation and maximize the
expression of their own mRNAs. This global inhibition of cellular
protein synthesis serves to ensure maximal viral gene expression and
to evade host immune response</description>
        <go id="GO:0039522"/>
    </keyword>
    <keyword id="KW-1100">
        <name>Inhibition of host NF-kappa-B by virus</name>
        <description>Viral protein involved in the inhibition of host NF-kappa-B. This
protein is a pleiotropic transcription factor which is present in
almost all cell types and is involved in many biological processes
such as inflammation, immunity, differentiation, cell growth,
tumorigenesis and apoptosis. Many viruses have developed strategies to
inhibit the NF-kappa-B pathway in order to evade host immunity and
inhibit production of proinflammatory cytokines</description>
        <go id="GO:0085034"/>
    </keyword>
    <keyword id="KW-1102">
        <name>Inhibition of host PKR by virus</name>
        <description>Viral protein involved in the evasion of the interferon pathway by
inhibiting the interferon induced PKR/EIF2AK2 protein. During viral
replication of RNA viruses, dsRNA is produced leading to the
activation of the PKR/EIF2AK2 kinase. Once activated, PKR/EIF2AK2
autophosphorylates and catalyzes the phosphorylation of many
substrates including the translation initiation factor EIF2S1, leading
to the inhibition of the initiation of protein synthesis. Several
viral proteins prevent PKR/EIF2AK2 activation by direct interaction
while others target PKR/EIF2AK2 to degradation</description>
        <go id="GO:0039580"/>
        <go id="GO:0030291"/>
    </keyword>
    <keyword id="KW-1101">
        <name>Inhibition of host poly(A)-binding protein by virus</name>
        <description>Viral protein involved in the inhibition of host translation by
inhibiting the poly(A)-binding protein PABPC1. Viruses have evolved
ways of interacting with the host translational machinery to shutoff
host gene expression. This global inhibition of cellular protein
synthesis serves to ensure maximal viral gene expression and to evade
host immune response. One common target is the translation initiation
factor PABPC1. Some viruses proteolytically cleave PABPC1, while
others displace PABPC1 from EIF4G1</description>
        <go id="GO:0039604"/>
    </keyword>
    <keyword id="KW-1103">
        <name>Inhibition of host pre-mRNA processing by virus</name>
        <description>Viral protein involved in the disruption of host pre-mRNA processing
Viruses have evolved ways of interacting with the cellular RNA
splicing machinery and regulate splicing of cellular pre-mRNAs as a
part of the mechanism for shutting down the synthesis of host
proteins. This global inhibition of cellular protein synthesis serves
to ensure maximal viral gene expression and to evade host immune
response</description>
        <go id="GO:0039524"/>
    </keyword>
    <keyword id="KW-1088">
        <name>Inhibition of host RIG-I by virus</name>
        <description>Viral protein involved in the evasion of host innate defense by
inhibiting the DDX58/RIG-I protein. Upon recognition of viral RNA, the
cytosolic receptor DDX58/RIG-I initiates an antiviral signaling
cascade by interacting with downstream partners. Several viral
proteins inhibit DDX58/RIG-I via direct interaction while others via
proteolytic cleavage</description>
        <go id="GO:0039540"/>
    </keyword>
    <keyword id="KW-1113">
        <name>Inhibition of host RLR pathway by virus</name>
        <description>Viral protein involved in the evasion of host innate defense by
inhibiting the DDX58/RIG-I-like receptor (RLR) pathway leading to the
triggering of interferon-mediated response. This pathway starts with
the recognition of viral RNA by host proteins including DDX58/RIG-I or
IFIH1. Then, the signal is transmitted through MAVS and TRAFs leading
to the activation and nuclear localization of transcription factors
IRF3 and IRF7 to induce IFNalpha/beta transcription and protein
production. Many viruses interact with components of this pathway to
inhibit production of interferons and establishment of the antiviral
state</description>
        <go id="GO:0039532"/>
    </keyword>
    <keyword id="KW-1104">
        <name>Inhibition of host RNA polymerase II by virus</name>
        <description>Viral protein involved in the disruption of the host RNA polymerase
II. Many viruses induce alterations in the cellular gene expression
Among these, shutoff of host transcription by targeting RNA polymerase
II is commonly used. Indeed, many viruses are able to modify RNAP II
CTD including Herpes virus, HIV, Epstein-Barr virus or Bunyamwera
virus</description>
        <go id="GO:0039523"/>
    </keyword>
    <keyword id="KW-1105">
        <name>Inhibition of host STAT1 by virus</name>
        <description>Viral protein involved in the evasion of the type I, II and III
interferon pathways by inhibiting the STAT1 protein. Upon viral
infection, STAT1 is activated by IFN-gamma, IFN-alpha/beta, or IFN-
lambda that bind to specific cell surface receptors. While IFN-gamma
induces STAT1 homodimerization, IFN-alpha/beta and IFN-lambda
stimulate heterodimerization of STAT1 and STAT2, both leading to STAT1
nuclear localization and subsequent induction of IFN-stimulated genes
Many viruses interfere with STAT1 activation, often by preventing
STAT1 phosphorylation and nuclear localization</description>
        <go id="GO:0039563"/>
    </keyword>
    <keyword id="KW-1106">
        <name>Inhibition of host STAT2 by virus</name>
        <description>Viral protein involved in the evasion of type I and III interferon
pathways by inhibiting STAT2 protein. Upon viral infection, STAT2 is
activated by IFN-alpha/beta or IFN-lambda that bind to specific cell
surface receptors. In turn, IFN-alpha/beta (or IFN-lambda) induces
heterodimerization of STAT1 and STAT2 by phosphorylation, leading to
STAT2 nuclear localization and subsequent induction of IFN-stimulated
genes. Many viruses interfere with STAT2 activation, often by
preventing STAT2 phosphorylation and nuclear localization</description>
        <go id="GO:0039564"/>
    </keyword>
    <keyword id="KW-1107">
        <name>Inhibition of host TAP by virus</name>
        <description>Viral protein involved in the evasion of host adaptive immune response
by inhibiting the TAP complex. Transporter associated with antigen
(TAP), composed of two subunits TAP1 and TAP2, is required for the
translocation of peptides into the ER, where they are loaded onto MHC
class I. Thereafter, the viral peptides are presented to cytotoxic T
lymphocytes at the cell surface and trigger immune response. The
loading of peptide on MHC by TAP is targeted by several viruses
including herpesviruses and retroviruses</description>
        <go id="GO:0039588"/>
    </keyword>
    <keyword id="KW-1108">
        <name>Inhibition of host tapasin by virus</name>
        <description>Viral protein involved in the evasion of host adaptive immune response
by inhibiting the tapasin/TAPBP protein. tapasin/TAPBP is a type I
transmembrane protein essential for the optimal expression of stable
MHC class I molecules on host cell surface. Its helps the MHC class I
molecules to remain in a peptide receptive state, avoiding
irreversible denaturation. Several retroviruses and DNA viruses encode
proteins interacting with tapasin/TAPBP and inhibiting its activity</description>
        <go id="GO:0046776"/>
    </keyword>
    <keyword id="KW-1223">
        <name>Inhibition of host TBK1 by virus</name>
        <description>Viral protein involved in the evasion of host innate defenses by
inhibiting the TBK1 kinase. Upon viral infection, Toll-like receptors
(TLRs) or DNA recognition receptors recognize foreign material and
transmit the signal to TBK1 that in turn phosphorylates and activates
IRF3 and IRF7. Once phosphorylated, IRF3 and/or IRF7 translocate into
the nucleus to drive transcription of interferons. Several viruses
including herpes simplex virus 1 or vaccinia virus interact directly
with and inhibit TBK1 to prevent IRFs activation</description>
        <go id="GO:0039723"/>
    </keyword>
    <keyword id="KW-1084">
        <name>Inhibition of host tetherin by virus</name>
        <description>Viral protein involved in the evasion of host immune defense by
inhibiting the BST2/tetherin protein. BST2/tetherin is an alpha
interferon-inducible cellular factor that impairs the release of many
enveloped viruses, including human immunodeficiency virus type 1 (HIV-
1), HIV-2, as well as other retroviruses. Several viruses manage to
circumvent the antiviral activity of BST2/tetherin either by sending
BST2/tetherin to degradation (HIV-1) or by lowering the presence of
BST2 on cell surfaces (HIV-2)</description>
        <go id="GO:0039587"/>
    </keyword>
    <keyword id="KW-1225">
        <name>Inhibition of host TLR pathway by virus</name>
        <description>Viral protein involved in the evasion of host innate defenses by
inhibiting the Toll-like recognition receptor (TLR) pathway. This
pathway usually starts with the recognition of viruses by host TLRs
including TLR3 or TLR4. Then, the signal is transmitted through MYD88
(or TRIF) and then to TBK1 leading to the activation and nuclear
localization of transcription factors IRF3 and/or IRF7 to induce
IFNalpha/beta transcription and production of proinflammatory
cytokines through activation of the NF-kappaB signaling pathway. Many
viruses interact with components of this pathway to inhibit production
of interferons and establishment of the antiviral state</description>
        <go id="GO:0039722"/>
    </keyword>
    <keyword id="KW-1110">
        <name>Inhibition of host TRAFs by virus</name>
        <description>Viral protein involved in the evasion of host innate defense by
inhibiting TRAF proteins. After viral infection, the cellular
signaling pathway leading to production of interferons is activated
and several TRAF family members including TRAF2, TRAF3, and TRAF5
participate in this cascade. Many viruses encode protein able to
interact with TRAF members to inhibit their antiviral activity</description>
        <go id="GO:0039527"/>
    </keyword>
    <keyword id="KW-1112">
        <name>Inhibition of host TYK2 by virus</name>
        <description>Viral protein involved in the evasion of the type I and III interferon
pathways by inhibiting the host TYK2 protein. Upon viral infection,
the TYK2 protein is activated by IFNalpha/beta or IFN-lambda
stimulation leading to a series of phosphorylation events that induce
transcription of several hundred IFN-responsive genes. Several viruses
have evolved mechanisms to inhibit TYK2 activity thereby preventing
the subsequent activation of downstream partners STAT1 and STAT2</description>
        <go id="GO:0039574"/>
    </keyword>
    <keyword id="KW-0396">
        <name>Initiation factor</name>
        <name>Translation initiation factor</name>
        <description>Protein which plays an important role in initiating the translation of
a mRNA molecule into a polypeptide. Initiation factors help to form
the complex between the mRNA and a ribosome</description>
        <go id="GO:0003743"/>
        <go id="GO:0006413"/>
    </keyword>
    <keyword id="KW-0399">
        <name>Innate immunity</name>
        <description>Protein involved in innate immunity, an inborn defense mechanism used
by organisms to defend themselves against invasion by pathogens
(bacteria, fungi, viruses, etc.). Initially discovered in insects
which are devoid of an adaptive immune system and rely only on innate
immune reactions for their defense, this immediate response
accomplishes many activities including recognition and effector
functions. Recognition is mediated by broad specificity, pattern
recognition, receptors which recognize many related molecular
structures (e.g. polysaccharides, polynucleotides) present in
microorganisms but not found in the host. The innate responses include
the release of antimicrobial peptides, production of cytokines, acute-
phase proteins, complement. Although many different innate immune
mechanisms are deployed for host defence, a unifying theme of innate
immunity is the use of germline-encoded pattern recognition receptors
for pathogens or damaged self components, such as the Toll-like
receptors, nucleotide-binding domain leucine-rich repeat (LRR)-
containing receptors, retinoic acid-inducible gene I-like RNA
helicases and C-type lectin receptors</description>
        <go id="GO:0045087"/>
    </keyword>
    <keyword id="KW-1153">
        <name>Inner capsid protein</name>
        <description>Viral protein that is a component of the inner layer of a double or
triple concentric icosahedral capsid. Inner capsids are part of
reoviridae and cystoviridae virions</description>
        <go id="GO:0039625"/>
    </keyword>
    <keyword id="KW-0398">
        <name>Inositol biosynthesis</name>
        <name>Inositol biosynthetic process</name>
        <name>Inositol synthesis</name>
        <name>Inositol anabolism</name>
        <name>Inositol formation</name>
        <description>Protein involved in the synthesis of inositol, a cyclic hexahydric
alcohol. It occurs in various forms, of which myo-inositol, a
constituent of phospholipids, is the most important</description>
        <go id="GO:0006021"/>
    </keyword>
    <keyword id="KW-0978">
        <name>Insecticide resistance</name>
        <name>Resistance to insecticide</name>
        <description>Protein that confers, on insect vectors and pests, the ability to
withstand insecticide action. Insecticides are chemicals that
selectively kill insects. Insecticide resistance usually occurs by two
broad mechanisms. The first is where the insect may produce large
amounts of enzymes, such as esterases which either break down the
insecticide molecule or bind to it so tightly that it cannot function
(a process known as sequestration). The second mechanism involves
mutation of the insecticide target site, such as the
acetylcholinesterase enzyme in the nervous system. This effectively
blocks the action of the insecticide</description>
    </keyword>
    <keyword id="KW-0401">
        <name>Integrin</name>
        <description>Protein of the integrin family of cell surface heterodimeric receptors
that mediates dynamic cell-to-cell as well as cell-to-matrix adhesion
Integrins function as mechanochemical sensors and transducers able to
change rapidly and reversibly their adhesive functions by modulating
their ligand-binding affinity. Each subunit has a large N-terminal
extracellular domain followed by a transmembrane domain and a short C-
terminal cytoplasmic region. Some subclasses of integrins share a
common beta chain while having different alpha chains</description>
        <go id="GO:0007229"/>
    </keyword>
    <keyword id="KW-0991">
        <name>Intellectual disability</name>
        <name>Mental deficiency</name>
        <name>Mental retardation</name>
        <name>Mental subnormality</name>
        <description>Protein which, if defective, is involved in intellectual disability, a
disorder appearing during development and characterized by subnormal
intellectual functioning and impaired adaptive behavior</description>
    </keyword>
    <keyword id="KW-0922">
        <name>Interferon antiviral system evasion</name>
        <name>Antiviral state evasion</name>
        <name>Interferon response evasion</name>
        <description>Viral protein which prevents the activation of the antiviral state
induced by interferon (IFN) in the host cell, thereby allowing the
virus to replicate optimally. The antiviral state is the result of a
signaling pathway induced by IFN-alpha or IFN-beta following viral
infection. It leads to the transcription of various cellular antiviral
genes coding for host defense proteins</description>
        <go id="GO:0019049"/>
    </keyword>
    <keyword id="KW-1154">
        <name>Intermediate capsid protein</name>
        <description>Viral protein that is a component of the intermediate layer of a
triple concentric icosahedral capsid. Intermediate capsids are part of
reoviridae virions</description>
        <go id="GO:0039626"/>
    </keyword>
    <keyword id="KW-0403">
        <name>Intermediate filament</name>
        <description>Intermediate filaments (IF) are proteins which are primordial
components of the cytoskeleton and the nuclear envelope. They
generally form filamentous structures 8 to 14 nm wide and intermediate
in size between microtubules and microfilaments. This family of
protein includes cytokeratins, vimentin, desmin, glial fibrillary
acidic protein, neurofilament proteins and nestin. All IF proteins are
structurally similar in that they consist of: a central rod domain
which is arranged in coiled-coiled alpha-helices, with at least two
short characteristic interruptions; an N-terminal non-helical domain
(head) of variable length; and an C-terminal domain (tail) which is
also non-helical and shows extreme length variation between different
IF proteins</description>
        <go id="GO:0005882"/>
    </keyword>
    <keyword id="KW-0988">
        <name>Intrahepatic cholestasis</name>
        <description>Protein which, if defective, causes intrahepatic cholestasis, a
condition characterized by stoppage or suppression of the bile flow
from the liver to the duodenum without extrahepatic bile duct
obstruction</description>
    </keyword>
    <keyword id="KW-0404">
        <name>Intron homing</name>
        <name>Intron transposition</name>
        <description>Endonucleases involved in intron homing, a genetic event leading to
the transfer of an intron DNA sequence. This type of intron mobility
depends on site-specific restriction endonucleases encoded by the
mobile introns</description>
        <go id="GO:0006314"/>
    </keyword>
    <keyword id="KW-0405">
        <name>Iodination</name>
        <name>Iodinated</name>
        <description>Protein which is posttranslationally modified by the replacement of at
least one hydrogen by iodine</description>
    </keyword>
    <keyword id="KW-0407">
        <name>Ion channel</name>
        <description>Protein which is part of a transmembrane protein complex that forms a
hydrophilic channel across the lipid bilayer through which specific
inorganic ions can diffuse down their electrochemical gradients. The
channels are usually gated and only open in response to a specific
stimulus, such as a change in membrane potential (voltage-gated) or
the binding of a ligand (ligand-gated channel)</description>
        <go id="GO:0034220"/>
        <go id="GO:0034702"/>
    </keyword>
    <keyword id="KW-0872">
        <name>Ion channel impairing toxin</name>
        <description>Protein which interferes with the function of ion channels, which are
hydrophilic channels across the lipid bilayer through which specific
inorganic ions can diffuse down their electrochemical gradients</description>
        <go id="GO:0099106"/>
    </keyword>
    <keyword id="KW-0406">
        <name>Ion transport</name>
        <description>Protein involved in the transport of ions. Such proteins are usually
transmembrane and mediate a movement of ions across cell membranes
Transport may be passive (facilitated diffusion; down the
electrochemical gradient), or active (against the electrochemical
gradient). Active transport requires energy which may come from light,
oxidation reactions, ATP hydrolysis, or cotransport of other ions or
molecules</description>
        <go id="GO:0006811"/>
    </keyword>
    <keyword id="KW-1028">
        <name>Ionotropic glutamate receptor inhibitor</name>
        <description>Protein that inhibits ionotropic glutamate receptor (iGluR). iGluRs
are glutamate-gated ion channels that mediate excitatory
neurotransmission in the central nervous system. Based on both
molecular and pharmacological criteria, iGluRs have been divided into
two major classes, the non-NMDA class, which includes both AMPA and
kainate subtypes of receptors, and the NMDA class</description>
    </keyword>
    <keyword id="KW-0408">
        <name>Iron</name>
        <name>Fe cation</name>
        <name>Iron ion</name>
        <name>Fe ion</name>
        <name>Iron cation</name>
        <name>Fe</name>
        <description>Protein which binds at least one iron atom, or protein whose function
is iron-dependent. Iron is a metal, chemical symbol Fe</description>
    </keyword>
    <keyword id="KW-0409">
        <name>Iron storage</name>
        <description>Protein involved in the storage of iron</description>
        <go id="GO:0006879"/>
    </keyword>
    <keyword id="KW-0410">
        <name>Iron transport</name>
        <name>Iron ion transport</name>
        <name>Iron cation transport</name>
        <name>Fe transport</name>
        <description>Protein involved in the transport of iron</description>
        <go id="GO:0006826"/>
    </keyword>
    <keyword id="KW-0411">
        <name>Iron-sulfur</name>
        <name>Iron-sulfur cluster</name>
        <description>Protein which binds at least one iron-sulfur cluster, e.g. 2Fe-2S,
3Fe-4S, 4Fe-4S</description>
        <go id="GO:0051536"/>
    </keyword>
    <keyword id="KW-0412">
        <name>Isoleucine biosynthesis</name>
        <name>Isoleucine anabolism</name>
        <name>Isoleucine biosynthetic process</name>
        <name>Isoleucine formation</name>
        <name>Isoleucine synthesis</name>
        <description>Protein involved in the synthesis of the hydrophobic amino acid
isoleucine</description>
        <go id="GO:0009097"/>
    </keyword>
    <keyword id="KW-0413">
        <name>Isomerase</name>
        <description>Enzyme that catalyzes the 1,1-, 1,2- or 1,3-hydrogen shift. The 1,1-
hydrogen shift is an inversion at an asymmetric carbon center
(racemases, epimerases). The 1,2-hydrogen shift involved a hydrogen
transfer between two adjacent carbon atoms, one undergoing oxidation,
the other reduction (aldose-ketose isomerases). The 1,3-hydrogen
shifts are allylic or azaallylic (when nitrogen is one of the three
atoms) isomerizations</description>
        <go id="GO:0016853"/>
    </keyword>
    <keyword id="KW-1017">
        <name>Isopeptide bond</name>
        <description>Protein which is posttranslationally modified by the formation of an
amide bond between an amino-group and a carboxyl-group at least one of
which is not an alpha group. An isopeptide bond involves the side
chain of one or two amino acid residues. Because there are few enzymes
that hydrolyze isopeptide bonds, the formation of interchain
isopeptide bonds can produce stably linked protein dimers, multimers
or complexes, such as blood clots</description>
    </keyword>
    <keyword id="KW-0414">
        <name>Isoprene biosynthesis</name>
        <name>Isoprene anabolism</name>
        <name>Isoprene biosynthetic process</name>
        <name>Isoprene synthesis</name>
        <name>Isoprene formation</name>
        <description>Protein involved in the synthesis of isoprene, an important organic
unit of 5 carbons in plants. It is used to build up isoprenoids,
including carotenoids, terpenes and natural rubber</description>
        <go id="GO:0008299"/>
    </keyword>
    <keyword id="KW-1184">
        <name>Jasmonic acid signaling pathway</name>
        <name>JA mediated signaling</name>
        <name>Jasmonate signaling pathway</name>
        <name>Jasmonic acid mediated signaling</name>
        <name>JA signaling pathway</name>
        <name>Jasmonate mediated signaling</name>
        <description>Protein involved in the jasmonic acid (jasmonate, JA) signaling
pathway (e.g. transport and signal transduction) that regulates many
aspects of plant growth, development and cellular signaling (e.g
growth inhibition, senescence, tuber formation, response to wounding,
plant defense, and leaf abscission). This phytohormone and its
derivatives such as methyl jasmonate (MeJA) can be synthesized from
the fatty acid linolenic acid in the oxylipin octadecanoid pathway</description>
    </keyword>
    <keyword id="KW-0979">
        <name>Joubert syndrome</name>
        <name>Cerebellar vermis agenesis</name>
        <name>Joubert-Boltshauser syndrome</name>
        <name>JBTS</name>
        <name>Cerebelloparenchymal disorder IV</name>
        <name>JS</name>
        <name>CPD IV</name>
        <description>Protein which, if defective, causes Joubert syndrome, an autosomal
recessive multisystem disorder characterized by cerebellar ataxia,
developmental delay, hypotonia, neonatal breathing abnormalities and
oculomotor apraxia. Neuroradiologically, it is characterized by
cerebellar vermis hypoplasia/aplasia, thickened and reoriented
superior cerebellar peduncles, and an abnormally large interpeduncular
fossa, giving the appearance of the 'molar tooth sign' on transaxial
slices. A wide clinical variability with a marked variation in
severity and inconsistent presence of the following features is
observed: episodic apnea-hyperpnea, abnormal eye movements, occipital
meningoencephalocele, polydactyly, nephronophthisis or cystic
dysplasia of the kidney, chorioretinal coloboma and retinal dysplasia
The variable association of ocular and renal abnormalities with
cerebellar features typical of Joubert syndrome defines the cerebello-
oculo-renal syndromes (CORSs)</description>
    </keyword>
    <keyword id="KW-0956">
        <name>Kallmann syndrome</name>
        <name>HHA</name>
        <name>KMS</name>
        <name>Hypogonadotropic hypogonadism and anosmia</name>
        <name>Kallmann's syndrome</name>
        <name>Kallmann de Morsier syndrome</name>
        <name>Dysplasia olfactogenitalis of De Morsier</name>
        <description>Protein which, if defective, causes Kallmann syndrome, a disorder
characterized by the association of hypogonadotropic hypogonadism with
anosmia or hyposmia. Kallmann syndrome is caused by impaired embryonic
development of the olfactory system and the GnRH-synthesizing neurons
The main clinical features consist of the association of micropenis
and cryptorchidism in young boys, the absence of spontaneous puberty,
and a partial or total loss of the sense of smell (anosmia). In some
patients other developmental anomalies can be present such as renal
agenesis, cleft lip/palate, selective tooth agenesis and bimanual
synkinesis</description>
    </keyword>
    <keyword id="KW-1012">
        <name>Kartagener syndrome</name>
        <name>KTGS</name>
        <name>Dextrocardia-bronchiectasis-sinusitis syndrome</name>
        <name>Siewert syndrome</name>
        <description>Protein which, if defective, causes Kartagener syndrome, a rare and
genetically heterogeneous disorder characterized by the combination of
primary ciliary dyskinesia and situs inversus viscerum</description>
    </keyword>
    <keyword id="KW-0415">
        <name>Karyogamy</name>
        <description>Protein involved in the fusion of the nuclei of two gametes after
cytoplasmic fusion</description>
        <go id="GO:0000741"/>
    </keyword>
    <keyword id="KW-0880">
        <name>Kelch repeat</name>
        <description>Protein containing at least one Kelch repeat</description>
    </keyword>
    <keyword id="KW-0416">
        <name>Keratin</name>
        <description>Fibrous proteins rich in cysteine and the chief constituent of horn,
nails, hair, epidermis and feathers. Two major conformational groups
have been characterized, alpha-keratin, whose peptide backbone forms
an alpha-helix, and beta-keratin, whose backbone forms a zigzag or
pleated sheet structure</description>
        <go id="GO:0005882"/>
    </keyword>
    <keyword id="KW-0417">
        <name>Keratinization</name>
        <description>Protein involved in keratinization, the process in which the cytoplasm
of the outermost cells of the vertebrate epidermis is replaced by
keratin. Keratinization occurs in the stratum corneum, feathers, hair,
claws, nails, hooves, and horns</description>
        <go id="GO:0031424"/>
    </keyword>
    <keyword id="KW-0418">
        <name>Kinase</name>
        <name>Phosphotransferase</name>
        <description>Enzyme that catalyzes the transfer of phosphate (phosphoryl or
pyrophosphoryl transfer) usually from ATP to a second substrate</description>
        <go id="GO:0016301"/>
    </keyword>
    <keyword id="KW-0995">
        <name>Kinetochore</name>
        <description>The kinetochore is a complex assembled at centromeric region of DNA,
which provides the major attachment point for the spindle
microtubules. In monocentric chromosomes, the kinetochores of point
centromeres bind a single microtubule and the larger kinetochores of
regional centromeres interact with a number of microtubules. In
holocentric chromosomes, the kinetochores bind the diffuse centromere
along the length of the chromosomes</description>
        <go id="GO:0000776"/>
    </keyword>
    <keyword id="KW-0419">
        <name>Kinetoplast</name>
        <description>Protein associated with the kinetoplast DNA (kDNA), the mitochondrial
DNA of trypanosomatid protozoa. kDNA is a massive network, composed of
thousands of topologically interlocked DNA circles. Each cell contains
one network condensed into a disk-shaped structure within the matrix
of its single mitochondrion. The kDNA circles are of two types,
maxicircles present in a few dozen copies and minicircles present in
several thousand copies</description>
    </keyword>
    <keyword id="KW-0960">
        <name>Knottin</name>
        <name>ICK</name>
        <name>Inhibitor Cystine Knot</name>
        <description>Small disulfide-rich protein characterized by a special 'disulfide
through disulfide knot'. This knot is obtained when one disulfide
bridge crosses the macrocycle formed by two other disulfides and the
interconnecting backbone (disulfide III-VI goes through disulfides I-
IV and II-V). The knottin structure is found in some plant protease
inhibitors, cyclotides, toxins from cone snails, spiders, insects,
horseshoe crabs and scorpions, gurmarin-like peptides, agouti-related
proteins, and some antimicrobial peptides</description>
    </keyword>
    <keyword id="KW-0420">
        <name>Kringle</name>
        <description>Protein containing at least one kringle domain, a triple-looped,
disulfide cross-linked domain of approximately 80 amino acids in
length and involved in protein-protein interactions</description>
    </keyword>
    <keyword id="KW-0953">
        <name>Lacrimo-auriculo-dento-digital syndrome</name>
        <name>LADD syndrome</name>
        <name>Lacrimoauriculodentodigital syndrome</name>
        <name>Levy-Hollister syndrome</name>
        <description>Protein which, if defective, causes lacrimo-auriculo-dento-digital
syndrome. Lacrimo-auriculo-dento-digital syndrome, a form of
ectodermal dysplasia, is an autosomal dominant multiple congenital
anomaly. It is characterized by aplastic/hypoplastic lacrimal and
salivary glands and ducts, cup-shaped ears, hearing loss, hypodontia
and enamel hypoplasia, and distal limb segments anomalies. In addition
to these cardinal features, facial dysmorphism, malformations of the
kidney and respiratory system and abnormal genitalia have been
reported. Craniosynostosis and severe syndactyly are not observed</description>
    </keyword>
    <keyword id="KW-0421">
        <name>Lactation</name>
        <description>Protein involved in lactation, the secretion of milk by mammary
glands</description>
        <go id="GO:0007595"/>
    </keyword>
    <keyword id="KW-0422">
        <name>Lactose biosynthesis</name>
        <name>Lactose formation</name>
        <name>Lactose biosynthetic process</name>
        <name>Lactose anabolism</name>
        <name>Lactose synthesis</name>
        <description>Protein involved in the synthesis of lactose, a disaccharide of
glucose and galactose present in milk</description>
        <go id="GO:0005989"/>
    </keyword>
    <keyword id="KW-0423">
        <name>Lactose metabolism</name>
        <name>Lactose metabolic process</name>
        <description>Protein involved in the biochemical reactions with lactose, a
disaccharide of glucose and galactose, found in milk</description>
        <go id="GO:0005988"/>
    </keyword>
    <keyword id="KW-0424">
        <name>Laminin EGF-like domain</name>
        <description>Protein containing at least one laminin EGF-like domain. Laminins are
the major noncollagenous components of basement membranes. Their
subunits contain consecutive repeats of about 60 amino acids, which
include 8 conserved cysteines that form disulfide bonds (C1-C3, C2-C4,
C5-C6, C7-C8). The tertiary structure of this domain is remotely
similar, in its N-terminal, to that of the EGF-like module</description>
    </keyword>
    <keyword id="KW-0425">
        <name>Lantibiotic</name>
        <description>Lanthionine-containing peptide antibiotics are peptides produced by
Gram-positive bacteria which cause cell death of other Gram-positive
bacteria</description>
        <go id="GO:0005102"/>
        <go id="GO:0031640"/>
    </keyword>
    <keyword id="KW-0426">
        <name>Late protein</name>
        <description>Bacteriophage or viral protein expressed in a later phase of the
infectious cycle</description>
    </keyword>
    <keyword id="KW-1252">
        <name>Latency-replication decision</name>
        <description>Viral protein part of a genetic system that takes part in the decision
of the outcome of the infection: latency or replication. Expression of
genetic switch proteins control the expression of viral genes that act
as effectors in either the establishment of latency (lysogeny) or in
promoting productive replication (lytic cycle). Interactions between
proteins involved in switch regulatory processes and host proteins
often influence the decision</description>
        <go id="GO:0098689"/>
    </keyword>
    <keyword id="KW-0427">
        <name>LDL</name>
        <description>Protein constituent of the low-density lipoproteins or protein which
binds LDLs. LDLs are plasma lipoproteins rich in cholesterol esters,
synthesized from the very low-density lipoprotein (VLDL), and which
transport cholesterol to peripheral tissue and regulate de novo
cholesterol synthesis</description>
        <go id="GO:0034362"/>
    </keyword>
    <keyword id="KW-1027">
        <name>Lead</name>
        <name>Lead cation</name>
        <name>Lead ion</name>
        <name>Pb</name>
        <name>Pb ion</name>
        <name>Pb cation</name>
        <description>Protein which binds at least one lead atom, or protein whose function
is lead-dependent. Lead is a metal, chemical symbol Pb</description>
    </keyword>
    <keyword id="KW-0428">
        <name>Leader peptide</name>
        <description>Short peptide sequences translated from bacterial leader RNA sequences
which are involved in transcriptional or translation attenuation,
mechanisms that modulate mRNA transcription or translation</description>
    </keyword>
    <keyword id="KW-0901">
        <name>Leber congenital amaurosis</name>
        <description>Protein which, if defective, causes Leber congenital amaurosis, a
clinically and genetically heterogeneous type of blindness transmitted
as an autosomal recessive trait and occurring at or shortly after
birth. It is associated with an atypical form of diffuse pigmentation
and commonly with optic atrophy and attenuation of the retinal
vessels</description>
    </keyword>
    <keyword id="KW-0429">
        <name>Leber hereditary optic neuropathy</name>
        <description>Protein which, if defective, causes Leber hereditary optic neuropathy,
a mitochondrial disease leading to bilateral, painless loss of central
vision due to selective degeneration of the retinal ganglion cells and
their axons. The disease arises during young adult life and displays
sex-dependent incomplete penetrance and male predominance</description>
    </keyword>
    <keyword id="KW-0430">
        <name>Lectin</name>
        <description>Protein which specifically binds carbohydrates. Lectins are obtained
particularly from seeds of leguminous plants but also from other plant
and animal sources. They contain binding sites for specific mono-and
oligosaccharides. They agglutinate cells by binding to specific sugar
residues in membrane glycoproteins</description>
        <go id="GO:0030246"/>
    </keyword>
    <keyword id="KW-0431">
        <name>Leigh syndrome</name>
        <description>Protein which, if defective, causes Leigh syndrome, a
neurodegenerative disorder characterized by the subacute onset of
psychomotor retardation, hypotonia, ataxia, weakness, vision loss, eye
movement abnormalities, seizures, dysphagia, and lactic acidosis
Pathological features include spongy degeneration of the neuropile of
the basal ganglia, thalamus, brain stem, and spinal cord. The syndrome
is caused by a variety of defects of enzymes involved in energy
metabolism, including cytochrome c oxidase (COX), the mitochondrial
encoded ATP6 subunit of ATP synthase, and the X-linked E1-alpha
subunit of pyruvate dehydrogenase</description>
    </keyword>
    <keyword id="KW-0432">
        <name>Leucine biosynthesis</name>
        <name>Leucine anabolism</name>
        <name>Leucine formation</name>
        <name>Leucine biosynthetic process</name>
        <name>Leucine synthesis</name>
        <description>Protein involved in the synthesis of the hydrophobic amino acid
leucine</description>
        <go id="GO:0009098"/>
    </keyword>
    <keyword id="KW-0433">
        <name>Leucine-rich repeat</name>
        <name>LRR</name>
        <description>Protein containing at least one leucine-rich repeat (LRR)</description>
    </keyword>
    <keyword id="KW-1026">
        <name>Leukodystrophy</name>
        <description>Protein which, if defective, causes leukodystrophy, any of a group of
diseases that affect the formation or maintenance of myelin in the
central nervous system</description>
    </keyword>
    <keyword id="KW-0434">
        <name>Leukotriene biosynthesis</name>
        <name>Leukotriene formation</name>
        <name>Leukotriene anabolism</name>
        <name>Leukotriene biosynthetic process</name>
        <name>Leukotriene synthesis</name>
        <description>Protein involved in the synthesis of leukotrienes, eicosanoid hormones
first isolated from leukocytes. They are thought to mediate the
allergic response that causes lung constriction and muscle contraction
in asthma</description>
        <go id="GO:0019370"/>
    </keyword>
    <keyword id="KW-0435">
        <name>Li-Fraumeni syndrome</name>
        <name>Sarcoma family syndrome of Li and Fraumeni</name>
        <name>LFS</name>
        <name>SBLA syndrome</name>
        <description>Protein which, if defective, causes Li-Fraumeni syndrome (LFS), an
autosomal dominant familial cancer predisposition syndrome associated
with soft-tissue sarcoma, breast cancer, leukemia, osteosarcoma,
melanoma, and cancer of the colon, pancreas, adrenal cortex and brain
