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        UniProt Knowledgebase:
          Swiss-Prot Protein Knowledgebase
          TrEMBL Protein Database
        SIB Swiss Institute of Bioinformatics; Geneva, Switzerland
        European Bioinformatics Institute (EBI); Hinxton, United Kingdom
        Protein Information Resource (PIR); Washington DC, USA
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Description: Controlled vocabulary of keywords
Name:        keywlist.txt
Release:     2024_02 of 27-Mar-2024

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  This document lists the keywords and categories used in the UniProt
  knowledgebase (Swiss-Prot and TrEMBL). The keywords are classified into
  the following 10 categories:

    * Biological process
    * Cellular component
    * Coding sequence diversity
    * Developmental stage
    * Disease
    * Domain
    * Ligand
    * Molecular function
    * PTM
    * Technical term

  The definition of the keywords and categories usage as well as other
  information is provided in the following format:

  ---------  ---------------------------     ------------------------------
  Line code  Content                         Occurrence in an entry
  ---------  ---------------------------     ------------------------------
  ID         Identifier (keyword)            Once; starts a keyword entry
  IC         Identifier (category)           Once; starts a category entry
  AC         Accession (KW-xxxx)             Once
  DE         Definition                      Once or more
  SY         Synonyms                        Optional; once or more
  GO         Gene ontology (GO) mapping      Optional; once or more
  HI         Hierarchy                       Optional; once or more
  WW         Relevant WWW site               Optional; once or more
  CA         Category                        Once per keyword entry;
                                             absent in category entries
  //         Terminator                      Once; ends an entry

___________________________________________________________________________
ID   2Fe-2S.
AC   KW-0001
DE   Protein which contains at least one 2Fe-2S iron-sulfur cluster: 2 iron
DE   atoms complexed to 2 inorganic sulfides and 4 sulfur atoms of
DE   cysteines from the protein.
SY   [2Fe-2S] cluster; [Fe2S2] cluster; 2 iron, 2 sulfur cluster binding;
SY   Di-mu-sulfido-diiron; Fe2/S2 (inorganic) cluster; Fe2S2.
GO   GO:0051537; 2 iron, 2 sulfur cluster binding
HI   Ligand: Iron; Iron-sulfur; 2Fe-2S.
HI   Ligand: Metal-binding; Iron-sulfur; 2Fe-2S.
HI   Ligand: Metal-binding; 2Fe-2S.
CA   Ligand.
//
ID   3D-structure.
AC   KW-0002
DE   Protein, or part of a protein, whose three-dimensional structure has
DE   been resolved experimentally (for example by X-ray crystallography or
DE   NMR spectroscopy) and whose coordinates are available in the PDB
DE   database. Can also be used for theoretical models.
HI   Technical term: 3D-structure.
CA   Technical term.
//
ID   3Fe-4S.
AC   KW-0003
DE   Protein which contains at least one 3Fe-4S iron-sulfur cluster: 3 iron
DE   atoms complexed to 4 inorganic sulfides and 3 sulfur atoms of
DE   cysteines from the protein. In a number of iron-sulfur proteins, the
DE   4Fe-4S cluster can be reversibly converted by oxidation and loss of
DE   one iron ion to a 3Fe-4S cluster.
GO   GO:0051538; 3 iron, 4 sulfur cluster binding
HI   Ligand: Iron; Iron-sulfur; 3Fe-4S.
HI   Ligand: Metal-binding; Iron-sulfur; 3Fe-4S.
HI   Ligand: Metal-binding; 3Fe-4S.
CA   Ligand.
//
ID   4Fe-4S.
AC   KW-0004
DE   Protein which contains at least one 4Fe-4S iron-sulfur cluster: 4 iron
DE   atoms complexed to 4 inorganic sulfides and 4 sulfur atoms of
DE   cysteines from the protein. In a number of iron-sulfur proteins, the
DE   4Fe-4S cluster can be reversibly converted by oxidation and loss of
DE   one iron ion to a 3Fe-4S cluster.
GO   GO:0051539; 4 iron, 4 sulfur cluster binding
HI   Ligand: Iron; Iron-sulfur; 4Fe-4S.
HI   Ligand: Metal-binding; Iron-sulfur; 4Fe-4S.
HI   Ligand: Metal-binding; 4Fe-4S.
CA   Ligand.
//
ID   Abscisic acid biosynthesis.
AC   KW-0937
DE   Protein involved in the synthesis of abscisic acid (ABA) (5-(1-
DE   hydroxy-2,6,6,trimethyl-4-oxocyclohex-2-en-1-y1)-3-methylpenta-2,4-
DE   dienoic acid). ABA is a plant hormone which play a role in many
DE   aspects of plant growth, development and cellular signaling (e.g. seed
DE   dormancy, seed maturation, vegetative growth and responses to various
DE   environmental stimuli such as stomatal closure during drought). This
DE   phytohormone can be synthesized from farnesyl diphosphate (direct C15
DE   pathway) or from 9-cis-violaxanthine (indirect C40 pathway).
SY   ABA anabolism; ABA biosynthesis; ABA formation; ABA synthesis;
SY   Abscisic acid anabolism; Abscisic acid biosynthetic process;
SY   Abscisic acid formation; Abscisic acid synthesis.
GO   GO:0009688; abscisic acid biosynthetic process
HI   Biological process: Abscisic acid biosynthesis.
CA   Biological process.
//
ID   Abscisic acid signaling pathway.
AC   KW-0938
DE   Protein involved in the abscisic acid (ABA) (5-(1-hydroxy-
DE   2,6,6,trimethyl-4-oxocyclohex-2-en-1-y1)-3-methylpenta-2,4-dienoic
DE   acid) signaling pathway (e.g. transport and signal transduction) that
DE   regulates many aspects of plant growth, development and cellular
DE   signaling (e.g. seed dormancy, seed maturation, vegetative growth and
DE   responses to various environmental stimuli such as stomatal closure
DE   during drought). This phytohormone can be synthesized from farnesyl
DE   diphosphate (direct C15 pathway) or from 9-cis-violaxanthine (indirect
DE   C40 pathway).
SY   ABA mediated signaling; ABA signaling pathway;
SY   Abscisic acid mediated signaling.
GO   GO:0009738; abscisic acid-activated signaling pathway
HI   Biological process: Abscisic acid signaling pathway.
CA   Biological process.
//
ID   Acetoin biosynthesis.
AC   KW-0005
DE   Protein involved in the synthesis of acetoin (3-hydroxy-2-butanone).
DE   Acetoin is a component of the butanediol cycle (butanediol
DE   fermentation) in microorganisms.
SY   3-hydroxy-2-butanone anabolism; 3-hydroxy-2-butanone biosynthesis;
SY   3-hydroxy-2-butanone biosynthetic process;
SY   3-hydroxy-2-butanone formation; 3-hydroxy-2-butanone synthesis;
SY   Acetoin anabolism; Acetoin biosynthetic process; Acetoin formation;
SY   Acetoin synthesis.
GO   GO:0045151; acetoin biosynthetic process
HI   Biological process: Acetoin biosynthesis.
CA   Biological process.
//
ID   Acetoin catabolism.
AC   KW-0006
DE   Protein involved in the degradation of acetoin (3-hydroxy-2-butanone).
DE   Acetoin is a component of the butanediol cycle (butanediol
DE   fermentation) in microorganisms.
SY   3-hydroxy-2-butanone breakdown;
SY   3-hydroxy-2-butanone catabolic process;
SY   3-hydroxy-2-butanone catabolism; 3-hydroxy-2-butanone degradation;
SY   Acetoin breakdown; Acetoin catabolic process; Acetoin degradation.
GO   GO:0045150; acetoin catabolic process
HI   Biological process: Acetoin catabolism.
CA   Biological process.
//
ID   Acetylation.
AC   KW-0007
DE   Protein which is posttranslationally modified by the attachment of at
DE   least one acetyl group; generally at the N-terminus.