Individuals with LFS are at increased risk for developing multiple
primary cancers</description>
    </keyword>
    <keyword id="KW-1071">
        <name>Ligand-gated ion channel</name>
        <name>LGIC</name>
        <name>Ligand-gated channel</name>
        <description>Protein which forms or is a component of a ligand-gated channel
Ligand-gated channels are transmembrane ion channels whose
permeability is increased by the binding of a specific ligand, such as
neurotransmitters, ionositol triphosphates, and cyclic nucleotides</description>
    </keyword>
    <keyword id="KW-0436">
        <name>Ligase</name>
        <description>Enzyme that catalyzes the joining of two molecules coupled with the
breakdown of a pyrophosphate bond in ATP or a similar triphosphate
Sometimes the terms "synthase", "synthetase" or "carboxylase" are also
used for this class of enzymes</description>
        <go id="GO:0016874"/>
    </keyword>
    <keyword id="KW-0437">
        <name>Light-harvesting polypeptide</name>
        <description>Proteins which form part of the antenna complex, a light-harvesting
system found in photosynthetic bacteria which absorb light radiation
and transfer the excitation energy to the reaction centres</description>
        <go id="GO:0030076"/>
    </keyword>
    <keyword id="KW-0438">
        <name>Lignin biosynthesis</name>
        <name>Lignin formation</name>
        <name>Lignin biosynthetic process</name>
        <name>Lignin synthesis</name>
        <name>Lignin anabolism</name>
        <description>Protein involved in the synthesis of lignin, a polymer of
phenylpropanoid subunits found in the walls of plant cells such as
xylem and sclerenchyma fibres. Lignin imparts strength to the wall and
protects against degradation by microorganisms</description>
        <go id="GO:0009809"/>
    </keyword>
    <keyword id="KW-0439">
        <name>Lignin degradation</name>
        <name>Lignin catabolism</name>
        <name>Lignin breakdown</name>
        <name>Lignin catabolic process</name>
        <description>Protein involved in the breakdown of lignin, a polymer of
phenylpropanoid subunits found in the walls of plant cells such as
xylem and sclerenchyma fibres. It imparts strength to the wall and
protects against degradation by microorganisms</description>
        <go id="GO:0046274"/>
    </keyword>
    <keyword id="KW-0440">
        <name>LIM domain</name>
        <name>LIM motif</name>
        <description>Protein which contains at least one LIM domain, a conserved cysteine-
rich domain of approximately 60 amino acids with seven conserved
cysteines and a histidine. The LIM domain binds two zinc ions and
seems to be involved in protein-protein interactions</description>
    </keyword>
    <keyword id="KW-0947">
        <name>Limb-girdle muscular dystrophy</name>
        <name>LGMD</name>
        <name>Muscular dystrophy limb-girdle type</name>
        <description>Protein which, if defective, causes limb-girdle muscular dystrophy, a
degenerative myopathy without nervous system involvement. The disease
is characterized by slowly progressive wasting and weakness of the
proximal muscles of arms and legs around the pelvic or shoulder
girdles, elevated creatine kinase levels and dystrophic features on
muscle biopsy. Onset of symptoms is in late childhood, adolescence or
even adult life. Limb-girdle muscular dystrophy is a genetically
heterogeneous disorder. Inheritance can be autosomal dominant or
autosomal recessive</description>
    </keyword>
    <keyword id="KW-0441">
        <name>Lipid A biosynthesis</name>
        <name>Lipid A biosynthetic process</name>
        <name>Lipid A formation</name>
        <name>Lipid A anabolism</name>
        <name>Lipid A synthesis</name>
        <description>Protein involved in the synthesis of lipid A (endotoxin), the
hydrophobic anchor of lipopolysaccharide (LPS). Lipid A is a
glucosamine-based phospholipid that makes up the outer monolayer of
the outer membranes of most Gram-negative bacteria</description>
        <go id="GO:0009245"/>
    </keyword>
    <keyword id="KW-0444">
        <name>Lipid biosynthesis</name>
        <name>Lipid biosynthetic process</name>
        <name>Lipid anabolism</name>
        <name>Lipid formation</name>
        <description>Protein involved in the synthesis of lipids, a diverse class of
compounds which are insoluble in water but soluble in organic
solvents. They include fats, oils, triacylglycerols, fatty acids,
glycolipids, phospholipids and steroids</description>
        <go id="GO:0008610"/>
    </keyword>
    <keyword id="KW-0442">
        <name>Lipid degradation</name>
        <name>Lipid catabolism</name>
        <name>Lipid catabolic process</name>
        <name>Lipid breakdown</name>
        <description>Protein involved in the breakdown of lipids, a diverse class of
compounds, insoluble in water but soluble in organic solvents, and
which include fats, oils, triacylglycerols, fatty acids, glycolipids,
phospholipids and steroids</description>
        <go id="GO:0016042"/>
    </keyword>
    <keyword id="KW-0551">
        <name>Lipid droplet</name>
        <name>Spherosome</name>
        <name>Lipid bodies</name>
        <name>Lipid body</name>
        <name>Oleosome</name>
        <name>Oil body</name>
        <name>Oil bodies</name>
        <name>Monolayer-surrounded lipid storage body</name>
        <name>Adiposome</name>
        <name>Lipid particle</name>
        <description>Protein characteristic of a lipid droplet, a dynamic cytoplasmic
organelle which consists of an heterogeneous macromolecular assembly
of lipids and proteins covered by a unique phospholipid monolayer
Lipid droplets may play a role in lipid metabolism and storage, and
they may be involved in the regulation of intracellular trafficking
and signal transduction</description>
    </keyword>
    <keyword id="KW-0443">
        <name>Lipid metabolism</name>
        <name>Lipid metabolic process</name>
        <description>Protein involved in the biochemical reactions of lipids. Lipids are a
diverse class of compounds which are insoluble in water but soluble in
organic solvents. They include fats, oils, triacylglycerols, fatty
acids, glycolipids, phospholipids and steroids</description>
        <go id="GO:0006629"/>
    </keyword>
    <keyword id="KW-0445">
        <name>Lipid transport</name>
        <description>Protein involved in the transport of lipids, a diverse class of
compounds which are insoluble in water but soluble in organic
solvents. They include fats, oils, triacylglycerols, fatty acids,
glycolipids, phospholipids and steroids</description>
        <go id="GO:0006869"/>
    </keyword>
    <keyword id="KW-0446">
        <name>Lipid-binding</name>
        <description>Protein which binds one or more lipids</description>
        <go id="GO:0008289"/>
    </keyword>
    <keyword id="KW-0448">
        <name>Lipopolysaccharide biosynthesis</name>
        <name>Lipopolysaccharide biosynthetic process</name>
        <name>Lipopolysaccharide synthesis</name>
        <name>Lipopolysaccharide anabolism</name>
        <name>Lipopolysaccharide formation</name>
        <description>Protein involved in the synthesis of lipopolysaccharides (LPS), the
main constituents of the outer cell wall of Gram-negative bacteria
LPS are composed of lipid molecules joined to polysaccharides and are
highly immunogenic</description>
        <go id="GO:0009103"/>
    </keyword>
    <keyword id="KW-0449">
        <name>Lipoprotein</name>
        <name>Lipidated</name>
        <description>Protein which is posttranslationally modified by the attachment of at
least one lipid or fatty acid, e.g. farnesyl, palmitate and myristate</description>
    </keyword>
    <keyword id="KW-0450">
        <name>Lipoyl</name>
        <description>Protein which contains at least one lipoyl-binding domain. Lipoic acid
is an essential cofactor for E2 acyltransferases and some other
proteins</description>
    </keyword>
    <keyword id="KW-0451">
        <name>Lissencephaly</name>
        <description>Protein which, if defective, causes lissencephaly, a brain
malformation characterized by the absence (agyria) or reduction
(pachygyria) of brain surface convolutions (gyri), in association with
abnormal organisation of the cortical layers. It results from neuronal
migration defects during embryogenesis. Two large groups can be
distinguished: classical lissencephaly (and its variants) and
cobblestone lissencephaly. Lissencephaly means "smooth brain"</description>
    </keyword>
    <keyword id="KW-0452">
        <name>Lithium</name>
        <name>Li cation</name>
        <name>Lithium cation</name>
        <name>Li</name>
        <name>Li ion</name>
        <name>Lithium ion</name>
        <description>Protein whose function is lithium-dependent. Lithium is an alkali
metal, chemical symbol Li</description>
    </keyword>
    <keyword id="KW-0454">
        <name>Long QT syndrome</name>
        <name>LQTS</name>
        <description>Protein which, if defective, causes the long QT syndrome, a heart
disease which manifests itself by a prolonged QT interval on the ECG
and, clinically, by a propensity for tachyarrhythmias, causing
syncopes and sudden cardiac death. LQTS may be drug-induced, but
mutations in genes coding for cardiac ion-channels are the cause of
the hereditary forms: Romano-Ward syndrome (RWS), and Jervell and
Lange-Nielsen Syndrome (JLNS)</description>
    </keyword>
    <keyword id="KW-0886">
        <name>LTQ</name>
        <name>Lysine topaquinone</name>
        <name>Lysine tyrosylquinone</name>
        <description>Protein which contains at least one lysine tyrosylquinone (LTQ) cross-
link modification. LTQ is formed by oxidation of the phenol ring of a
tyrosine to form tyrosylquinone (topaquinone) followed by covalent
cross-linking with a lysine residue</description>
    </keyword>
    <keyword id="KW-0455">
        <name>Luminescence</name>
        <name>Bioluminescence</name>
        <description>Protein involved in luminescence, the property of giving off light
without emitting a corresponding degree of heat</description>
        <go id="GO:0008218"/>
    </keyword>
    <keyword id="KW-0456">
        <name>Lyase</name>
        <description>Enzyme that catalyzes the cleavage of C-C, C-O, C-S, C-N or other
bonds by other means than by hydrolysis or oxidation, with two
substrates in one reaction direction, and one in the other. In the
latter direction, a molecule (of carbon dioxide, water, etc) is
eliminated, thus creating a new double bond or a new ring</description>
        <go id="GO:0016829"/>
    </keyword>
    <keyword id="KW-0457">
        <name>Lysine biosynthesis</name>
        <name>Lysine formation</name>
        <name>Lysine anabolism</name>
        <name>Lysine biosynthetic process</name>
        <name>Lysine synthesis</name>
        <description>Protein involved in the synthesis of the essential basic amino acid
lysine</description>
        <go id="GO:0009085"/>
    </keyword>
    <keyword id="KW-0458">
        <name>Lysosome</name>
        <description>Protein found in the lysosome, a membrane-limited organelle present in
all eukaryotic cells, which contains a large number of hydrolytic
enzymes that are used for the intracellular degradation of
macromolecules</description>
    </keyword>
    <keyword id="KW-0460">
        <name>Magnesium</name>
        <name>Mg ion</name>
        <name>Magnesium cation</name>
        <name>Magnesium ion</name>
        <name>Mg</name>
        <name>Mg cation</name>
        <description>Protein which binds at least one magnesium atom, or protein whose
function is magnesium-dependent. Magnesium is a metallic element,
chemical symbol Mg</description>
    </keyword>
    <keyword id="KW-1281">
        <name>Magnetosome</name>
        <description>Protein located in or on the magnetosome, a membrane-bound bacterial
organelle that envelops crystals of magnetic iron minerals in
magnetotactic bacteria. Magnetosomes form linear chains that align
along the cellular motility axis at midcell and function in bacterial
navigation along the Earth's magnetic field. They are formed by
invagination of the cell inner membrane; in some species they remain
connected to the inner membrane, in others they pinch off to form
independent intracellular vesicles</description>
    </keyword>
    <keyword id="KW-0461">
        <name>Malaria</name>
        <description>Protein involved in malaria, a human disease caused by Plasmodium, a
parasitic protozoan that grows by sexual reproduction in the Anopheles
mosquito</description>
    </keyword>
    <keyword id="KW-0462">
        <name>Maltose metabolism</name>
        <name>Maltose metabolic process</name>
        <description>Protein involved in the biochemical reactions with maltose, a
disaccharide of glucose. Maltose is produced by the hydrolysis of
starch</description>
        <go id="GO:0000023"/>
    </keyword>
    <keyword id="KW-0463">
        <name>Mandelate pathway</name>
        <description>Enzyme involved in the mandelate pathway. These enzymes enable various
microorganisms to grow using D(-)-, L(+)- or DL-mandelate (2-hydroxy-
2-phenylacetate) as the sole source of carbon and energy</description>
        <go id="GO:0018924"/>
    </keyword>
    <keyword id="KW-0464">
        <name>Manganese</name>
        <name>Mn</name>
        <name>Mn cation</name>
        <name>Mn ion</name>
        <name>Manganese cation</name>
        <name>Manganese ion</name>
        <description>Protein which binds at least one manganese atom, or protein whose
function is manganese-dependent. Manganese is a metallic element,
chemical symbol Mn</description>
    </keyword>
    <keyword id="KW-0465">
        <name>Mannose-binding</name>
        <description>Protein which binds mannose, a 6-carbon aldose sugar, that is found in
many glycoproteins and polysaccharides</description>
        <go id="GO:0005537"/>
    </keyword>
    <keyword id="KW-0466">
        <name>Maple syrup urine disease</name>
        <description>Protein which, if defective, causes maple syrup urine disease, an
autosomal recessive disorder characterized by mental and physical
retardation, feeding problems and a maple syrup odour to the urine</description>
    </keyword>
    <keyword id="KW-0467">
        <name>Mast cell degranulation</name>
        <description>Protein involved in mast cell degranulation. Mast cell is a large,
ovoid cell of hematopoietic lineage, with a centrally located nucleus
and numerous large, intensely basophilic granules. The binding of an
antigen to its specific immunoglobulin-E antibody on the mast cell
surface triggers the release of the MC granules. Mast cells are
involved in hypersensitivity reactions</description>
        <go id="GO:0043303"/>
    </keyword>
    <keyword id="KW-0981">
        <name>Meckel syndrome</name>
        <name>MKS</name>
        <name>Meckel-Gruber syndrome</name>
        <name>Dysencephalia splanchnocystica</name>
        <name>Gruber syndrome</name>
        <description>Protein which, if defective, causes Meckel syndrome, an autosomal
recessive disorder characterized by a combination of renal cysts and
variably associated features, including developmental anomalies of the
central nervous system (usually occipital encephalocele), hepatic
ductal dysplasia and cysts, and polydactyly</description>
    </keyword>
    <keyword id="KW-0469">
        <name>Meiosis</name>
        <description>Protein involved in meiotic processes or in regulation of meiosis
Meiosis is the nuclear division which results in the daughter nuclei
each containing half the number of chromosomes of the parent. It
comprises two distinct nuclear divisions, the first and second meiotic
divisions (which may be separated by cell division), the actual
reduction in chromosome number takes place during the first division</description>
        <go id="GO:0051321"/>
    </keyword>
    <keyword id="KW-0470">
        <name>Melanin biosynthesis</name>
        <name>Melanin formation</name>
        <name>Melanin synthesis</name>
        <name>Melanin anabolism</name>
        <name>Melanin biosynthetic process</name>
        <description>Protein involved in the synthesis of melanin. Melanins are brown or
black pigments found in skin, hair, feathers, etc. They are irregular
polymeric structures produced from tyrosine. Melanins can be divided
into 3 groups: allomelanins in the plant kingdom, and eumelanins and
phaeomelanins in the animal kingdom</description>
        <go id="GO:0042438"/>
    </keyword>
    <keyword id="KW-0867">
        <name>MELAS syndrome</name>
        <description>Protein which, if defective, causes mitochondrial encephalomyopathy
with lactic acidosis and stroke-like episodes (MELAS) syndrome, a
genetically heterogeneous disorder, characterized by episodic
vomiting, seizures, and recurrent cerebral insults resembling strokes
and causing hemiparesis, hemianopsia, or cortical blindness</description>
    </keyword>
    <keyword id="KW-0471">
        <name>Melatonin biosynthesis</name>
        <name>Melatonin anabolism</name>
        <name>Melatonin formation</name>
        <name>Melatonin biosynthetic process</name>
        <name>Melatonin synthesis</name>
        <description>Protein involved in the synthesis of melatonin (N-acetyl 5-
methoxytryptamine), a neurohormone synthesized by lower plants and in
the pineal gland in animals. In humans, it is involved in the
regulation of sleep, mood, puberty, ovarian cycles and in the
establishment of circadian rhythms. In lower vertebrates, it causes
aggregation of pigment in melanophores, and thus lightens skin</description>
        <go id="GO:0030187"/>
    </keyword>
    <keyword id="KW-0472">
        <name>Membrane</name>
        <description>Protein which is membrane-bound or membrane-associated. A membrane is
the layer which forms the boundary of cells and intracellular
organelles. It is composed of two oriented lipid layers in which
proteins are embedded and acts as a selective permeability barrier</description>
    </keyword>
    <keyword id="KW-0473">
        <name>Membrane attack complex</name>
        <description>Component of the membrane attack complex which groups the complement
plasma glycoproteins C5b, C6, C7, C8 and polymeric C9 on biological
membranes. The complex forms transmembrane channels which displace
lipid molecules and other constituents, thus disrupting the
phospholipid bilayer of target cells leading to cell lysis by osmotic
leakage. The formation of the membrane attack complex is the terminal
step in the complement cascade</description>
        <go id="GO:0005579"/>
    </keyword>
    <keyword id="KW-0474">
        <name>Menaquinone biosynthesis</name>
        <name>Menaquinone anabolism</name>
        <name>Vitamin K2 synthesis</name>
        <name>Vitamin K2 biosynthetic process</name>
        <name>Menaquinone formation</name>
        <name>Vitamin K2 biosynthesis</name>
        <name>Menaquinone biosynthetic process</name>
        <name>Vitamin K2 anabolism</name>
        <name>Vitamin K2 formation</name>
        <name>Menaquinone synthesis</name>
        <description>Protein involved in the synthesis of menaquinone, a derivative of 2-
methyl-1,4-naphthoquinone in which the 3-position is substituted with
a variable-length polyisoprene chain. In mammals, menaquinone is an
important component of the blood coagulation system. Mammals need to
obtain this vitamin by their diet or from the bacterial flora of the
gut</description>
        <go id="GO:0009234"/>
    </keyword>
    <keyword id="KW-0475">
        <name>Mercuric resistance</name>
        <name>Mercuric cation resistance</name>
        <name>Mercuric ion resistance</name>
        <name>Resistance to mercury ion</name>
        <description>Protein that confers bacteria or other microorganisms the ability to
withstand mercury salts</description>
        <go id="GO:0046689"/>
    </keyword>
    <keyword id="KW-0476">
        <name>Mercury</name>
        <name>Mercury ion</name>
        <name>Hg</name>
        <name>Hg cation</name>
        <name>Hg ion</name>
        <name>Mercury cation</name>
        <description>Protein which binds mercury and/or is involved in the cleavage of
carbon-mercury bonds. Mercury is the only liquid metallic element,
chemical symbol is Hg</description>
    </keyword>
    <keyword id="KW-0477">
        <name>Merozoite</name>
        <description>Protein expressed in the merozoite stage of sporozoite parasites, an
invasive stage in the life cycle produced by schizogony or asexual
reproduction in which the nucleus of a cell undergoes division several
times. This results in a multinucleate schizont which subsequently
gives rise to a number of uninucleate cells called merozoites</description>
    </keyword>
    <keyword id="KW-0478">
        <name>Metachromatic leukodystrophy</name>
        <name>Metachromatic leucodystrophy</name>
        <description>Protein which, if defective, causes metachromatic leukodystrophy, a
disease characterized by intralysosomal or myelin membrane storage of
cerebroside-3-sulfate. Whereas storage occurs in many cells, the
disease almost exclusively affects oligodendrocytes. Patients suffer
from a progressive demyelination, which causes a variety of
neurological symptoms, including gait disturbances, ataxias, optical
atrophy, dementia, seizures and spastic tetraparesis</description>
    </keyword>
    <keyword id="KW-0479">
        <name>Metal-binding</name>
        <description>Protein which binds metals</description>
        <go id="GO:0046872"/>
    </keyword>
    <keyword id="KW-0480">
        <name>Metal-thiolate cluster</name>
        <description>Protein which binds at least a cluster composed of metal coordinated
via cysteinyl thiolate bridges to cysteine ligands</description>
        <go id="GO:0046872"/>
    </keyword>
    <keyword id="KW-0481">
        <name>Metalloenzyme inhibitor</name>
        <description>Protein that inhibits metalloenzymes, enzymes which contains metal
ions</description>
        <go id="GO:0004857"/>
    </keyword>
    <keyword id="KW-0482">
        <name>Metalloprotease</name>
        <name>Metallopeptidase</name>
        <description>Proteolytic enzyme which use a metal for its catalytic mechanism. Most
metalloproteases are zinc-dependent, some use cobalt</description>
        <go id="GO:0008237"/>
    </keyword>
    <keyword id="KW-0483">
        <name>Metalloprotease inhibitor</name>
        <name>Metallopeptidase inhibitor</name>
        <description>Protein that inhibits metalloproteases, which are peptide hydrolases
that use a metal in the catalytic mechanism</description>
        <go id="GO:0030414"/>
    </keyword>
    <keyword id="KW-0484">
        <name>Methanogenesis</name>
        <name>Methane synthesis</name>
        <name>Methane biosynthetic process</name>
        <name>Methane biosynthesis</name>
        <description>Protein involved in methanogenesis, the energy yielding formation of
methane by methanogenic bacteria</description>
        <go id="GO:0015948"/>
    </keyword>
    <keyword id="KW-0485">
        <name>Methanol utilization</name>
        <description>Protein involved in the utilization of methanol</description>
        <go id="GO:0015945"/>
    </keyword>
    <keyword id="KW-0486">
        <name>Methionine biosynthesis</name>
        <name>Methionine biosynthetic process</name>
        <name>Methionine formation</name>
        <name>Methionine anabolism</name>
        <name>Methionine synthesis</name>
        <description>Protein involved in the synthesis of the hydrophobic amino acid
methionine, an essential amino acid in human diets which contains a
thioether linkage</description>
        <go id="GO:0009086"/>
    </keyword>
    <keyword id="KW-0487">
        <name>Methotrexate resistance</name>
        <name>Resistance to methotrexate</name>
        <description>Protein that confers the ability to withstand methotrexate, an
inhibitor of dehydrofolate reductase (DHFR). Methotrexate resistance
occurs usually as a result of mutation or amplification of the DHFR
gene</description>
        <go id="GO:0031427"/>
    </keyword>
    <keyword id="KW-0488">
        <name>Methylation</name>
        <name>Methylated</name>
        <description>Protein which is posttranslationally modified by the attachment of at
least one methyl group</description>
    </keyword>
    <keyword id="KW-0489">
        <name>Methyltransferase</name>
        <description>Enzyme that transfers methyl groups from one compound to another</description>
        <go id="GO:0008168"/>
        <go id="GO:0032259"/>
    </keyword>
    <keyword id="KW-0490">
        <name>MHC I</name>
        <description>A heterodimeric membrane protein composed of two non-covalently linked
polypeptide chains, a major histocompatibility complex (MHC)-encoded
alpha chain and a non-MHC-encoded subunit B2M/beta2-microglobulin
Each MHC molecule consists of an extracellular peptide-binding cleft,
followed by an immunoglobulin (Ig)-like domain and transmembrane and
cytoplasmic domains. The amino-terminal alpha-1 and alpha-2 segments
of the alpha chain form the peptide-binding cleft. Expressed on all
nucleated cells, displays peptides derived from cytosolic proteins for
recognition by CD8-positive T cells. By scanning MHC I molecules, CD8-
positive T cells can detect infected or tumor cells and eliminate
them</description>
        <go id="GO:0002474"/>
        <go id="GO:0042612"/>
    </keyword>
    <keyword id="KW-0491">
        <name>MHC II</name>
        <description>A heterodimeric membrane protein composed of two non-covalently linked
alpha and beta polypeptide chains, both major histocompatibility
complex (MHC)-encoded. Each MHC molecule consists of an extracellular
peptide-binding cleft followed by an immunoglobulin (Ig)-like domain
and transmembrane and cytoplasmic domains. The amino-terminal alpha-1
and beta-1 segments interact to form the peptide-binding cleft
Expressed on professional antigen presenting cells, displays peptides
derived from endocytosed proteins for recognition by CD4-positive
helper T cells. By scanning MHC II molecules, CD4-positive T cells
activate effector mechanisms that eliminate extracellular microbes</description>
        <go id="GO:0002504"/>
        <go id="GO:0042613"/>
    </keyword>
    <keyword id="KW-1013">
        <name>Microphthalmia</name>
        <name>Microphthalmos</name>
        <description>Protein which, if defective, causes microphthalmia, a developmental
anomaly in which the eyeballs are abnormally small. Disease severity
ranges from moderate reduction of the size of a single eye to complete
bilateral absence of ocular tissues. Microphthalmia can occur in
isolation or as part of a syndrome</description>
    </keyword>
    <keyword id="KW-0492">
        <name>Microsome</name>
        <description>Protein found in microsomes, a heterogenous set of vesicles 20-200 nm
in diameter and formed from the endoplasmic reticulum when cells are
disrupted. The vesicles are isolated by differential centrifugation
and are composed of three structural features: rough vesicles, smooth
vesicles and ribosomes. Numerous enzyme activities are associated with
the microsomal fraction</description>
        <go id="GO:0043231"/>
    </keyword>
    <keyword id="KW-1177">
        <name>Microtubular inwards viral transport</name>
        <description>Viral protein that allows the active transport of complete particles
and viral components along microtubules toward the intracellular
replication sites during virus entry. This transport, which usually
involves motor proteins like dynein or polymerization/depolymerization
reactions as a driving force, is mostly used by viruses that replicate
their genome near or in the nucleus. Neurotropic viruses for example,
often enter neurons at the terminal axon and their viral genome must
be moved retrogradely to cell bodies. Viruses such as adenovirus,
Adeno-associated virus, rabies virus, canine parvovirus, vaccinia,
foamy virus, human papillomavirus 16 and herpes virus utilize this
type of intracellular transport</description>
        <go id="GO:0075521"/>
    </keyword>
    <keyword id="KW-1189">
        <name>Microtubular outwards viral transport</name>
        <description>Viral protein that allows the active transport of viral components and
assembled, complete particles along microtubules toward the cell
periphery during virus egress. This transport, which usually involves
interaction with motor proteins like kinesin or
polymerization/depolymerization reactions as a driving force, is
mostly used by viruses that replicate their genome near or in the
nucleus and allows newly assembled viral progeny to reach the plasma
membrane. Herpes simplex virus for example is transported
anterogradely along the axon</description>
        <go id="GO:0039701"/>
    </keyword>
    <keyword id="KW-0493">
        <name>Microtubule</name>
        <description>Protein associated with or component of the microtubule. The
microtubule is formed by the arrangement of 13 parallel protofilaments
arising from end-to-end aggregation of the tubulin alpha/beta-dimers
Microtubules are associated with various other proteins (MAPs, dynein,
kinesin) and are involved in structures responsible for cellular
movement such as flagella or cilia. Microtubules of the ciliary
axoneme are more permanent than cytoplasmic and spindle microtubules
Microtubule formation is inhibited by agents such as colchicine,
vinblastine or vincristine</description>
        <go id="GO:0005874"/>
    </keyword>
    <keyword id="KW-0494">
        <name>Milk protein</name>
        <description>Protein found in milk, a fluid secreted by female mammals to provide
food for their offspring. It consists of water, proteins, soluble
carbohydrates, electrolytes, lipids and vitamins</description>
    </keyword>
    <keyword id="KW-0495">
        <name>Mineral balance</name>
        <name>Regulation of bone mineralization</name>
        <description>Protein that influences the equilibrium of minerals present in bone,
e.g., fetuin</description>
        <go id="GO:0030500"/>
    </keyword>
    <keyword id="KW-0496">
        <name>Mitochondrion</name>
        <description>Protein encoded by or localized in the mitochondrion, a
semiautonomous, self-reproducing organelle that occurs in the
cytoplasm of all cells of most, but not all, eukaryotes. Each
mitochondrion is surrounded by a double limiting membrane. The inner
membrane is highly invaginated, and its projections are called
cristae. Mitochondria are the sites of the reactions of oxidative
phosphorylation, which result in the formation of ATP. The size and
coding capacity of the mitochondrial DNA varies considerably in
different organisms, and encodes rRNAs, tRNAs and essential
mitochondrial proteins</description>
    </keyword>
    <keyword id="KW-0999">
        <name>Mitochondrion inner membrane</name>
        <name>Mitochondrial inner membrane</name>
        <name>Inner mitochondrial membrane</name>
        <description>Protein found in or associated with the inner membrane of a
mitochondrion, the membrane which separates the mitochondrial matrix
from the intermembrane space</description>
    </keyword>
    <keyword id="KW-1135">
        <name>Mitochondrion nucleoid</name>
        <name>Mitochromosome</name>
        <name>Mitochondrial nucleoid</name>
        <description>Protein found associated with the mitochondrial nucleoid, the
mitochondrial pseudocompartment formed by the chromatin-dense area
This region, which is functionally equivalent to the eukaryotic
nucleus, is not surrounded by a membrane</description>
    </keyword>
    <keyword id="KW-1000">
        <name>Mitochondrion outer membrane</name>
        <name>Mitochondrial outer membrane</name>
        <name>Outer mitochondrial membrane</name>
        <description>Protein found in or associated with the outer membrane of a
mitochondrion, the mitochondrial membrane facing the cytoplasm</description>
    </keyword>
    <keyword id="KW-0497">
        <name>Mitogen</name>
        <description>Protein which can induce mitosis of certain eukaryotic cells, i.e. it
stimulates cellular proliferation</description>
        <go id="GO:0051781"/>
    </keyword>
    <keyword id="KW-0498">
        <name>Mitosis</name>
        <description>Protein involved in mitosis, the nuclear division in eukaryotic cells
involving the exact duplication and separation of the chromosome
threads so that each daughter nucleus carries a chromosome complement
identical to that of the parent nucleus. Mitosis is divided into four
substages: prophase, metaphase, anaphase and telophase</description>
    </keyword>
    <keyword id="KW-1025">
        <name>Mitosome</name>
        <description>Protein localized in the mitosome, an organelle found in
"amitochondrial" unicellular organisms which do not have the
capability of gaining energy from oxidative phosphorylation. Mitosomes
are almost certainly derived from mitochondria, they have a double
membrane and most proteins are delivered to them by a targeting
sequence. Unlike mitochondria, mitosomes do not contain any DNA. The
mitosome functions in iron-sulphur cluster assembly</description>
    </keyword>
    <keyword id="KW-0499">
        <name>Mobility protein</name>
        <description>Protein involved in the conjugative transfer of plasmid DNA. These
proteins provide the function of nicking the DNA at a certain point,
guiding the 5' end of the nicked strand into the recipient cell,
recircularization, and perhaps the priming of complementary strand
synthesis in the recipient</description>
    </keyword>
    <keyword id="KW-1119">
        <name>Modulation of host cell apoptosis by virus</name>
        <description>Viral protein involved in the modulation of host cell apoptosis by
acting different steps of the process. Several viruses encode proteins
that inhibit apoptosis while other viruses use apoptosis to their
advantage to suppress immune response or to disseminate</description>
        <go id="GO:0052150"/>
    </keyword>
    <keyword id="KW-1120">
        <name>Modulation of host cell cycle by viral cyclin-like protein</name>
        <description>Viral protein sharing sequence homology with cellular cyclins. Most
viral cyclin homologues are closely related in sequence to the
cellular D-type cyclins, which are implicated in regulating the
transit of cells from G1 into S and are thought to operate via the
inactivation of the retinoblastoma tumour suppressor protein</description>
        <go id="GO:0060153"/>
    </keyword>
    <keyword id="KW-1121">
        <name>Modulation of host cell cycle by virus</name>
        <description>Viral protein involved in the modulation of host cell cycle. The cell
cycle can be divided into four stages: G1, S, G2 and mitosis, while
cells resting are termed quiescent cells (G0). Viruses have evolved
strategies to modulate cell cycle progression including stimulation of
S phase entry from G1 or G0 or cell cycle arrest at G2/M for example
This regulation allows viruses to maximize their own replication</description>
        <go id="GO:0044071"/>
    </keyword>
    <keyword id="KW-1122">
        <name>Modulation of host chromatin by virus</name>
        <description>Viral protein involved in the regulation of host chromatin structure
Chromatin has a major role in life cycle of many viruses, and a lot of
them have evolved mechanisms to modulate chromatin-related processes
For example, histone acetyltransferases, histone deacetylases or
histones are common targets of viruses</description>
        <go id="GO:0039525"/>
    </keyword>
    <keyword id="KW-1118">
        <name>Modulation of host dendritic cell activity by virus</name>
        <description>Viral protein involved in the modulation of host dendritic cell
activity. Dendritic cells operate at the interface between the innate
and adaptive immune response by their ability to sample their
environment for pathogenic products, to process them, and to present
viral antigens to T-cells. This results in T cell proliferation and
the induction of virus-specific adaptive immune responses. Therefore
impairing dendritic cell function by viruses is an effective strategy
to disrupt the host immune response</description>
        <go id="GO:0039673"/>
    </keyword>
    <keyword id="KW-1123">
        <name>Modulation of host E3 ubiquitin ligases by virus</name>
        <description>Viral protein involved in the modulation of cellular E3 ubiquitin
ligases. In general, viral proteins redirect cellular E3 ubiquitin
ligases to select specific host proteins for proteasomal degradation
The aim of this subversion is the creation of a favorable environment
for virus replication and dissemination</description>
        <go id="GO:0039648"/>
    </keyword>
    <keyword id="KW-1124">
        <name>Modulation of host immunity by viral IgG Fc receptor-like protein</name>
        <description>Viral protein acting as an IgG Fc receptors, able to bind IgG and
inhibit host Fc-dependent immune activation. Fc receptors are proteins
found at the surface of certain cells of the immune system including
macrophages, monocytes, natural killer cells or B-cells. They allow
these cells to bind to antibodies that are attached to the surface of
infected cells or pathogens, helping these cells to identify and
eliminate pathogens</description>
        <go id="GO:0075528"/>
    </keyword>
    <keyword id="KW-1131">
        <name>Modulation of host NK-cell activity by virus</name>
        <description>Viral protein involved in the modulation of host NK-cell activity
Natural killer (NK) cells are critical in defense against viral
infections, since they provide host protection by releasing cytokines
such as IFN-gamma or by direct lysis of infected targets. Therefore,
during viral infections, viruses and NK cells are in a constant battle
and many viruses have developed a variety of strategies to modulate NK
cell activity</description>
        <go id="GO:0039671"/>
    </keyword>
    <keyword id="KW-1126">
        <name>Modulation of host PP1 activity by virus</name>
        <description>Protein phosphatase-1 (PP1) is a member of the Serine/Threonine
phosphatases. The enzyme regulates many important physiological
processes, including gene transcription, translation, metabolism, cell
growth and division. Different viruses including asfivirus, herpes
simplex virus or papillomavirus interact with and modulate PPP1
phosphatase activity to dephosphorylate specific cellular substrates
including EIF2S1. Upon viral infection, the host PKR/EIF2AK2 triggers
the phosphorylation of EIF2S1 leading to a complete translational
shut-off. By dephosphroylating EIF2S1 with PPP1CA, viruses manage to
circumvent this antiviral response and prevent translational shut-off</description>
        <go id="GO:0039606"/>
        <go id="GO:0004865"/>
    </keyword>
    <keyword id="KW-1127">
        <name>Modulation of host ubiquitin pathway by viral deubiquitinase</name>
        <description>Viral protein possessing deubiquitinating activity. Hijacking the
ubiquitin system plays an essential role during viral replication
Therefore, several viruses including EBV or HCMV encode for proteins
able to remove ubiquitin or ubiquitin-like proteins from their
substrate</description>
        <go id="GO:0039648"/>
    </keyword>
    <keyword id="KW-1128">
        <name>Modulation of host ubiquitin pathway by viral E3 ligase</name>
        <description>Viral protein functioning as a cellular E3 ubiquitin ligase. These
viral proteins usually target several host proteins for proteasomal
degradation</description>
        <go id="GO:0039648"/>
    </keyword>
    <keyword id="KW-1129">
        <name>Modulation of host ubiquitin pathway by viral ubl</name>
        <description>Viral protein sharing sequence similarity with host ubiquitin. Several
of these homologues are present in large DNA viruses such as
entomopoxvirus or canarypoxvirus and are thought to modulate host
ubiquitin pathway</description>
        <go id="GO:0039648"/>
    </keyword>
    <keyword id="KW-1130">
        <name>Modulation of host ubiquitin pathway by virus</name>
        <description>Viral protein involved in the modulation of the host ubiquitin
pathway. The ubiquitination pathway comprises E1, E2, and E3 ligases
that conjugate ubiquitin to protein substrate. Usually, the host E3
ligase determines the substrate specificity. Some viruses encode E3
ligases that modulate the substrate specificity of host E3 ligases
Alternatively, some viruses encode deubiquitinases able to remove
ubiquitin or ubiquitin-like proteins from their substrate</description>
        <go id="GO:0039648"/>
    </keyword>
    <keyword id="KW-1254">
        <name>Modulation of host virulence by virus</name>
        <description>Viral factor that modulates its bacterial host's virulence against a
third organism. These virulence factors are mostly expressed from
integrated viral genomes and have diverse functions. Bacterial host,
and populations, and the encoding (pro)virus probably benefit from the
expression of such factors. For example, Bor and Lom outer membrane
proteins encoded by bacteriophage lambda modify the virulence of the
host bacteria against a eukaryotic target. Some enteric
bacterioviruses direct alterations in lipopolysaccharide biosynthesis,
resulting in bacterial immune evasion of its eukaryotic target. Other
prokaryotic viruses encode exotoxins changing their host bacteria into
serious pathogens. A well-known bacterial exotoxin encoded by a
provirus is the diphtheria toxin</description>
        <go id="GO:0098676"/>
    </keyword>
    <keyword id="KW-0500">
        <name>Molybdenum</name>
        <name>Mo</name>
        <name>Molybdenum ion</name>
        <name>Mo ion</name>
        <name>Mo cation</name>
        <name>Molybdenum cation</name>
        <description>Protein which binds molybdenum (or molybdopterin) or protein involved
in the transport of molybdenum, a metallic element, chemical symbol
Mo. It plays an essential role in the active site of all eukaryotic
Mo-containing enzymes. In plants, Mo enzymes are important for nitrate
assimilation, phytohormone synthesis, and purine catabolism. Mo is
often coordinated to the sulfur atoms of a pterin derivative
(molybdopterin [MPT]), thereby forming the active Molybdenum cofactor
(Moco), which is highly conserved in eukaryotes, eubacteria, and
archaebacteria</description>
    </keyword>
    <keyword id="KW-0501">
        <name>Molybdenum cofactor biosynthesis</name>
        <name>Moco anabolism</name>
        <name>Moco synthesis</name>
        <name>Moco biosynthetic process</name>
        <name>Moco biosynthesis</name>
        <name>Molybdopterin anabolism</name>
        <name>Molybdenum cofactor biosynthetic process</name>
        <name>Molybdenum cofactor formation</name>
        <name>Molybdenum cofactor anabolism</name>
        <name>Molybdopterin synthesis</name>
        <name>Molybdopterin formation</name>
        <name>Molybdopterin biosynthesis</name>
        <name>Moco formation</name>
        <name>Molybdenum cofactor synthesis</name>
        <name>Molybdopterin biosynthetic process</name>
        <description>Protein involved in the synthesis of the molybdenum cofactor (Moco), a
molybdenum atom coordinated to the sulfur atoms of a pterin derivative
(molybdopterin [MPT]). It is highly conserved in eukaryotes,
eubacteria, and archaebacteria. In prokaryotes, two operons are
directly associated with biosynthesis of the pterin moiety and its
side chain while additional loci play a role in the acquisition of
molybdenum and/or activation of the cofactor</description>
        <go id="GO:0006777"/>
    </keyword>
    <keyword id="KW-0502">
        <name>Monoclonal antibody</name>
        <description>Antibody produced by a single clone of B cells and thus consisting of
a population of identical antibody molecules all specicfic for a
single antigenic determinant. They are produced from cultured
hybridoma cell lines for research and commercial purposes</description>
        <go id="GO:0003823"/>
    </keyword>
    <keyword id="KW-0503">
        <name>Monooxygenase</name>
        <description>Enzymes that reduce molecular oxygen by incorporating one oxygen atom
into its substrate and the other one in water</description>
        <go id="GO:0004497"/>
    </keyword>
    <keyword id="KW-0504">
        <name>Morphogen</name>
        <description>Diffusible protein that influence morphogenesis or embryonic
development. These proteins carry information relating, for example,
to a position in the embryo, and thus, determine the differentiation
that cells perceiving this information will undergo. They are thought
to act as a function of a threshold of their concentration</description>
        <go id="GO:0009653"/>
        <go id="GO:0016015"/>
    </keyword>
    <keyword id="KW-0505">
        <name>Motor protein</name>
        <description>Protein that walks or slides along microtubules or microfilaments
using the energy provided by ATP or GTP hydrolysis, e.g. dyneins,
myosins and kinesins. Or protein which mediates motility by other non
enzymatic processes, e.g. prestin, a bidirectional voltage-to-force
converter</description>
    </keyword>
    <keyword id="KW-0506">
        <name>mRNA capping</name>
        <name>Messenger RNA capping</name>
        <description>Protein involved in the modification (capping) of the 5' end of
eukaryotic mRNAs. This modification occurs after the beginning of
transcription in the nucleus, and consists of adding a guanosine
nucleotide to the 5'-end of mRNAs and then, methylating the guanosine
Capping protects mRNAs at their termini against attack by phosphatases
and other nucleases and promotes mRNA function at the level of
initiation of translation</description>
        <go id="GO:0006370"/>
    </keyword>
    <keyword id="KW-0507">
        <name>mRNA processing</name>
        <name>Messenger RNA processing</name>
        <description>Protein involved in the processing of the primary mRNA transcript to
yield a functional mRNA. This includes 5' capping, 3' cleavage and
polyadenylation, as well as mRNA splicing and RNA editing</description>
        <go id="GO:0006397"/>
    </keyword>
    <keyword id="KW-0508">
        <name>mRNA splicing</name>
        <name>Messenger RNA splicing</name>
        <description>Protein involved in the process by which nonsense sequences or
intervening sequences (introns) are removed from pre-mRNA to generate
a functional mRNA (messenger RNA) that contains only exons</description>
        <go id="GO:0008380"/>
    </keyword>
    <keyword id="KW-0509">
        <name>mRNA transport</name>
        <name>Messenger RNA transport</name>
        <description>Protein which is involved in the mechanism of export of mRNAs from the
nucleus to the cytoplasm</description>
        <go id="GO:0051028"/>
    </keyword>
    <keyword id="KW-0942">
        <name>Mucolipidosis</name>
        <description>Protein which, if defective, causes mucolipidosis, a group of
inherited metabolic diseases characterised by the accumulation of
excessive amounts of acid mucopolysaccharides, sphingolipids, and/or
glycolipids in visceral and mesenchymal cells. Abnormal amounts of
sphingolipids or glycolipids are present in neural tissue. Mental
retardation and skeletal changes are common. All mucolipidosis are
lysosomal disorders and are inherited in an autosomal recessive
manner</description>
    </keyword>
    <keyword id="KW-0510">
        <name>Mucopolysaccharidosis</name>
        <description>Protein which, if defective, causes mucopolysaccharidosis. These
inherited diseases are characterized by excessive accumulation and
secretion of oligomucopoloysaccharide due to the deficiency of enzymes
involved in the degradation of glycosaminoglycans
(mucopolysaccharides). They are progressive and often display a wide
spectrum of clinical severity within one enzyme deficiency</description>
    </keyword>
    <keyword id="KW-0511">
        <name>Multifunctional enzyme</name>
        <description>Protein that contains at least two distinct enzymatic activities and
two distinct active sites</description>
        <go id="GO:0008152"/>
        <go id="GO:0003824"/>
    </keyword>
    <keyword id="KW-0514">
        <name>Muscle protein</name>
        <description>Characteristic protein of a muscle cell. The major ones are myosin and
actin, which are responsible for the contraction and relaxation of
muscles</description>
    </keyword>
    <keyword id="KW-0515">
        <name>Mutator protein</name>
        <description>Protein which is encoded by a mutator gene (mutator). Generally, these
are genes within which certain mutations cause an increase in
frequency of spontaneous mutations in other genes. Mutator proteins
are therefore thought to be responsible for inaccurate DNA
replication</description>
    </keyword>
    <keyword id="KW-1060">
        <name>Myofibrillar myopathy</name>
        <description>Protein which, if defective, causes myofibrillar myopathy, a group of
morphologically homogeneous, but genetically heterogeneous
neuromuscular disorders. The morphologic changes in skeletal muscle
result from disintegration of the sarcomeric Z disc and the
myofibrils, followed by abnormal ectopic accumulation of multiple
proteins involved in the structure of the Z disc. Clinical
manifestations are variable and can involve the skeletal, cardiac and
smooth muscle</description>
    </keyword>
    <keyword id="KW-0517">
        <name>Myogenesis</name>
        <name>Muscle development</name>
        <name>Muscle formation</name>
        <description>Protein involved in the differentiation and development of the muscle
Myogenesis is controlled by myogenic factors, a family of muscle-
specific transcription factors that contain a conserved helix-loop-
helix domain which is homologous to the myc family of proteins</description>
        <go id="GO:0007517"/>
    </keyword>
    <keyword id="KW-0518">
        <name>Myosin</name>
        <description>A motor protein which uses the energy provided by the hydrolysis of
ATP to drive movements along actin filaments. Different types of
myosin are found in eukaryotic cells</description>
        <go id="GO:0016459"/>
    </keyword>
    <keyword id="KW-0959">
        <name>Myotoxin</name>
        <description>Protein which causes muscle necrosis. Myotoxins are principally found
in snake venoms. The myotoxic activity can be monitored by
morphological analysis and by the increase of plasma creatine kinase
(CK) activity. The increase in plasma CK levels results from
sarcolemmal damage due to myotoxic components of the venom</description>
    </keyword>
    <keyword id="KW-0519">
        <name>Myristate</name>
        <name>n-tetradecanoate</name>
        <name>Myristylated</name>
        <description>Protein which is posttranslationally modified by the attachment of at
least one myristate group. The myristate (14-carbon saturated fatty
acid) group is attached through an amide bond to the N-terminal
glycine residue of the mature form of a protein or to an internal
lysine residue. Myristoylproteins may be cytoplasmic or membrane-
associated</description>
    </keyword>
    <keyword id="KW-0520">
        <name>NAD</name>
        <name>Nicotinic adenine dinucleotide</name>
        <name>Nicotinamide adenine dinucleotide</name>
        <description>Enzymes which use NAD(H) as an electron acceptor or as a cofactor
Nicotinamide adenine dinucleotide, an important redox coenzyme that
participates in a variety of enzymatic reactions in which it serves as
an electron carrier by being alternately oxidized (NAD+) and reduced
(NADH). NAD also functions as an ADP-ribose donor in ADP-ribosylation
reactions</description>
    </keyword>
    <keyword id="KW-0521">
        <name>NADP</name>
        <name>Nicotinic adenine dinucleotide phosphate</name>
        <name>Nicotinamide adenine dinucleotide phosphate</name>
        <description>Enzymes which use NADP(H) as an electron acceptor or as a cofactor
Nicotinamide adenine dinucleotide phosphate, a redox coenzyme that
participates in a variety of enzymatic reactions in which it serves as
an electron carrier by being alternately oxidized (NADP+) and reduced
(NADPH). Analogue of NAD, but NADPH is used extensively in
biosynthetic, rather than catabolic pathways as well as in
photosynthesis</description>
    </keyword>
    <keyword id="KW-1210">
        <name>Necrosis</name>
        <name>Necroptosis</name>
        <name>Necrotic cell death</name>
        <name>Necrotic programmed cell death</name>
        <description>Protein involved in necrotic programmed cell death. Necrosis is a form
of traumatic cell death that results from acute cellular injury due
infection, toxins, trauma, etc. Necrosis is characterized by blebbing,
mitochondrial fission, loss of cell membrane integrity and an
uncontrolled release of products of cell death into the intracellular
space. This initiates an inflammatory response in the surrounding
tissue often resulting is a build-up of dead tissue and cell debris
at, or near, the site of the cell death</description>
        <go id="GO:0012501"/>
    </keyword>
    <keyword id="KW-1057">
        <name>Nemaline myopathy</name>
        <name>Rod body myopathy</name>
        <name>NEM</name>
        <name>Rod myopathy</name>
        <name>NM</name>
        <description>Protein which, if defective, causes nemaline myopathy, a hereditary
neuromuscular disorder characterized by generally non-progressive
muscle weakness of varying severity, and abnormal thread- or rod-like
structures in muscle fibers on histologic examination. The age of
onset varies from birth to adulthood. The main clinical manifestations
include weakness (usually most severe in the face, the neck flexors,
and the proximal limb muscles), hypotonia, and depressed or absent
deep tendon reflexes. Nemaline myopathy is divided into several broad
groups classified by onset and severity of motor and respiratory
involvement</description>
    </keyword>
    <keyword id="KW-0166">
        <name>Nematocyst</name>
        <name>Cnidocyst</name>
        <description>Protein localized in the nematocyst, an organelle found in nematoblast
(cnidoblast) cells. When matured, these stinging organelles store
toxins and can deliver them when the cnidocil (a short extension of
the nematocyst) is stimulated by a prey or another stimulus. These
proteins are principally found in anemones and jellyfishes</description>
    </keyword>
    <keyword id="KW-0983">
        <name>Nephronophthisis</name>
        <name>NPHP</name>
        <description>Protein which, if defective, causes nephronophthisis, a chronic
tubulo-interstitial nephritis that progresses to end-stage renal
failure. Clinical features include anemia, polyuria, polydipsia,
isosthenuria, and death in uremia. Some children present with
extrarenal symptoms such as tapeto-retinal degeneration, mental
retardation, cerebellar ataxia, bone anomalies or liver involvement</description>
    </keyword>
    <keyword id="KW-0523">
        <name>Neurodegeneration</name>
        <description>Protein which, if defective, causes neurodegeneration</description>
    </keyword>
    <keyword id="KW-0524">
        <name>Neurogenesis</name>
        <name>Nervous system development</name>
        <name>Nervous system formation</name>
        <description>Protein involved in neurogenesis, which involves the differentiation
and development of the nervous system</description>
        <go id="GO:0007399"/>
    </keyword>
    <keyword id="KW-0525">
        <name>Neuronal ceroid lipofuscinosis</name>
        <name>CLN</name>
        <name>NCL</name>
        <description>Protein which, if defective, causes neuronal ceroid lipofuscinosis, a
group of neurodegenerative, lysosome storage disorders characterized
by intracellular accumulation of autofluorescent wax-like lipid
materials in brain and other tissues. Neuronal ceroid lipofuscinoses
are associated with variable yet progressive symptoms including
seizures, dementia, visual loss, and/or cerebral atrophy</description>
    </keyword>
    <keyword id="KW-0622">
        <name>Neuropathy</name>
        <description>Protein which, if defective, causes neuropathy, a functional
disturbance or pathological change in the peripheral nervous system,
sometimes limited to non-inflammatory lesions as opposed to those of
neuritis. Neuropathies affecting a specific nerve may be named for the
nerve. The terms mononeuropathy and polyneuropathy may be used to
denote whether one or several nerves are involved</description>
    </keyword>
    <keyword id="KW-0527">
        <name>Neuropeptide</name>
        <description>Peptides released by neurons as intercellular messengers. Many
neuropeptides are also hormones released by non-neuronal cells. They
have direct synaptic effects (peptide neurotransmitters) or indirect
modulatory effects on the nervous system (peptide neuromodulators)</description>
        <go id="GO:0007218"/>
    </keyword>
    <keyword id="KW-0528">
        <name>Neurotoxin</name>
        <description>Proteins, often exquisitely toxic, that inhibit neuronal function
Neurotoxins act typically against sodium channels or block or enhance
synaptic transmission. Most venoms contain neurotoxic substances</description>
    </keyword>
    <keyword id="KW-0529">
        <name>Neurotransmitter</name>
        <description>Protein, released by the axon terminal in response to an electrical
impulse, which travels across the synapse to either excite or inhibit
the target cell</description>
        <go id="GO:0007268"/>
    </keyword>
    <keyword id="KW-0530">
        <name>Neurotransmitter biosynthesis</name>
        <name>Neurotransmitter biosynthetic process</name>
        <name>Neurotransmitter anabolism</name>
        <name>Neurotransmitter formation</name>
        <name>Neurotransmitter synthesis</name>
        <description>Protein involved in the synthesis of neurotransmitters. The proteins
are released by the axon terminal in response to an electrical impulse
and travel across the synapse to either excite or inhibit the target
cell</description>
    </keyword>
    <keyword id="KW-0531">
        <name>Neurotransmitter degradation</name>
        <name>Neurotransmitter breakdown</name>
        <name>Neurotransmitter catabolic process</name>
        <name>Neurotransmitter catabolism</name>
        <description>Protein involved in the breakdown of neurotransmitters. The proteins
are released by the axon terminal in response to an electrical impulse
and travel across the synapse to either excite or inhibit the target
cell</description>
    </keyword>
    <keyword id="KW-0532">
        <name>Neurotransmitter transport</name>
        <description>Protein involved in the transport of neurotransmitters. The proteins
are released by the axon terminal in response to an electrical impulse
and travel across the synapse to either excite or inhibit the target
cell</description>
        <go id="GO:0006836"/>
    </keyword>
    <keyword id="KW-0533">
        <name>Nickel</name>
        <name>Ni ion</name>
        <name>Nickel cation</name>
        <name>Ni</name>
        <name>Ni cation</name>
        <name>Nickel ion</name>
        <description>Protein which binds at least one nickel atom, or protein whose
function is nickel-dependent. Nickel is a metal, chemical symbol Ni</description>
    </keyword>
    <keyword id="KW-0996">
        <name>Nickel insertion</name>
        <name>Ni insertion</name>
        <description>Protein which is involved in the creation and/or insertion of a nickel
metallocenter into another protein, without necessarily binding the
metal itself</description>
    </keyword>
    <keyword id="KW-0921">
        <name>Nickel transport</name>
        <name>Nickel cation transport</name>
        <name>Nickel ion transport</name>
        <name>Ni transport</name>
        <description>Protein involved in the transport of nickel</description>
        <go id="GO:0015675"/>
    </keyword>
    <keyword id="KW-1054">
        <name>Niemann-Pick disease</name>
        <name>NPD</name>
        <name>Niemann's disease</name>
        <description>Protein which, if defective, causes Niemann-Pick disease. Niemann-Pick
disease comprises an inherited group of congenital lipidoses in which
sphingolipids accumulate in cells, especially in the
reticuloendothelial system, due to defective lysosomal storage. The
disease is clinically characterized by progressive degeneration of the
central nervous system with visceral accumulation of cholesterol and
sphingomyelin. The clinical phenotype is highly variable and different
types are distinguished by age of onset, degree of central nervous
system involvement and by the amount of sphingomyelin
phosphodiesterase activity</description>
    </keyword>
    <keyword id="KW-0534">
        <name>Nitrate assimilation</name>
        <description>Protein involved in the uptake, from the environment, of nitrates,
inorganic or organic salts and esters of nitric acid. This includes
the uptake and transport into cells by nitrate transporters, with the
sequential reduction to nitrite and ammonium, catalyzed by the enzymes
nitrate reductase and nitrite reductase, respectively</description>
        <go id="GO:0042128"/>
    </keyword>
    <keyword id="KW-0944">
        <name>Nitration</name>
        <name>Nitrated</name>
        <description>Protein which is posttranslationally modified by replacement of a
hydrogen on an aromatic ring of one or more tyrosine or tryptophan
residues by a nitro (NO2) group</description>
    </keyword>
    <keyword id="KW-0535">
        <name>Nitrogen fixation</name>
        <description>Protein involved in nitrogen fixation, the reduction of gaseous
nitrogen to ammonia. This process is carried out only by prokaryotes
who are either free-living or form symbiotic associations with plants
or other organisms (e.g. termites, protozoa)</description>
    </keyword>
    <keyword id="KW-0536">
        <name>Nodulation</name>
        <description>Protein involved in nodulation, the formation of nitrogen-fixing
nodules on roots of both leguminous plants and the Parasponia genus</description>
        <go id="GO:0009877"/>
    </keyword>
    <keyword id="KW-1010">
        <name>Non-syndromic deafness</name>
        <name>Isolated deafness</name>
        <description>Protein which, if defective, causes inability to hear in the absence
of other clinical signs and symptoms. Most forms of non-syndromic
deafness are associated with permanent hearing loss caused by damage
to structures in the inner ear</description>
    </keyword>
    <keyword id="KW-0866">
        <name>Nonsense-mediated mRNA decay</name>
        <name>NMD</name>
        <description>Protein involved in nonsense-mediated messenger RNA (mRNA) decay, a
critical process of selective degradation of mRNAs that contain
premature stop codons</description>
        <go id="GO:0000184"/>
    </keyword>
    <keyword id="KW-0914">
        <name>Notch signaling pathway</name>
        <description>Protein involved in the Notch signaling, a signaling pathway involved
in cell-cell communications that regulates a broad spectrum of cell-
fate determinations. Notch proteins are transmembrane receptors, which
are cleaved by the gamma-secretase complex upon activation and
released from the cell membrane and turn into transcriptional
activators after their association with SU(H) proteins</description>
        <go id="GO:0007219"/>
    </keyword>
    <keyword id="KW-0906">
        <name>Nuclear pore complex</name>
        <name>NPC</name>
        <name>Nuclear pore</name>
        <description>Protein associated predominantly with the nuclear pore complex (NPC)
NPCs constitute the exclusive means of nucleocytoplasmic transport in
eukaryotes during interphase. NPCs allow the passive diffusion of ions
and small molecules (up to about 20 kDa or 5 nm) and the active,
nuclear transport receptor (karyopherin: importin and exportin)-
mediated bidirectional transport of macromolecules such as proteins,
RNAs, ribonucleoprotein (RNPs), and ribosomal subunits (up to about 10
MDa) across the double-membrane nuclear envelope. NPC components,
collectively referred to as nucleoporins (NUPs), can play the role of
both NPC structural components and of docking or interaction partners
for transiently associated nuclear transport factors. The NPC is
composed of at least 30 distinct subunits, shows 8-fold rotational
symmetry with specialized structures on the cyto- and nucleoplasmic
side and in the nuclear envelope embedded core. The MW varies from
about 44-60 MDa in S. cerevisiae to 60-120 MDa in vertebrates, yet the
overall architecture is conserved</description>
    </keyword>
    <keyword id="KW-0540">
        <name>Nuclease</name>
        <description>Enzyme that degrades nucleic acids into shorter oligonucleotides or
single nucleotide subunits by hydrolyzing sugar-phosphate bonds in the
nucleic acid backbone</description>
        <go id="GO:0004518"/>
    </keyword>
    <keyword id="KW-0542">
        <name>Nucleomorph</name>
        <description>Protein associated with the nucleomorph. A nucleomorph is a remnant
nucleus found between the outer two and inner two membranes of the
plastid in cryptomonads and chlorarachniophyte algae</description>
    </keyword>
    <keyword id="KW-0544">
        <name>Nucleosome core</name>
        <description>Protein characteristic of the nucleosome, a repeating structural unit
in chromatin that packages DNA to give the chromatin a 'beads-on-a-
string' appearance. Each repeat consists of approximately 146 base
pairs of DNA wound around a disk-shaped protein core which is composed
of two of each of the nucleosomal histones H2A, H2B, H3 and H4</description>
        <go id="GO:0000786"/>
    </keyword>
    <keyword id="KW-0545">
        <name>Nucleotide biosynthesis</name>
        <name>Nucleotide synthesis</name>
        <name>Nucleotide formation</name>
        <name>Nucleotide biosynthetic process</name>
        <name>Nucleotide anabolism</name>
        <description>Protein involved in the synthesis of a nucleotide, a phosphate ester
of a nucleoside consisting of a purine or pyrimidine base linked to
ribose or deoxyribose phosphates</description>
        <go id="GO:0009165"/>
    </keyword>
    <keyword id="KW-0546">
        <name>Nucleotide metabolism</name>
        <name>Nucleotide metabolic process</name>
        <description>Protein involved in the biochemical reactions of nucleotides
Nucleotides are phosphate esters of a nucleoside consisting of a
purine or pyrimidine base linked to ribose or deoxyribose phosphates</description>
        <go id="GO:0009117"/>
    </keyword>
    <keyword id="KW-0547">
        <name>Nucleotide-binding</name>
        <description>Protein which binds a nucleotide, a phosphate ester of a nucleoside
consisting of a purine or pyrimidine base linked to ribose or
deoxyribose phosphates</description>
        <go id="GO:0000166"/>
    </keyword>
    <keyword id="KW-0548">
        <name>Nucleotidyltransferase</name>
        <description>Enzyme which transfers a nucleotide from one compound to another</description>
        <go id="GO:0016779"/>
    </keyword>
    <keyword id="KW-0539">
        <name>Nucleus</name>
        <description>Protein located in the nucleus of a cell</description>
    </keyword>
    <keyword id="KW-0549">
        <name>Nylon degradation</name>
        <name>Nylon breakdown</name>
        <name>Nylon catabolism</name>
        <name>Nylon catabolic process</name>
        <description>Protein involved in the degradation of nylon, a polymer whose main
chain comprises recurrent amide groups. These compounds are generally
formed from combinations of diamines, diacids and amino acids</description>
        <go id="GO:0019876"/>
    </keyword>
    <keyword id="KW-0550">
        <name>Obesity</name>
        <description>Protein which, if defective, causes obesity, a disorder characterized
by excessive deposition of fat</description>
    </keyword>
    <keyword id="KW-0552">
        <name>Olfaction</name>
        <description>Protein involved in olfaction, the process of smelling</description>
        <go id="GO:0007608"/>
    </keyword>
    <keyword id="KW-0553">
        <name>Oncogene</name>
        <name>Oncoprotein</name>
        <description>Protein encoded by an oncogene, which promotes cell transformation
Examples include viral homologs of cellular proto-oncogenes such as
the transcription factors v-myc and v-jun, the growth factor v-fgr,
the regulatory GTPase v-ras, and papillomavirus protein E6</description>
    </keyword>
    <keyword id="KW-0554">
        <name>One-carbon metabolism</name>
        <name>One-carbon compound metabolic process</name>
        <description>Protein involved in the biochemical reactions with one-carbon groups,
e.g., methyl and formyl groups</description>
        <go id="GO:0006730"/>
    </keyword>
    <keyword id="KW-0896">
        <name>Oogenesis</name>
        <description>Protein involved in egg development and maturation. A process whereby
primordial germ cells form mature ova</description>
        <go id="GO:0048477"/>
    </keyword>
    <keyword id="KW-0555">
        <name>Opioid peptide</name>
        <description>Endogenous peptides with opiate-like activity</description>
        <go id="GO:0001515"/>
    </keyword>
    <keyword id="KW-0994">
        <name>Organellar chromatophore</name>
        <description>Protein encoded by the organellar chromatophore genome or a protein
targeted to the organellar chromatophore. The organellar chromatophore
is the photosynthetic inclusion found in Paulinella species, which are
photosynthetic thecate amoeba. It probably derives from a different
endosymbiotic event than that which led to all other plastids. Houses
the machinery necessary for photosynthesis and CO(2) fixation; it also
has the genetic capacity to synthesize some amino acids, some fatty
acids and a few cofactors. It contains thylakoid membranes, and a
residual peptidoglycan wall between the 2 envelope membranes. There
are 1 or 2 chromatophores per cell</description>
    </keyword>
    <keyword id="KW-0556">
        <name>Organic radical</name>
        <description>Protein which is posttranslationally modified by the formation of a
stable radical. E.g., P09373 is posttranslationally interconverted,
under anaerobic conditions, from an inactive to an active form that
carries a stable radical localized to a specific glycine at the C-
terminal region of the polypeptidic chain</description>
    </keyword>
    <keyword id="KW-0892">
        <name>Osteogenesis</name>
        <name>Bone formation</name>
        <name>Ossification</name>
        <description>Protein involved in osteogenesis, the mechanism of bone formation
wether intramembranous or endochondral. In intramembranous
ossification, bone is formed by differentiation of mesenchymal cells
into osteoblasts with absence of a cartilaginous model. The flat bones
of the skull, the sternum, and the scapula are examples of bones that
develop by intramembranous ossification. The term endochondral refers
to the close association of the developing bone with the pre-existing
hyaline cartilage model of that bone. The long bones of the limbs
(including the phalanges) and the ribs develop by endochondral
ossification</description>
        <go id="GO:0001503"/>
    </keyword>
    <keyword id="KW-1065">
        <name>Osteogenesis imperfecta</name>
        <name>Glass bone disease</name>
        <name>Fragilitas ostium</name>
        <name>Lobstein's disease</name>
        <name>Lobstein disease</name>
        <name>Brittle bone disease</name>
        <description>Protein which, if defective, causes osteogenesis imperfecta, a bone
disorder characterized by low bone mass, and brittle, osteoporotic and
easily fractured bones. It may also present with blue sclerae, loose
joints, and imperfect dentin formation</description>
    </keyword>
    <keyword id="KW-0987">
        <name>Osteopetrosis</name>
        <description>Protein which, if defective, causes osteopetrosis, an hereditary
disorder characterized by abnormally dense bone due to reduced bone
resorption, and by the common occurrence of fractures of affected
bones</description>
    </keyword>
    <keyword id="KW-1285">
        <name>Osteoporosis</name>
        <description>Protein which, if defective, is associated with osteoporosis, a very
common skeletal disorder, especially in women. Osteoporosis is
characterized by a decrease in bone mass and a deterioration in bone
microarchitecture without alteration in the composition of bone,
leading to enhanced fragility of the skeleton and a greater risk of
fracture. Osteoporosis is present when the bone mineral density is
over 2.5 standard deviations below the young adult reference in the
same sex. If fractures are present the condition is referred to as
severe osteoporosis. The main cause of osteoporosis is the continuous
loss of bone during life, which is exacerbate in women after
menopause</description>
    </keyword>
    <keyword id="KW-1152">
        <name>Outer capsid protein</name>
        <description>Viral protein that is a component of the outer layer of a double or
triple concentric icosahedral capsid. Outer capsids are part of
reoviridae and cystoviridae virions</description>
        <go id="GO:0039624"/>
    </keyword>
    <keyword id="KW-0558">
        <name>Oxidation</name>
        <description>Protein which is posttranslationally modified by oxidation of a
residue</description>
    </keyword>
    <keyword id="KW-0560">
        <name>Oxidoreductase</name>
        <description>Enzyme that catalyzes the oxidation of one compound with the reduction
of another</description>
        <go id="GO:0016491"/>
    </keyword>
    <keyword id="KW-0561">
        <name>Oxygen transport</name>
        <description>Protein involved in the transport of oxygen (e.g. hemoglobin and
myoglobin)</description>
        <go id="GO:0015671"/>
        <go id="GO:0005344"/>
    </keyword>
    <keyword id="KW-0925">
        <name>Oxylipin biosynthesis</name>
        <name>Oxylipin biosynthetic process</name>
        <name>Oxylipin formation</name>
        <name>Oxylipin anabolism</name>
        <name>Oxylipin synthesis</name>
        <description>Protein involved in the synthesis of oxygenated fatty acids
(oxylipins), including jasmonic acid (jasmonate) (JA) and its
derivatives. Oxylipins regulate many defense and developmental
pathways in plants. JA is involved in wound-mediated signaling
pathways, plant defense, and reproductive development. It acts as a
growth inhibitor and promotes senescence</description>
        <go id="GO:0031408"/>
    </keyword>
    <keyword id="KW-0562">
        <name>Pair-rule protein</name>
        <description>A protein encoded by a pair-rule gene. These are developmental genes
in Drosophila involved in delimiting segments in the early embryos
Mutations in pair rule genes affect every alternate segment</description>
        <go id="GO:0007366"/>
        <go id="GO:0007275"/>
    </keyword>
    <keyword id="KW-0563">
        <name>Paired box</name>
        <description>Protein which contains a paired box domain, a conserved domain of
about 120 amino acids, which is generally located in the N-terminal
section of various proteins</description>
    </keyword>
    <keyword id="KW-0564">
        <name>Palmitate</name>
        <name>n-hexadecanoate</name>
        <name>Palmitoylated</name>
        <description>Protein which is posttranslationally modified by the attachment of at
least one palmitate group. The palmitate (16-carbon saturated fatty
acid) group is usually attached to cysteine via a thioester bond
Lysine, serine and threonine may also serve as palmitate acceptors
Many palmitoylproteins are membrane associated either directly through
the palmitate moiety or as transmembrane proteins anchored by the
fatty acid. However, a few are actually secreted from cells</description>
    </keyword>
    <keyword id="KW-1007">
        <name>Palmoplantar keratoderma</name>
        <name>PPK</name>
        <name>Hyperkeratosis palmaris et plantaris</name>
        <name>Keratoderma palmaris et plantaris</name>
        <name>Palmoplantar keratosis</name>
        <name>Keratosis palmoplantaris</name>
        <description>Protein which, if defective, causes hereditary palmoplantar
keratoderma (PPK), a genetically and clinically diverse group of
cutaneous disorders characterized by abnormal thickening of the skin
on the palms and soles. It results from excessive keratin formation
leading to hypertrophy of the stratum corneum (hyperkeratosis). PPKs
are distinguished from each other on the basis of mode of inheritance,
presence of transgrediens (defined as contiguous extension of
hyperkeratosis beyond the palmar and/or plantar skin), association
with other skin findings and/or abnormalities of other organs, and
extent of epidermal involvement (diffuse, focal, punctate). Diffuse
PPK is characterized by uniform involvement of the palmoplantar
surface; focal PPK consists of localized areas of hyperkeratosis
located mainly on pressure points and sites of recurrent friction;
punctate PPK shows multiple small, hyperkeratotic papules or nodules
on the palms and soles</description>
    </keyword>
    <keyword id="KW-0566">
        <name>Pantothenate biosynthesis</name>
        <name>Pantothenate formation</name>
        <name>Pantothenate biosynthetic process</name>
        <name>Pantothenate synthesis</name>
        <name>Pantothenate anabolism</name>
        <description>Protein involved in the synthesis of pantothenate</description>
        <go id="GO:0015940"/>
    </keyword>
    <keyword id="KW-0907">
        <name>Parkinson disease</name>
        <name>Parkinson's disease</name>
        <name>PD</name>