SY   Acetylated; N-acetylated.
HI   PTM: Acetylation.
CA   PTM.
//
ID   Acetylcholine receptor inhibiting toxin.
AC   KW-0008
DE   Toxin which interferes with the function of the nicotinic
DE   acetylcholine receptor (nAChR). The nAChR is a postsynaptic membrane
DE   protein that undergoes an extensive conformational change upon binding
DE   to acetylcholine, leading to opening of an ion-conducting channel
DE   across the plasma membrane. These toxins are mostly found in snake and
DE   cone snail venoms.
SY   nAChR inhibitor; Nicotinic AChR inhibitor.
GO   GO:0030550; acetylcholine receptor inhibitor activity
HI   Molecular function: Toxin; Neurotoxin; Postsynaptic neurotoxin; Acetylcholine receptor inhibiting toxin.
CA   Molecular function.
//
ID   Actin capping.
AC   KW-0117
DE   Protein that binds to the free end of the actin filament and thereby
DE   blocks further addition of subunits.
SY   Actin filament capping; F-actin capping.
GO   GO:0051693; actin filament capping
HI   Molecular function: Actin capping.
CA   Molecular function.
//
ID   Actin-binding.
AC   KW-0009
DE   Protein which binds to actin, and thereby can modulate the properties
DE   and/or functions of the actin filament.
SY   Actin filament binding.
GO   GO:0003779; actin binding
HI   Molecular function: Actin-binding.
CA   Molecular function.
//
ID   Actin-dependent inwards viral transport.
AC   KW-1178
DE   Viral protein that allows the active transport of viral material along
DE   actin filaments toward the intracellular replication sites during
DE   virus entry. This transport probably involves motor proteins like
DE   myosins or polymerization/depolymerization reactions as a driving
DE   force. Viruses such as poliovirus may utilize this type of
DE   intracellular transport.
GO   GO:0039680; actin-dependent intracellular transport of virus towards nucleus
HI   Biological process: Virus entry into host cell; Cytoplasmic inwards viral transport; Actin-dependent inwards viral transport.
CA   Biological process.
//
ID   Activation of host autophagy by virus.
AC   KW-1072
DE   Viral protein involved in the activation of host autophagy. Autophagy
DE   is a major intracellular pathway in the delivery of cytoplasmic
DE   material to lysosomes for degradation. It is also essential for the
DE   removal of pathogenic protein aggregates from the cell during
DE   infection. Although autophagy is clearly important for antiviral
DE   immune response, it can also be activated by viruses and serves as
DE   platform for viral replication. Some viruses such as poliovirus, use
DE   the autophagic pathway as a nonlytic mechanism for viral release.
GO   GO:0039520; induction by virus of host autophagy
HI   Biological process: Host-virus interaction; Activation of host autophagy by virus.
CA   Biological process.
//
ID   Activation of host caspases by virus.
AC   KW-1073
DE   Viral protein involved in the activation of host cell apoptosis by
DE   acting on host caspases. While many viruses encode protein that
DE   inhibit apoptosis, viruses can also use apoptosis to their advantage
DE   to suppress immune response or to disseminate. Therefore, some viral
DE   proteins are able to cleave or activate caspases in order to promote
DE   apoptosis.
GO   GO:0019051; induction by virus of host apoptotic process
HI   Biological process: Host-virus interaction; Modulation of host cell apoptosis by virus; Activation of host caspases by virus.
CA   Biological process.
//
ID   Activation of host NF-kappa-B by virus.
AC   KW-1074
DE   Viral protein involved in the activation of host NF-kappa-B. This
DE   protein is a pleiotropic transcription factor which is present in
DE   almost all cell types and is involved in many biological processed
DE   such as inflammation, immunity, differentiation, cell growth,
DE   tumorigenesis and apoptosis. Several viruses have developed strategies
DE   to activate the NF-kappa-B pathway in order to promote viral
DE   replication and prevent virus-induced apoptosis.
GO   GO:0039652; induction by virus of host NF-kappaB cascade
HI   Biological process: Host-virus interaction; Activation of host NF-kappa-B by virus.
CA   Biological process.
//
ID   Activator.
AC   KW-0010
DE   Protein that positively regulates either the transcription of one or
DE   more genes, or the translation of mRNA.
SY   Positive activator.
HI   Molecular function: Activator.
CA   Molecular function.
//
ID   Acute phase.
AC   KW-0011
DE   Protein involved in acute phase, a response of the vertebrate body to
DE   insults, infections, immunological reactions or inflammatory
DE   processes; characterised by redness (rubor), heat (calor), swelling
DE   (tumor), pain (dolor) and sometimes loss of function.
SY   Acute-phase reaction; Acute-phase response.
GO   GO:0006953; acute-phase response
HI   Biological process: Acute phase.
CA   Biological process.
//
ID   Acyltransferase.
AC   KW-0012
DE   Enzyme catalyzing the transfer of acyl- (RCO-) groups.
GO   GO:0016746; acyltransferase activity
HI   Molecular function: Transferase; Acyltransferase.
CA   Molecular function.
//
ID   Adaptive immunity.
AC   KW-1064
DE   Protein involved in adaptive immunity. Vertebrates can develop a broad
DE   and almost infinite repertoire of antigen-specific receptors, which
DE   allows vertebrates to recognize almost any potential pathogen or toxin
DE   and to mount antigen-specific responses to it. Two types of adaptive
DE   immunity systems have evolved in vertebrates in order to generate
DE   immune receptor diversity. The jawed vertebrates strategy uses the
DE   V(D)JC recombination to achieve combinatorial diversity of
DE   immunoglobulin-based B cell receptors and T cell receptors. The
DE   jawless vertebrate strategy uses the somatic rearrangements of
DE   variable leucine-rich cassettes in the variable lymphocyte receptors
DE   (VLRs). The hallmarks of an adaptive immune system is the production
DE   of antigen-specific recognition receptor by somatic gene
DE   rearrangement. The long life of some antigen-primed cytotoxic
DE   lymphocytes and plasma cells provide protective memory to prevent
DE   reinvasion.
SY   Acquired immunity.
GO   GO:0002250; adaptive immune response
HI   Biological process: Immunity; Adaptive immunity.
WW   https://www.nature.com/articles/nri2686
CA   Biological process.
//
ID   ADP-ribosylation.
AC   KW-0013
DE   Protein which is posttranslationally modified by the attachment of at
DE   least one ADP-ribosyl group.
SY   Adenosinediphospho-ribosylation; ADP-ribosylated.
HI   PTM: ADP-ribosylation.
CA   PTM.
//
ID   Age-related macular degeneration.
AC   KW-0913
DE   Protein which, if defective, causes age-related macular degeneration
DE   (ARMD), the most common cause of irreversible vision loss in the
DE   developed world. In most patients, the disease is manifest as
DE   ophthalmoscopically visible yellowish accumulations of protein and
DE   lipid (known as drusen) that lie beneath the retinal pigment
DE   epithelium and within an elastin-containing structure known as Bruch's
DE   membrane. ARMD is likely to be a mechanistically heterogeneous group
DE   of disorders, and the specific disease mechanisms that underlie the
DE   vast majority of cases are currently unknown. However, a number of
DE   studies have suggested that both genetic and environmental factors are
DE   likely to play a role.
SY   ARMD.
HI   Disease: Age-related macular degeneration.
CA   Disease.
//
ID   Aicardi-Goutieres syndrome.
AC   KW-0948
DE   Protein which, if defective, causes Aicardi-Goutieres syndrome, a
DE   genetic disorder that is phenotypically similar to in utero viral
DE   infection. The disease is characterized by severe neurological
DE   dysfunction in infancy, leading to progressive microcephaly,
DE   spasticity, dystonic posturing, profound psychomotor retardation and
DE   often death in early childhood.
SY   AGS; Cree encephalitis; Pseudo-torch syndrome;
SY   Pseudotoxoplasmosis syndrome.