        <name>Paralysis agitans</name>
        <description>Protein which, if defective, causes classic Parkinson disease
Parkinson disease is a complex multifactorial neurodegenerative
disorder, usually occurring in late life, although an early onset and
a juvenile form are known. Typical features are masklike facies,
tremor of resting muscles, a slowing of voluntary movements
(bradykinesia), festinating gait and postural instability. The signs
and symptoms of the disease are the consequence of a striatal
deficiency of dopamine, resulting from neuronal death in the
substantia nigra. Parkinson disease is characterized by the presence
of Lewy bodies, intraneuronal inclusions found in many brain regions
which are not entirely specific to, but are a highly sensitive marker
for, Parkinson disease</description>
    </keyword>
    <keyword id="KW-0908">
        <name>Parkinsonism</name>
        <description>Protein which, if defective, causes parkinsonism. Parkinsonism refers
to disorders, both genetic and non-genetic, characterized by four
primary parkinsonian symptoms: tremor, rigidity, postural instability
and bradykinesia, resulting from the loss or dysfunction of dopamine-
producing neurons in the substantia nigra. Lewy bodies, intraneuronal
accumulations of aggregated proteins, may or may not be present in the
brain of the patients</description>
    </keyword>
    <keyword id="KW-0568">
        <name>Pathogenesis-related protein</name>
        <name>PR protein</name>
        <description>Protein induced in several plant species when they are infected by
viruses, viroids, fungi or bacteria. The occurrence of these proteins
is not pathogen-specific, but determined by the type of reaction of
the host plant. They form a protective barrier against pathogens by
collecting at infection sites and act to decrease susceptibility of
plants. They may have anti-fungal or anti-bacterial activity</description>
        <go id="GO:0009607"/>
    </keyword>
    <keyword id="KW-0570">
        <name>Pentose shunt</name>
        <name>Hexose monophosphate pathway</name>
        <name>Pentose phosphate pathway</name>
        <name>Phosphogluconate oxidative pathway</name>
        <description>Protein involved in the pentose shunt, the biochemical pathway in
which glucose-6-phosphate is oxidized to 6-phosphogluconate with the
production of NADPH. Then 6-phosphogluconate is converted to ribulose-
5-phosphate and CO2 and a second molecule of NADH. This pathway is an
important source of NADPH and ribose-5-phosphate</description>
        <go id="GO:0006098"/>
    </keyword>
    <keyword id="KW-0571">
        <name>Peptide transport</name>
        <description>Protein involved in the transport of peptides</description>
        <go id="GO:0015833"/>
    </keyword>
    <keyword id="KW-0573">
        <name>Peptidoglycan synthesis</name>
        <name>Pseudomurein biosynthetic process</name>
        <name>Murein biosynthesis</name>
        <name>Peptidoglycan biosynthesis</name>
        <name>Pseudomurein synthesis</name>
        <name>Pseudomurein anabolism</name>
        <name>Peptidoglycan anabolism</name>
        <name>Peptidoglycan formation</name>
        <name>Pseudomurein formation</name>
        <name>Murein synthesis</name>
        <name>Peptidoglycan biosynthetic process</name>
        <name>Murein biosynthetic process</name>
        <name>Murein formation</name>
        <name>Pseudomurein biosynthesis</name>
        <name>Murein anabolism</name>
        <description>Protein involved in the synthesis of peptidoglycan which consists of a
glycosaminoglycan formed by alternating residues of D-glucosamine and
either muramic acid {2-amino-3-O-[(R)-1-carboxyethyl]-2-deoxy-D-
glucose} or L-talosaminuronic acid (2-amino-2-deoxy-L-taluronic acid),
which are usually N-acetylated or N-glycoloylated. The carboxyl group
of the muramic acid is commonly substituted by a peptide containing
residues of both L- and D-amino acids, whereas that of L-
talosaminuronic acid is substituted by a peptide consisting of L-amino
acids only. These peptide units may be cross-linked by a peptide bond,
thereby giving rise to a giant macromolecule that forms the rigid cell
wall (sacculus or murein sacculus). This macromolecule is known to
occur as a monomolecular layer between the inner and outer membrane in
Gram-negative bacteria and as a multimolecular layer, often associated
covalently or non-covalently with various additional compounds
(teichoic acids, neutral polysaccharides. etc.) in Gram-positive
bacteria. In the archaebacteria, several organisms contain a
peptidoglycan, also called pseudomurein, which differs in certain
respects from those of the eubacteria</description>
        <go id="GO:0009252"/>
    </keyword>
    <keyword id="KW-0572">
        <name>Peptidoglycan-anchor</name>
        <description>Protein that is covalently anchored to the peptidoglycan of a cell
wall envelope. In Gram-positive bacteria, binding proceeds through a
transpeptidation mechanism which requires a C-terminal sorting signal
with a conserved LPXTG or LPXAG motif; an amide bond is created
between the alpha-carboxyl group of the conserved threonine,
alternatively alanine, and the amino group of peptidoglycan cross-
bridges. In Gram-negative bacteria, binding proceeds through the
formation of an isopeptide bond between the epsilon-amino group of a
lysine and the alpha-carboxyl group of a peptidoglycan diaminopimelic
acid</description>
    </keyword>
    <keyword id="KW-0574">
        <name>Periplasm</name>
        <description>Protein located in the space between the inner membrane and the outer
membrane (cell wall) of Gram negative bacteria and some eukaryotic
algae. Also used for proteins located in the region between the plasma
membrane and the cell wall in fungi</description>
    </keyword>
    <keyword id="KW-0575">
        <name>Peroxidase</name>
        <description>Enzyme that catalyzes the oxidation of a substrate by reducing
peroxide to water. These enzymes are often located in peroxisomes</description>
        <go id="GO:0004601"/>
    </keyword>
    <keyword id="KW-0576">
        <name>Peroxisome</name>
        <description>Protein found in or associated with the peroxisome, a small eukaryotic
organelle limited by a single membrane, specialized for carrying out
oxidative reactions. Contains mainly peroxidases, several other
oxidases and catalase. The catalase regulates the contents of the
produced toxic hydrogen peroxide thus protecting the cell. Beta-
oxidation of fatty acids is another major function of peroxisomes. In
plants and fungi this degradation occurs only in this cellular
compartment</description>
    </keyword>
    <keyword id="KW-0962">
        <name>Peroxisome biogenesis</name>
        <name>Peroxisome assembly</name>
        <name>Peroxisome formation</name>
        <description>Protein which is involved in the formation, organization and
maintenance of the peroxisome. The peroxisome is a small eukaryotic
organelle limited by a single membrane, specialized for carrying out
oxidative reactions</description>
        <go id="GO:0007031"/>
    </keyword>
    <keyword id="KW-0958">
        <name>Peroxisome biogenesis disorder</name>
        <name>PBD</name>
        <name>Peroxisome-biogenesis disorder</name>
        <description>Protein which, if defective, causes peroxisome biogenesis disorder, a
group of peroxisomal disorders arising from a failure of protein
import into the peroxisomal membrane or matrix. The PBD group is
comprised of four disorders: Zellweger syndrome (ZWS), neonatal
adrenoleukodystrophy (NALD), infantile Refsum disease (IRD), and
classical rhizomelic chondrodysplasia punctata type 1 (RCDP1). ZWS,
NALD and IRD are distinct from RCDP1 and constitute a clinical
continuum of overlapping phenotypes known as Zellweger spectrum. The
PBD group is genetically heterogeneous with at least 12 distinct
genetic groups as concluded from complementation studies</description>
    </keyword>
    <keyword id="KW-1059">
        <name>Peters anomaly</name>
        <description>Protein which, if defective, causes Peters anomaly, an ocular disorder
characterized by congenital central corneal leukoma, absence of the
posterior corneal stroma and Descemet membrane, and a variable degree
of iris and lenticular attachments to the central aspect of the
posterior cornea</description>
    </keyword>
    <keyword id="KW-0577">
        <name>PHA biosynthesis</name>
        <name>Poly(3-hydroxyalkanoate) biosynthesis</name>
        <name>PHA synthesis</name>
        <name>Poly(3-hydroxyalkanoate) anabolism</name>
        <name>Poly(3-hydroxyalkanoate) synthesis</name>
        <name>Poly(3-hydroxyalkanoate) formation</name>
        <name>PHA formation</name>
        <name>Poly(3-hydroxyalkanoate) biosynthetic process</name>
        <name>PHA anabolism</name>
        <name>PHA biosynthetic process</name>
        <description>Protein involved in the synthesis of poly(3-hydroxyalkanoates) (PHA)
In Pseudomonas oleovorans large amounts of this polyester are
synthesized when cells are grown under nitrogen-limiting conditions
When nitrogen is further supplied in the medium, the accumulated PHA
is degraded</description>
        <go id="GO:0042621"/>
    </keyword>
    <keyword id="KW-0581">
        <name>Phagocytosis</name>
        <description>Protein that is involved in phagocytosis or that renders the organism
resistant to phagocytosis, the process by which a cell is engulfed and
broken down by another for purposes of defense or sustenance</description>
        <go id="GO:0006909"/>
    </keyword>
    <keyword id="KW-0582">
        <name>Pharmaceutical</name>
        <description>Protein which is used or may be used as a pharmaceutical drug, e.g. to
treat specific diseases</description>
    </keyword>
    <keyword id="KW-0583">
        <name>PHB biosynthesis</name>
        <name>PHB anabolism</name>
        <name>PHB biosynthetic process</name>
        <name>Poly-(3-hydroxybutyrate) anabolism</name>
        <name>Poly-(3-hydroxybutyrate) biosynthetic process</name>
        <name>Poly-hydroxybutyrate synthesis</name>
        <name>Poly-beta-hydroxybutyrate anabolism</name>
        <name>Poly-(3-hydroxybutyrate) formation</name>
        <name>Poly-(3-hydroxybutyrate) synthesis</name>
        <name>Poly-(3-hydroxybutyrate) biosynthesis</name>
        <name>Poly-beta-hydroxybutyrate formation</name>
        <name>Poly-beta-hydroxybutyrate synthesis</name>
        <name>Poly-hydroxybutyrate formation</name>
        <name>Poly-beta-hydroxybutyrate biosynthetic process</name>
        <name>Poly-hydroxybutyrate biosynthetic process</name>
        <name>PHB formation</name>
        <name>Poly-hydroxybutyrate anabolism</name>
        <name>Poly-hydroxybutyrate biosynthesis</name>
        <name>PHB synthesis</name>
        <name>Poly-beta-hydroxybutyrate biosynthesis</name>
        <description>Protein involved in the synthesis of poly-hydroxybutyrate (PHB). It
accumulates in a variety of bacteria as an energy source. This
polyester is thermoplastic with biodegradable properties</description>
        <go id="GO:0042619"/>
    </keyword>
    <keyword id="KW-0584">
        <name>Phenylalanine biosynthesis</name>
        <name>Phenylalanine formation</name>
        <name>Phenylalanine biosynthetic process</name>
        <name>Phenylalanine synthesis</name>
        <name>Phenylalanine anabolism</name>
        <description>Protein involved in the biosynthesis of the aromatic amino acid
phenylalanine</description>
        <go id="GO:0009094"/>
    </keyword>
    <keyword id="KW-0585">
        <name>Phenylalanine catabolism</name>
        <name>Phenylalanine breakdown</name>
        <name>Phenylalanine degradation</name>
        <name>Phenylalanine catabolic process</name>
        <description>Protein involved in the degradation of the aromatic amino acid
phenylalanine</description>
        <go id="GO:0006559"/>
    </keyword>
    <keyword id="KW-0586">
        <name>Phenylketonuria</name>
        <description>Protein which, if defective, causes phenylketonuria, an autosomal
recessive disorder in which the body is unable to break down the amino
acid phenylalanine. The resulting buildup of phenylalanine in the body
causes intellectual disability, mental disturbances, eczema and skin
pigmentation</description>
    </keyword>
    <keyword id="KW-0587">
        <name>Phenylpropanoid metabolism</name>
        <name>Phenylpropanoid metabolic process</name>
        <description>Protein involved in the biochemical reactions with phenylpropanoids</description>
        <go id="GO:0009698"/>
    </keyword>
    <keyword id="KW-0588">
        <name>Pheromone</name>
        <description>Proteins which acts as a pheromone. Pheromones are odours of
conspecifics which elicit an adaptive behavioral response, e.g. insect
sex pheromones. Generally, they are comprised of mixtures of compounds
and behavioral responsiveness to them is largely instinctual,
sexually-dimorphic, and attributable to a specialized component(s) of
the olfactory system</description>
        <go id="GO:0005186"/>
    </keyword>
    <keyword id="KW-0589">
        <name>Pheromone response</name>
        <name>Response to pheromone</name>
        <name>Pheromone response pathway</name>
        <description>Protein involved in the pheromone response</description>
        <go id="GO:0019236"/>
    </keyword>
    <keyword id="KW-0590">
        <name>Pheromone-binding</name>
        <description>Protein which binds pheromones, the odours of conspecifics which
elicit an adaptive behavioral response, e.g. insect sex pheromones</description>
        <go id="GO:0005550"/>
    </keyword>
    <keyword id="KW-0592">
        <name>Phosphate transport</name>
        <description>Protein involved in the transport of phosphate</description>
        <go id="GO:0006817"/>
    </keyword>
    <keyword id="KW-0593">
        <name>Phospholipase A2 inhibitor</name>
        <description>Protein which inhibits phospholipase A2 (EC 3.1.1.4) (PA2), an enzyme
which releases fatty acids from the second carbon group of glycerol
Phospholipase A2 inhibitors are widely distributed in venoms and
digestive secretions</description>
        <go id="GO:0019834"/>
    </keyword>
    <keyword id="KW-0594">
        <name>Phospholipid biosynthesis</name>
        <name>Phospholipid anabolism</name>
        <name>Phospholipid formation</name>
        <name>Phospholipid biosynthetic process</name>
        <name>Phospholipid synthesis</name>
        <description>Protein involved in the synthesis of phospholipids, the major lipid
component of most cellular membranes. Phospholipids are usually
composed of two fatty acid chains esterified to two of the carbons of
glycerol phosphate, the phosphate being esterified to a hydroxyl group
of another hydrophilic compound, such as choline, ethanolamine or
serine</description>
        <go id="GO:0008654"/>
    </keyword>
    <keyword id="KW-0595">
        <name>Phospholipid degradation</name>
        <name>Phospholipid catabolic process</name>
        <name>Phospholipid catabolism</name>
        <name>Phospholipid breakdown</name>
        <description>Protein involved in the breakdown of phospholipids, the major lipid
component of most cellular membranes. Phospholipids are usually
composed of two fatty acid chains esterified to two of the carbons of
glycerol phosphate, the phosphate being esterified to a hydroxyl group
of another hydrophilic compound, such as choline, ethanolamine or
serine</description>
        <go id="GO:0009395"/>
    </keyword>
    <keyword id="KW-1208">
        <name>Phospholipid metabolism</name>
        <name>Phospholipid metabolic process</name>
        <description>Protein involved in the metabolism of phospholipids, the major lipid
component of most cellular membranes. Phospholipids are usually
composed of two fatty acid chains esterified to two of the carbons of
glycerol phosphate, the phosphate being esterified to a hydroxyl group
of another hydrophilic compound, such as choline, ethanolamine or
serine</description>
    </keyword>
    <keyword id="KW-0918">
        <name>Phosphonate transport</name>
        <description>Protein involved in the transport of phosphonates. Phosphonates are a
class of organophosphorus compounds characterized by a chemically
stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread
among naturally occurring compounds in all kingdoms of wildlife, but
only prokaryotic microorganisms are able to cleave this bond. Certain
bacteria such as Escherichia coli can use alkylphosphonates as a
phosphorus source</description>
        <go id="GO:0015716"/>
    </keyword>
    <keyword id="KW-0596">
        <name>Phosphopantetheine</name>
        <name>Pantetheine 4'phosphate</name>
        <description>Protein which contains at least one phosphopantetheine as the
prosthetic group. In acyl carrier proteins (ACP) for example, it
serves as a 'swinging arm' for the attachment of activated fatty acid
and amino-acid groups</description>
    </keyword>
    <keyword id="KW-0597">
        <name>Phosphoprotein</name>
        <name>Phosphorylation</name>
        <description>Protein which is posttranslationally modified by the attachment of
either a single phosphate group, or of a complex molecule, such as 5'-
phospho-DNA, through a phosphate group. Target amino acid is usually
serine, threonine or tyrosine residues (mostly in eukaryotes),
aspartic acid or histidine residues (mostly in prokaryotes)</description>
    </keyword>
    <keyword id="KW-0598">
        <name>Phosphotransferase system</name>
        <name>Phosphoenolpyruvate-dependent sugar phosphotransferase system</name>
        <name>Sugar phosphotransferase system</name>
        <name>PTS</name>
        <description>Protein involved in the phosphotransferase system, the major
carbohydrate transport system in bacteria. This phosphotransferase
system catalyzes the transfer of the phosphoryl group from
phosphoenolpyruvate to incoming sugar substrates concomitant with
their translocation across the cell membrane</description>
        <go id="GO:0009401"/>
    </keyword>
    <keyword id="KW-0599">
        <name>Photoprotein</name>
        <description>Luminescent proteins, which are involved in the phenomenon of light
emission in certain living organisms. E.g., green fluorescent protein
which is unique among fluorescent proteins in that its chromophore is
not a separately synthesized prostethic group but is composed of
modified amino acid residues within its polypeptide chain</description>
        <go id="GO:0008218"/>
    </keyword>
    <keyword id="KW-0600">
        <name>Photoreceptor protein</name>
        <name>Light-sensing protein</name>
        <name>Photosensor protein</name>
        <description>Protein involved in the convertion of light directly into a signal
These proteins are classified in a limited number of families based on
the chemical structure of the light-absorbing chromophores involved,
and also on protein sequence similarities to discriminate the many
photoreceptor proteins that bind a flavin derivative. Accordingly, the
most important families are the rhodopsins, the phytochromes, the
xanthopsins, the cryptochromes, the phototropins and the BLUF
proteins</description>
        <go id="GO:0009881"/>
    </keyword>
    <keyword id="KW-0601">
        <name>Photorespiration</name>
        <description>Protein involved in a light-dependent process to convert 2-phospho-
glycolate (2-PG) into 3-phospho-D-glycerate (3-PG), where oxygen is
consumed and carbon dioxide released. It takes place in plants and
cyanobacteria during the light period, since in the presence of O(2)
their type of Rubisco can catalyze the oxidative fragmentation of
ribulose 1,5-biphosphate to 3-PG and 2-PG. 2-PG inhibits the Calvin
cycle enzyme triose-phosphate isomerase, and so must be eliminated
quickly. In plants 2-PG is recycled to 3-PG via reactions in
peroxisomes, mitochondria as well as chloroplasts. For every 2
molecules of 2-PG, one molecule of 3-PG is formed and one molecule of
CO(2) is lost. In cyanobacteria it seems there are two mechanisms to
deal with 2-PG; a path similar to that described for plants and the
bacterial-like glycerate pathway</description>
        <go id="GO:0009853"/>
    </keyword>
    <keyword id="KW-0602">
        <name>Photosynthesis</name>
        <description>Protein involved in photosynthesis, the process in which light energy
is absorbed by photosynthetic pigments (e.g. chlorophyll) and
converted to chemical energy (usually ATP and NADPH, =light reaction)
This energy is subsequently used as an energy source for the reduction
of carbon dioxide to carbohydrate (=Calvin cycle). The general
reaction is: CO(2) + 2H(2)A = (CH(2)O) + 2A + H(2)O, where 2H(2)A is
any reduced compound that can serve as an electron donor. In plants,
algae and cyanobacteria H(2)O serves as a reductant, generating O(2)
Non-oxygenic organisms use other electron donors, for example H(2)S in
purple sulfur bacteria, generating sulfur</description>
        <go id="GO:0015979"/>
    </keyword>
    <keyword id="KW-0603">
        <name>Photosystem I</name>
        <name>P700</name>
        <name>PSI</name>
        <description>Protein involved in photosystem I (PSI), a complex that uses light
energy to mediate electron flow in the chloroplast thylakoid membrane
of plants and in cyanobacteria. In linear electron flow, PSII is
coupled to PSI and produces a pH gradient, ATP and NADPH. In cyclic
electron flow, PSI generates a pH gradient and ATP. PSI is excited
best by light at about 700 nm, and is thus sometimes called P700. PSI
is an iron-sulfur type reaction center (RC), sharing a common ancestor
with the RCs of Heliobacteriaceae, green sulfur and green non-sulfur
bacteria</description>
        <go id="GO:0009522"/>
    </keyword>
    <keyword id="KW-0604">
        <name>Photosystem II</name>
        <name>PSII</name>
        <name>P680</name>
        <description>Protein involved in photosystem II (PSII), a complex that uses light
energy to mediate electron flow in the chloroplast thylakoid membrane
of plants and in cyanobacteria. PSII splits water, releasing hydrogen
ions and molecular oxygen. PSII cannot use photons of a wavelength
greater than 680 nm, and is thus sometimes called P680. PSII is a
quinone type rection center (RC), sharing a common ancestor with the
RCs of purple bacteria</description>
        <go id="GO:0009523"/>
    </keyword>
    <keyword id="KW-0605">
        <name>Phycobilisome</name>
        <description>Protein found in phycobilisome, an accessory light energy harvesting
structure on the outer face of the thylakoid membranes in
cyanobacteria and red algae. Phycobilisomes are mainly composed of
phycobiliproteins (such as allophycocyanin, phycocyanin and
phycoerythrin) together with linker polypeptides</description>
        <go id="GO:0030089"/>
    </keyword>
    <keyword id="KW-0607">
        <name>Phytochrome signaling pathway</name>
        <description>Protein involved in the relay of information from the activated
phytochrome molecule to target genes. Different phytochromes use both
separate and common early signaling pathways. These pathways converge
downstream in a process of signal integration that regulates
photomorphogenesis and the circadian clock. This provides the means by
which information from specific wavelengths of light may be amplified
and coordinated</description>
        <go id="GO:0009585"/>
        <go id="GO:0010017"/>
    </keyword>
    <keyword id="KW-0608">
        <name>Pigment</name>
        <description>Protein which binds or transport pigments, any coloring matter in
animals, plants or microorganisms</description>
        <go id="GO:0031409"/>
    </keyword>
    <keyword id="KW-0611">
        <name>Plant defense</name>
        <description>Protein involved in plant defense, either as part of preexisting,
developmentally regulated defense barriers (such as thionins,
defensins or hydroxyproline-rich glycoproteins fortifying the cell
wall) or as components of the defense responses induced upon pathogen
infection during hypersensitive cell death (HR), local acquired
resistance (LAR) or systemic acquired resistance (SAR). This includes
proteins involved in various pathways, such as the gene-for-gene
resistance, the salicylic acid (SA)-dependant resistance, the
jasmonate (JA) and/or ethylene (ET)-dependant resistance and the
induced systemic resistance (ISR), as well as the final products of
those pathways such as the pathogenesis-related proteins</description>
        <go id="GO:0006952"/>
    </keyword>
    <keyword id="KW-0614">
        <name>Plasmid</name>
        <description>Protein encoded on a plasmid, a self-replicating circular DNA that is
found in a variety of bacterial, archaeal, fungal, algal and plant
species, and can be transferred from one organism to another. Plasmids
often carry antibiotic-resistant genes and are widely used in
molecular biology as vectors of genes and in cloning</description>
    </keyword>
    <keyword id="KW-0615">
        <name>Plasmid copy control</name>
        <description>Protein involved in the plasmid copy control, the ability of a plasmid
to control its own copy number in a cell. Copy number is a function of
the rate at which DNA synthesis is initiated</description>
        <go id="GO:0006276"/>
    </keyword>
    <keyword id="KW-0616">
        <name>Plasmid partition</name>
        <description>Protein involved in plasmid partition, the process whereby newly
replicated plasmids are distributed properly to daughter cells during
cell division</description>
        <go id="GO:0030541"/>
    </keyword>
    <keyword id="KW-0617">
        <name>Plasminogen activation</name>
        <description>Protein involved in the plasminogen activation which occurs when an
heterogeneous group of proteolytic enzymes convert plasminogen to
plasmin</description>
    </keyword>
    <keyword id="KW-0934">
        <name>Plastid</name>
        <description>Protein encoded by or localized in a plastid, a semi-autonomous, self-
reproducing organelle. Plastids are remnants of a photosynthetic
organism that was engulfed by the host, although not all are now
photosynthetic. Plastid genomes encode genes for rRNAs, tRNAs and
between about 28 and 150 proteins. Plastids can be categorized in 4
main groups: chloroplasts, cyanelles, apicoplasts and non-
photosynthetic. The latter are found is some land plants (Epifagus
virginiana), chlorophyte algae (Prototheca wickerhamii) and euglenoids
(Astasis longa), which do not encode the genes necessary for
photosynthesis and so are not photosynthetic but still contain a
plastid. Non-photosynthetic plastids probably do not contain
thylakoids</description>
    </keyword>
    <keyword id="KW-1001">
        <name>Plastid inner membrane</name>
        <name>Plastidic inner membrane</name>
        <name>Inner plastidic membrane</name>
        <name>Inner plastid membrane</name>
        <description>Protein found in or associated with the inner membrane of a plastid,
which separates the plastid stroma from the intermembrane space</description>
    </keyword>
    <keyword id="KW-1002">
        <name>Plastid outer membrane</name>
        <name>Plastidic outer membrane</name>
        <name>Outer plastidic membrane</name>
        <name>Outer plastid membrane</name>
        <description>Protein found in or associated with the outer membrane of a plastid,
which is the membrane facing the cytoplasm</description>
    </keyword>
    <keyword id="KW-0618">
        <name>Plastoquinone</name>
        <description>Protein which interacts with plastoquinone, a substituted quinone
called plastoquinone because it appeared concentrated in the
chloroplasts of higher plants. Plastoquinone transfers electrons from
the photosystem II reaction center to the cytochrome bf complex and
carries protons across the photosynthetic membrane</description>
    </keyword>
    <keyword id="KW-1202">
        <name>Platelet aggregation activating toxin</name>
        <description>Toxin which induces agonist-induced platelet aggregation, the self-
adhesion of platelets via adhesion molecules. Numerous snake venom
families have the capacity to induce platelet aggregation</description>
    </keyword>
    <keyword id="KW-1201">
        <name>Platelet aggregation inhibiting toxin</name>
        <description>Toxin which inhibits agonist-induced platelet aggregation, the self-
adhesion of platelets via adhesion molecules. Numerous snake venom
families have the capacity to inhibit platelet aggregation</description>
    </keyword>
    <keyword id="KW-0620">
        <name>Polyamine biosynthesis</name>
        <description>Protein involved in polyamine biosynthesis. The polyamines, e.g
putrescine, cadaverine, agmatine, spermidine and spermine, are wide-
spread in all organisms, and have been shown to play a role in the
regulation of growth and differentiation of virtually all types of
cells</description>
        <go id="GO:0006596"/>
    </keyword>
    <keyword id="KW-0624">
        <name>Polysaccharide degradation</name>
        <description>Protein involved in polysaccharide degradation, the breakdown of
polysaccharides</description>
        <go id="GO:0000272"/>
    </keyword>
    <keyword id="KW-0625">
        <name>Polysaccharide transport</name>
        <description>Protein involved in the transport of polysaccharides</description>
        <go id="GO:0015774"/>
    </keyword>
    <keyword id="KW-1021">
        <name>Pontocerebellar hypoplasia</name>
        <name>PCH</name>
        <name>Pontocerebellar atrophy</name>
        <description>Protein which, if defective, causes pontocerebellar hypoplasia, a
heterogeneous group of congenital disorders characterized by
hypoplasia and atrophy of the cerebellar cortex, dentate nuclei,
pontine nuclei and inferior olives. Additional defects of other brain
and spinal cord structures can be present, resulting in clinical
manifestations that vary among cases</description>
    </keyword>
    <keyword id="KW-1172">
        <name>Pore-mediated penetration of viral genome into host cell</name>
        <name>Membrane puncture-mediated penetration of viral genome into host cell</name>
        <description>Virion-associated pore-forming protein that induces the formation of a
transmembrane pore or channel in the host membrane(s) to allow the
viral genome to enter the host cytoplasm. This mechanism is used by
non-enveloped viruses such as human rhinovirus 2 or poliovirus. Many
tailed bacteriophages carry specialized proteins which open a pore or
a channel in the host membrane(s) to allow penetration of the virion
tail into host envelope and genome delivery into host cytoplasm</description>
        <go id="GO:0044694"/>
    </keyword>
    <keyword id="KW-0626">
        <name>Porin</name>
        <description>Membrane protein which in a multimeric form constitutes a water-filled
transmembrane channel (a pore). This pore allows the passage of ions
and numerous other, non-specific molecules through the membrane. Found
in the mitochondrial and plastid outer membrane of eukaryotes, in many
Gram-negative bacteria, at least some Corynebacterineae, archaea and
in sea anemones</description>
        <go id="GO:0015288"/>
        <go id="GO:0046930"/>
    </keyword>
    <keyword id="KW-0627">
        <name>Porphyrin biosynthesis</name>
        <description>Protein involved in the synthesis of porphyrins which are compounds
that contain the porphin structure, e.g. four pyrrole rings connected
by methine bridges in a cyclic configuration to which a variety of
side chains are attached. Porphyrins often chelate metal ions (Fe, Mg,
Co, Zn, Cu, Ni). Examples are, heme proteins (which contain iron
porphyrins) like myoglobin, hemoglobin, cytochromes, or related
macrocycles including chlorophylls (which have a central magnesium
ion) and pheophytins (which are metal free) and vitamin B-12 (which
has cobalt)</description>
        <go id="GO:0006779"/>
    </keyword>
    <keyword id="KW-0628">
        <name>Postsynaptic cell membrane</name>
        <name>Postsynaptic membrane</name>
        <description>Protein characteristic of the postsynaptic membrane. In a chemical
synapse, the postsynaptic membrane is the membrane that receives a
signal (binds neurotransmitter) from the presynaptic cell and responds
via depolarisation or hyperpolarisation. The postsynaptic membrane is
separated from the presynaptic membrane by the synaptic cleft</description>
    </keyword>
    <keyword id="KW-0629">
        <name>Postsynaptic neurotoxin</name>
        <description>Protein which acts as a neurotoxin at the postsynaptic membrane. They
bind to acetylcholine receptors and so inhibit their activity</description>
        <go id="GO:0035792"/>
    </keyword>
    <keyword id="KW-0630">
        <name>Potassium</name>
        <description>Protein which binds at least one potassium, or protein whose function
is potassium-dependent. Potassium is an alkali metal, chemical symbol
K</description>
    </keyword>
    <keyword id="KW-0631">
        <name>Potassium channel</name>
        <description>Protein which is part of a transmembrane protein complex that forms a
hydrophilic channel across the lipid bilayer through which potassium
ions can diffuse down their electrochemical gradient. The channels are
gated and only open in response to a specific stimulus, such as a
change in membrane potential (voltage-gated). They are important for
the regulation of the resting membrane potential and for the control
of the shape and frequency of action potentials</description>
        <go id="GO:0071805"/>
        <go id="GO:0005267"/>
    </keyword>
    <keyword id="KW-0632">
        <name>Potassium channel impairing toxin</name>
        <description>Protein which interferes with the function of potassium channels which
are membrane proteins forming a channel in a biological membrane
selectively permeable to potassium ions. They are found in various
venoms from snakes, scorpions and spiders</description>
        <go id="GO:0015459"/>
    </keyword>
    <keyword id="KW-0633">
        <name>Potassium transport</name>
        <description>Protein involved in the transport of potassium ions</description>
        <go id="GO:0006813"/>
    </keyword>
    <keyword id="KW-0634">
        <name>PQQ</name>
        <name>Pyrroloquinoline quinone</name>
        <name>Methoxatin</name>
        <description>Protein which non-covalently binds at least one pyrroloquinoline
quinone (PQQ) cofactor</description>
    </keyword>
    <keyword id="KW-0884">
        <name>PQQ biosynthesis</name>
        <name>Pyrroloquinoline quinone biosynthesis</name>
        <description>Protein involved in the biosynthesis of the cofactor pyrroloquinoline
quinone (PQQ)</description>
        <go id="GO:0018189"/>
    </keyword>
    <keyword id="KW-0635">
        <name>Pregnancy</name>
        <description>Protein which plays a role in pregnancy, the condition of having a
developing embryo or fetus in the body, after union of an ovum and
spermatozoon</description>
        <go id="GO:0007565"/>
    </keyword>
    <keyword id="KW-1066">
        <name>Premature ovarian failure</name>
        <name>Primary ovarian insufficiency</name>
        <description>Protein which, if defective, causes premature ovarian failure, a
condition characterized by the arrest of normal ovarian function
before the age of 40 years, due to a primary ovarian defect. It is
characterized by absent menarche (primary amenorrhea) or premature
depletion of ovarian follicles (secondary amenorrhea)</description>
    </keyword>
    <keyword id="KW-0636">
        <name>Prenylation</name>
        <description>Protein which is posttranslationally modified by the attachment of at
least one prenyl group (e.g. farnesyl, geranylgeranyl) usually on
cysteine residues which are at or near the C-terminal extremity</description>
    </keyword>
    <keyword id="KW-0637">
        <name>Prenyltransferase</name>
        <description>Enzyme that catalyzes the transfer of an isoprenoid (farnesyl or
geranylgeranyl) usually on cysteine residues, which are three residues
away from the C-terminal extremity</description>
        <go id="GO:0004659"/>
    </keyword>
    <keyword id="KW-0638">
        <name>Presynaptic neurotoxin</name>
        <description>Protein which acts as a neurotoxin at the presynaptic membrane and
usually blocks neuromuscular transmission</description>
        <go id="GO:0044231"/>
    </keyword>
    <keyword id="KW-0990">
        <name>Primary ciliary dyskinesia</name>
        <name>PCD</name>
        <name>CILD</name>
        <name>ICS</name>
        <name>Immotile cilia syndrome</name>
        <description>Protein which, if defective, causes primary ciliary dyskinesia, a rare
and genetically heterogeneous disorder characterized by sino-pulmonary
disease, laterality defects and male infertility. Primary ciliary
dyskinesia is due to dysfunction of motile cilia and flagella in
various organ systems</description>
    </keyword>
    <keyword id="KW-0982">
        <name>Primary hypomagnesemia</name>
        <description>Protein which, if defective, causes primary hypomagnesemia. Primary
hypomagnesemia defines a heterogeneous group of disorders
characterized by low magnesium serum content due to primary renal or
intestinal magnesium wasting. Primary hypomagnesemia disorders
generally share symptoms of magnesium depletion, such as tetany and
generalized convulsions. They often include associated disturbances in
calcium excretion</description>
    </keyword>
    <keyword id="KW-0905">
        <name>Primary microcephaly</name>
        <description>Protein which, if defective, causes primary microcephaly. This is a
neurodevelopmental condition characterized by a head circumference
more than 3 standard deviations below the age, sex and ethnically
matched mean, and absence of other syndromic features or significant
neurological deficits. Brain weight is markedly reduced and the
cerebral cortex is disproportionately small. Primary microcephaly is
also known as true microcephaly or microcephaly vera</description>
    </keyword>
    <keyword id="KW-1274">
        <name>Primary mitochondrial disease</name>
        <name>PMD</name>
        <name>Mitochondrial encephalomyopathy</name>
        <name>Mitochondrial myopathy</name>
        <name>Respiratory chain disorder</name>
        <name>Mitochondrial disorder</name>
        <name>Oxidative phosphorylation disorder</name>
        <description>Protein which, if defective, causes any one of a clinically
heterogeneous group of disorders arising from dysfunction of the
mitochondrial respiratory chain. The phenotypic spectrum ranges from
isolated diseases affecting single organs to severe multisystem
disorders. Common clinical features include ptosis, external
ophthalmoplegia, proximal myopathy and exercise intolerance,