HI   Disease: Aicardi-Goutieres syndrome.
CA   Disease.
//
ID   AIDS.
AC   KW-0014
DE   Protein encoded by the human immunodeficiency viruses HIV-1 or HIV-2,
DE   which are the cause of acquired immunodeficiency syndrome (AIDS). This
DE   disease is characterized by a severe defect of cell-mediated immunity
DE   which is often accompanied by cancers such as Kaposi's sarcoma, as
DE   well as secondary infections such as tuberculosis.
SY   Acquired immunodeficiency syndrome.
HI   Disease: AIDS.
CA   Disease.
//
ID   Albinism.
AC   KW-0015
DE   Protein which, if defective, causes albinism, a genetically determined
DE   or environmentally induced absence of pigmentation in animals normally
DE   pigmented. This can lead for example to lack of pigmentation in hair,
DE   skin and eyes.
HI   Disease: Albinism.
CA   Disease.
//
ID   Alginate biosynthesis.
AC   KW-0016
DE   Protein involved in the synthesis of alginate. Alginate is an
DE   exopolysaccharide in the cell walls of brown algae and in the capsular
DE   material of certain strains of Pseudomonas and Azotobacter, in which
DE   it provides a protective barrier against host immune defenses and
DE   antibiotics.
SY   Alginate anabolism; Alginate formation; Alginate synthesis;
SY   Alginic acid anabolism; Alginic acid biosynthesis;
SY   Alginic acid formation; Alginic acid synthesis.
GO   GO:0042121; alginic acid biosynthetic process
HI   Biological process: Alginate biosynthesis.
CA   Biological process.
//
ID   Alkaloid metabolism.
AC   KW-0017
DE   Protein involved in a biochemical reaction with alkaloids, a group of
DE   nitrogenous organic molecules (mostly heterocyclic) usually found in
DE   plants. Various alkaloids have toxic or medical properties, such as
DE   caffeine, morphine and nicotine.
SY   Alkaloid metabolic process.
GO   GO:0009820; alkaloid metabolic process
HI   Biological process: Alkaloid metabolism.
CA   Biological process.
//
ID   Alkylphosphonate uptake.
AC   KW-0019
DE   Protein involved in alkylphosphonate uptake. Certain bacteria such as
DE   Escherichia coli can use alkylphosphonates as a phosphorus source.
GO   GO:0015716; organic phosphonate transport
HI   Biological process: Alkylphosphonate uptake.
CA   Biological process.
//
ID   Allergen.
AC   KW-0020
DE   Protein that stimulates the production of, and reacts with, antibodies
DE   (IgE) thus creating an allergic reaction (immediate-type
DE   hypersensitivity). Examples are pollen allergens from plants, venom
DE   allergens from insects, dust-mite allergens, and animal hair
DE   allergens.
HI   Disease: Allergen.
CA   Disease.
//
ID   Allosteric enzyme.
AC   KW-0021
DE   Enzyme whose activity is modified by the noncovalent binding of an
DE   allosteric effector at a site other than the active site. This binding
DE   mediates conformational changes, altering its catalytic or binding
DE   properties.
GO   GO:0003824; catalytic activity
GO   GO:0008152; metabolic process
HI   Molecular function: Allosteric enzyme.
CA   Molecular function.
//
ID   Alpha-amylase inhibitor.
AC   KW-0022
DE   Protein that inhibits alpha-amylase, an enzyme that catalyzes the
DE   endohydrolysis of 1,4-alpha-glucosidic linkages in oligosaccharides
DE   and polysaccharides.
GO   GO:0015066; alpha-amylase inhibitor activity
HI   Molecular function: Alpha-amylase inhibitor.
CA   Molecular function.
//
ID   Alport syndrome.
AC   KW-0023
DE   Protein which, if defective, causes Alport syndrome, an hereditary
DE   disorder characterized by a progressive glomerulonephritis leading to
DE   end-stage renal disease, often associated with sensorineural hearing
DE   loss and ocular abnormalities.
HI   Disease: Alport syndrome.
CA   Disease.
//
ID   Alternative initiation.
AC   KW-0024
DE   Protein for which at least two isoforms exist due to the usage of
DE   alternative initiation codons in the same mRNA (the resulting isoforms
DE   differ in their N-terminus if they are in frame).
HI   Coding sequence diversity: Alternative initiation.
CA   Coding sequence diversity.
//
ID   Alternative promoter usage.
AC   KW-0877
DE   Protein for which at least two isoforms exist due to the alternative
DE   usage of promoters.
HI   Coding sequence diversity: Alternative promoter usage.
CA   Coding sequence diversity.
//
ID   Alternative splicing.
AC   KW-0025
DE   Protein for which at least two isoforms exist due to distinct pre-mRNA
DE   splicing events.
HI   Coding sequence diversity: Alternative splicing.
CA   Coding sequence diversity.
//
ID   Alzheimer disease.
AC   KW-0026
DE   Protein which, if defective, causes Alzheimer disease, a
DE   neurodegenerative disorder characterized by progressive dementia and
DE   global loss of cognitive abilities. The condition primarily occurs
DE   after age 60, and is marked pathologically by severe cortical atrophy,
DE   senile plaques, neurofibrillary tangles, and neuropil threads. Early-
DE   onset forms also occurr.
SY   Alzheimer's disease.
HI   Disease: Alzheimer disease.
CA   Disease.
//
ID   Amelogenesis imperfecta.
AC   KW-0986
DE   Protein which, if defective, causes amelogenesis imperfecta, a
DE   clinically and genetically heterogeneous group of disorders affecting
DE   the dental enamel. The enamel may be hypoplastic, hypomineralized or
DE   both, and affected teeth may be discoloured, sensitive or prone to
DE   disintegration either pre-eruption or post-eruption. In the
DE   hypoplastic type of amelogenesis imperfecta, the enamel is of normal
DE   hardness but does not develop to normal thickness. In the
DE   hypomineralized type, the enamel is of normal thickness but opaque or
DE   yellowish white without lustre on newly erupted teeth; it is so soft
DE   that it is lost soon after eruption. Amelogenesis imperfecta
DE   occasionally occurs in conjunction with other dental, oral and extra-
DE   oral features.
HI   Disease: Amelogenesis imperfecta.
CA   Disease.
//
ID   Amidation.
AC   KW-0027
DE   Peptide which is posttranslationally modified by C-terminal amidation.
DE   The amino acid to be modified is almost always followed by a glycine,
DE   which provides the amide group. In a first reaction step the glycine
DE   is oxidized to form alpha-hydroxy-glycine. The oxidized glycine
DE   cleaves into the C-terminally amidated peptide and an N-glyoxylated
DE   peptide. C-terminal amidation is essential to the biological activity
DE   of many neuropeptides and hormones. In a few cases alpha-oxidative
DE   cleavage of an amino acid other than glycine has been observed. All
DE   such cases are additionally annotated with the word "atypical" in the
DE   feature description.
SY   Amidated.
HI   PTM: Amidation.
CA   PTM.
//
ID   Amino-acid biosynthesis.
AC   KW-0028
DE   Protein involved in the synthesis of naturally-occuring amino acids.
DE   In addition to their use for protein biosynthesis, they are the
DE   precursors of many molecules such as purines, pyrimidines, histamines,
DE   adrenaline and melanin.
SY   Amino-acid anabolism; Amino-acid formation; Amino-acid synthesis.
GO   GO:0008652; amino acid biosynthetic process
HI   Biological process: Amino-acid biosynthesis.
CA   Biological process.
//
ID   Amino-acid transport.
AC   KW-0029
DE   Protein involved in the transport of amino acids.
SY   Amino acid transport.
GO   GO:0006865; amino acid transport
HI   Biological process: Transport; Amino-acid transport.
CA   Biological process.
//
ID   Aminoacyl-tRNA synthetase.