cardiomyopathy, sensorineural deafness, optic atrophy, pigmentary
retinopathy, encephalopathy, seizures, stroke-like episodes, ataxia,
and spasticity. Mitochondrial disorders can be caused by mutations of
mitochondrial DNA or nuclear DNA that either affect oxidative
phosphorylation proteins directly, or affect respiratory chain
function by impacting the production of the complex machinery needed
to run this process</description>
    </keyword>
    <keyword id="KW-0639">
        <name>Primosome</name>
        <description>Component of the complex involved in the synthesis of RNA primer
sequences used in DNA replication. Main components are primases and
replicative DNA helicases that move as a unit along the replication
fork</description>
        <go id="GO:1990077"/>
        <go id="GO:0006269"/>
    </keyword>
    <keyword id="KW-0640">
        <name>Prion</name>
        <description>Protein which is able to form a prion, a self-propagating protein
conformation (infectious protein). Formation of prions involves
conversion of the native proteins into an infectious, amyloid form
This class of proteins includes the members of the prion family which
can form proteinaceous infectious particles responsible for
transmissible spongiform encephalopathies (TSE) in many animals, such
as Kuru and Creutzfeldt-Jakob syndrome in humans, scrapies in sheep
and BSE in cattle. These prion diseases represent special cases of
neurodegenerative amyloidoses, because they result from the
transmissibility and infectivity of the amyloid</description>
    </keyword>
    <keyword id="KW-0935">
        <name>Progressive external ophthalmoplegia</name>
        <description>Protein which, if defective, causes progressive external
ophthalmoplegia with mitochondrial DNA deletions. Progressive external
ophthalmoplegia (PEO) is characterized by ptosis and weakness of the
extraocular muscles. Typical symptoms are ophthalmoparesis and
exercise intolerance. Some people also may develop cardiomyopathy,
cataracts, ataxia, peripheral neuropathy, hypogonadism or major
depression. The diagnosis depends on the demonstration, by Southern
blotting, of multiple deletions of mtDNA in muscle biopsy specimens
Both autosomal dominant and autosomal recessive inheritance can occur
The autosomal recessive form, which is often associated with
multisystemic disorders, is clinically more heterogenous than the
autosomal dominant form and can be more severe</description>
    </keyword>
    <keyword id="KW-0641">
        <name>Proline biosynthesis</name>
        <description>Protein involved in the biosynthesis of the cyclic amino acid proline
The structure of proline differs from the structure of other amino
acids in that its side chain is bonded to the nitrogen of the amino
group as well as to the carbon atom. This makes the amino group a
secondary amine, and because of this, proline is also described as an
imino acid. The presence of proline residues strongly influences the
secondary structure of proteins</description>
        <go id="GO:0006561"/>
    </keyword>
    <keyword id="KW-0642">
        <name>Proline metabolism</name>
        <description>Protein involved in a biochemical reaction with the cyclic amino acid
proline. The structure of proline differs from the structure of other
amino acids in that its side chain is bonded to the nitrogen of the
amino group as well as to the carbon atom. This makes the amino group
a secondary amine, and because of this, proline is also described as
an imino acid. The presence of proline residues strongly influences
the secondary structure of proteins</description>
        <go id="GO:0006560"/>
    </keyword>
    <keyword id="KW-0643">
        <name>Prostaglandin biosynthesis</name>
        <description>Protein involved in the biosynthesis of prostaglandins. Prostaglandins
are fatty acids composed of 20 carbons with a substituted cyclopentane
ring. There are four major classes of prostaglandin, which differ in
the position of the double bonds and/or the oxygen substituents on the
ring: PGA, PGB, PGE, and PGF. They are found in many mammalian
tissues</description>
        <go id="GO:0001516"/>
    </keyword>
    <keyword id="KW-0644">
        <name>Prostaglandin metabolism</name>
        <description>Protein involved in a biochemical reaction with prostaglandins
Prostaglandins are fatty acids composed of 20 carbons with a
substituted cyclopentane ring. There are four major classes of
prostaglandin, which differ in the position of the double bonds and/or
the oxygen substituents on the ring: PGA, PGB, PGE, and PGF. They are
found in many mammalian tissues</description>
        <go id="GO:0006693"/>
    </keyword>
    <keyword id="KW-0645">
        <name>Protease</name>
        <name>Peptidase</name>
        <name>Peptide hydrolase</name>
        <name>Proteinase</name>
        <description>Enzyme which hydrolyzes peptide bonds</description>
        <go id="GO:0008233"/>
        <go id="GO:0006508"/>
    </keyword>
    <keyword id="KW-0646">
        <name>Protease inhibitor</name>
        <description>Protein which inhibits or antagonizes the biosynthesis of proteases or
their activity</description>
        <go id="GO:0030414"/>
        <go id="GO:0010466"/>
    </keyword>
    <keyword id="KW-0647">
        <name>Proteasome</name>
        <name>Macropain</name>
        <name>Prosome</name>
        <description>Protein which is part of the proteasome, a large protein complex in
the cytosol that is responsible for degrading proteins which have been
marked for destruction by ubiquitination or by some other means</description>
        <go id="GO:0000502"/>
    </keyword>
    <keyword id="KW-0648">
        <name>Protein biosynthesis</name>
        <description>Protein involved in the biosynthesis of proteins from mRNA molecules
This process, called translation, is carried out by ribosomes, where
activated amino acids are added to the nascent polypeptide chain</description>
        <go id="GO:0006412"/>
    </keyword>
    <keyword id="KW-0649">
        <name>Protein kinase inhibitor</name>
        <description>Protein which inhibits the activity of a protein kinase</description>
        <go id="GO:0004860"/>
    </keyword>
    <keyword id="KW-0904">
        <name>Protein phosphatase</name>
        <name>Phosphoprotein phosphatase</name>
        <description>Enzyme that catalyzes the hydrolysis of phosphate monoesters bonds of
phosphoserines, phosphothreonines, phosphotyrosines or phosphoaspartic
acids. While many protein phosphatases inhibit the activities of
phosphorylation cascades, some activate them</description>
        <go id="GO:0004721"/>
    </keyword>
    <keyword id="KW-0650">
        <name>Protein phosphatase inhibitor</name>
        <description>Protein which inhibits the activity of a protein phosphatase</description>
        <go id="GO:0004864"/>
    </keyword>
    <keyword id="KW-0651">
        <name>Protein splicing</name>
        <description>Protein which undergoes protein self-splicing, a posttranslational
modification involving the excision of an intervening protein sequence
(intein) from a protein precursor and the concomitant ligation of the
flanking protein fragments (exteins) to form a mature extein protein
and the free intein</description>
    </keyword>
    <keyword id="KW-0652">
        <name>Protein synthesis inhibitor</name>
        <description>Protein which blocks the synthesis of proteins (translation) through
various mechanisms, including hydrolysis of cellular tRNA, and
inactivation of the 60S subunits of eukaryotic ribosome</description>
        <go id="GO:0017148"/>
    </keyword>
    <keyword id="KW-0653">
        <name>Protein transport</name>
        <description>Protein involved in the intracellular transport of proteins from one
location to another. All proteins (except the ones synthesized in
mitochondria and plastids) are synthesized on ribosomes in the
cytosol. Most proteins remain in the cytosol. Proteins with a signal
sequence either become plasma membrane components or are exported from
the cell of origin</description>
        <go id="GO:0015031"/>
    </keyword>
    <keyword id="KW-0654">
        <name>Proteoglycan</name>
        <description>Protein containing one or more covalently linked and usually sulfated
glycosaminoglycans, (e.g., chondroitin sulfate, dermatan sulfate,
heparan sulfate, heparin, keratan sulfate). Glycosaminoglycans are
polysaccharides made of repeating disaccharides (usually 40-100
times), which consist of uronic acid (or galactose) and hexosamines
Aggrecan, for example, is the major component in articular cartilage</description>
    </keyword>
    <keyword id="KW-1267">
        <name>Proteomics identification</name>
        <description>Protein whose amino acid sequence has been partially or completely
confirmed using publicly available mass spectrometry based data. The
mapping from the mass spectrometry data to UniProtKB sequences may be
subject to quality metrics from both UniProt and the data providers</description>
    </keyword>
    <keyword id="KW-0655">
        <name>Prothrombin activator</name>
        <description>Protein which activates prothrombin, the inactive precursor of
thrombin. For example, staphylocoagulase, an extracellular protein
produced by Staphylococcus aureus, forms a complex with prothrombin
which can clot fibrinogen without any proteolytic cleavage of
prothrombin</description>
        <go id="GO:0010952"/>
        <go id="GO:0016504"/>
    </keyword>
    <keyword id="KW-0656">
        <name>Proto-oncogene</name>
        <description>Protein whose normal cellular gene can be converted into a cancer-
promoting oncogene by activating mutations, chromosomal translocation
or DNA amplification. Once activated a proto-oncogene can promote cell
transformation in culture or tumorigenesis in animals. Examples
include the regulatory GTPase HRAS, which is commonly activated by
dominant gain of function point mutations, and the transcription
factor MYC, which can be activated by both chromosomal amplification
and chromosomal translocation</description>
    </keyword>
    <keyword id="KW-1275">
        <name>Proton-gated sodium channel impairing toxin</name>
        <description>Protein which interferes with the function of proton-gated sodium
channels (ASICs) which are membrane proteins forming a channel in a
biological membrane selectively permeable to sodium ions, and open in
response to an increase of extracellular protons. These toxins are
found in various venoms from snakes, spiders, sea anemones, and cone
snails</description>
    </keyword>
    <keyword id="KW-0657">
        <name>Pseudohermaphroditism</name>
        <description>Protein which, if defective, causes pseudohermaphroditism, a condition
in humans in which the individual has gonads of one sex but shows
ambiguous morphologic criteria of sex</description>
    </keyword>
    <keyword id="KW-0658">
        <name>Purine biosynthesis</name>
        <description>Protein involved in the biosynthesis of purine, a nitrogenous
heterocyclic base, e.g. adenine, guanine, hypoxanthine and xanthine
De novo synthesis involves a complex, energy-expensive pathway that
yields inosine 5'-monophosphate (IMP), a purine ribonucleotide. AMP
and GMP are then formed from IMP in separate pathways. Adenine and
guanine are found in both DNA and RNA. Hypoxanthine and xanthine are
important intermediates in the synthesis and degradation of the purine
nucleotides</description>
        <go id="GO:0006164"/>
    </keyword>
    <keyword id="KW-0659">
        <name>Purine metabolism</name>
        <description>Protein involved in a biochemical reaction with purines. Purines are
nitrogenous heterocyclic bases, e.g. adenine, guanine, hypoxanthine
and xanthine. The degradation of purines leads to uric acid, which is
excreted in primates, birds and some other animals. In many other
vertebrates uric acid is degraded further to the excretory product
allantoin</description>
        <go id="GO:0006144"/>
    </keyword>
    <keyword id="KW-0660">
        <name>Purine salvage</name>
        <description>Protein involved in the biosynthesis of purine nucleotides from free
purines salvaged from their catabolism. This process is less expensive
energetically and exerts feedback control on the de novo synthesis</description>
        <go id="GO:0006166"/>
    </keyword>
    <keyword id="KW-0661">
        <name>Putrescine biosynthesis</name>
        <name>1,4-butanediamine biosynthesis</name>
        <name>1,4-diaminobutane biosynthesis</name>
        <description>Protein involved in the biosynthesis of putrescine, a foul-smelling
polyamine. This metabolic precursor of the polyamines spermine and
spermidine is often produced during breakdown of some of the amino
acids by bacteria</description>
        <go id="GO:0009446"/>
    </keyword>
    <keyword id="KW-0662">
        <name>Pyridine nucleotide biosynthesis</name>
        <description>Protein involved in the biosynthesis of the pyridine nucleotides NAD
and NADP. NAD may be synthesized de novo from aspartate and
dihydroxyacetone phosphate or from tryptophan. NAD may also be
synthesized from nicotinamide or nicotinic acid. NADP is formed via
the phosphorylation of NAD by NAD+ kinase</description>
        <go id="GO:0019363"/>
    </keyword>
    <keyword id="KW-0663">
        <name>Pyridoxal phosphate</name>
        <description>Protein which uses at least one pyridoxal phosphate as cofactor or
protein required for its synthesis. This coenzyme, derived from
vitamin B6, is important in amino acid metabolism, e.g., in reactions
involving transamination, decarboxylation, racemization, elimination
or replacement</description>
    </keyword>
    <keyword id="KW-0664">
        <name>Pyridoxine biosynthesis</name>
        <name>Pyridoxol biosynthesis</name>
        <name>Vitamin B6 biosynthesis</name>
        <description>Protein involved in the biosynthesis of pyridoxine, a precursor to the
coenzyme pyridoxal phosphate</description>
        <go id="GO:0008615"/>
    </keyword>
    <keyword id="KW-0665">
        <name>Pyrimidine biosynthesis</name>
        <description>Protein involved in the biosynthesis of pyrimidine, a nitrogenous
heterocyclic base, e.g. uracil, thymine, cytosine and orotic acid
Pyrimidines are synthesized from carbamoyl phosphate and aspartate
Ribose-5-phosphate is then attached to yield pyrimidine
ribonucleotides. Cytosine is found in both DNA and RNA. Uracil is
found only in RNA. Thymine is normally found in DNA. Sometimes tRNA
contains some thymine as well as uracil</description>
        <go id="GO:0006221"/>
    </keyword>
    <keyword id="KW-0666">
        <name>Pyrogen</name>
        <description>Protein producing fever. The major endogenous pyrogen in mammals is
probably interleukin-1, which is produced by activated macrophages and
acts on the hypothalamic thermoregulatory centre</description>
        <go id="GO:0001660"/>
    </keyword>
    <keyword id="KW-0668">
        <name>Pyropoikilocytosis</name>
        <name>HPP</name>
        <description>Protein which, if defective, causes hereditary pyropoikilocytosis
(HPP), a recessively inherited hemolytic anemia characterized by
microspherocytosis, poikilocytosis (deformation of the erythrocytes),
and an unusual thermal sensitivity of red cells. Frequently associated
with abnormalities in alpha-spectrin, one of the principal structural
proteins of the erythrocyte membrane skeleton</description>
    </keyword>
    <keyword id="KW-0873">
        <name>Pyrrolidone carboxylic acid</name>
        <name>Pyro-Glu</name>
        <name>Pyroglutamic acid</name>
        <description>Protein which is posttranslationally modified by the cyclization of a
N-terminal glutamine</description>
    </keyword>
    <keyword id="KW-0669">
        <name>Pyrrolysine</name>
        <description>Protein which contains a pyrrolysine, a naturally occurring amino acid
so far only found in some archaeal proteins. Pyrrolysine is a lysine
in an amide linkage to (4R,5R)-4-substituted-pyrroline-5-carboxylate</description>
    </keyword>
    <keyword id="KW-0670">
        <name>Pyruvate</name>
        <description>Protein which uses at least one pyruvate as cofactor (pyruvoyl) or
substrate, or protein required for pyruvate synthesis or degradation
Pyruvate is an intermediate compound in the metabolism of
carbohydrates, proteins and fats</description>
    </keyword>
    <keyword id="KW-0671">
        <name>Queuosine biosynthesis</name>
        <name>Nucleoside Q biosynthesis</name>
        <description>Protein involved in the synthesis of queuosine (nucleoside Q), a
modified guanosine derivative found only in tRNAs for aspartic acid,
asparagine, histidine and tyrosine. It can pair with either C or U</description>
        <go id="GO:0008616"/>
    </keyword>
    <keyword id="KW-0672">
        <name>Quinate metabolism</name>
        <description>Protein involved in the biochemical reactions of quinate. Quinate is
the ionized form of quinic acid which is found in plants, e.g. in
cinchona bark</description>
        <go id="GO:0019630"/>
    </keyword>
    <keyword id="KW-0874">
        <name>Quinone</name>
        <description>Protein which interacts with quinones. Quinones are aromatic
dicarbonyl compounds, where the two carbonyl groups are usually in the
para position. Most naturally occuring quinones contain a long
isoprenoid side chain, and are divided in two major structural groups,
the naphtoquinones and benzoquinones; the number of isoprene units
depends on the organism. These highly hydrophobic molecules are mainly
involved in electron transport, as electron carriers in redox
reactions. For example, ubiquinone (coenzyme Q) and menaquinone
(vitamin K2) are essential components of the respiratory electron
transport chain. Plastoquinone, found in chloroplasts and in
cyanobacteria, functions as one of the carrier molecules of the
electron transport chain in photosynthesis. Phylloquinone (vitamin K1)
is the major form of vitamin K found in plants. Chlorobiumquinone,
demethylmenaquinone, alpha-tocopherolquinone, rhodoquinone,
epoxyubiquinone and caldariellaquinone are other quinones found in
several species</description>
        <go id="GO:0048038"/>
    </keyword>
    <keyword id="KW-0673">
        <name>Quorum sensing</name>
        <description>Protein involved in quorum sensing (QS). QS is a phenomenon whereby
the accumulation of signaling molecules enables a single cell to sense
the number of bacteria (cell density). The bacterial reponse to QS
includes adaptation to availability of nutrients, defence against
other microorganisms which may compete for the same nutrients and the
avoidance of toxic compounds potentially dangerous for the bacteria</description>
        <go id="GO:0009372"/>
    </keyword>
    <keyword id="KW-0674">
        <name>Reaction center</name>
        <description>Protein which is a component of the reaction center, a system
consisting of proteins and cofactors which facilitate light energy and
electron transfer in plants. The system also acts as a light-driven
electron pump across the photosynthetic membrane of photosynthetic
bacteria</description>
    </keyword>
    <keyword id="KW-0675">
        <name>Receptor</name>
        <description>Protein which binds to, or responds to, a ligand with high
specificity</description>
    </keyword>
    <keyword id="KW-0676">
        <name>Redox-active center</name>
        <description>Protein which possesses at least one active center which mediates its
participation in redox reactions, usually via reversible oxidation of
a cysteine residue leading to a cysteine-sulfenic acid that can either
be stabilized, or react with an unmodified cysteine residue and form a
stable but reversible disulfide bond</description>
    </keyword>
    <keyword id="KW-1185">
        <name>Reference proteome</name>
        <description>Protein which is part of a reference proteome. Reference proteomes are
a subset of proteomes that have been selected either manually or
algorithmically according to a number of criteria to provide a broad
coverage of the tree of life and a representative cross-section of the
taxonomic diversity found within UniProtKB, as well as the proteomes
of well-studied model organisms and other species of interest for
biomedical research</description>
    </keyword>
    <keyword id="KW-0677">
        <name>Repeat</name>
        <description>Protein which contains a stretch of amino acids present in multiple
copies</description>
    </keyword>
    <keyword id="KW-0678">
        <name>Repressor</name>
        <description>Protein which interferes with transcription, usually by binding to
specific sites on DNA. Also used for proteins which repress
translation</description>
    </keyword>
    <keyword id="KW-0679">
        <name>Respiratory chain</name>
        <name>Electron transport chain</name>
        <name>Respiration chain</name>
        <description>Protein involved in respiratory chain. In aerobic respiration
electrons are transferred from metabolites to molecular oxygen through
a series of redox reactions mediated by an electron transport chain
The resulting free energy is used for the formation of ATP and NAD. In
anaerobic respiration analogous reactions take place with an inorganic
compound other than oxygen as ultimate electron acceptor</description>
        <go id="GO:0070469"/>
    </keyword>
    <keyword id="KW-0680">
        <name>Restriction system</name>
        <name>Restriction-modification system</name>
        <description>Protein involved in the restriction system present in many bacteria
and archaea. This defense mechanism is composed principally of a
restriction endonuclease and a methylase. The restriction endonuclease
cuts the invading DNA of viruses (or phages) at a specific recognition
site. The bacterial DNA is protected by the methylase which adds a
methyl group to a specific nucleotide, immediately following
replication, in the same target site as the restriction enzyme</description>
        <go id="GO:0009307"/>
    </keyword>
    <keyword id="KW-1258">
        <name>Restriction-modification system evasion by virus</name>
        <description>Viral anti-restriction protein that counteracts the host restriction-
modification (R-M) system. R-M system is a prokaryotic host defense
system that recognizes incoming unmodified viral DNA and rapidly
degrades it. Methylation and phosphorothioation (S-modification) are
two known modifications used by the host to to label its genomic DNA
as 'self'. Many prokaryotic viruses have evolved antirestriction
strategies such as expressing their own methylase, stimulating the
host methylase so that it confers protection to the virus genome or
shutting down host restriction endonuclease</description>
        <go id="GO:0099018"/>
    </keyword>
    <keyword id="KW-0681">
        <name>Retinal protein</name>
        <description>Protein found in the retina or, in the case of bacteriorhodopsin, in
the purple membrane of halobacteria, and which acts as a photoreceptor
and which binds a retinal chromophore</description>
        <go id="GO:0007602"/>
    </keyword>
    <keyword id="KW-0682">
        <name>Retinitis pigmentosa</name>
        <description>Protein which, if defective, causes retinitis pigmentosa, a hereditary
progressive degeneration of the neuroepithelium of the retina,</description>
    </keyword>
    <keyword id="KW-0683">
        <name>Retinol-binding</name>
        <name>Vitamin A-binding</name>
        <description>Protein which binds retinol, one of the active form of Vitamin A, a
fat-soluble vitamin derived from carotenes. It is a precursor of
retinal, the light-absorbing group of visual pigments. Vitamin A is
also required for growth</description>
        <go id="GO:0019841"/>
    </keyword>
    <keyword id="KW-0684">
        <name>Rhamnose metabolism</name>
        <name>6-deoxy-L-mannose metabolism</name>
        <description>Protein involved in the biochemical reactions of rhamnose. Rhamnose is
a methylpentose sugar structurally derived from mannose. The L-isomer
occurs naturally as a component of many plant glycosides and in
lipopolysaccharides of some bacteria with 2 membranes (Gram-negative
bacteria)</description>
        <go id="GO:0019299"/>
    </keyword>
    <keyword id="KW-0685">
        <name>Rhizomelic chondrodysplasia punctata</name>
        <name>RCDP</name>
        <description>Protein which, if defective, causes rhizomelic chondrodysplasia
punctata (RCDP). This lethal autosomal recessive disease is
characterized by proximal limb shortening, severely disturbed
endochondrial bone formation, and intellectual disability. RCDP type 1
(RCDP1) is the classical and most common form. It is a peroxisome
biogenesis disorder caused by mutations in the PEX7 gene, which
encodes the PTS2-receptor peroxin-7. RCDP type 2 (RCDP2) and RCDP type
3 (RCDP3) result from single peroxisomal enzyme deficiencies:
dihydroxyacetone phosphate synthase is deficient in RCDP2 and
dihydroxyacetone phosphate acyltransferase in RCDP3. Both enzymes are
involved in the biosynthesis of plasmalogens</description>
    </keyword>
    <keyword id="KW-0686">
        <name>Riboflavin biosynthesis</name>
        <name>Vitamin B2 biosynthesis</name>
        <description>Protein involved in the synthesis of riboflavin (Vitamin B2), which
consists of ribose attached to a flavin moiety. It is synthesized by
all green plants and most microorganisms and occurs free in milk, the
retina, whey and urine. It is found in most cells as a component of
the coenzymes flavin adenine dinucleotide (FAD) and flavin
mononucleotide (FMN)</description>
        <go id="GO:0009231"/>
    </keyword>
    <keyword id="KW-0687">
        <name>Ribonucleoprotein</name>
        <description>Proteins conjugated with ribonucleic acid (RNA). Ribonucleoprotein are
involved in a wide range of cellular processes. Besides ribosomes, in
eukaryotic cells both initial RNA transcripts in the nucleus (hnRNA)
and cytoplasmic mRNAs exist as complexes with specific sets of
proteins. Processing (splicing) of the former is carried out by small
nuclear RNPs (snRNPs). Other examples are the signal recognition
particle responsible for targetting proteins to endoplasmic reticulum
and a complex involved in termination of transcription</description>
        <go id="GO:1990904"/>
    </keyword>
    <keyword id="KW-0688">
        <name>Ribosomal frameshifting</name>
        <description>Protein produced by programmed ribosomal frameshifting, a
translational recoding mechanism which causes the ribosome to alter
its reading of the genetic code to produce either an alternative
product not directly encoded by the mRNA or two or more different
isoforms</description>
        <go id="GO:0075523"/>
    </keyword>
    <keyword id="KW-0689">
        <name>Ribosomal protein</name>
        <description>Protein of the ribosome, large ribonucleoprotein particles where the
translation of messenger RNA (mRNA) into protein occurs. They are both
free in the cytoplasm and attached to membranes of eukaryotic and
prokaryotic cells. Ribosomes are also present in all plastids and
mitochondria, where they translate organelle-encoded mRNA</description>
        <go id="GO:0005840"/>
    </keyword>
    <keyword id="KW-1197">
        <name>Ribosomal skipping</name>
        <description>Protein produced by ribosomal 'skipping', in which a specific sequence
in the nascent peptide chain prevents the ribosome from creating the
peptide bond with the next proline. Nevertheless, translation
continues and gives rise to a second chain. This mechanism results in
apparent co-translational cleavage of the polyprotein. This process is
induced by a '2A-like', or CHYSEL (cis-acting hydrolase element)
sequence</description>
    </keyword>
    <keyword id="KW-0690">
        <name>Ribosome biogenesis</name>
        <description>Protein involved in the synthesis of ribosomes</description>
        <go id="GO:0042254"/>
    </keyword>
    <keyword id="KW-0691">
        <name>RNA editing</name>
        <description>Protein which is derived from an RNA which has been modified by RNA
editing, a process that changes the nucleotide sequence of an RNA from
that of the DNA template encoding it. RNA editing can be due to
nucleotide conversion, insertion and/or deletion</description>
    </keyword>
    <keyword id="KW-0692">
        <name>RNA repair</name>
        <description>Protein involved in the repair of RNA, the various biochemical
processes by which damaged RNA can be restored</description>
        <go id="GO:0042245"/>
    </keyword>
    <keyword id="KW-1159">
        <name>RNA suppression of termination</name>
        <description>Protein which is derived from an mRNA by suppression of termination, a
process in which a tRNA misreads a termination codon thereby producing
a longer protein. RNA secondary structure after the stop codon plays a
role in this process. The efficiency of suppression of termination is
about 10% for most viruses. Termination suppression is involved in
polyprotein synthesis of gamma and epsilon retroviruses, as well as
all togaviridae</description>
    </keyword>
    <keyword id="KW-1158">
        <name>RNA termination-reinitiation</name>
        <description>Protein which is derived from an mRNA by termination-reinitiation, a
process in which ribosomes translate the upstream ORF but following
termination, a proportion of 40S subunits remain tethered to the mRNA
and reinitiates at the start codon of the downstream ORF to another
open reading frame. Termination-reinitiation operates in animals and
yeast translational systems</description>
    </keyword>
    <keyword id="KW-1156">
        <name>RNA translational shunting</name>
        <description>Protein which is derived from an mRNA by translational shunting, a
process in which ribosomes are loaded onto mRNA at the 5'-cap
structure, start scanning for a short distance before bypassing the
large internal leader region and initiating at a downstream start
site. Shunting operates in plants, animals, and yeast translational
systems, both in vivo and in vitro</description>
    </keyword>
    <keyword id="KW-0694">
        <name>RNA-binding</name>
        <description>Protein which binds to RNA</description>
        <go id="GO:0003723"/>
    </keyword>
    <keyword id="KW-0695">
        <name>RNA-directed DNA polymerase</name>
        <name>Reverse transcriptase</name>
        <description>Enzyme (EC 2.7.7.49) which synthesizes (-)DNA on a (+)RNA template
They are encoded by the pol gene of retroviruses and by certain
retrovirus-like elements</description>
        <go id="GO:0003964"/>
    </keyword>
    <keyword id="KW-0696">
        <name>RNA-directed RNA polymerase</name>
        <description>Enzyme (EC 2.7.7.48) which synthesizes (+)RNA on a (-)RNA template
They are encoded by many viruses</description>
        <go id="GO:0003968"/>
    </keyword>
    <keyword id="KW-0943">
        <name>RNA-mediated gene silencing</name>
        <name>TGS</name>
        <name>RNAi</name>
        <name>RNA interference</name>
        <name>Post-transcriptional gene silencing</name>
        <name>PTGS</name>
        <name>Quelling</name>
        <name>Cosuppression</name>
        <name>Transcriptional gene silencing</name>
        <description>Protein involved in RNA-mediated gene silencing. This term describes a
number of related processes which use 21- to 25-nucleotide RNAs to
repress the expression of specific target genes. These processes
include the post-transcriptional regulation of mRNA by either RNA
interference (RNAi) or endogenously encoded microRNAs (miRNAs) and the
transcriptional regulation of mRNA by RNAi-mediated chromatin
silencing. RNAi is generally triggered by the presence of dsRNA
produced by bidirectional transcription or by the transcription of an
inverted repeat or hairpin sequence. dsRNA is processed into small
interfering RNAs (siRNAs) of around 21 nucleotide which are then
incorporated into the RNA-induced silencing complex (RISC), which
cleaves mRNAs with sequences fully complementary to the siRNA. miRNAs
differ from siRNAs principally in their biogenesis. miRNA genes encode
precursors with complex hairpin structures which are processed by
endonucleolytic cleavage to form mature miRNAs. Like siRNAs, miRNAs
function in RISC-like complexes. Animal miRNAs generally inhibit
translation of target mRNAs following imperfect base pairing to the
3'-untranslated region (3'-UTR), while most plant miRNAs show nearly
precise complementarity to coding regions of target mRNAs and trigger
mRNA degradation similar to siRNAs. Finally, in RNAi-mediated
chromatin silencing, siRNAs derived from repeat element transcripts
are incorporated into the nuclear RNAi-induced initiator of
transcriptional silencing complex (RITS), where they guide chromatin
modifications such as histone methylation which lead to
transcriptional silencing</description>
        <go id="GO:0031047"/>
    </keyword>
    <keyword id="KW-0697">
        <name>Rotamase</name>
        <description>Enzyme (EC 5.2.1.8) which accelerates the folding of proteins by
catalyzing the cis-trans isomerization of proline imidic peptide bonds
in oligopeptides</description>
        <go id="GO:0003755"/>
    </keyword>
    <keyword id="KW-0698">
        <name>rRNA processing</name>
        <name>Ribosomal RNA processing</name>
        <description>Protein involved in the processing of the primary rRNA transcript to
yield a functional rRNA. This includes the cleavage and other
modifications</description>
        <go id="GO:0006364"/>
    </keyword>
    <keyword id="KW-0699">
        <name>rRNA-binding</name>
        <description>Protein which binds to ribosomal RNA</description>
        <go id="GO:0019843"/>
    </keyword>
    <keyword id="KW-1219">
        <name>Ryanodine-sensitive calcium-release channel impairing toxin</name>
        <name>Ryanodine receptor inhibitor</name>
        <name>Ryr inhibitor</name>
        <description>Protein which interferes with the function of ryanodine receptors
(Ryr) which are a class of intracellular calcium channels in various
forms of excitable animal tissue like muscles and neurons. These
toxins are mostly found in scorpion and snake venom</description>
    </keyword>
    <keyword id="KW-0949">
        <name>S-adenosyl-L-methionine</name>
        <name>radical S- adenosylmethionine</name>
        <name>S-adenosyl methionine</name>
        <name>AdoMet radical</name>
        <name>S-adenosyl-methionine</name>
        <name>SAM radical</name>
        <name>S-adenosylmethionine</name>
        <name>SAM</name>
        <name>AdoMet</name>
        <description>Protein which binds at least one S-adenosyl-L-methionine (SAM), or
protein whose function is SAM-dependent. S-adenosyl-L-methionine, a
conjugate of the nucleotide adenosine and the amino acid methionine,
is a substrate/cofactor in numerous enzyme-catalyzed reactions
Enzymatic reactions that involve interactions of proteins with S-
adenosyl-L-methionine include transfer of methyl, thiomethyl,
aminoalkyl and adenosyl groups. It not only provides methyl groups to
be transferred in numerous biological reactions, but also acts as a
precursor in the biosynthesis of polyamines and metal ion chelating
compounds. It is also a source of catalytic 5'-deoxyadenosyl radicals
produced as reaction intermediates by a superfamily of radical
enzymes. It is also involved in decarboxylation reactions</description>
    </keyword>
    <keyword id="KW-0701">
        <name>S-layer</name>
        <description>Protein of the paracrystalline mono-layered assembly which coats the
surface of bacteria and archaea</description>
    </keyword>
    <keyword id="KW-0702">
        <name>S-nitrosylation</name>
        <description>Protein which is posttranslationally modified by the attachment of a
nitric oxide group on the sulfur atom of one or more cysteine
residues</description>
    </keyword>
    <keyword id="KW-0703">
        <name>Sarcoplasmic reticulum</name>
        <description>Protein found in a special form of agranular reticulum located in the
sarcoplasm of striated muscle. The agranular reticulum comprises and
comprising a system of smooth-surfaced tubules which form a plexus
around each myofibril</description>
    </keyword>
    <keyword id="KW-0704">
        <name>Schiff base</name>
        <description>Enzyme which forms a covalent enzyme-substrate complex, a Schiff's
base or ketimine between the amino group of a lysine residue of the
enzyme and the carbonyl group of the substrate</description>
    </keyword>
    <keyword id="KW-1211">
        <name>Schizophrenia</name>
        <name>SCZD</name>
        <description>Protein which, if defective, is associated with schizophrenia, a
multifactorial psychotic disorder characterized by disturbances in the
form and content of thought (e.g. delusions, hallucinations), in mood
(e.g. inappropriate affect), in sense of self and relationship to the
external world (e.g. loss of ego boundaries, withdrawal), and in
behavior (e.g bizarre or apparently purposeless behavior)</description>
    </keyword>
    <keyword id="KW-0705">
        <name>SCID</name>
        <name>Severe congenital immunodeficiency disease</name>
        <name>Severe combined immunodeficiency disease</name>
        <description>Protein which, if defective, causes severe combined (or congenital)
immunodeficiency disease. An heterogeneous group of inherited
disorders characterized by gross functional impairment of the immune
system</description>
    </keyword>
    <keyword id="KW-0964">
        <name>Secreted</name>
        <description>Protein secreted into the cell surroundings</description>
    </keyword>
    <keyword id="KW-0708">
        <name>Seed storage protein</name>
        <description>Protein required for the development or growth of seeds</description>
        <go id="GO:0045735"/>
    </keyword>
    <keyword id="KW-0709">
        <name>Segmentation polarity protein</name>
        <name>Segment polarity protein</name>
        <description>Protein involved in the division of the embryo into segments and which
is responsible for determining the internal polarity of the segments
Segment polarity gene mutations are lethal and change the pattern and,
often the polarity, of every segment</description>
        <go id="GO:0007367"/>
    </keyword>
    <keyword id="KW-0711">
        <name>Selenium</name>
        <description>Protein which binds at least one selenium, or protein whose function
is selenium-dependent. Selenium is a nonmetallic trace element,
chemical symbol Se</description>
    </keyword>
    <keyword id="KW-0712">
        <name>Selenocysteine</name>
        <name>3-selenyl-L-alanine</name>
        <description>Protein which contains a selenocysteine, a naturally occurring amino
acid in both eukaryotic and prokaryotic organisms</description>
    </keyword>
    <keyword id="KW-0713">
        <name>Self-incompatibility</name>