AC   KW-0030
DE   Enzyme that activates an amino acid for translation by forming an
DE   aminoacyladenylate intermediate and then links this activated amino
DE   acid to the corresponding tRNA molecule (amino acid-tRNA, aminoacyl-
DE   tRNA). In general, a specific aminoacyl-tRNA synthase is available for
DE   each amino acid.
SY   Amino acid translase; Aminoacyl-tRNA ligase; Aminoacyl-tRNA synthase.
GO   GO:0004812; aminoacyl-tRNA ligase activity
HI   Molecular function: Ligase; Aminoacyl-tRNA synthetase.
CA   Molecular function.
//
ID   Aminopeptidase.
AC   KW-0031
DE   Enzyme that catalyzes the removal of amino acids from the N-terminus
DE   of peptides and proteins.
GO   GO:0004177; aminopeptidase activity
HI   Molecular function: Hydrolase; Protease; Aminopeptidase.
CA   Molecular function.
//
ID   Aminotransferase.
AC   KW-0032
DE   Enzyme that catalyzes the transfer of an alpha-amino group from an
DE   amino acid to an alpha-keto acid. The amino group is usually
DE   covalently bound by the prosthetic group pyridoxal phosphate.
SY   Transaminase.
GO   GO:0008483; transaminase activity
HI   Molecular function: Transferase; Aminotransferase.
CA   Molecular function.
//
ID   Ammonia transport.
AC   KW-0924
DE   Protein involved in the transport of ammonia/ammonium. Ammonia is an
DE   excellent nitrogen source for many bacteria, fungi, and plants, but it
DE   can be cytotoxic, especially for animal cells at high concentration.
DE   Its transport across cellular membranes is thus of high biological
DE   relevance. Ammonia (NH3) is a weak base and exists predominantly as
DE   the ammonium ion (NH4+) in biological fluids.
SY   Ammonium transport.
GO   GO:0072488; ammonium transmembrane transport
HI   Biological process: Transport; Ammonia transport.
CA   Biological process.
//
ID   Amphibian defense peptide.
AC   KW-0878
DE   Protein specifically found in the skin of animals belonging to the
DE   vertebrate class amphibia, that includes frogs, toads, newts,
DE   salamanders and worm-like apoda. The skins of anuran amphibians, in
DE   addition to mucous glands, contain highly specialized poison glands,
DE   which, in reaction to stress or attack, exude a complex noxious
DE   species-specific cocktail of biologically active molecules. These
DE   secretions often contain a plethora of peptides such as neuropeptides
DE   and hormones. The frog dermatous glands also synthesize and store an
DE   extraordinarily rich variety of wide-spectrum antimicrobial peptides
DE   that are released onto the outer layer of the skin to provide an
DE   effective and fast-acting defense against harmful microorganisms.
GO   GO:0006952; defense response
HI   Molecular function: Amphibian defense peptide.
CA   Molecular function.
//
ID   Amyloid.
AC   KW-0034
DE   Proteins which may form wide, insoluble, unbranched filaments
DE   possessing a cross-beta sheet quaternary structure, where the beta
DE   sheets are oriented perpendicular to the fibre axis. Amyloid fibrils
DE   may be involved in abnormal protein depositions, or amyloidosis, such
DE   as Alzheimer's or Parkinson's diseases. Functional amyloids, found in
DE   a wide range of organism, from bacteria to mammals are involved in
DE   diverse functions such as biofilm formation, formation of aerial
DE   hyphae, long-term memory or regulation of melanin biosynthesis.
SY   Amyloid fibre-forming; Amyloid fibril-forming;
SY   Amyloid filament-forming; Amyloid-forming; Amyloid-like fibre-forming;
SY   Amyloid-like fibril-forming; Amyloid-like filament-forming;
SY   Functional amyloid.
HI   Cellular component: Amyloid.
CA   Cellular component.
//
ID   Amyloidosis.
AC   KW-1008
DE   Protein which, if defective, causes amyloidosis, a vast group of
DE   diseases defined by the accumulation of amyloid in tissues.
DE   Amyloidoses are classified according to clinical signs, biochemical
DE   type of amyloid protein involved, and the extent of amyloid deposition
DE   (generalized or localized). Most amyloidoses are multisystemic
DE   diseases affecting several organs or systems. Mainly affected organs
DE   are the kidneys, heart, gastrointestinal tract, liver, skin,
DE   peripheral nerves and eyes, but any organ can be affected. The most
DE   frequent forms are primary amyloidosis, also known as light-chain
DE   immunoglobulin amyloidosis (AL), reactive or inflammatory amyloidosis,
DE   also known as acquired amyloidosis (AA), and transthyretin amyloidosis
DE   (ATTR). Localized amyloidosis affecting the brain is characteristic of
DE   Alzheimer's disease, trisomy 21, and prion diseases (transmissible
DE   spongiform encephalitis, Creutzfeldt-Jakob disease, Gerstmann-
DE   Straussler-Scheinker syndrome, fatal familial insomnia). In prion
DE   diseases the amyloid precursor is the prion protein.
HI   Disease: Amyloidosis.
CA   Disease.
//
ID   Amyloplast.
AC   KW-0035
DE   Protein found in the amyloplast, a colorless plant plastid that forms
DE   and stores starch. Amyloplasts are found in many tissues, particularly
DE   in storage tissues.
GO   GO:0009501; amyloplast
HI   Cellular component: Plastid; Amyloplast.
CA   Cellular component.
//
ID   Amyotrophic lateral sclerosis.
AC   KW-0036
DE   Protein which, if defective, causes amyotrophic lateral sclerosis
DE   (ALS), a degenerative disorder of motor neurons in the cortex, brain
DE   stem and spinal cord. ALS is characterized by muscular weakness and
DE   atrophy.
SY   ALS.
HI   Disease: Neurodegeneration; Amyotrophic lateral sclerosis.
CA   Disease.
//
ID   Angiogenesis.
AC   KW-0037
DE   Protein involved in angiogenesis, the sprouting or splitting of
DE   capillaries from pre-existing vasculature. Angiogenesis plays an
DE   important role for example during embryonic development, normal growth
DE   of tissues and maintenance of the normal vasculature, wound healing,
DE   tumor growth and metastasis.
SY   Vascularization.
GO   GO:0001525; angiogenesis
HI   Biological process: Angiogenesis.
CA   Biological process.
//
ID   Anion exchange.
AC   KW-0039
DE   Protein involved in the exchange of anions across a membrane. Anion
DE   exchange is a cellular transport function which contributes to the
DE   regulation of cell pH and volume by a functionally related anion
DE   exchanger protein family.
SY   Anion exchanger activity.
GO   GO:0015297; antiporter activity
HI   Biological process: Transport; Ion transport; Anion exchange.
CA   Biological process.
//
ID   ANK repeat.
AC   KW-0040
DE   Protein containing at least one ANK repeat, a conserved domain of
DE   approximately 33 amino acids, that was originally identified in
DE   ankyrin. It has been described as an L-shaped structure consisting of
DE   a beta-hairpin and two alpha-helices. Many ankyrin repeat regions are
DE   known to function as protein-protein interaction domains.
SY   ANK motif; Ankyrin repeat.
HI   Domain: ANK repeat.
CA   Domain.
//
ID   Annexin.
AC   KW-0041
DE   Protein containing at least one annexin repeat, a conserved domain of
DE   61 residues, which is present in proteins of the annexin family in
DE   either four or eight copies. The annexin calcium binding sites are
DE   found within the repeated domains.
SY   Annexin repeat.
HI   Domain: Annexin.
CA   Domain.
//
ID   Antenna complex.
AC   KW-0042
DE   Component of an antenna complex or protein regulating the expression
DE   of such components. Antenna complexes are light-harvesting systems
DE   (LHC) which are protein-pigment complexes in or on photosynthetic
DE   membranes. LHCs receive radiant energy and transfer it to the reaction
DE   centers; an array of LHCs is often referred to as an "antenna". LHCs
DE   typically include one or more associated pigments (phycobilins,
DE   chlorophylls, bacteriochlorophylls and carotenoids).