        <description>Protein involved in the self-incompatibility system, which is to say
the inability of pollen grains to fertilize flowers of the same plant
or a close relative. This mechanism ensures out-breeding in certain
plant species</description>
        <go id="GO:0060320"/>
    </keyword>
    <keyword id="KW-0980">
        <name>Senior-Loken syndrome</name>
        <name>Juvenile nephronophthisis with Leber amaurosis</name>
        <name>Senior-Loeken syndrome</name>
        <name>Renal-retinal syndrome</name>
        <name>Renal dysplasia and retinal aplasia</name>
        <name>Loken-Senior syndrome</name>
        <description>Protein which, if defective, causes Senior-Loken syndrome, a
genetically and clinically heterogeneous disease characterized by
nephronophthisis and retinal abnormalities manifesting as congenital
retinal blindness or retinitis pigmentosa. Senior-Loken syndrome can
be associated with manifestations such as cerebellar ataxia and
skeletal abnormalities including cone epiphyses</description>
    </keyword>
    <keyword id="KW-0716">
        <name>Sensory transduction</name>
        <description>Protein involved in sensory transduction, the process by which a cell
converts an extracellular signal, such as light, taste, sound, touch
or smell, into electric signals</description>
        <go id="GO:0050896"/>
    </keyword>
    <keyword id="KW-0717">
        <name>Septation</name>
        <description>Protein involved in septation, the formation of a separating wall
(septum) between daughter cells during cell division</description>
        <go id="GO:0000917"/>
    </keyword>
    <keyword id="KW-0718">
        <name>Serine biosynthesis</name>
        <description>Protein involved in the synthesis of the amino acid serine, a
constituent of proteins and precursor of several metabolites,
including cysteine, glycine and choline. Serine is mostly formed from
3-phosphoglycerate in a 3-step reaction pathway</description>
        <go id="GO:0006564"/>
    </keyword>
    <keyword id="KW-0719">
        <name>Serine esterase</name>
        <description>Enzyme which catalyzes the hydrolysis of esters and is characterized
by a catalytically active serine residue in its active site</description>
        <go id="GO:0052689"/>
    </keyword>
    <keyword id="KW-0720">
        <name>Serine protease</name>
        <name>Serine endopeptidase</name>
        <name>Serine proteinase</name>
        <name>Serine peptidase</name>
        <description>Proteolytic enzyme with a serine residue (Ser) in its active site. The
reactivity of the serine residue is ensured by the vicinity of a
histidine and an aspartate residue (catalytic triad), all three
residues are required for the charge relay system to take place</description>
        <go id="GO:0008236"/>
    </keyword>
    <keyword id="KW-0721">
        <name>Serine protease homolog</name>
        <description>Protein which is related to serine proteases but seems to have no
proteolytic activity</description>
    </keyword>
    <keyword id="KW-0722">
        <name>Serine protease inhibitor</name>
        <name>Serine endopeptidase inhibitor</name>
        <name>Serine peptidase inhibitor</name>
        <name>Serine proteinase inhibitor</name>
        <description>Protein which inhibits serine proteases, a group of proteolytic
enzymes which are characterized by a catalytically active serine
residue in their active site</description>
        <go id="GO:0004867"/>
    </keyword>
    <keyword id="KW-0723">
        <name>Serine/threonine-protein kinase</name>
        <description>Protein which catalyzes the phosphorylation of serine or threonine
residues on target proteins by using ATP as phosphate donor. Such
phosphorylation may cause changes in the function of the target
protein. Protein kinases share a conserved catalytic core common to
both serine/ threonine and tyrosine protein kinases</description>
        <go id="GO:0004674"/>
    </keyword>
    <keyword id="KW-0724">
        <name>Serotonin biosynthesis</name>
        <name>5-hydroxytryptamine</name>
        <name>5-HT</name>
        <description>Protein involved in the synthesis of the biochemical messenger and
regulator serotonin which is formed by the hydroxylation and
subsequent decarboxylation of L-tryptophan. In humans, serotonin
mediates several important physiological functions, including
neurotransmission, gastrointestinal motility, hemostasis and
cardiovascular integrity</description>
        <go id="GO:0042427"/>
    </keyword>
    <keyword id="KW-0726">
        <name>Sexual differentiation</name>
        <description>Protein involved in both the determination of cells to become sexual
tissue in embryonic development and in the process by which male and
female tissue becomes structurally and functionally specialized during
embryonic development</description>
        <go id="GO:0007548"/>
    </keyword>
    <keyword id="KW-0727">
        <name>SH2 domain</name>
        <description>Protein with at least one Src homology 2 (SH2) domain. The SH2 domain,
which was first identified in the oncoproteins Src and Fps, is about
100 amino-acid residues long. It functions as a regulatory module of
intracellular signaling cascades by interacting with high affinity to
phosphotyrosine-containing target peptides in a sequence-specific and
strictly phosphorylation-dependent manner</description>
    </keyword>
    <keyword id="KW-0728">
        <name>SH3 domain</name>
        <description>Protein with at least one Src homology 3 (SH3) domain It is a small
protein domain of about 50 amino-acid residues first identified as a
conserved sequence in the non-catalytic part of several cytoplasmic
protein tyrosine kinases (e.g. Src). Since then, it has been found in
a great variety of other intracellular or membrane-associated
proteins. The SH3 module might mediate the assembly of specific
protein complexes by binding to proline-rich peptides</description>
    </keyword>
    <keyword id="KW-0729">
        <name>SH3-binding</name>
        <description>Protein with at least one SH3-binding site and which mediates the
binding to the Src homology 3 (SH3) region, a module present in a
large group of proteins, including cytoskeletal elements and signaling
proteins</description>
        <go id="GO:0017124"/>
    </keyword>
    <keyword id="KW-0940">
        <name>Short QT syndrome</name>
        <name>SQTS</name>
        <description>Protein which, if defective, causes short QT syndrome, a heart
disorder characterized by the presence of a short QT interval on ECG,
associated with syncope, palpitations, cardiac arrest and sudden
death</description>
    </keyword>
    <keyword id="KW-0730">
        <name>Sialic acid</name>
        <description>Protein with at least one sialic acid. The term "sialic acid" refers
to the group of sugars including neuraminic acid and its derivatives,
not to a specific sugar. They are widely distributed in bacteria and
animal tissue as components of polysaccharides, glycoproteins and
glycolipids. They are typically the terminal residues on cell surface
oligosaccharides</description>
    </keyword>
    <keyword id="KW-0731">
        <name>Sigma factor</name>
        <description>Initiation factors that bind to bacterial DNA-dependent RNA
polymerases and promote attachment to specific initiation sites on
DNA. Following attachment, the sigma factor is released</description>
        <go id="GO:0016987"/>
        <go id="GO:0006355"/>
    </keyword>
    <keyword id="KW-0732">
        <name>Signal</name>
        <name>Signal sequence</name>
        <name>Signal peptide</name>
        <description>Protein which has a signal sequence, a peptide usually present at the
N-terminus of proteins and which is destined to be either secreted or
part of membrane components. The signal sequence (usually 20-30 amino
acids long) interacts with the signal recognition particle and directs
the ribosome to the endoplasmic reticulum where co-translational
insertion takes place. Signal peptides are highly hydrophobic but have
some positively charged amino acids. Normally, the signal sequence is
removed from the growing peptide chain by specific peptidases (signal
peptidases) located on the cisternal face of the endoplasmic
reticulum</description>
    </keyword>
    <keyword id="KW-0733">
        <name>Signal recognition particle</name>
        <description>Protein of the signal recognition particle (SRP) which is a cytosolic
ribonucleoprotein complex that induces elongation arrest of nascent
presecretory and membrane proteins until the ribosome becomes
associated with the rough endoplasmic reticulum or the prokaryotic
cytoplasmic membrane</description>
        <go id="GO:0005786"/>
    </keyword>
    <keyword id="KW-0734">
        <name>Signal transduction inhibitor</name>
        <description>Protein which inhibits signal transduction, the process by which
extracellular signals induce intracellular responses. Usually a
hormone or neurotransmitter binds to a cell surface receptor which is
coupled to a second messenger system, such as that involving cAMP, or
to an ion channel. The final downstream consequence of signal
transduction is a change in the cell's function, such as a
modification in glucose uptake or in cell division. Such a change may
be the result of an activation or an inhibition event</description>
        <go id="GO:0009968"/>
    </keyword>
    <keyword id="KW-0735">
        <name>Signal-anchor</name>
        <description>Single-pass transmembrane protein (type II, III, and IV) possessing a
membrane-spanning domain which targets the protein to the ER membrane
Typical features of signal-anchors are the presence of positively
charged residues on the amino terminal side followed by an apolar
segment of approx. 20 residues. The amino-acid composition is not very
different from typical signal sequences</description>
    </keyword>
    <keyword id="KW-0736">
        <name>Signalosome</name>
        <name>COP9 signalosome</name>
        <name>COP9 complex</name>
        <name>COP9 signalosome complex</name>
        <name>CSN</name>
        <description>Protein of the signalosome complex, a multifunctional protein complex
essential for development and possibly involved in the regulation of
protein degradation</description>
        <go id="GO:0008180"/>
    </keyword>
    <keyword id="KW-0737">
        <name>Silk protein</name>
        <description>Protein found in silk, a strong, soft, lustrous fiber made of fibroin,
a structural protein consisting almost entirely of stacked
antiparallel beta pleated sheets. It is produced by certain spiders
and by the larvae of certain bombycine moths</description>
    </keyword>
    <keyword id="KW-0915">
        <name>Sodium</name>
        <description>Protein which binds at least one sodium, or protein whose function is
sodium-dependent. Sodium is an alkali metal, chemical symbol Na</description>
    </keyword>
    <keyword id="KW-0894">
        <name>Sodium channel</name>
        <description>Protein which is part of a cation channel permeable for sodium found
in the plasma membrane and in intracellular membranes. Sodium channels
have been classified according to their gating mechanisms, which may
depend on changes in the transmembrane electric field (voltage-gated
sodium channels) or not (non-voltage-gated sodium channels, e.g
degenerins which are permeable also to lithium and potassium)
Voltage-gated sodium channels, by opening in response to membrane
depolarization, allow sodium entry and thus the propagation of
depolarization along the plasma membrane of nerve, muscle and other
electrically excitable cells. They play a role in different processes
such as sensation, emotions, thought and movement. Another class of
sodium channel is the degenerin/epithelial sodium channel (ENaC)
superfamily, which is a group of proteins involved in diverse
biological processes, including sodium homeostasis, salt taste,
nociception, pain transduction, touch sensation and
mechanotransduction</description>
        <go id="GO:0005272"/>
    </keyword>
    <keyword id="KW-0739">
        <name>Sodium transport</name>
        <description>Protein involved in the movement of sodium ions across energy-
transducing cell membranes. Primary active sodium transport is coupled
to an energy-yielding chemical reaction such as ATP hydrolysis
Secondary active transport utilizes the voltage and ion gradients
produced by the primary transport to drive the cotransport of other
ions or molecules. These may be transported in the same (symport) or
opposite (antiport) direction</description>
        <go id="GO:0006814"/>
    </keyword>
    <keyword id="KW-0740">
        <name>Sodium/potassium transport</name>
        <description>Protein involved in the active transport system which simultaneously
moves two potassium ions into the cell and three sodium ions out of
the cell</description>
        <go id="GO:0006813"/>
        <go id="GO:0006814"/>
    </keyword>
    <keyword id="KW-0741">
        <name>SOS mutagenesis</name>
        <description>Protein involved in the DNA repair system also known as error-prone
repair in which apurinic DNA molecules are repaired by the
incorporation of a base that may be the wrong base but that permits
replication</description>
    </keyword>
    <keyword id="KW-0742">
        <name>SOS response</name>
        <name>SOS repair system</name>
        <name>SOS system</name>
        <name>SOS response system</name>
        <description>Protein involved in an SOS response, which implies the coordinated
activation of diverse unlinked genes (ca. 20 in E.coli) involved in
DNA repair, error-prone DNA replication, etc., in response to severe
DNA damage. The SOS system is tightly regulated and its expression
only occurs when absolutely required</description>
        <go id="GO:0009432"/>
    </keyword>
    <keyword id="KW-0744">
        <name>Spermatogenesis</name>
        <description>Protein involved in sperm cell development. A process whereby
primordial germ cells form mature spermatozoa, which includes
spermatocytogenesis (successive mitotic and meiotic divisions) and
spermiogenesis (a metamorphic change)</description>
        <go id="GO:0007283"/>
    </keyword>
    <keyword id="KW-0745">
        <name>Spermidine biosynthesis</name>
        <name>N-(3-aminopropyl)-1,4-butanediamine</name>
        <description>Protein involved in the synthesis of spermidine, a widely distributed
polyamine which acts as a growth factor for some microorganisms and
stabilizes the membrane structure of bacteria, as well as the
structure of ribosomes, some viruses and the DNA of many organisms</description>
        <go id="GO:0008295"/>
    </keyword>
    <keyword id="KW-0746">
        <name>Sphingolipid metabolism</name>
        <description>Protein involved in the biochemical reactions of sphingolipids. These
are structurally complex saponifiable lipids which contain a fatty
acid covalently linked to the amino alcohol sphingosine (or a related
base), as backbone structure, to which is attached a polar head group
They are synthesized in the Golgi complex and are important membrane
components in both plant and animal cells. They are present in
especially large amounts in brain and nerve tissue</description>
        <go id="GO:0006665"/>
    </keyword>
    <keyword id="KW-0950">
        <name>Spinocerebellar ataxia</name>
        <name>Autosomal dominant cerebellar ataxia</name>
        <name>SCA</name>
        <name>Olivopontocerebellar atrophy</name>
        <name>Spinocerebellar atrophy</name>
        <name>Autosomal dominant spinocerebellar ataxia</name>
        <name>OPCA</name>
        <name>ADCA</name>
        <description>Protein which, if defective, causes autosomal dominant spinocerebellar
ataxia, a clinically and genetically heterogeneous group of autosomal
dominant cerebellar ataxias (ADCA). Patients show progressive
incoordination of gait and often poor coordination of hands, speech
and eye movements. Spinocerebellar ataxia is caused by degeneration of
the cerebellum with variable involvement of the brainstem and spinal
cord. Three clinical types are distinguished, according to the extent
of extra-cerebellar signs: cerebellar ataxia with additional features
like optic atrophy, ophthalmoplegia, bulbar and extrapyramidal signs,
peripheral neuropathy and dementia, is known as ADCA type I;
cerebellar ataxia with retinal degeneration and pigmentary macular
dystrophy is defined as ADCA type II; pure cerebellar ataxia without
additional signs is classified as ADCA type III</description>
    </keyword>
    <keyword id="KW-0747">
        <name>Spliceosome</name>
        <description>Protein of the spliceosome, a very large complex of small nuclear
RNA/protein particles (snRNPs) which assemble with pre-mRNA to achieve
RNA splicing</description>
        <go id="GO:0005681"/>
    </keyword>
    <keyword id="KW-0748">
        <name>Sporozoite</name>
        <description>Protein expressed in the sporozoite stage which is the infectious
stage of the malaria parasite. Malaria is transmitted by mosquitos to
the vertebrate host. This term also refers to the motile infectious
stage of other sporozoans (parasitic protozoans)</description>
    </keyword>
    <keyword id="KW-0749">
        <name>Sporulation</name>
        <description>Protein involved in the production of spores, i.e. sporulation</description>
        <go id="GO:0030435"/>
    </keyword>
    <keyword id="KW-0750">
        <name>Starch biosynthesis</name>
        <description>Protein involved in the synthesis of starch, the carbohydrate storage
of plants. Starch consists of amylose (a linear alpha(1-4)-glucan) and
amylopectin (an alpha(1-4)-glucan with alpha(1-6)-branch points)
Starch (glucans and amylopectins) is synthesised via the ADP-glucose
pathway by three key enzymes: ADP-glucose pyrophosphorylase, starch
synthases and starch branching enzymes. The randomly branched glucan
molecules are then specifically debranched via a debranching enzyme in
order to produce amylopectins. Amylopectins are branched in highly
ordered clusters and are crystalline in nature, but also contain
covalently bound phosphate</description>
        <go id="GO:0019252"/>
    </keyword>
    <keyword id="KW-0751">
        <name>Stargardt disease</name>
        <name>SD</name>
        <description>Protein which, if defective, causes Stargardt disease (SD). SD is a
hereditary degeneration of the macula lutea occurring between the ages
of six and twenty, marked by rapid loss of visual accuity and by
abnormal appearance and pigmentation of the macular aerea</description>
    </keyword>
    <keyword id="KW-0752">
        <name>Steroid biosynthesis</name>
        <description>In vivo synthesis of steroids (steroidogenesis), a large group of
complex polycyclic lipids that consist of a 17-carbon ring system
Examples are bile acids, sterols, various hormones and saponins</description>
        <go id="GO:0006694"/>
    </keyword>
    <keyword id="KW-0753">
        <name>Steroid metabolism</name>
        <description>Protein involved in the biochemical reactions of steroids. Steroids
are a large group of complex tetracyclic lipids that consist of a 17-
carbon-ring system. Examples are bile acids, sterols, various hormones
and saponins</description>
        <go id="GO:0008202"/>
    </keyword>
    <keyword id="KW-0754">
        <name>Steroid-binding</name>
        <description>Protein which binds steroids</description>
        <go id="GO:0005496"/>
    </keyword>
    <keyword id="KW-0755">
        <name>Steroidogenesis</name>
        <description>Biosynthesis of steroid hormones which takes place in the mitochondria
of the adrenal cortex. Oxidation of two adjacent carbon atoms in the
side chain of cholesterol, followed by the cleavage between them,
produces pregnenolone, a precursor of all other steroid hormones. The
hydroxylation and oxygenation reactions are catalyzed by cytochrome
P450 and mixed-functions oxidases that use NADPH and O2</description>
        <go id="GO:0006694"/>
    </keyword>
    <keyword id="KW-0756">
        <name>Sterol biosynthesis</name>
        <description>Protein involved in the synthesis of sterols, any steroid alcohol
which are components of cell membranes in plants, animals and fungi</description>
        <go id="GO:0016126"/>
    </keyword>
    <keyword id="KW-1207">
        <name>Sterol metabolism</name>
        <description>Protein involved in the metabolism of sterols, any steroid alcohol
Sterols are components of cell membranes in plants, animals and fungi</description>
    </keyword>
    <keyword id="KW-0757">
        <name>Stickler syndrome</name>
        <name>STL</name>
        <description>Protein which, if defective, causes Stickler syndrome (STL), also
known as hereditary progressive arthro-ophthalmopathy. It is a
genetically and phenotypically heterogeneous disorder with ocular,
oro-facial, auditory and skeletal manifestations. Clinical features
include high myopia, vitreo-retinal degeneration, retinal detachment,
cleft palate, midfacial hypoplasia, osteoarthritis, and sensorineural
hearing loss. Inheritance is autosomal dominant</description>
    </keyword>
    <keyword id="KW-0758">
        <name>Storage protein</name>
        <description>Protein which is a source of nutrients for the development or growth
of an organism</description>
        <go id="GO:0045735"/>
    </keyword>
    <keyword id="KW-0759">
        <name>Streptomycin biosynthesis</name>
        <description>Protein involved in the synthesis of streptomycin, an antibiotic
substance produced by the soil actinomycete Streptomyces griseus. The
three parts of the molecule (streptidine-6-P, dTDP-dihydrostreptose
and N-methyl-glucosamine) are synthesized by separate biochemical
pathways and the subunits brought together at the end. The final
intermediate in the pathway, streptomycin P, becomes biologically
active upon removal of the phosphate. The synthesis of the key
streptomycin biosynthesis enzymes is mainly regulated by differing
levels of factor A. Streptomycin binds to the small subunit of
ribosomes of prokaryotic cells and causes inhibition and misreading</description>
        <go id="GO:0019872"/>
    </keyword>
    <keyword id="KW-0346">
        <name>Stress response</name>
        <description>Protein involved in the response to stress, a change in state or
activity of a cell or an organism (in terms of movement, secretion,
enzyme production, gene expression, etc.) as a result of some
stressful conditions. The stress is usually, but not necessarily,
exogenous (e.g. temperature, humidity, ionizing radiation,
hypertonicity, amino acid deprivation)</description>
    </keyword>
    <keyword id="KW-0762">
        <name>Sugar transport</name>
        <description>Protein involved in the transfer of sugars across a biological
membrane by a carrier protein</description>
        <go id="GO:0071702"/>
    </keyword>
    <keyword id="KW-0763">
        <name>Sulfate respiration</name>
        <name>Dissimilatory sulfate reduction</name>
        <description>Protein involved in sulfate respiration, which is the use of sulfate
(or other oxidized compounds of sulfur) as the terminal electron
acceptor in the anaerobic respiratory metabolism of sulfate- or
sulfur-reducing bacteria</description>
        <go id="GO:0009061"/>
    </keyword>
    <keyword id="KW-0764">
        <name>Sulfate transport</name>
        <description>Protein involved in the translocation of sulfate, or sulfate-
containing compounds, such as thiosulfate, across a biological
membrane</description>
        <go id="GO:0008272"/>
    </keyword>
    <keyword id="KW-0765">
        <name>Sulfation</name>
        <name>Sulfatation</name>
        <description>Protein which is posttranslationally modified by the attachment of at
least one sulfate group to a tyrosine residue. Serine and threonine
may also serve as sulfate group acceptors</description>
    </keyword>
    <keyword id="KW-0766">
        <name>Superantigen</name>
        <name>SAG</name>
        <description>Bacterial or virus secreted protein that induces a strong T-lymphocyte
activity. When a normal antigen stimulates 0,001% of the body's T-
cells, superantigens can stimulate up to 20% of body's T-cells. They
simultaneously interact with the Vb domain of the T-cell receptor
(TCR) and with the class II major histocompatibility complex (MHC)
molecules on the surface of an antigen-presenting cell. This compels
the MHC to interact with the TCR, thereby inducing T-cells activation
Most superantigens are bacterial toxins, but some are produced by
viruses. Staphylococcal enterotoxins are the best known superantigens</description>
    </keyword>
    <keyword id="KW-1260">
        <name>Superinfection exclusion</name>
        <description>Viral protein that is expressed by a prokaryotic virus, integrated or
not, to help protect the host cell from superinfection, a process by
which a cell that has previously been infected by one virus
subsequently gets coinfected with a different strain of the virus, or
another virus. Superinfection exclusion can be achieved for example by
expressing viral enzymes that alter a portion of a surface receptor
thereby blocking entry of incoming viruses with this receptor
specificity. Exclusion protein can also target and block the ejection
and/or DNA delivery by new incoming phages</description>
        <go id="GO:0098669"/>
    </keyword>
    <keyword id="KW-0941">
        <name>Suppressor of RNA silencing</name>
        <name>Suppressor of RNA interference</name>
        <name>Suppressor of RNAi</name>
        <description>Protein which suppresses host RNA-mediated gene silencing. The most
common form of RNA-mediated gene silencing is RNA interference (RNAi),
a sequence-specific RNA-degradation mechanism that operates as a
natural antiviral system in plants and invertebrates cells. RNAi is
mediated by small interfering RNAs (siRNA) of about 21- to 25-nt that
target homologous RNAs for destruction. RNA silencing by endogenous
micro-RNAs (miRNAs) may also play a role in the antiviral defences of
mammals. miRNAs differ from siRNAs in that they generally base pair
imperfectly with target RNAs and inhibit their translation by an
unknown mechanism</description>
    </keyword>
    <keyword id="KW-0767">
        <name>Surface film</name>
        <description>Protein found in the film of pulmonary surfactants which cover the
alveolar surface of the mammalian lung. These surfactants are composed
of 90% phospholipids and 10% proteins</description>
        <go id="GO:0005576"/>
    </keyword>
    <keyword id="KW-0768">
        <name>Sushi</name>
        <description>Protein which contains at least one sushi domain, a motif of
approximately 60 amino acids characterized by a framework of four
conserved half-cystine residues (1-3 and 2-4 disulfide-bonded) and
several other highly conserved residues including proline, tryptophan,
tyrosine/phenylalanine and cysteine. This type of structure, also
designated SCR (Short Consensus Repeat), is predominantly present in
proteins associated with the complement system</description>
    </keyword>
    <keyword id="KW-0769">
        <name>Symport</name>
        <description>Protein involved in the transport of solutes across a biological
membrane in one direction, which depends on the transport of another
solute in the same direction. One molecule can move up an
electrochemical gradient because the movement of the other molecule is
more favorable. Example: the sodium/glucose co-transport</description>
        <go id="GO:0015293"/>
    </keyword>
    <keyword id="KW-0770">
        <name>Synapse</name>
        <description>Protein found in the synapses. Synapses are the communicating cell-
cell junctions that allow signals to pass from a nerve cell to a
target cell. In a chemical synapse, the signal is carried by a
neurotransmitter which diffuses across a narrow synaptic cleft and
activates a receptor on the postsynaptic membrane of the target cell
The target may be a dendrite, cell body, neuronal axon, a specialized
region of a muscle or a secretory cell. In an electrical synapse, a
direct connection is made between the cytoplasms of two cells via gap
junctions</description>
    </keyword>
    <keyword id="KW-0771">
        <name>Synaptosome</name>
        <description>Protein found in synaptosomes, the pinched-off nerve endings and their
contents of vesicles and cytoplasm together with the attached
subsynaptic area of the membrane of the postsynaptic cell. They are
largely artificial structures produced by fractionation after
selective centrifugation of nervous tissue homogenates</description>
        <go id="GO:0043005"/>
    </keyword>
    <keyword id="KW-1180">
        <name>Syncytium formation induced by viral infection</name>
        <name>Polykaryons formation in virally infected cells</name>
        <name>Induction by virus of host cell-cell fusion</name>
        <description>Viral protein that mediates fusion of an infected cell with
neighboring cells leading to the formation of multi-nucleate enlarged
cells called syncytia. Usually these syncytia are the result of
expression of a viral fusion protein at the host cell membrane during
viral replication. Viruses such as herpesviruses are known to induce
the formation of syncytia</description>
        <go id="GO:0060141"/>
    </keyword>
    <keyword id="KW-0772">
        <name>Systemic lupus erythematosus</name>
        <name>SLE</name>
        <description>Protein involved in the systemic lupus erythematosus (SLE), a chronic
autoimmune disease where the immune system is over-active and produces
too many abnormal antibodies that react with the patient's own
tissues. The exact cause of lupus is not known, but heredity,
environment and hormonal changes may be involved. The immune complex
deposition in many tissues leads to the manifestations of the disease
Immune complexes can be deposited in glomeruli, skin, lungs, synovium,
mesothelium, and other places. Many SLE patients develop renal
complications</description>
    </keyword>
    <keyword id="KW-1279">
        <name>T cell receptor</name>
        <description>The T cell receptor (TCR) is the antigen receptor expressed on CD4-
positive and CD8-positive T lymphocytes that recognizes complexes of
peptides bound to self-MHC molecules on the surface of antigen
presenting cells. Structurally, TCR is composed of a heterodimer of
two disulfide-linked transmembrane polypeptide chains designated alpha
and beta, each containing one terminal immunoglobulin (Ig)-like
variable domain, one Ig-like constant domain, a hydrophobic
transmembrane region and a short cytoplasmic region. A less common
type of TCR, composed of gamma and delta chains, is found on a small
subset of T cells and recognizes different forms of antigens. Each T
cell expresses a unique TCR that is generated by randomly assorting
genes. This ensures that T cells can respond (at the population level)
to almost any infection</description>
        <go id="GO:0042101"/>
    </keyword>
    <keyword id="KW-1140">
        <name>T=1 icosahedral capsid protein</name>
        <description>Viral protein that forms an icosahedral capsid with a T=1 symmetry to
protect the viral genome. The T=1 capsid is composed of 60 subunits,
each subunit occupying a quasi-equivalent position. The capsid
diameter ranges from 18 to 35 nm</description>
        <go id="GO:0039615"/>
    </keyword>
    <keyword id="KW-1146">
        <name>T=13 icosahedral capsid protein</name>
        <description>Viral protein that forms an icosahedral capsid with a T=13 symmetry to
protect the viral genome. The T=13 capsid is composed of 780 subunits,
each subunit occupying a quasi-equivalent position. Its diameter
ranges from 70 to 80 nm</description>
        <go id="GO:0039621"/>
    </keyword>
    <keyword id="KW-1149">
        <name>T=147 icosahedral capsid protein</name>
        <description>Viral protein that forms an icosahedral capsid with a T=147 symmetry
to protect the viral genome. The T=147 capsid is composed of 8820
subunits. Its diameter is about 185 nm</description>
        <go id="GO:0039627"/>
    </keyword>
    <keyword id="KW-1147">
        <name>T=16 icosahedral capsid protein</name>
        <description>Viral protein that forms an icosahedral capsid with a T=16 symmetry to
protect the viral genome. The T=16 capsid is composed of 960 subunits,
each subunit occupying a quasi-equivalent position. Its diameter is
about 100 nm</description>
        <go id="GO:0039622"/>
    </keyword>
    <keyword id="KW-1150">
        <name>T=169 icosahedral capsid protein</name>
        <description>Viral protein that forms an icosahedral capsid with a T=169 symmetry
to protect the viral genome. The T=169 capsid is composed of 10140
subunits. Its diameter is about 165-190 nm</description>
        <go id="GO:0039628"/>
    </keyword>
    <keyword id="KW-1141">
        <name>T=2 icosahedral capsid protein</name>
        <description>Viral protein that forms an icosahedral capsid with a T=2* symmetry to
protect the viral genome. The T=2* capsid is composed of 120 subunits
The T=2* symmetry does not exist under the rules described by Caspar
and Klug, strictly speaking the capsid has a T=1 symmetry composed of
60 dimeric subunits. The capsid diameter is about 40 nm</description>
        <go id="GO:0039616"/>
    </keyword>
    <keyword id="KW-1151">
        <name>T=219 icosahedral capsid protein</name>
        <description>Viral protein that forms an icosahedral capsid with a T=219 symmetry
to protect the viral genome. The T=219 capsid is composed of 13140
subunits. Its diameter is about 130-160 nm</description>
        <go id="GO:0039629"/>
    </keyword>
    <keyword id="KW-1148">
        <name>T=25 icosahedral capsid protein</name>
        <description>Viral protein that forms an icosahedral capsid with a T=25 symmetry to
protect the viral genome. The T=25 capsid is composed of 1500
subunits, each subunit occupying a quasi-equivalent position. Its
diameter is about 90 nm</description>
        <go id="GO:0039623"/>
    </keyword>
    <keyword id="KW-1142">
        <name>T=3 icosahedral capsid protein</name>
        <description>Viral protein that forms an icosahedral capsid with a T=3 symmetry to
protect the viral genome. The T=3 capsid is composed of 180 subunits,
each subunit occupying a quasi-equivalent position. The capsid
diameter ranges from 26 to 40 nm</description>
        <go id="GO:0039617"/>
    </keyword>
    <keyword id="KW-1144">
        <name>T=4 icosahedral capsid protein</name>
        <description>Viral protein that forms an icosahedral capsid with a T=4 symmetry to
protect the viral genome. The T=4 capsid is composed of 240 subunits,
each subunit occupying a quasi-equivalent position. The capsid
diameter ranges from 30 to 40 nm</description>
        <go id="GO:0039619"/>
    </keyword>
    <keyword id="KW-1145">
        <name>T=7 icosahedral capsid protein</name>
        <description>Viral protein that forms an icosahedral capsid with a T=7 symmetry to
protect the viral genome. The T=7 capsid is composed of 420 subunits,
each subunit occupying a quasi-equivalent position. Papillomavirus and
Polyomavirus T=7 capsids are composed of pentameric capsomeres for a
total of 360 capsid proteins. Its diameter ranges from 45 to 60 nm</description>
        <go id="GO:0039620"/>
    </keyword>
    <keyword id="KW-1143">
        <name>T=pseudo3 icosahedral capsid protein</name>
        <description>Viral protein that forms an icosahedral capsid with a pseudo T=3
symmetry to protect the viral genome. The pseudo T=pseudo3 capsid is
composed of 180 subunits. Each subunit does not occupy a quasi-
equivalent position, therefore the structure is called pseudo. The
capsid diameter ranges from 26 to 40 nm</description>
        <go id="GO:0039618"/>
    </keyword>
    <keyword id="KW-1137">
        <name>Tachyzoite</name>
        <name>Endodyozoite</name>
        <name>Endozoite</name>
        <description>Protein expressed in the infectious tachyzoite stage, a rapidly
growing, lytic and disease-causing stage in the life stage of
coccidians (e.g. Toxoplasmy). Tachyzoites, which can infect most
nucleated cells, replicate inside a parasitophorous vacuole, egress,
and then infect neighboring cells. Aggregates of numerous tachyzoites
are called clones, terminal colonies, or groups</description>
    </keyword>
    <keyword id="KW-1266">
        <name>Target cell cytoplasm</name>
        <name>Target cytoplasm</name>
        <description>Protein found in a target cell cytoplasm, the contents of a target
cell within the plasma membrane and which, in eukaryotic cells,
surrounds the host nucleus. This term is used to describe a toxin
located in the cytoplasm of a target cell</description>
    </keyword>
    <keyword id="KW-1052">
        <name>Target cell membrane</name>
        <name>Target cytoplasmic membrane</name>
        <name>Target plasma membrane</name>
        <name>Target plasmalemma</name>
        <description>Protein found in or associated with a target cell membrane, the
selectively permeable membrane which separates the target cell
cytoplasm from its surroundings. This term is used to describe a toxin
located to the cell membrane of a target cell</description>
    </keyword>
    <keyword id="KW-1053">
        <name>Target membrane</name>
        <description>Protein which is membrane-bound or membrane-associated with the target
membrane, a lipid bilayer which surrounds target cell enclosed spaces
and compartments. This selectively permeable structure is essential
for effective separation of a target cell or targeet cell organelle
from its surroundings. This term is used to describe a toxin located
to a membrane of a target cell</description>
        <go id="GO:0044218"/>
    </keyword>
    <keyword id="KW-0919">
        <name>Taste</name>
        <name>Gustation</name>
        <description>Protein involved in taste signal transduction. Human perceives five
basic taste qualities: bitter, salty, sour, sweet, and umami, the
taste of glutamate. Taste perception begins when a taste-eliciting
molecule, or tastant, interacts with specialized receptors in the
membrane of taste receptor cells. Taste responses to bitter, sweet,
and umami compounds are initiated by G-protein-coupled receptors and
transduced via G-protein signaling cascades. Salty and sour tastes are
transduced by ion channels</description>
        <go id="GO:0050909"/>
    </keyword>
    <keyword id="KW-0776">
        <name>Taste-modifying protein</name>
        <name>TMP</name>
        <name>Sweet-taste protein</name>
        <description>Protein that function as a natural sweetener or flavor enhancer. TMPs
are found in the fruit or seed of several plants and show no primary
sequence similarity. TMPs interact with taste receptors in a potent
and specific manner. TMPs are natural and have been used by some