SY   Light-harvesting antenna; Light-harvesting complex.
GO   GO:0030076; light-harvesting complex
HI   Cellular component: Antenna complex.
CA   Cellular component.
//
ID   Antibiotic.
AC   KW-0044
DE   Protein with antibacterial activity.
SY   Antibacterial; Bactericide.
GO   GO:0042742; defense response to bacterium
HI   Molecular function: Antimicrobial; Antibiotic.
CA   Molecular function.
//
ID   Antibiotic biosynthesis.
AC   KW-0045
DE   Protein involved in the synthesis of antibiotics. Antibiotics are
DE   organic compounds produced by living organims that can selectively
DE   inhibit the growth of, or kill bacteria.
SY   Antibiotic anabolism; Antibiotic formation; Antibiotic synthesis.
GO   GO:0017000; antibiotic biosynthetic process
HI   Biological process: Antibiotic biosynthesis.
CA   Biological process.
//
ID   Antibiotic resistance.
AC   KW-0046
DE   Protein that confers, on bacteria, the ability to withstand
DE   antibiotics. The resistance is often due either to mutations that
DE   prevent antibiotic binding to the protein or to amplification of the
DE   gene encoding the protein.
SY   Resistance to antibiotic.
GO   GO:0046677; response to antibiotic
HI   Biological process: Antibiotic resistance.
CA   Biological process.
//
ID   Antifreeze protein.
AC   KW-0047
DE   Protein that lowers the freezing point of blood or other biological
DE   fluids by inhibiting the formation of water ice crystals.
SY   AFP; Ice structuring protein; ISP.
HI   Molecular function: Antifreeze protein.
CA   Molecular function.
//
ID   Antimicrobial.
AC   KW-0929
DE   Protein which has deleterious effects on any type of microbe. Microbe
DE   is a general term for microscopic unicellular organisms, such as
DE   bacteria, archaea, fungi and protista. While the term microbe is often
DE   also used for viruses, we do not apply the keyword antimicrobial to
DE   antiviral proteins.
HI   Molecular function: Antimicrobial.
CA   Molecular function.
//
ID   Antioxidant.
AC   KW-0049
DE   Protein capable of counteracting the damaging effects of oxidation,
DE   e.g. by trapping free radicals generated during the metabolic burst
DE   and possibly inhibiting ageing. Scavengers of highly reactive and
DE   harmful oxygen species.
GO   GO:0016209; antioxidant activity
HI   Molecular function: Antioxidant.
CA   Molecular function.
//
ID   Antiport.
AC   KW-0050
DE   Protein involved in the transport of a solute across a biological
DE   membrane coupled, directly, to the transport of a different solute in
DE   the opposite direction.
SY   Antiporter; Countertransporter; Exchanger; Exchange transporter.
GO   GO:0015297; antiporter activity
HI   Biological process: Transport; Antiport.
CA   Biological process.
//
ID   Antiviral defense.
AC   KW-0051
DE   Protein synthesized or activated in the cell in response to viral
DE   infection, or protein with specific antiviral activity within the
DE   cell. Eukaryotic cells have an innate immune mechanism to fight viral
DE   infection, which is activated through the interferon signaling pathway
DE   or through dsRNA detection in the cytoplasm. It leads to the
DE   establishment of an antiviral cell state, which prevents virus
DE   replication or induces apoptosis. Most viruses have developed specific
DE   proteins to prevent the establishment of an antiviral state. About
DE   half of all bacteria and most archaea have a CRISPR (clustered
DE   regularly interspersed short plaindromic repeats) system of adaptive
DE   immunity to exogenous DNA. CRISPRs clusters are tandem arrays of
DE   alternating repeats and spacers, where the spacers in some cases are
DE   homologous to sequences from virus and plasmid genomes. The CRISPR
DE   arrays are transcribed, processed and in some way aid in detection and
DE   resistance to foreign DNA. In at least a few bacteria (E.coli,
DE   S.epidermidis) it seems DNA is the target, whereas in Pyrococcus
DE   furiosis it seems the CRISPR system targets RNA.
GO   GO:0051607; defense response to virus
HI   Biological process: Antiviral defense.
CA   Biological process.
//
ID   Antiviral protein.
AC   KW-0930
DE   Protein with antiviral activity. Often this activity is fortuitous
DE   (e.g. a bacterial protein displaying anti-HIV activity).
GO   GO:0050688; regulation of defense response to virus
HI   Molecular function: Antiviral protein.
CA   Molecular function.
//
ID   Aortic aneurysm.
AC   KW-0993
DE   Protein which, if defective, causes aortic aneurysm. Aortic aneurysm
DE   is the dilation of the wall of the aorta. It forms a sac that is
DE   filled with fluid or clotted blood, often resulting in a pulsating
DE   tumor. Aortic aneurysms are classified by their location on the aorta.
HI   Disease: Aortic aneurysm.
CA   Disease.
//
ID   Apicoplast.
AC   KW-0933
DE   Protein encoded by the apicoplast genome or protein located in the
DE   apicoplast, a plastid found in some apicomplexan parasites which is a
DE   non-photosynthetic plastid relict. This organelle contains ring-like
DE   DNA of about 35 Kb as a third type of cell genome. Apicoplasts do not
DE   contain thylakoids; it is not yet clear if they contain internal
DE   membranes.
SY   Golgi-adjunct organelle; Thick-walled organelle.
GO   GO:0020011; apicoplast
HI   Cellular component: Plastid; Apicoplast.
CA   Cellular component.
//
ID   Apoplast.
AC   KW-0052
DE   Protein which is found in the part of the plant which is external to
DE   the living protoplast, ie the cell wall, the intercellular space and
DE   the lumina of dead cells such as xylem vessels and tracheids.
GO   GO:0048046; apoplast
HI   Cellular component: Apoplast.
CA   Cellular component.
//
ID   Apoptosis.
AC   KW-0053
DE   Protein involved in apoptotic programmed cell death. Apoptosis is
DE   characterized by cell morphological changes, including blebbing, cell
DE   shrinkage, nuclear fragmentation, chromatin condensation and
DE   chromosomal DNA fragmentation, and eventually death. Unlike necrosis,
DE   apoptosis produces cell fragments, called apoptotic bodies, that
DE   phagocytic cells are able to engulf and quickly remove before the
DE   contents of the cell can spill out onto surrounding cells and cause
DE   damage. In general, apoptosis confers advantages during an organism's
DE   life cycle.
SY   Active cell death; Apoptotic programmed cell death;
SY   Type I programmed cell death.
GO   GO:0006915; apoptotic process
HI   Biological process: Apoptosis.
CA   Biological process.
//
ID   Arabinose catabolism.
AC   KW-0054
DE   Protein involved in arabinose breakdown. Arabinose is a 5-carbon
DE   aldose sugar found in plant gums, pectins and bacterial cell wall
DE   polysaccharides.
SY   Arabinose breakdown; Arabinose catabolic process;
SY   Arabinose degradation.
GO   GO:0019568; arabinose catabolic process
HI   Biological process: Carbohydrate metabolism; Arabinose catabolism.
CA   Biological process.
//
ID   Archaeal flagellum.
AC   KW-0974
DE   The archaellum (archaeal flagellum) is the motility apparatus of
DE   archaea which propels the cell through liquid medium. The archaellum
DE   is the functional equivalent of the bacterial flagellum but its
DE   architecture, composition and mode of assembly is completely
DE   unrelated. The archaellum is thinner (10-15 nm) compared to the
DE   bacterial flagellum (18-24 nm). Its filament is assembled from
DE   archaellin subunits, which are N-glycosylated proteins. The archaellum
DE   is considered to be a type IV pilus-like structure and accordingly is
DE   assembled from the base into a 3-start helix. Archaellins have a type
DE   III signal sequence which is removed by the pre-archaellin peptidase.
DE   Core components of the assembly machinery are ArlI and ArlJ
DE   (previously FlaI, FlaJ) which are distantly related to PilB and PilC
DE   from type II secretion systems and type IV pills assembly systems.
DE   ArlI is a dual function ATPase which first assembles the filament and
DE   then rotates it by using the energy from ATP hydrolysis. Ion gradients
DE   are not used for archaellum rotation.
SY   Archaeal flagella; Archaeal flagellar apparatus; Archaellum.
GO   GO:0097589; archaeal-type flagellum
HI   Cellular component: Archaeal flagellum.
CA   Cellular component.
//
ID   Archaeal flagellum biogenesis.
AC   KW-1209
DE   Protein which is involved in the formation, organization or
DE   maintenance of the archaellum (archaeal flagellum) the motility
DE   apparatus of archaea which propels the cell through liquid medium. The
DE   archaellum is the functional equivalent of the bacterial flagellum but
DE   its architecture, composition and mode of assembly is completely
DE   unrelated. The archaellum is thinner (10-15 nm) compared to the
DE   bacterial flagellum (18-24 nm). Its filament is assembled from
DE   archaellin subunits (archaeal flagellin), N-glycosylated proteins. The
DE   archaellum is considered to be a type IV pilus-like structure and
DE   accordingly is assembled from the base into a 3-start helix.
DE   Archaellins have a type III signal sequence which is removed by the
DE   pre-archaellin peptidase. Core components of the assembly machinery
DE   are ArlI and ArlJ (previously FlaI, FlaJ) which are distantly related
DE   to PilB and PilC from type II secretion systems and type IV pills
DE   assembly systems. ArlI is a dual function ATPase which first assembles
DE   the filament and then rotates it by using the energy from ATP
DE   hydrolysis.
SY   Archaeal flagella biogenesis; Archaeal flagellar apparatus biogenesis.
HI   Biological process: Archaeal flagellum biogenesis.
CA   Biological process.
//
ID   Arginine biosynthesis.
AC   KW-0055
DE   Protein involved in the synthesis of the basic amino acid arginine
DE   (Arg).
SY   Arginine anabolism; Arginine biosynthetic process; Arginine formation;
SY   Arginine synthesis.
GO   GO:0006526; arginine biosynthetic process
HI   Biological process: Amino-acid biosynthesis; Arginine biosynthesis.
CA   Biological process.
//
ID   Arginine metabolism.
AC   KW-0056
DE   Protein involved in biochemical reactions with the basic amino acid
DE   arginine (Arg).
SY   Arginine metabolic process.
GO   GO:0006525; arginine metabolic process
HI   Biological process: Arginine metabolism.
CA   Biological process.
//
ID   Aromatic amino acid biosynthesis.
AC   KW-0057
DE   Protein involved in the synthesis of an amino acid with an aromatic
DE   side-chain: phenylalanine (Phe), tyrosine (Tyr) and tryptophan (Trp).
SY   Aromatic amino acid anabolism;
SY   Aromatic amino acid family biosynthetic process;
SY   Aromatic amino acid formation; Aromatic amino acid synthesis.
GO   GO:0009073; aromatic amino acid family biosynthetic process
HI   Biological process: Amino-acid biosynthesis; Aromatic amino acid biosynthesis.
CA   Biological process.
//
ID   Aromatic hydrocarbons catabolism.
AC   KW-0058
DE   Protein involved in the breakdown of aromatic hydrocarbons. Aromatic
DE   hydrocarbons are compounds which only contain carbon and hydrogen,
DE   examples include the common pollutants benzene and naphthalene.
SY   Aromatic compound catabolic process; Aromatic hydrocarbons breakdown;
SY   Aromatic hydrocarbons degradation.
GO   GO:0019439; aromatic compound catabolic process
HI   Biological process: Aromatic hydrocarbons catabolism.
CA   Biological process.
//
ID   Arsenical resistance.
AC   KW-0059
DE   Protein that confers, on bacteria and other microorganisms, the
DE   ability to withstand aromatic compounds of arsenic.
SY   Arsenic resistance; Resistance to arsenic.
GO   GO:0046685; response to arsenic-containing substance
HI   Biological process: Arsenical resistance.
CA   Biological process.
//
ID   Ascorbate biosynthesis.
AC   KW-0060
DE   Protein involved in the synthesis of ascorbate, the ionized form of
DE   ascorbic acid (vitamin C). Ascorbic acid is derived from glucose via
DE   the uronic acid pathway. This water-soluble vitamin is essential for
DE   the synthesis of bone, cartilage and dentine. It is required in the
DE   diet of primates and some other species that cannot synthesize L-
DE   ascorbic acid because of their deficiency in L-gulono-gamma-lactone
DE   oxidase, a key enzyme for the biosynthesis of this vitamin.
SY   Ascorbate anabolism; Ascorbate biosynthetic process;
SY   Ascorbate formation; Ascorbate synthesis; Ascorbic acid anabolism;
SY   Ascorbic acid biosynthesis; Ascorbic acid biosynthetic process;
SY   Ascorbic acid formation; Ascorbic acid synthesis; Vitamin C anabolism;
SY   Vitamin C biosynthesis; Vitamin C biosynthetic process;
SY   Vitamin C formation; Vitamin C synthesis.
GO   GO:0019853; L-ascorbic acid biosynthetic process
HI   Biological process: Ascorbate biosynthesis.
CA   Biological process.
//
ID   Asparagine biosynthesis.
AC   KW-0061
DE   Protein involved in the synthesis of the polar amino acid asparagine
DE   (Asn).
SY   Asparagine anabolism; Asparagine biosynthetic process;
SY   Asparagine formation; Asparagine synthesis.
GO   GO:0006529; asparagine biosynthetic process
HI   Biological process: Amino-acid biosynthesis; Asparagine biosynthesis.
CA   Biological process.
//
ID   Aspartic protease inhibitor.
AC   KW-0062
DE   Protein which inhibits the catalytic activity of an aspartyl protease,
DE   a class of proteases that contains an active site aspartate residue
DE   (Asp), e.g. pepsin, HIV retropepsin, renin, etc.
SY   Aspartic proteinase inhibitor; Aspartic-type endopeptidase inhibitor;
SY   Aspartyl protease inhibitor.
GO   GO:0019828; aspartic-type endopeptidase inhibitor activity
HI   Molecular function: Protease inhibitor; Aspartic protease inhibitor.
CA   Molecular function.
//
ID   Aspartyl esterase.
AC   KW-0063
DE   Enzyme which catalyzes the hydrolysis of esters and is characterized
DE   by a catalytically active aspartic acid residue in its active site.
GO   GO:0045330; aspartyl esterase activity
HI   Molecular function: Hydrolase; Aspartyl esterase.
CA   Molecular function.
//
ID   Aspartyl protease.
AC   KW-0064
DE   Proteolytic enzyme with an aspartate residue (Asp) in its active site.
DE   There are many families of aspartyl proteases. The most well known one
DE   is the pepsin family (A1 in MEROPS classification) which is known to
DE   exist in vertebrates, fungi, plants, retroviruses and some plant
DE   viruses.
SY   Acid protease; Aspartate protease; Aspartic protease;
SY   Aspartic proteinase; Aspartic-type endopeptidase; Aspartyl proteinase.
GO   GO:0004190; aspartic-type endopeptidase activity
HI   Molecular function: Hydrolase; Protease; Aspartyl protease.
CA   Molecular function.
//
ID   Asperger syndrome.
AC   KW-1270
DE   Protein which, if defective, is involved in Asperger syndrome, a
DE   complex, multifactorial disorder. It is characterized by clinically
DE   significant impairment of social interaction, and restricted
DE   repetitive and stereotyped patterns of behavior. Asperger syndrome is
DE   primarily distinguished from autism by the higher cognitive abilities
DE   and a more normal and timely development of language and communicative
DE   phrases.
HI   Disease: Autism spectrum disorder; Asperger syndrome.
CA   Disease.
//
ID   Asthma.