cultures for centuries. West Africans have long used TMPs to improve
flavor and suppress bitterness of food and drink</description>
    </keyword>
    <keyword id="KW-0876">
        <name>Taxol biosynthesis</name>
        <name>Paclitaxel biosynthesis</name>
        <description>Protein involved in the synthesis of taxol, a complex diterpenoid
isolated from the bark of yew (Taxus) species. Taxol is a potent
antimitotic agent with activity against a number of leukamias and
solid tumors. It has become a chemotherapeutic drug under the generic
name of paclitaxel</description>
        <go id="GO:0042617"/>
    </keyword>
    <keyword id="KW-0777">
        <name>Teichoic acid biosynthesis</name>
        <name>C polysaccharide biosynthesis</name>
        <description>Protein involved in the synthesis of teichoic acid, a polymer of
mainly glycerol phosphate or ribitol phosphate substituted extensively
with amino acids and/or sugars. Teichoic acid occurs in the cell wall
of Gram-positive bacteria</description>
        <go id="GO:0019350"/>
    </keyword>
    <keyword id="KW-0778">
        <name>Tellurium resistance</name>
        <description>Protein that confers resistance to tellurium</description>
        <go id="GO:0046690"/>
    </keyword>
    <keyword id="KW-0779">
        <name>Telomere</name>
        <description>Protein involved in telomere replication, length regulation,
structure, etc. The telomere is a nucleoprotein structure comprising
the terminal section of a eukaryotic chromosome. It has a specialized
structure which is replicated by a special process, thereby
counteracting the tendency of a chromosome to be shortened during each
round of replication</description>
    </keyword>
    <keyword id="KW-0780">
        <name>Terminal addition</name>
        <description>Protein involved in the random addition of deoxynucleoside 5'-
triphosphate to the 3'end of a DNA initiator</description>
        <go id="GO:0006304"/>
        <go id="GO:0003912"/>
    </keyword>
    <keyword id="KW-0783">
        <name>Tetrahydrobiopterin biosynthesis</name>
        <description>Protein involved in the synthesis of tetrahydrobiopterin, the reduced
form of dihydrobiopterin, a reduced pteridine derivative related to
folic acid. It is a coenzyme for the enzyme phenylalanine-4-
hydroxylase which is involved in phenylalanine degradation</description>
        <go id="GO:0006729"/>
    </keyword>
    <keyword id="KW-0784">
        <name>Thiamine biosynthesis</name>
        <name>Thiamin biosynthesis</name>
        <name>Aneurin biosynthesis</name>
        <name>Vitamin B1 biosynthesis</name>
        <description>Protein involved in the synthesis of thiamine, a water-soluble vitamin
member of the vitamin B complex. It occurs in cells largely as its
active coenzyme form thiamine pyrophosphate, formerly called
cocarboxylase. Thiamine is necessary in the diet of most vertebrates
and some microorganisms. Its deficiency causes beriberi in man and
polyneuritis in birds. Thiamine pyrophosphate serves as coenzyme in
aldehyde-group transfers</description>
        <go id="GO:0009228"/>
    </keyword>
    <keyword id="KW-0785">
        <name>Thiamine catabolism</name>
        <name>Aneurin catabolism</name>
        <name>Vitamin B1 catabolism</name>
        <name>Thiamin catabolism</name>
        <description>Protein involved in the degradation of thiamine, a water-soluble
vitamin which is a member of the vitamin B complex. It occurs in cells
largely as its active coenzyme form thiamine pyrophosphate, formerly
called cocarboxylase. Thiamine is necessary in the diet of most
vertebrates and some microorganisms. Its deficiency causes beriberi in
man and polyneuritis in birds. Thiamine pyrophosphate serves as a
coenzyme in aldehyde-group transfers</description>
        <go id="GO:0009230"/>
    </keyword>
    <keyword id="KW-0786">
        <name>Thiamine pyrophosphate</name>
        <name>TDP</name>
        <name>Thiamin diphosphate</name>
        <name>TPP</name>
        <name>Thiamin pyrophosphate</name>
        <description>Protein which contains at least one thiamine pyrophosphate, the active
form of vitamin B1 (thiamine). It is a required coenzyme for the
pyruvate decarboxylase, pyruvate dehydrogenase and ketoglutarate
dehydrogenase reactions</description>
    </keyword>
    <keyword id="KW-0787">
        <name>Thick filament</name>
        <description>Protein found in, or associated with, the thick filaments which are
formed by bipolar myosin-II filaments (12-14 nm in diameter, 1.6 mm
long) found striated muscle. Myosin filaments elsewhere are often
referred to as 'thick filaments', although their length may be
considerably less. The myosin heads project from the thick filament in
a regular fashion</description>
        <go id="GO:0032982"/>
    </keyword>
    <keyword id="KW-0882">
        <name>Thioester bond</name>
        <name>Thiolester bond</name>
        <description>Protein which is posttranslationally modified by the formation of a
thioester crosslink between two amino acids in the polypeptidic
chain(s), usually formed between a cysteine side chain and the
carboxamide group of an asparagine or glutamine side chain</description>
    </keyword>
    <keyword id="KW-0883">
        <name>Thioether bond</name>
        <description>Protein which is posttranslationally modified by the formation of a
thioether crosslink between two amino acids in the polypeptidic
chain(s), usually formed between a cysteine side chain and the side
chain of a serine or a threonine</description>
    </keyword>
    <keyword id="KW-0788">
        <name>Thiol protease</name>
        <name>Thiol peptidase</name>
        <name>Thiol proteinase</name>
        <name>Sulfhydryl protease</name>
        <description>Proteolytic enzyme with a cysteine residue (Cys) in its active site
There are many families of thiol proteases. The most well known one is
the papain family (C1 in MEROPS classification) which is known to
exist in most eukaryotes</description>
        <go id="GO:0008234"/>
    </keyword>
    <keyword id="KW-0789">
        <name>Thiol protease inhibitor</name>
        <name>Thiol peptidase inhibitor</name>
        <name>Thiol proteinase inhibitor</name>
        <description>Protein which inhibits the activity of a thiol protease, a class of
proteases that contains an active site cysteine residue (Cys), e.g
papain, cathepsins, etc</description>
        <go id="GO:0004869"/>
    </keyword>
    <keyword id="KW-0791">
        <name>Threonine biosynthesis</name>
        <description>Protein involved in the synthesis of the essential amino acid
threonine</description>
        <go id="GO:0009088"/>
    </keyword>
    <keyword id="KW-0888">
        <name>Threonine protease</name>
        <description>Proteolytic enzyme with a threonine residue (Thr) in its active site
The prototype members of this class of enzymes are the proteasome
catalytic subunits</description>
        <go id="GO:0004298"/>
    </keyword>
    <keyword id="KW-0792">
        <name>Thrombophilia</name>
        <name>Recurrent venous thrombosis</name>
        <description>Protein which, if defective, causes thrombophilia, a disorder of
hemostasis in which the individuals are prone to serious spontaneous
thrombosis</description>
    </keyword>
    <keyword id="KW-0793">
        <name>Thylakoid</name>
        <description>Protein located in or on the thylakoid, a membranous cisterna of the
chloroplast. Thylakoids stack up to form the grana or stay as single
cisternae and interconnect the grana. The thylakoid contains the
photosynthetic pigments, reaction centers and electron-transport
chain. Thylakoid, where photosynthesis occurs, are also found in
cyanelles and in photosynthetic bacteria where they are the extensive
invaginations of the plasma membrane</description>
    </keyword>
    <keyword id="KW-0795">
        <name>Thyroid hormone</name>
        <description>Protein precursor of thyroid hormones which are secreted by the thymus
gland and participate in the development of the lymphoid system as
well as the maturation of the cellular immune response. Also used for
proteins which bind thyroid hormones or thyroid hormone receptor
antagonists</description>
    </keyword>
    <keyword id="KW-0893">
        <name>Thyroid hormones biosynthesis</name>
        <description>Protein involved in the synthesis of thyroid hormones</description>
        <go id="GO:0042446"/>
    </keyword>
    <keyword id="KW-0796">
        <name>Tight junction</name>
        <description>Protein which is a component of the tight junction or are associated
with it. These specialized regions of the plasma membrane prevent the
diffusion of dissolved molecules between adjacent epithelial cells,
seal off body cavities such as intestine or stomach lumen and prevent
the diffusion of membrane proteins and glycolipids between the apical
and basolateral regions of the plasma membrane</description>
    </keyword>
    <keyword id="KW-0797">
        <name>Tissue remodeling</name>
        <description>Protein involved in tissue remodeling. As an example the matrix-
degrading plasminogen activators (PAs) and matrix metalloproteinases
(MMPs) are general proteolytic enzyme systems which mediate tissue
remodeling and tissue destruction in a variety of physiological and
pathological conditions, including ovulation, angiogenesis,
implantation, tumor invasion and inflammatory diseases such as
rheumatoid arthritis (RA)</description>
        <go id="GO:0048771"/>
    </keyword>
    <keyword id="KW-0798">
        <name>TonB box</name>
        <description>Protein with a TonB box. In Escherichia coli the TonB protein
interacts with outer membrane receptor proteins that carry out high-
affinity binding and energy-dependent uptake of specific substrates
into the periplasmic space. These substrates are either poorly
permeable through the porin channels or are encountered at very low
concentrations. In the absence of TonB these receptors bind their
substrates but do not carry out active transport. TonB also interacts
with some colicins and is involved in the energy dependent,
irreversible steps of bacteriophages phi-80 and T1 infection</description>
    </keyword>
    <keyword id="KW-0799">
        <name>Topoisomerase</name>
        <description>Enzymes capable of altering the degree of supercoiling of double-
stranded DNA molecules. Various topoisomerases can increase or relax
supercoiling, convert single-stranded rings to intertwined double-
stranded rings, tie and untie knots in single stranded and duplex
rings or catenate and decatenate duplex rings. Any enzyme that cleaves
only one strand of a DNA duplex and then reseals it is classified as a
type I topoisomerase (Topo I). Type II topoisomerases (Topo II) change
DNA topology by breaking and rejoining double-stranded DNA</description>
        <go id="GO:0003916"/>
    </keyword>
    <keyword id="KW-0800">
        <name>Toxin</name>
        <description>Naturally-produced poisonous protein that damages or kills other
cells, or the producing cells themselves in some cases in bacteria
Toxins are produced by venomous and poisonous animals, some plants,
some fungi and some pathogenic bacteria. Animal toxins (mostly from
snakes, scorpions, spiders, sea anemones and cone snails) are
generally secreted in the venom of the animal</description>
        <go id="GO:0090729"/>
    </keyword>
    <keyword id="KW-1277">
        <name>Toxin-antitoxin system</name>
        <name>Toxin-antitoxin module</name>
        <description>Bacterial, archaeal or viral protein belonging to a toxin-antitoxin
(TA) system. Toxin protein expression is poisonous to the cell and is
counteracted by its co-expressed, short-lived "antidote" antitoxin
Antitoxins can be protein (type II, IV, V, VI) or RNA (type I, III)
and act directly or indirectly on the toxin protein or transcript
Genes for the 2 components are closely linked; in many type II TA
systems the toxin-antitoxin complex regulates transcription of its
operon. Toxins belong to recognizable protein families, antitoxins
usually do not. Orphan toxin genes are occasionally found in complete
genomes</description>
    </keyword>
    <keyword id="KW-0801">
        <name>TPQ</name>
        <name>Topaquinone</name>
        <description>Protein which is posttranslationally modified on a tyrosine residue to
form TPQ. This modification of a strictly conserved active-site
tyrosine residue proceeds via the hydroxylation of tyrosine to Topa
(Trihydroxyphenylalanine) and then to TPQ (Topaquinone). It is a self-
processing pathway requiring only the protein, copper and molecular
oxygen. TPQ is the redox cofactor of most copper-containing amine
oxidases</description>
    </keyword>
    <keyword id="KW-0802">
        <name>TPR repeat</name>
        <name>Tetratricopeptide repeat</name>
        <description>Protein with at least one TPR repeat. The TPR repeat of typically 34
amino acids was first described in the yeast cell division control
protein 23 (CDC23) and later found to occur in a large number of
proteins. A function for this repeat seems to be protein-protein
interaction</description>
    </keyword>
    <keyword id="KW-0804">
        <name>Transcription</name>
        <description>Protein involved in the transfer of genetic information from DNA to
messenger RNA (mRNA) by DNA-directed RNA polymerase. In the case of
some RNA viruses, protein involved in the transfer of genetic
information from RNA to messenger RNA (mRNA) by RNA-directed RNA
polymerase</description>
    </keyword>
    <keyword id="KW-0889">
        <name>Transcription antitermination</name>
        <description>Protein involved in transcription antitermination, the process whereby
RNA polymerase is allowed to read through specific RNA secondary
structures that normally terminate transcription</description>
        <go id="GO:0031564"/>
    </keyword>
    <keyword id="KW-0805">
        <name>Transcription regulation</name>
        <description>Protein involved in the regulation of the transcription process</description>
    </keyword>
    <keyword id="KW-0806">
        <name>Transcription termination</name>
        <description>Protein involved in transcription termination</description>
        <go id="GO:0006353"/>
    </keyword>
    <keyword id="KW-0807">
        <name>Transducer</name>
        <description>Protein which converts an input signal into an output signal of a
different form</description>
        <go id="GO:0007165"/>
    </keyword>
    <keyword id="KW-0808">
        <name>Transferase</name>
        <description>Enzyme that transfers a chemical group, e.g. a methyl group or a
glycosyl group from one compound (donor) to another compound
(acceptor)</description>
        <go id="GO:0016740"/>
    </keyword>
    <keyword id="KW-0809">
        <name>Transit peptide</name>
        <description>Proteins which have an N-terminal presequence which directs them to an
organelle (chloroplast, mitochondria, microbody, cyanelle). The
transit peptide is required for their transport across the relevant
membranes from their site of synthesis in the cytoplasm</description>
    </keyword>
    <keyword id="KW-0810">
        <name>Translation regulation</name>
        <description>Protein involved in the regulation of peptide formation on ribosomes,
directed by messenger RNA (mRNA)</description>
        <go id="GO:0006417"/>
    </keyword>
    <keyword id="KW-1155">
        <name>Translational shunt</name>
        <name>Ribosomal shunt</name>
        <name>Shunting</name>
        <name>Ribosome shunt</name>
        <description>Protein which is involved in the translational shunt, an unusual
translation process in which ribosomes are loaded onto mRNA at the 5'-
cap structure, start scanning for a short distance before bypassing
the large internal leader region and initiating at a downstream start
site. Shunting operates in plants, animals, and yeast translational
systems, both in vivo and in vitro</description>
    </keyword>
    <keyword id="KW-1278">
        <name>Translocase</name>
        <description>Protein that uses enzyme activity to effect transmembrane transport,
as exemplified by transmembrane transport coupled to ATP hydrolysis
and oxidoreductases involved in transmembrane proton or electron
transport. Not to be confused with ligand-gated ion channels or other
transmembrane transporters without enzyme activity</description>
    </keyword>
    <keyword id="KW-0811">
        <name>Translocation</name>
        <description>Protein involved in the transport of proteins across a membrane. As an
example translocation into the nucleus occurs via nuclear pores which
allow rapid diffusion of small molecules. Larger molecules (maximum 9
nm) take longer. Translocation into the mitochondria or chloroplast
occurs at sites of adhesion between the outer and inner membranes and
is driven by ATP hydrolysis as well as the electrochemical gradient of
the inner membrane</description>
        <go id="GO:0015031"/>
    </keyword>
    <keyword id="KW-0812">
        <name>Transmembrane</name>
        <description>Protein with at least one transmembrane domain, a membrane-spanning
helical or beta-stranded domain embedded in a membrane</description>
    </keyword>
    <keyword id="KW-1134">
        <name>Transmembrane beta strand</name>
        <description>Protein with at least one transmembrane beta stranded domain, a
membrane-spanning stretch, typically 5-10 amino acids long, whose
peptide backbones are almost fully extended with the sidechains of two
neighboring residues projected in the opposite direction from the
backbone. Two or more hydrogen bonded (parallel or anti-parallel) beta
strands form a beta sheet. A beta barrel is formed by a closed beta
sheet around a central pore. Beta barrels consist usually of an even
number of beta strands (between 8 and 24), they are found only in
bacterial outer membranes, mitochondria and plastids</description>
    </keyword>
    <keyword id="KW-1133">
        <name>Transmembrane helix</name>
        <name>Pauling-Corey-Branson alpha helix</name>
        <name>Alpha-helical transmembrane</name>
        <description>Protein with at least one transmembrane helical domain, a membrane-
spanning domain with an hydrogen-bonded helical configuration,
including alpha-, 3-10-, and pi-helices. The transmembrane alpha-helix
is very common, while the 3-10-helix is found at the ends of alpha-
helices and the pi-helix, is more rare</description>
    </keyword>
    <keyword id="KW-0813">
        <name>Transport</name>
        <description>Protein involved in the transport of a molecule (metabolite, protein,
etc), a ion or an electron across cell membranes, inside the cell or
in a tissue fluid</description>
    </keyword>
    <keyword id="KW-0814">
        <name>Transposable element</name>
        <name>Transposon</name>
        <description>Protein encoded by a transposable element, or transposon, a mobile DNA
segment that can replicate and insert a copy at another site within
the genome. Simple transposons only contains genes needed for
insertion. More complex types also carry genes with functions
unrelated to insertion, e.g. genes for resistance to antibiotics or
heavy metals</description>
    </keyword>
    <keyword id="KW-0815">
        <name>Transposition</name>
        <description>Protein involved in the movement of a specific DNA sequence
- generally known as a transposable element or transposon - to another
location within the genome by replication of the sequence and
insertion of the copy at its target site, at random or at some
specific site. Proteins necessary for the transposition, such as the
enzyme transposase, are usually encoded by the transposable element
itself</description>
        <go id="GO:0032196"/>
    </keyword>
    <keyword id="KW-0816">
        <name>Tricarboxylic acid cycle</name>
        <name>TCA cycle</name>
        <name>Citric acid cycle</name>
        <name>Krebs cycle</name>
        <description>Protein involved in the tricarboxylic acid cycle, a series of
metabolic reactions in aerobic cellular respiration, which occurs in
the mitochondria of animals and plants and in which acetyl-CoA, formed
from pyruvate produced during glycolysis, is completely oxidized to
CO2 via the interconversion of various carboxylic acids. It results in
the reduction of NAD and FAD to NADH and FADH2, whose reducing power
is then used indirectly in the synthesis of ATP by oxidative
phosphorylation. The TCA cycle also provides intermediates for many
other biosynthetic processes</description>
        <go id="GO:0006099"/>
    </keyword>
    <keyword id="KW-0817">
        <name>Trimethoprim resistance</name>
        <description>Protein that confers, on bacteria or other microorganisms, the ability
to withstand the antibacterial agent trimethroprim that inhibits
dihydrofolate reductase (DHFR), an enzyme required for de novo glycine
and purine synthesis</description>
        <go id="GO:0046677"/>
    </keyword>
    <keyword id="KW-0818">
        <name>Triplet repeat expansion</name>
        <description>Protein encoded by a gene which has a triplet repeat expansion, i.e
the increase of triplet (trinucleotide) repeats within the gene
sequence. The length of such repeats is frequently polymorphic, and
there is often a correlation between repeat length and disease
severity</description>
    </keyword>
    <keyword id="KW-0819">
        <name>tRNA processing</name>
        <name>tRNA biosynthesis</name>
        <name>Transfer RNA processing</name>
        <description>Protein involved in the processing of the primary tRNA transcript to
yield a functional tRNA. Transcription of tRNA genes results in a
large precursor molecule which may even contain sequences for several
tRNA molecules. This primary transcript is subsequently processed by
cleavage and by modification of the appropriate bases</description>
        <go id="GO:0008033"/>
    </keyword>
    <keyword id="KW-0820">
        <name>tRNA-binding</name>
        <name>Transfer RNA binding</name>
        <description>Protein which binds transfer RNA, for example some ribosomal proteins
or some aminoacyl-tRNA synthetases</description>
        <go id="GO:0000049"/>
    </keyword>
    <keyword id="KW-1138">
        <name>Trophozoite</name>
        <description>Protein expressed in the trophozoite stage, a motile replicating and
disease-causing stage of in the life cycle of some sporozoan
parasites</description>
    </keyword>
    <keyword id="KW-0821">
        <name>Trypanosomiasis</name>
        <description>Protein involved in trypanosomiasis, a human or animal disease caused
by Trypanosoma, a genus of parasitic flagellate protozoa. Such
diseases include African sleeping sickness, Nagana and American
Chagas' disease</description>
    </keyword>
    <keyword id="KW-0822">
        <name>Tryptophan biosynthesis</name>
        <description>Protein involved in the synthesis of the aromatic amino acid
tryptophan (Trp) in bacteria, fungi and plants from chorismate. Trp is
needed to synthesize proteins and as a precursor to niacin, serotonin
and melatonin</description>
        <go id="GO:0000162"/>
    </keyword>
    <keyword id="KW-0823">
        <name>Tryptophan catabolism</name>
        <description>Protein involved in the degradation of the aromatic amino acid
tryptophan (Trp)</description>
        <go id="GO:0006569"/>
    </keyword>
    <keyword id="KW-0824">
        <name>TTQ</name>
        <name>Tryptophan tryptophylquinone</name>
        <description>Protein which contains at least one tryptophan tryptophylquinone (TTQ)
cross-link modification. TTQ, the cofactor of methylamine
dehydrogenase (MADH), is formed by oxidation of the indole ring of a
tryptophan to form tryptophylquinone followed by covalent cross-
linking with another tryptophan residue. MADH converts primary amines
to their corresponding aldehydes plus ammonia. During the catalytic
cycle, TTQ mediates electron transfer from the substrate to a copper
protein, amicyanin. These electrons are transferred to the respiratory
chain via a C-type cytochrome</description>
    </keyword>
    <keyword id="KW-0825">
        <name>Tumor antigen</name>
        <name>Cancer antigen</name>
        <description>Protein on the surfaces of tumor cells detected by cell-mediated
immunity. Different categories of tumor antigens which induce
cytotoxic T lymphocyte (CTL) responses in vitro and in vivo, have been
identified. These are, namely, "cancer testis" (CT) antigens expressed
in different tumours and normal testis, melanocyte differentiation
antigens, point mutations of normal genes, self antigens that are
overexpressed in malignant tissues and viral antigens</description>
    </keyword>
    <keyword id="KW-0043">
        <name>Tumor suppressor</name>
        <name>Anti-oncogene</name>
        <name>Antitumor</name>
        <description>Protein that suppresses tumorigenesis. Tumor suppressors generally
function as negative regulators of cell cycle progression or cell
proliferation. They may act to enforce cell cycle arrest in response
to specific signals, such as DNA damage, thereby allowing DNA repair
to occur prior to DNA replication. Tumor suppressors that act in this
way include TP53 and its downstream effector CDKN1A/p21. They may also
act to induce programmed cell death (apoptosis) in response to
specific developmental signals or under circumstances where DNA repair
cannot be completed. Tumor suppressors that act in this way include
PTEN and BAX</description>
    </keyword>
    <keyword id="KW-0826">
        <name>Tungsten</name>
        <description>Protein which binds at least one tungsten atom, or protein whose
function is tungsten-dependent. Tungsten is a metallic element,
chemical symbol W</description>
    </keyword>
    <keyword id="KW-0902">
        <name>Two-component regulatory system</name>
        <name>Two-component sensory transduction system</name>
        <name>Two-component system</name>
        <name>Phosphorelay system</name>
        <name>Phospho-relay system</name>
        <name>Two-component signal transduction system</name>
        <description>Protein involved in a system responding to environmental changes
characterized usually by a sensor kinase in the cell membrane that
phosphorylates itself in response to a signal and a response regulator
to which the phosphoryl group is transferred. The responder is
typically a DNA-binding protein that regulates transcription. Several
of these systems are quite complex, involving many proteins in a
signaling cascade or contributing to several responses simultaneously
They are involved in a variety processes such as chemotaxis,
osmoregulation, magnesium transport, pH tolerance, sporulation, or
response of virulent species to host cell's environments</description>
        <go id="GO:0000160"/>
    </keyword>
    <keyword id="KW-0827">
        <name>Tyrosine biosynthesis</name>
        <description>Protein involved in the synthesis of the aromatic amino acid tyrosine
In microorganisms and plants, tyrosine is synthesized from chorismate
via a simple pathway using prephenate as an intermediate. In rat, this
nonessential amino acid is produced by hydroxylating the essential
amino acid phenylalanine</description>
        <go id="GO:0006571"/>
    </keyword>
    <keyword id="KW-0828">
        <name>Tyrosine catabolism</name>
        <description>Protein involved in the degradation of the aromatic amino acid
tyrosine. In mammals, tyrosine degradation is catalyzed by a series of
5 enzymatic reactions which yield acetoacetate (ketogenic) and the
Krebs cycle intermediate fumarate (glucogenic)</description>
        <go id="GO:0006572"/>
    </keyword>
    <keyword id="KW-0829">
        <name>Tyrosine-protein kinase</name>
        <description>Enzyme which catalyzes the transfer of the terminal phosphate of ATP
to a specific tyrosine residue on its target protein. Many of these
kinases play significant roles in development and cell division
Tyrosine-protein kinases can be divided into two subfamilies: receptor
tyrosine kinases, which have an intracellular tyrosine kinase domain,
a transmembrane domain and an extracellular ligand-binding domain; and
non-receptor (cytoplasmic) tyrosine kinases, which are soluble,
cytoplasmic kinases</description>
        <go id="GO:0004713"/>
    </keyword>
    <keyword id="KW-0830">
        <name>Ubiquinone</name>
        <name>CoQ</name>
        <name>Coenzyme Q</name>
        <description>Protein which interacts with ubiquinone. This fat soluble benzoquinone
has a long isoprenoid side chain, which varies in length depending on
the species. For example, S.cerevisiae has CoQ-6, E.coli has CoQ-8,
rat and R.capsulatus have CoQ-9 and S.pombe, G.suboxydans and humans
have CoQ-10. Ubiquinone is a carrier of hydrogen atoms (protons plus
electrons) and functions as an ubiquitous coenzyme in redox reactions,
where it is first reduced to the enzyme-bound intermediate radical
semiquinone and in a second reduction to ubiquinol (Dihydroquinone;
CoQH2). Ubiquinone is not tightly bound or covalently linked to a
protein complex but is very mobile</description>
    </keyword>
    <keyword id="KW-0831">
        <name>Ubiquinone biosynthesis</name>
        <name>Coenzyme Q biosynthesis</name>
        <name>CoQ biosynthesis</name>
        <description>Protein involved in the synthesis of ubiquinone which involves the
conversion of chorismate into 4-hydroxy-benzoate, to which is added
six to ten isoprene units to form polyprenyl phenol. The addition of a
further oxygen atom at C3, followed by the transfer of three methyl
groups from S-adenosine methionine gives rise to ubiquinol, which is
further reduced to ubiquinone (6-polyprenyl-2,3-dimethoxy-5-methyl-
1,4-benzoquinone)</description>
        <go id="GO:0006744"/>
    </keyword>
    <keyword id="KW-0832">
        <name>Ubl conjugation</name>
        <name>Ubiquitination</name>
        <name>Ubiquitin-like modifier conjugation</name>
        <name>Sumoylation</name>
        <name>Ubiquitin conjugation</name>
        <name>Ubiquitinylation</name>
        <description>Protein which is posttranslationally modified by the attachment of at
least one ubiquitin-like modifier protein, such as ubiquitin, SUMO,
APG12, URM1 or RUB1. Ubiquitin, for example, is linked through a
isopeptide bond between its C-terminus and the epsilon group of a
lysine residue present on either another ubiquitin-like modifier
protein or a target protein</description>
    </keyword>
    <keyword id="KW-0833">
        <name>Ubl conjugation pathway</name>
        <name>Ubiquitin-like modifier conjugation pathway</name>
        <name>Ubiquitin conjugation pathway</name>
        <description>Protein involved in ubiquitin-like modifier processing, activation,
conjugation or deconjugation such as Ubl-activating enzymes (E1s),
Ubl-conjugating enzymes (E2s), Ubl-protein ligases (E3s), some thiol
proteases (Ubiquitin carboxyl-terminal hydrolases (UCH), Ubiquitin-
specific processing proteases (UBP) and ubiquitin-like proteases) and
the ubiquitin-like modifier proteins. Besides signaling proteolysis,
ubiquitination for example can be a signal for trafficking, kinase
activation and other nonproteolytic fates</description>
    </keyword>
    <keyword id="KW-0834">
        <name>Unfolded protein response</name>
        <name>UPR</name>
        <name>ER stress pathway</name>
        <name>ER stress response</name>
        <description>Protein involved in the unfolded protein response. An accumulation of
unfolded proteins in the ER lumen triggers a stress response,
resulting in the transcriptional induction in the nucleus of a set of
genes, whose products are involved in protein folding, assembly and
modification as well as in phospholipid biosynthesis. The unfolded
protein response (UPR) is the intracellular pathway that mediates
signaling from the endoplasmic reticulum (ER) to the nucleus. UPR is
also tightly linked to ER-associated protein degradation (ERAD). UPR
is a ubiquitous mechanism observed in all eukaryotes from humans to
yeast</description>
        <go id="GO:0006986"/>
    </keyword>
    <keyword id="KW-0835">
        <name>Urea cycle</name>
        <name>Krebs-Henseleit cycle</name>
        <description>Protein involved in the urea cycle. This is a metabolic pathway in
which ammonia, produced during amino acid degradation, is converted to
urea in the liver, through a series of reactions that are distributed
between the mitochondrial matrix and the cytosol</description>
        <go id="GO:0000050"/>
    </keyword>
    <keyword id="KW-0836">
        <name>Usher syndrome</name>
        <name>Usher's syndrome</name>
        <name>Sensorineural deafness with retinitis pigmentosa</name>
        <description>Protein which, if defective, causes Usher syndrome, an autosomal
recessive disorder characterized by sensorineural hearing loss and
retinitis pigmentosa leading to visual impairment. There are three
clinical subtypes: Usher syndrome type 1 (USH1), characterized by
congenital profound deafness, constant vestibular dysfunction, and
prepubertal onset of retinitis pigmentosa; Usher syndrome type 2
(USH2), associated with moderate to severe hearing loss, normal
vestibular function, and onset of retinitis pigmentosa during the
second decade of life; and Usher syndrome type 3 (USH3), characterized
by progressive hearing loss, variable vestibular function, and adult
onset retinitis pigmentosa</description>
    </keyword>
    <keyword id="KW-0926">
        <name>Vacuole</name>
        <description>Protein related to the vacuole of a cell. The precise form and
function of vacuoles may vary between phyla. Plant vacuoles are among
the best characterized. They are generally large fluid-filled
compartments in the cytoplasm, bounded by a membrane called the
tonoplast; individual vacuoles can fuse to form larger species
Examples include the lytic vacuole, the storage vacuole and the
lutoid. One important function of plant vacuoles is the maintenance of
hydrostatic pressure. Other eukaryotes employ vacuoles for a variety
of purposes, including storage (as in the yeast lysosome/vacuole),
secretion and phagocytosis. In Protozoa, contractile vacuoles can be
used to discharge water from the cytoplasm to the external
environment</description>
    </keyword>
    <keyword id="KW-0837">
        <name>Vanadium</name>
        <description>Protein whose function is vanadium-dependent. Vanadium is a transition
metal, chemical symbol V</description>
    </keyword>
    <keyword id="KW-0838">
        <name>Vasoactive</name>
        <description>Protein which is vasoactive, i.e. has a constricting or dilating
effect on the caliber of blood vessels</description>
        <go id="GO:0097746"/>
    </keyword>
    <keyword id="KW-0839">
        <name>Vasoconstrictor</name>
        <description>Protein which constricts the caliber of blood vessels</description>
        <go id="GO:0042310"/>
    </keyword>
    <keyword id="KW-0840">
        <name>Vasodilator</name>
        <description>Protein which dilates the caliber of blood vessels</description>
        <go id="GO:0042311"/>
    </keyword>
    <keyword id="KW-1233">
        <name>Viral attachment to host adhesion receptor</name>
        <description>Virion surface protein implicated in the initial binding to a specific
host adhesion molecule. Adhesion receptors can be for example
proteoglycans, sialic acids or a protein receptor. This initial
attachment is not sufficient for triggering virus entry into host
cell. In prokaryotic viruses, the primary attachment is called
reversible adsorption</description>
        <go id="GO:0098671"/>
    </keyword>
    <keyword id="KW-1161">
        <name>Viral attachment to host cell</name>
        <name>Virion attachment to host cell surface</name>
        <description>Viral surface protein implicated in the binding to specific host
surface molecule(s). This binding can lead to virion entry into the
host cell, it can trigger signaling pathways, or it can allow the
virion to be carried by the host cell to a specific organ</description>
        <go id="GO:0019062"/>
    </keyword>
    <keyword id="KW-1240">
        <name>Viral attachment to host cell flagellum</name>
        <description>Virion protein involved in the primary attachment to host flagellar
receptor. This attachment allows the prokaryotic virus to move along
the host flagellum to find its entry receptor for viral genome
penetration. Some prokaryotic viruses such as bacteriophages Chi or
PV22 specifically interact with their host's flagellum, move toward
the base of the flagellum to come in contact with the host cytoplasmic
membrane and deliver the viral genome into the host cytoplasm</description>
        <go id="GO:0098931"/>
    </keyword>
    <keyword id="KW-1175">
        <name>Viral attachment to host cell pilus</name>
        <description>Virion protein involved in the interaction with bacterial pili, which
are retractile filaments that protrude from bacteria with 2 membranes
(Gram-negative bacteria). Binding to the pilus is followed by
retraction of the pilus, which translocates the bound virion to the
bacterial surface and allows subsequent viral genome penetration into
host cytoplasm. Bacteriophages M13, f1, fd, R17, Qbeta, Pf1, Pf3,
phiKMV or phi6 for example utilize the host cell pilus as an
attachment structure</description>
        <go id="GO:0039666"/>
    </keyword>
    <keyword id="KW-1234">
        <name>Viral attachment to host entry receptor</name>
        <description>Virion surface protein implicated in the binding to a secondary
specific host surface molecule(s), which triggers the internalization
of viral genome and possibly other viral components into the host
cell. In prokaryotic viruses, the attachment to a host entry receptor
is called irreversible adsorption</description>
        <go id="GO:0098670"/>
    </keyword>
    <keyword id="KW-1226">
        <name>Viral baseplate protein</name>
        <description>Viral protein part of the virion base plate of tailed prokaryotic
viruses such as Caudovirales. The baseplate is a multiprotein
component at the end of the tail and to which fibers of tailed phages
may be attached. Sometimes referred to as the tail tip or tip
structure in Siphoviridae</description>
        <go id="GO:0098025"/>
    </keyword>
    <keyword id="KW-1198">
        <name>Viral budding</name>
        <description>Viral protein involved in the budding of a viral particle through a
cellular membrane into the extracellular space or into a cellular
compartment</description>
        <go id="GO:0046755"/>
    </keyword>
    <keyword id="KW-1187">
        <name>Viral budding via the host ESCRT complexes</name>
        <description>Viral protein which recruits the cellular ESCRT (Endosomal Sorting
Complex Required for Transport) to mediate host-assisted viral
budding. Specific motifs in enveloped viruses' proteins called late
assembly domains (L-domains) are responsible for recruiting the ESCRT
machinery directly or via ESCRT-associated proteins like PDCD6IP</description>
        <go id="GO:0039702"/>
    </keyword>
    <keyword id="KW-0118">
        <name>Viral capsid assembly</name>
        <name>Viral procapsid assembly</name>
        <description>Viral protein involved in the assembly of the capsid. In most cases
virion assembly is spontaneous, but viruses like adenoviruses,
herpesviruses, microviruses and tailed bacteriophages need the help of
scaffolding proteins to assemble their capsid. Maturation steps that
remove the scaffolding proteins and induce structural changes in the
assembled capsid are also often part of the assembly process</description>
        <go id="GO:0019069"/>
    </keyword>
    <keyword id="KW-1273">
        <name>Viral capsid maturation</name>
        <name>Viral procapsid maturation</name>
        <description>Viral protein involved in the refolding and structural rearrangements
of the procapsid shell that give rise to the more stable mature capsid
structure. These maturation events occur during the intracellular
capsid assembly process. In many cases, procapsid maturation is
initiated by the activation of a viral protease. Most bacterial
viruses as well as Herpesviruses assemble as a procapsid that mature
through a massive conformational change of the surface shell</description>
        <go id="GO:0046797"/>
    </keyword>
    <keyword id="KW-1242">
        <name>Viral contractile tail ejection system</name>
        <name>Viral genome injection via long contractile tail</name>
        <description>Viral protein that constitutes the contractile ejection system carried
by some tailed prokaryotic viruses such as the Myoviridae. This
structure is able to penetrate the host cell envelope, to deliver the
viral genome, and possibly some specific proteins, into the cell
cytoplasm. A contractile ejection system is composed at least of the
contractile sheath, the internal noncontractile tube, the baseplate
and the terminator complex. Sheath contraction drives the rigid
internal tube through the host cell envelope. Proteins of the ejection
apparatus can play an active or a structural role in ejection</description>
        <go id="GO:0099000"/>
    </keyword>
    <keyword id="KW-1194">
        <name>Viral DNA replication</name>
        <description>Viral protein involved in the synthesis of multiple copies of the
viral DNA genome. The replicated genomes provide support for further
viral transcription or are assembled into progeny virions</description>
        <go id="GO:0039693"/>
    </keyword>
    <keyword id="KW-0261">
        <name>Viral envelope protein</name>
        <description>Protein of the viral envelope, a lipoprotein membrane which forms the
outermost layer of the virion in certain viruses</description>
        <go id="GO:0019031"/>
    </keyword>
    <keyword id="KW-1255">
        <name>Viral exotoxin</name>
        <description>Virally encoded toxin that acts as a host virulence factor against
another organism. Viral exotoxins are mostly expressed from integrated
viral genomes. Bacterium host, bacterial populations, and the encoding
virus/provirus probably benefit from the expression of such exotoxins
Although prokaryotic viruses can kill their host if they switch to the
lytic cycle, provirus encoding exotoxins (e.g. shiga toxin, diphtheria
toxin) are often retained for the sake of bacterial utility</description>
    </keyword>
    <keyword id="KW-1249">
        <name>Viral extrusion</name>
        <description>Viral protein involved in the extrusion of viral particles from the
host prokaryotic cell. Extrusion is a concerted mechanism of assembly
and secretion used by filamentous phages to release mature viral
particles without inducing host cell lysis</description>
        <go id="GO:0099045"/>
    </keyword>
    <keyword id="KW-1253">
        <name>Viral genome circularization</name>
        <description>Viral protein that is involved in or facilitates the conversion of a
linear double stranded DNA viral genome into a circular form, either
by homologous recombination between redundant ends or by association
of complementary single stranded ends (sticky ends). Circular genomes
can support rolling circle replication and, for many viruses, genome
circularization is also necessary for latency</description>
        <go id="GO:0099009"/>
    </keyword>
    <keyword id="KW-1171">
        <name>Viral genome ejection through host cell envelope</name>
        <name>Viral genome ejection through host membranes</name>
        <description>Viral protein that constitutes the ejection system carried by some
prokaryotic viruses. These structures are able to penetrate the host
cell envelope in order to deliver the viral genome, and possibly also
some specific proteins, into the cell cytoplasm</description>
        <go id="GO:0039678"/>
    </keyword>
    <keyword id="KW-1250">
        <name>Viral genome excision</name>
        <description>Viral protein involved in latent provirus DNA excision from the host
genome following induction. Bacteriophage lambda for example expresses
an excisionase that manages excision of the viral genome from the host
genome</description>
        <go id="GO:0032359"/>
    </keyword>
    <keyword id="KW-1179">
        <name>Viral genome integration</name>
        <description>Viral protein involved in the integration of a virus genome into the
host DNA. Integrated viral DNA is referred to as a provirus in the
case of retroviruses or prophage in the case of prokaryotic viruses
The integrated viral genome does not necessarily make new DNA copies
of itself while integrated into a host genome. Instead, it can remain
latent and be passively replicated along with the host genome and
passed on to the original cell's offspring; all descendants of the
infected cell will also bear it in their genomes. The host's
environmental conditions changes can however reactivate the virus
leading to viral transcription and production of new infectious
viruses (productive infection). Integration is a crucial step in
replication of retroviruses, as well as some phages. Integration is
not part of the viral replication cycle of phycodnaviruses, adeno-
associated virus type 2, and human herpesvirus 6A genome, but can
occasionally occur</description>
        <go id="GO:0075713"/>
        <go id="GO:0044826"/>
    </keyword>
    <keyword id="KW-0231">
        <name>Viral genome packaging</name>
        <description>Protein involved in actively packaging the replicated viral genome
into a protective shell or envelope. Such packaging proteins are
present for example in adenoviruses, herpesviruses and tailed
bacteriophages. In bacteriophages, the packaging proteins complex is
involved in recognizing and selecting a neo-synthesized viral genome
in order to translocate it into a pre-assembled empty procapsid. DNA
cleavage is sometimes coupled to genome packaging as well as
maturation steps that induce structural changes in the assembled
capsid</description>
        <go id="GO:0019072"/>
    </keyword>
    <keyword id="KW-0899">
        <name>Viral immunoevasion</name>
        <name>Viral host defense evasion</name>
        <name>Viral immune evasion</name>
        <name>Immunoevasin</name>
        <description>Viral protein involved in evading host innate and adaptive immune
responses, allowing optimized viral replication, propagation, or
persistence in the host. The protein allows viruses to avoid/escape
immune detection or neutralize/inactivate the host immune defenses to
ensure virus survival within its host. The innate immune system is a
non-specific defense system found in all cellular organisms. In
metazoans and plants, it includes the intracellular pattern
recognition receptors (PRRs) that detect pathogen-associated molecular
patterns (PAMPs). In plants and invertebrates, it includes the RNA
interference (RNAi) system. Plants also have effector-triggered
immunity (ETI). In metazoans, it includes the cell-dependent
mechanisms (e.g. phagocytes) or secreted factors. Bacteria and archaea
have an innate immune system relying on various systems (e.g. the
restriction-modification system, Pycsar). The adaptive (or acquired)
immune system is a specific defense. In vertebrates, it is mediated by
T and B lymphocytes expressing specific receptors. Bacteria and
archaea have adaptive immunity, the CRISPR-Cas system</description>
        <go id="GO:0019049"/>
    </keyword>
    <keyword id="KW-1182">
        <name>Viral ion channel</name>
        <name>Viroporin</name>
        <description>Small transmembrane protein that homo-oligomerizes to form a viral ion
channel usually expressed in the viral envelope and host cell
membranes. These channels affect membrane permeability to ions and
play an important role in facilitating virus entry, assembly and
release, as well as modulating the ion homeostasis of host cells
Viral ion channels are not necessarily required for the production of
infectious virions, although their expression usually significantly
increases growth. During influenza A virus entry for example, the M2
proton channel allows protons from the acidic endosome to enter the
enveloped virion, initiating pH-dependent uncoating of the genome. In
certain influenza A subtypes, M2 also equilibrates the intraluminal pH
of the trans-Golgi network with the cytoplasm, preventing premature
conformational changes in the viral fusion protein during budding</description>
        <go id="GO:0015267"/>
        <go id="GO:0033644"/>
    </keyword>
    <keyword id="KW-1251">
        <name>Viral latency</name>
        <name>Viral lysogeny</name>
        <description>Viral protein expressed primarily to establish, maintain or terminate
latency, the part of the viral life cycle during which a virus lies
dormant (latent) within a cell. This part of the virus life cycle is
called the lysogenic part in prokaryotic viruses. During latency, the
viral genome can either exist as a provirus integrated in the host
genome (proviral latency) or as a linear or circular plasmid in the
host cell (episomal latency). The virus does not replicate, but is
passively duplicated when the host divides. In eukaryotes for example,
HHV-1 and HHV-3 establish episomal latency in neurons. HIV is
integrated as a provirus in the genome of resting CD4-positive T
cells, allowing the virus to persist for years. Following changes in
the environmental conditions of the host, reactivation of the virus
can occur leading to viral transcription and production of new
infectious viruses</description>
        <go id="GO:0019042"/>
    </keyword>
    <keyword id="KW-1276">
        <name>Viral latency initiation and maintenance</name>
        <description>Viral protein expressed primarily to establish and maintain latency,
the part of the viral life cycle during which a virus lies dormant
(latent) within a cell. This part of the virus life cycle is called
the lysogenic part in prokaryotic viruses. During latency, the viral
genome can either exist as a provirus integrated in the host genome
(proviral latency) or as a linear or circular plasmid in the host cell
(episomal latency). The virus does not replicate, but is passively
duplicated when the host divides</description>
    </keyword>
    <keyword id="KW-1243">
        <name>Viral long flexible tail ejection system</name>
        <name>Viral genome injection via long noncontractile tail</name>
        <description>Viral protein that constitutes the noncontractile ejection system
carried by some long-tailed prokaryotic viruses such as the
Siphoviridae. This ejection system is composed at least of a
noncontractile tube and a tail tip which is able to penetrate the host
cell envelope to deliver the viral genome, and possibly some specific
proteins, into the cell cytoplasm. Proteins of the ejection apparatus
can play an active or a structural role in ejection</description>
        <go id="GO:0099001"/>
    </keyword>
    <keyword id="KW-0468">
        <name>Viral matrix protein</name>
        <description>Protein that organises and maintains virion structure. It usually
interacts directly with cellular membranes and is involved in the
budding process. In some enveloped RNA viruses, it acts as a bridge
between virion membrane and nucleocapsid</description>
        <go id="GO:0039660"/>
    </keyword>
    <keyword id="KW-0916">
        <name>Viral movement protein</name>
        <description>Plant viral protein that enables the viral nucleic acid to move
between adjacent plant cells via the plasmodesmata</description>
        <go id="GO:0046740"/>
    </keyword>
    <keyword id="KW-0543">
        <name>Viral nucleoprotein</name>
        <name>Viral nucleocapsid protein</name>
        <description>Viral protein conjugated with nucleic acid (DNA or RNA)</description>
        <go id="GO:0019013"/>
    </keyword>
    <keyword id="KW-0842">
        <name>Viral occlusion body</name>
        <description>Protein component of the viral occlusion body, a crystalline protein
matrix which surrounds the nucleocapsids of some insect viruses
(baculoviridae, entomopoxvirinae, cypovirus). Viral occlusion bodies
are produced either in the nucleus (baculoviridae) or in the cytoplasm
(poxvirinae and cypovirus) of the infected cells and confer resistance
to adverse environmental conditions on viruses. They are made from
polyhedrin (nucleopolyhedrovirus, cypovirus), granulin (granulovirus),
spheroidin and spherulin (entomopox-virinae) and are dissolved by the
alkaline pH of the insect gut, thus resulting in the release of
infectious virus particles</description>
        <go id="GO:0039679"/>
    </keyword>
    <keyword id="KW-1162">
        <name>Viral penetration into host cytoplasm</name>
        <name>Virion penetration into host cell</name>
        <name>Translocation of virus into host cell</name>
        <description>Viral protein involved in the entry of the entire virion, some of its
contents or at least its genetic material into the host cell
cytoplasm. Entry is achieved through pore formation, membrane fusion,
pilus retraction, ejection, permeabilization and/or endocytosis
mechanisms. Penetration reactions occur mainly in five locations: the
cell membrane, early and late endosomes, caveosomes, and the ER. In
prokaryotes, membrane fusion, pore formation through a puncturing
device, ejection, pilus retraction or permeabilization occur at the
plasma membrane, as well as at the outer membrane in prokaryotes with
2 membranes</description>
        <go id="GO:0046718"/>
    </keyword>
    <keyword id="KW-1241">
        <name>Viral penetration into host cytoplasm via pilus retraction</name>
        <description>Viral protein involved in the entry of the virion into the host
cytoplasm via the host pili, which are retractile filaments that
protrude from bacteria with 2 membranes (Gram-negative bacteria)
Entry of bound prokaryotic viruses such as filamentous viruses is
achieved through the retraction of host pilus and translocation of the
virion through the basis of the pilus to reach the host cytoplasm
Examples of bacteriophages which utilize the host cell pilus to
penetrate into host cytoplasm are bacteriophages M13, f1, fd, R17</description>
        <go id="GO:0039667"/>
    </keyword>
    <keyword id="KW-1163">
        <name>Viral penetration into host nucleus</name>
        <name>Entry of virus into host nucleus</name>
        <name>Virion penetration into host nucleus</name>
        <name>Virion entry into host nucleus</name>
        <description>Viral protein necessary for the penetration of the viral genome into
the host cell nucleus either via active nuclear transport through
nuclear pore complexes (NPCs) or DNA injection through the nuclear
membrane. Nuclear membrane permeabilization might also be possible
Viruses can also enter the nucleus during mitosis when the nuclear
membrane temporarily disintegrates (e.g. most retroviruses). All these
strategies to cross the nuclear envelope barrier are associated with
various levels of capsid disassembly, since virus can pass intact
(e.g. papovaviruses) or, in the case of injection, only the viral
genome enters the nucleus (e.g. herpesviruses)</description>
        <go id="GO:0075732"/>
    </keyword>
    <keyword id="KW-1174">
        <name>Viral penetration via lysis of host organellar membrane</name>
        <description>Viral membrane-lytic protein, usually associated with the viral capsid
or released through partial programmed disassembly of the capsid, that
induces major rupture of the bilayer integrity of host endosomal,
lysosomal, or caveosomal membrane to allow viral escape and
penetration into the cytoplasm. These viral lytic proteins may need to
be activated, mostly through endosomal acidic pH or receptor binding
to display membrane lytic activity. Viruses such as human adenoviruses
group C and D lyse the host endosomal membrane to penetrate into the
host cytoplasm</description>
        <go id="GO:0039664"/>
    </keyword>
    <keyword id="KW-1173">
        <name>Viral penetration via permeabilization of host membrane</name>
        <name>Viral penetration via perforation of host membrane by virus</name>
        <name>Viral penetration via host membrane disruption by virus</name>
        <description>Viral membrane-penetration protein, usually associated with the viral
capsid or released through partial programmed disassembly of the
capsid, that locally permeabilizes the bilayer of a host membrane to
allow virion penetration into the cytoplasm. Viral membrane-
penetration proteins often need to be activated, mostly through
endosomal acidic pH or receptor binding to display their membrane
penetrating activity. Non-enveloped viruses such as parvovirus, human
reovirus, BDV, BTV, rotavirus, papillomavirus, Flock house virus
permeabilize the host endosomal membrane to penetrate the host
cytoplasm</description>
        <go id="GO:0140267"/>
    </keyword>
    <keyword id="KW-1181">
        <name>Viral primary envelope fusion with host outer nuclear membrane</name>
        <description>Viral protein implicated in fusion of the herpesviruses' primary
envelope with the host outer nuclear membrane during egress. During
egress, herpesviruses acquire a transitory, primary envelope as they
bud at the inner nuclear membrane and gain access to the perinuclear
space. This membrane is lost by fusing with the outer nuclear membrane
during nuclear exit</description>
        <go id="GO:0039700"/>
    </keyword>
    <keyword id="KW-1272">
        <name>Viral reactivation from latency</name>
        <name>Release from viral latency</name>
        <description>Viral protein involved in virus reactivation from latency to
replication, thereby putting an end to the latency phase in the viral
life cycle. Changes in the environmental conditions of the host often
reactivate the virus leading to viral transcription and production of
new infectious viruses (productive infection)</description>
        <go id="GO:0019046"/>
    </keyword>
    <keyword id="KW-1264">
        <name>Viral receptor tropism switching</name>
        <description>A switch in the host range specificity occurs in some bacterial
viruses through massive sequence variation of their host-binding
receptor. Sequence variation can be induced by site-specific inversion
of a DNA segment in their genome or by a diversity-generating
retroelement. Inversion is catalyzed by a specific recombinase called
invertase and consists of a reciprocal recombination event within two
inverted repeats present in the viral genome that leads to the
alternate expression of two different sets of genes involved in tail
fiber biosynthesis. Mu-like viruses and P1-like viruses, for example,
encode a recombinase responsible for the switch in the targeted host
Diversity-generating retroelements (DGR) like in BPP-1 virus also
allow tropism switching by creating a mutant copy of an invariant DNA
template repeat by transcription and reverse transcription and
introducing this mutated sequence in the receptor-binding protein
sequence</description>
        <go id="GO:0098678"/>
    </keyword>
    <keyword id="KW-1188">
        <name>Viral release from host cell</name>
        <description>Viral protein involved in the release of virions from an infected cell
to allow cell-to-cell spread of virus. Once assembled at the
replication site, viral particles can be released by budding,
exocytosis, extrusion or host cell lysis. Some viruses also mediate
direct transport of their viral genome to adjacent cells thanks to
movement proteins</description>
        <go id="GO:0019076"/>
    </keyword>
    <keyword id="KW-0693">
        <name>Viral RNA replication</name>
        <description>Viral protein involved in the SYnthesis of multiple copies of the
viral RNA genome. The replicated genomes provide support for further
viral transcription or are assembled into progeny virions</description>
        <go id="GO:0039694"/>
    </keyword>
    <keyword id="KW-1244">
        <name>Viral short tail ejection system</name>
        <name>Viral genome injection via short noncontractile tail</name>
        <description>Virion protein that constitutes the noncontractile ejection system
carried by some short-tailed prokaryotic viruses such as some
Podoviridae. This ejection system is composed at least of the tail
tube and ejection proteins. Upon receptor binding, proteins located
inside the capsid (head) rearrange to extend the tail tube, creating a
channel spanning the periplasmic space. This hydrophilic channel
directs the viral genome, and possibly some specific proteins, into
the cytoplasm and protects it from periplasmic nucleases. Once the
viral genome is in the host cytoplasm, the channel collapses and
seals. Bacteriophage T7 for example expresses ejection proteins that
partition into the host outer and cytoplasmic membranes and allow
transport of viral DNA across the host envelope. Proteins of the
ejection apparatus can play an active or a structural role in
ejection</description>
        <go id="GO:0099002"/>
    </keyword>
    <keyword id="KW-1245">
        <name>Viral tail assembly</name>
        <description>Viral protein involved in tail assembly. Some tailed bacteriophages
need chaperones that help with the assembly of their tail</description>
        <go id="GO:0098003"/>
    </keyword>
    <keyword id="KW-1246">
        <name>Viral tail fiber assembly</name>
        <description>Viral protein involved in tail fibers or spike assembly. Some tailed
bacteriophages need chaperones that help with the assembly of their
fibers or spikes. T4 for example encodes a general tail fiber
chaperone that is needed for the correct assembly of the short and
long tail fiber proteins</description>
        <go id="GO:0098004"/>
    </keyword>
    <keyword id="KW-1230">
        <name>Viral tail fiber protein</name>
        <description>Viral fibrous protein part of the virion fiber, which is a thin long
rod like structure, unique or multiple, appended to the tail of
prokaryotic viruses and used for attachment to the host cell. Shorter
appendages are called tail spikes (e.g. Podoviridae) or whiskers</description>
        <go id="GO:0098024"/>
    </keyword>
    <keyword id="KW-1227">
        <name>Viral tail protein</name>
        <description>Viral protein part of the virion tail of prokaryotic viruses such as
Caudovirales. The tail is usually composed of a tube, a tail sheath
when contractile, a base plate or tip and tail long or short fibers</description>
        <go id="GO:0098015"/>
    </keyword>
    <keyword id="KW-1229">
        <name>Viral tail sheath protein</name>
        <description>Viral protein part of the virion tail sheath of prokaryotic viruses
The tail sheath is an external contractile envelope wrapping the tail
tube in some viruses (e.g. Myoviridae)</description>
        <go id="GO:0098027"/>
    </keyword>
    <keyword id="KW-1228">
        <name>Viral tail tube protein</name>
        <description>Viral protein part of the virion tail tube of prokaryotic viruses such
as Caudovirales. The tail tube is the channel for DNA ejection into
the host cytoplasm and can be wrapped in an external contractile
envelope in some viruses (e.g. Myoviridae). Also called tail shaft in
some Siphoviridae</description>
        <go id="GO:0098026"/>
    </keyword>
    <keyword id="KW-1195">
        <name>Viral transcription</name>
        <description>Viral Protein involved in the synthesis of messenger RNAs. The process
can occur in the host cell nucleus or cytoplasm, and the genomic
template can be viral DNA or RNA, single- or double-stranded</description>
        <go id="GO:0019083"/>
    </keyword>
    <keyword id="KW-0946">
        <name>Virion</name>
        <description>Viral protein detected in the virion</description>
        <go id="GO:0044423"/>
    </keyword>
    <keyword id="KW-0917">
        <name>Virion maturation</name>
        <name>Viral procapsid maturation</name>
        <description>Viral protein involved in the maturation of the immature virion into
the mature virion, once the virion has been released from the host
cell. Maturation usually involves proteolysis events and changes in
the folding of the virion proteins</description>
        <go id="GO:0019075"/>
    </keyword>
    <keyword id="KW-0920">
        <name>Virion tegument</name>
        <description>Viral structural protein of the tegument, a protein structure that
resides between the capsid and envelope of herpesviruses and which
appears amorphous in electron micrographs</description>
    </keyword>
    <keyword id="KW-0843">
        <name>Virulence</name>
        <description>Protein involved in virulence, the degree of pathogenicity within a
group or species of microorganisms or viruses, as indicated by case
fatality rates and/or the ability of the organism to invade the
tissues of the host. In some cases, the virulence factor can be borne
by another organism in symbiosis with the one whose virulence is
increased. Some prokaryotic viruses/proviruses for example bear
exotoxins that increase the virulence of their host. A well-known
bacterial exotoxin encoded by a provirus is the diphtheria toxin</description>
    </keyword>
    <keyword id="KW-1164">
        <name>Virus endocytosis by host</name>
        <description>Viral protein involved in virus internalization by the host cell via
endocytosis. Endocytosis can occur via: clathrin-mediated endocytosis,
caveolin-mediated endocytosis or clathrin- and caveolae-independent
endocytosis</description>
        <go id="GO:0075509"/>
    </keyword>
    <keyword id="KW-1160">
        <name>Virus entry into host cell</name>
        <description>Viral protein involved in the virion entry into a host cell. Entry is
a multistep process that mostly requires binding to the target cell,
penetration into the host cell cytoplasm, intracellular transport of
viral components and genome release to the replication site of the
virus</description>
        <go id="GO:0046718"/>
    </keyword>
    <keyword id="KW-0844">
        <name>Vision</name>
        <description>Protein involved in vision, the special sense by which objects in the
external environment are perceived by the light they give off or
reflect, which stimulates the photoreceptors in the retina</description>
        <go id="GO:0007601"/>
    </keyword>
    <keyword id="KW-0845">
        <name>Vitamin A</name>
        <name>Retinol</name>
        <description>Protein which interacts with any form of the fat-soluble vitamin A
There are three active forms of vitamin A: retinol, retinal
(retinaldehyde) and retinoic acid, which are all derived from the
plant beta-carotene (provitamin A). Vitamin A is essential to night
vision and is also required for epithelium differentiation, bone
development, reproduction and the immune response. Symptoms associated
with a deficiency of vitamin A are night blindness, changes in the
eyes, poor bone development, weak tooth enamel and dry skin</description>
        <go id="GO:0016918"/>
    </keyword>
    <keyword id="KW-0847">
        <name>Vitamin C</name>
        <name>Ascorbic acid</name>
        <description>Protein which contains at least one vitamin C as cofactor. This water-
soluble vitamin is a reducing agent in a number of reactions. As
cofactor, it is required for the hydroxylation of proline residues in
collagen, and in many other metabolic reactions such as in the
catabolism of tyrosine and the synthesis of bile acids. Deficiency in
vitamin C leads to the disease scurvy</description>
        <go id="GO:0031418"/>
    </keyword>
    <keyword id="KW-0848">
        <name>Vitamin D</name>
        <description>Protein which interacts with any form of the fat-soluble vitamin D or
protein whose transcription is regulated by the biologically active
form of vitamin D, i.e. 1,25-dihydroxy vitamin D3 (1,25
dihydroxycholecalciferol) also termed calcitriol. Active calcitriol is
derived from ergosterol (produced in plants) and 7-dehydrocholesterol
(produced in the skin). Ergocalciferol (vitamin D2) and
cholecalciferol (vitamin D3) are formed by UV irradiation of
ergosterol and 7-dehydrocholesterol, respectively, and processed by
the same enzymatic pathway in the body to D2-calcitriol and D3-
calcitriol. Deficiency in vitamin D leads to the disease rickets, in
children, and osteomalacia, in adults</description>
        <go id="GO:0005499"/>
    </keyword>
    <keyword id="KW-0850">
        <name>VLDL</name>
        <description>Protein present in particles of Very Low-Density Lipoproteins or
protein which interacts with them. VLDL are composed of 50%
triacylglycerols, 12% cholesteryl esters, 7% free cholesterol, 18%
phospholipids, and 10% proteins including apoB-100, apoC-I, apoC-II,
apoC-III and apoE. Excess fatty acids or carbohydrate in the diet can
be converted into triacylglycerols in the liver and packaged into
VLDL. These lipoproteins are transported by the blood to muscle and
adipose tissue, where activation of lipoprotein lipase by apoC-II
causes the release of free fatty acids from the triacylglycerols of
the VLDL</description>
        <go id="GO:0034361"/>
    </keyword>
    <keyword id="KW-1218">
        <name>Voltage-gated calcium channel impairing toxin</name>
        <name>Cav channel inhibitor</name>
        <description>Protein which interferes with the function of voltage-gated calcium
channels (Cav) which are membrane proteins forming a channel in a
biological membrane selectively permeable to calcium ions and open in
response to a change in membrane potential. They are mostly found
spider and cone snail venoms</description>
    </keyword>
    <keyword id="KW-0851">
        <name>Voltage-gated channel</name>
        <name>Voltage-gated ion channel</name>
        <name>Voltage-gated cation channel</name>
        <description>Protein which is a component of a voltage-gated channel. Voltage-gated
ion channels are responsible for the electrical activity in a variety
of cell types. They probably exist in all life forms</description>
        <go id="GO:0034220"/>
        <go id="GO:0034702"/>
    </keyword>
    <keyword id="KW-0870">
        <name>Voltage-gated chloride channel impairing toxin</name>
        <description>Protein which interferes with the function of voltage-gated chloride
channels (ClC) which are membrane proteins forming a channel in a
biological membrane selectively permeable to chloride ions, and open
in response to a change in membrane potential. They are found in
venoms from scorpions</description>
        <go id="GO:0017081"/>
    </keyword>
    <keyword id="KW-1220">
        <name>Voltage-gated potassium channel impairing toxin</name>
        <description>Protein which interferes with the function of voltage-gated potassium
channels (Kv) which are membrane proteins forming a channel in a
biological membrane selectively permeable to potassium ions and open
in response to a change in membrane potential. They are mostly found
in scorpion and spider venoms</description>
    </keyword>
    <keyword id="KW-0738">
        <name>Voltage-gated sodium channel impairing toxin</name>
        <description>Protein which interferes with the function of voltage-gated sodium
channels (Nav) which are membrane proteins forming a channel in a
biological membrane selectively permeable to sodium ions, and open in
response to a change in membrane potential. They are found in various
venoms from snakes, scorpions and spiders</description>
        <go id="GO:0017080"/>
    </keyword>
    <keyword id="KW-0852">
        <name>von Willebrand disease</name>
        <description>Protein which, if defective, causes von Willebrand disease, a
hemorrhagic disorder in which the von Willebrand factor is either
quantitatively or qualitatively abnormal. Usually inherited as an
autosomal dominant trait though rare kindreds are autosomal recessive
Symptoms vary depending on severity and disease type but may include
prolonged bleeding time, deficiency of factor VIII and impaired
platelet adhesion</description>
    </keyword>
    <keyword id="KW-0897">
        <name>Waardenburg syndrome</name>
        <name>WS</name>
        <description>Protein which, if defective, causes Waardenburg syndrome, an autosomal
dominant disorder, characterized by sensorineural deafness associated
with pigmentary changes of the irides, hair and skin; each of these
features may be uni- or bilateral. On the basis of the presence or
absence of dystopia canthorum (lateral displacement of the inner
corner of the eye), Waardenburg syndrome type 1 (WS1) and type 2 (WS2)
are distinguished. Additionally, the association of WS1 with limb
anomalies defines Waardenburg syndrome type 3 (WS3), while the
association of Waardenburg features with Hirschsprung disease defines
Waardenburg syndrome type 4 (WS4)</description>
    </keyword>
    <keyword id="KW-0853">
        <name>WD repeat</name>
        <name>WD-40 repeat</name>
        <name>Trp-Asp repeat</name>
        <description>Protein which contains at least one WD repeat, a conserved domain of
about 40 amino acids in length. Most copies contain a central
conserved Trp-Asp motif</description>
    </keyword>
    <keyword id="KW-0855">
        <name>Whooping cough</name>
        <description>Protein involved in the induction of whooping cough, a respiratory
infection caused by the very small Gram-negative aerobic coccobacillus
Bordetella pertussis. It is characterized by paroxysmal coughing often
ending in a characteristic inspiratory gasp (whoop). The bacterium is
a pathogen for humans and possibly for higher primates</description>
    </keyword>
    <keyword id="KW-0856">
        <name>Williams-Beuren syndrome</name>
        <name>WBS</name>
        <description>Protein which, if defective, causes Williams-Beuren syndrome (WBS), a
contiguous gene deletion syndrome involving genes from chromosome band
7q11.23. It is a rare developmental autosomal dominant disorder
characterized by cardiovascular abnormalities, elfin face, mental and
statural deficiency, characteristic dental malformation, and infantile
hypercalcemia</description>
    </keyword>
    <keyword id="KW-0879">
        <name>Wnt signaling pathway</name>
        <name>Wnt signalling pathway</name>
        <name>Wnt signaling cascade</name>
        <name>Wnt signal transduction pathway</name>
        <description>Protein involved in the Wnt signaling pathway. Wnts are a large family
of cysteine-rich secreted glycoproteins that control development in
organisms ranging from nematodes to mammals. Wnt genes are defined by
sequence homology to the original members of the family, Wnt1 in the
mouse and wingless (wg) in Drosophila. Wnt signaling is a very complex
pathway which includes numerous ligands, receptors and transcriptional
effectors. There is a well-characterized canonical pathway as well as
diverse, less-characterized noncanonical pathways. Several components
of Wnt signaling are implicated in the genesis of human cancer</description>
        <go id="GO:0016055"/>
    </keyword>
    <keyword id="KW-0857">
        <name>Xeroderma pigmentosum</name>
        <description>Protein which, if defective, causes xeroderma pigmentosum, an
autosomal recessive disease characterized by extreme photosensitivity
to ultraviolet light and the development of multiple skin cancers</description>
    </keyword>
    <keyword id="KW-0858">
        <name>Xylan degradation</name>
        <name>Xylan hydrolysis</name>
        <description>Protein involved in the hydrolysis of xylan to xylose and other
sugars. Xylan is a major component of hemicellulose, which is the
second most common plant material in nature. The structures of xylans
are complex, and several enzymes are involved in their breakdown
Xylan degrading enzymes are produced by a variety of microorganisms</description>
        <go id="GO:0045493"/>
    </keyword>
    <keyword id="KW-0859">
        <name>Xylose metabolism</name>
        <description>Protein involved in the biochemical reactions with the 5-carbon sugars
xylose or xylulose. Xylose is the second most abundant sugar found in
hardwood and agricultural residues</description>
        <go id="GO:0042732"/>
    </keyword>
    <keyword id="KW-0861">
        <name>Zellweger syndrome</name>
        <name>ZWS</name>
        <name>Cerebrohepatorenal syndrome</name>
        <name>CHR syndrome</name>
        <name>Cerebro-hepato-renal syndrome</name>
        <description>Protein which, if defective, causes Zellweger syndrome, a fatal
peroxisome biogenesis disorder associated with severe abnormalities in
the brain, liver and kidney and death soon after birth. This disease
is characterized by the presence of empty peroxisomes in the cells due
to impaired transport of peroxisomal proteins into the peroxisomes</description>
    </keyword>
    <keyword id="KW-0862">
        <name>Zinc</name>
        <description>Protein which binds at least one zinc atom, or protein whose function
is zinc-dependent. Zinc is a metallic trace element, chemical symbol
Zn</description>
    </keyword>
    <keyword id="KW-0864">
        <name>Zinc transport</name>
        <description>Protein involved in the transport of zinc</description>
        <go id="GO:0006829"/>
    </keyword>
    <keyword id="KW-0863">
        <name>Zinc-finger</name>
        <description>Protein which contains at least one zinc finger. A small, functional,
independently folded domain that requires coordination of one or more
zinc ions to stabilize its structure. Zinc fingers vary widely in
structure, as well as in function, which ranges from DNA or RNA
binding to protein-protein interactions and membrane association</description>
        <go id="GO:0008270"/>
    </keyword>
    <keyword id="KW-0865">
        <name>Zymogen</name>
        <name>Proenzyme</name>
        <description>The enzymatically inactive precursor of mostly proteolytic enzymes</description>
    </keyword>
</keywordList>