AC   KW-1058
DE   Protein which, if defective, is associated with asthma, a bronchial
DE   disorder associated with airway inflammation, swelling and
DE   obstruction. It is marked by recurrent attacks of paroxysmal dyspnea,
DE   with wheezing due to spasmodic contraction of the bronchi.
HI   Disease: Asthma.
CA   Disease.
//
ID   Atherosclerosis.
AC   KW-0065
DE   Protein which, if defective, causes atherosclerosis, which is
DE   characterized by deposits of plaques (atheromas) in the blood vessels,
DE   thus narrowing the vessel lumen and restricting blood flow. Atheromas
DE   consist of lipids (cholesterol), carbohydrates, blood products,
DE   fibrous tissue and calcium deposits.
SY   Arteriosclerosis.
HI   Disease: Atherosclerosis.
CA   Disease.
//
ID   ATP synthesis.
AC   KW-0066
DE   Protein involved in the synthesis of adenosine 5'-triphosphate (ATP).
DE   ATP is a ribonucleotide adenosine (a purine base adenine linked to the
DE   sugar D-ribofuranose) which carries 3 phosphate groups esterified to
DE   the sugar moiety. It is the cell's source for energy and phosphate.
SY   Adenosine 5'-triphosphate anabolism;
SY   Adenosine 5'-triphosphate biosynthesis;
SY   Adenosine 5'-triphosphate biosynthetic process;
SY   Adenosine 5'-triphosphate formation; Adenosine triphosphate anabolism;
SY   Adenosine triphosphate biosynthesis;
SY   Adenosine triphosphate biosynthetic process;
SY   Adenosine triphosphate formation; ATP anabolism; ATP biosynthesis;
SY   ATP biosynthetic process; ATP formation.
GO   GO:0006754; ATP biosynthetic process
HI   Biological process: ATP synthesis.
CA   Biological process.
//
ID   ATP-binding.
AC   KW-0067
DE   Protein which binds adenosine 5'-triphosphate (ATP), a ribonucleotide
DE   adenosine (a purine base adenine linked to the sugar D-ribofuranose)
DE   that carries three phosphate groups esterified to the sugar moiety. It
DE   is the cell's source for energy and phosphate.
SY   Adenosine 5'-triphosphate binding; Adenosine triphosphate binding.
GO   GO:0005524; ATP binding
HI   Ligand: Nucleotide-binding; ATP-binding.
CA   Ligand.
//
ID   Atrial fibrillation.
AC   KW-1020
DE   Protein which, if defective, causes atrial fibrillation, a common
DE   cardiac arrhythmia marked by disorganized atrial electrical activity
DE   and rapid randomized contractions of small areas of the atrial
DE   myocardium, causing a totally irregular, and rapid, ventricular rate.
SY   AF; ATFB.
HI   Disease: Atrial fibrillation.
CA   Disease.
//
ID   Atrial septal defect.
AC   KW-0976
DE   Protein which, if defective, causes atrial septal defect, a congenital
DE   cardiac anomaly characterized by persistent patency of the atrial
DE   septum that results in blood flow between the atria. It is due to
DE   failure of fusion between either the septum secundum or the septum
DE   primum and the endocardial cushions.
SY   Atrioseptal defect.
HI   Disease: Atrial septal defect.
CA   Disease.
//
ID   Autism.
AC   KW-1269
DE   Protein which, if defective, is involved in autism, a pervasive
DE   developmental disorder. It is a complex, multifactorial disease
DE   characterized by impairments in reciprocal social interaction and
DE   communication, restricted and stereotyped patterns of interests and
DE   activities, and the presence of developmental abnormalities by 3 years
DE   of age. Most individuals with autism manifest moderate mental
DE   retardation.
SY   Autistic disorder.
HI   Disease: Autism spectrum disorder; Autism.
CA   Disease.
//
ID   Autism spectrum disorder.
AC   KW-1268
DE   Protein which, if defective, is involved in autism spectrum disorder,
DE   a clinically heterogeneous group of disorders that share common
DE   features of impaired social relationships, impaired language and
DE   communication, repetitive behaviors, and a restricted range of
DE   interests. The spectrum includes diverse phenotypic manifestations,
DE   such as classic autism, Asperger syndrome, childhood disintegrative
DE   disorder, Rett syndrome, and pervasive developmental disorder not
DE   otherwise specified.
SY   ASD.
HI   Disease: Autism spectrum disorder.
CA   Disease.
//
ID   Autocatalytic cleavage.
AC   KW-0068
DE   Protein catalyzing its own cleavage.
SY   Autocatalytic peptide cleavage.
HI   PTM: Autocatalytic cleavage.
CA   PTM.
//
ID   Autoimmune encephalomyelitis.
AC   KW-0069
DE   Protein which, if defective, causes autoimmune encephalomyelitis. This
DE   form of autoimmune inflammation of the brain and spinal cord causes
DE   demyelination.
SY   Autoimmune encephalitis.
HI   Disease: Autoimmune encephalomyelitis.
CA   Disease.
//
ID   Autoimmune uveitis.
AC   KW-0070
DE   Protein which, if defective, causes autoimmune inflammation of the
DE   uvea, which is the vascular middle coat of the eye, comprising the
DE   iris, ciliary body and choroid.
HI   Biological process: Sensory transduction; Vision; Autoimmune uveitis.
HI   Disease: Autoimmune uveitis.
CA   Disease.
//
ID   Autoinducer synthesis.
AC   KW-0071
DE   Protein involved in the synthesis of an autoinducer, a molecule which
DE   triggers the regulators of biosynthetic genes.
SY   Autoinducer anabolism; Autoinducer biosynthesis;
SY   Autoinducer biosynthetic process; Autoinducer formation.
HI   Biological process: Autoinducer synthesis.
CA   Biological process.
//
ID   Autophagy.
AC   KW-0072
DE   Protein participating in autophagy, a process of intracellular bulk
DE   degradation in which cytoplasmic components including organelles are
DE   sequestered within double-membrane vesicles that deliver the contents
DE   to the lysosome/vacuole for degradation. There are three primary forms
DE   of autophagy: chaperone-mediated autophagy, microautophagy and
DE   macroautophagy. During macroautophagy, the sequestering vesicles,
DE   termed autophagosomes, fuse with the lysosome or vacuole resulting in
DE   the delivery of an inner vesicle (autophagic body) into the lumen of
DE   the degradative compartment.
GO   GO:0006914; autophagy
HI   Biological process: Autophagy.
CA   Biological process.
//
ID   Auxin biosynthesis.
AC   KW-0073
DE   Protein involved in the synthesis of auxins. Auxins are plant hormones
DE   which play a role in many aspects of plant growth and development.
SY   Auxin anabolism; Auxin biosynthetic process; Auxin formation;
SY   Auxin synthesis.
GO   GO:0009851; auxin biosynthetic process
HI   Biological process: Auxin biosynthesis.
CA   Biological process.
//
ID   Auxin signaling pathway.
AC   KW-0927
DE   Protein involved in the auxin signaling pathway (e.g. transport and
DE   signal transduction) that regulates many aspects of plant growth and
DE   development (e.g. caulogenesis, rhizogenesis, tropisms, nodulation).
DE   The major form of this phytohormone is indole-3-acetic acid (IAA) that
DE   can be synthesized both from tryptophan (Trp) using Trp-dependent
DE   pathways and from an indolic Trp precursor via Trp-independent
DE   pathways. Plants can also obtain IAA by b-oxidation of indole-3-
DE   butyric acid (IBA), a second endogenous auxin, or by hydrolysing IAA
DE   conjugates, in which IAA is linked to amino acids, sugars or peptides.
SY   Auxin mediated signaling pathway.
GO   GO:0009734; auxin-activated signaling pathway
HI   Biological process: Auxin signaling pathway.
CA   Biological process.
//
ID   B-cell activation.
AC   KW-0075
DE   Protein involved in the activation and proliferation of B-cells. B-
DE   cells are activated by the binding of antigen to receptors on its cell
DE   surface which causes the cell to divide and proliferate. Some
DE   stimulated B-cells become plasma cells, which secrete antibodies.
DE   Others become long-lived memory B-cells which can be stimulated at a
DE   later time to differentiate into plasma cells.
GO   GO:0042113; B cell activation
HI   Biological process: B-cell activation.
CA   Biological process.
//
ID   Bacterial flagellum.
AC   KW-0975
DE   Bacterial protein present in a flagellum, a long hair-like cell
DE   surface appendage. The flagellar apparatus consists of the flagellar
DE   filament made of polymerized flagellin, the hook-like structure near
DE   the cell surface and a system of rings embedded in the cell enveloppe
DE   (the basal body or flagellar motor). The basal body and the hook
DE   anchor the whip-like filament to the cell surface. The flagellum is a
DE   rotating structure with switches propels the cell through a liquid
DE   medium.
SY   Bacterial flagella; Bacterial flagellar apparatus.
GO   GO:0009288; bacterial-type flagellum
HI   Cellular component: Bacterial flagellum.
CA   Cellular component.
//
ID   Bacterial flagellum biogenesis.
AC   KW-1005
DE   Protein which is involved in the formation, organization or
DE   maintenance of the bacterial flagellum, a long hair-like cell surface
DE   appendage. The flagellar apparatus consists of the flagellar filament
DE   made of polymerized flagellin, the hook-like structure near the cell
DE   surface and a system of rings embedded in the cell enveloppe (the
DE   basal body or flagellar motor). The basal body and the hook anchor the
DE   whip-like filament to the cell surface. The flagellum is a rotating
DE   structure whose switches propels the cell through a liquid medium.
SY   Bacterial flagella biogenesis;
SY   Bacterial flagellar apparatus biogenesis.
GO   GO:0044781; bacterial-type flagellum organization
HI   Biological process: Bacterial flagellum biogenesis.
CA   Biological process.
//
ID   Bacterial flagellum protein export.
AC   KW-1006
DE   Protein which is involved in the export of bacterial flagellar
DE   proteins. The bacterial flagellum export apparatus consists of six
DE   integral membrane proteins (FlhA, FlhB, FliO, FliP, FliQ and FliR) and
DE   three soluble proteins (FliH, FliI and FliJ), and is located at the
DE   base of the flagellum. This system is characterized by ATP hydrolysis
DE   and a lack of substrate signal peptide cleavage.
SY   Bacterial flagella protein export;
SY   Bacterial flagellar apparatus protein export;
SY   Bacterial flagellar protein export.
HI   Biological process: Transport; Protein transport; Bacterial flagellum protein export.
CA   Biological process.
//
ID   Bacterial host gene expression shutoff by virus.
AC   KW-1261
DE   Viral protein which prevents host gene expression by blocking host
DE   transcription or inducing the degradation of the bacterial chromosome.
DE   This gives viral transcripts a competitive edge to use the hijacked
DE   host translation machinery. Preventing the expression of host proteins
DE   is also a strategy to counteract the antiviral response.
HI   Biological process: Host-virus interaction; Host gene expression shutoff by virus; Bacterial host gene expression shutoff by virus.
CA   Biological process.
//
ID   Bacterial host transcription shutoff by virus.
AC   KW-1263
DE   Viral protein involved in inhibiting transcription of bacterial genes
DE   to ensure the shutoff of host proteins expression and give viral
DE   transcripts a competitive edge for access to the cellular translation
DE   machinery. Preventing the expression of host proteins is also a
DE   strategy to counteract the antiviral response. Some bacterial viruses
DE   inhibit the host RNAP: bacteriophage SPO1 for example is known to shut
DE   off host RNA synthesis.
HI   Biological process: Host-virus interaction; Host gene expression shutoff by virus; Bacterial host gene expression shutoff by virus; Bacterial host transcription shutoff by virus.
CA   Biological process.
//
ID   Bacterial microcompartment.
AC   KW-1283
DE   Protein located in or on a bacterial microcompartment (BMC),
DE   proteinaceous polyhedral shells that encapsulate enzymes. The
DE   selectively permeable organelles protect their contents from the
DE   cytoplasm and/or the cytoplasm from reactants in their interior.
DE   Examples of BMCs include carboxysomes, which enhance autotrophic CO(2)
DE   fixation by encapsulating RuBisCO and carbonic anhydrase, as well as
DE   BMCs involved in ethanolamine or propanediol degradation; both
DE   pathways make toxic intermediates. Artifical BMCs can be expressed and
DE   filled with cargo proteins for biotechnological uses. BMCs are found
DE   in many bacterial phyla; in most cases their cargo is unknown.
GO   GO:0031469; bacterial microcompartment
HI   Cellular component: Bacterial microcompartment.
CA   Cellular component.
//
ID   Bacteriochlorophyll.
AC   KW-0076
DE   Protein interacting with bacteriochlorophyll, a photosynthetic pigment
DE   found in non-oxygenic photosynthetic bacteria. It is a magnesium-
DE   porphyrin complex esterified to a long hydrophobic terpenoid side
DE   chain (the alcohol phytol). It differs from chlorophyll of oxygenic
DE   organisms in the substituents around the tetrapyrrole nucleus of the
DE   molecule, and in the absorption spectra. Different bacteria have
DE   different species of bacteriochlorophyll.
GO   GO:0042314; bacteriochlorophyll binding
HI   Ligand: Chromophore; Chlorophyll; Bacteriochlorophyll.
CA   Ligand.
//
ID   Bacteriochlorophyll biosynthesis.
AC   KW-0077
DE   Protein involved in the synthesis of bacteriochlorophylls. These
DE   photosynthetic pigments are magnesium-porphyrin complexes with a long
DE   hydrophobic terpenoid side chain (the alcohol phytol). Biosynthesis of
DE   bacteriochlorophyll is a light-independent reaction.
SY   Bacteriochlorophyll anabolism;
SY   Bacteriochlorophyll biosynthetic process;
SY   Bacteriochlorophyll formation; Bacteriochlorophyll synthesis.
GO   GO:0030494; bacteriochlorophyll biosynthetic process
HI   Biological process: Chlorophyll biosynthesis; Bacteriochlorophyll biosynthesis.
CA   Biological process.
//
ID   Bacteriocin.
AC   KW-0078
DE   Peptidic antibiotic, often plasmid encoded, produced by specific
DE   strains of bacteria that is lethal against other strains of the same
DE   or related species. E.g. bacteriocin, colicin, lantibiotic.
GO   GO:0031640; killing of cells of another organism
HI   Molecular function: Antimicrobial; Antibiotic; Bacteriocin.
CA   Molecular function.
//
ID   Bacteriocin biosynthesis.
AC   KW-0871
DE   Protein involved in the synthesis of a bacteriocin.
SY   Bacteriocin anabolism; Bacteriocin biosynthetic process;
SY   Bacteriocin formation; Bacteriocin synthesis.
GO   GO:0030152; bacteriocin biosynthetic process
HI   Biological process: Antibiotic biosynthesis; Bacteriocin biosynthesis.
CA   Biological process.
//
ID   Bacteriocin immunity.
AC   KW-0079
DE   Protein that confers to a bacteria immunity against a specific
DE   bacteriocin that it synthesizes.
GO   GO:0030153; bacteriocin immunity
HI   Biological process: Bacteriocin immunity.
CA   Biological process.
//
ID   Bacteriocin transport.
AC   KW-0080
DE   Protein involved in the export of a bacteriocin (bacterial
DE   antibiotic).
GO   GO:0043213; bacteriocin transport
HI   Biological process: Transport; Protein transport; Bacteriocin transport.
CA   Biological process.
//
ID   Bacteriolytic enzyme.
AC   KW-0081
DE   Enzyme, e.g. lysozyme or endopeptidase, essential for lysis of
DE   bacterial cell walls.
GO   GO:0003824; catalytic activity
GO   GO:0008152; metabolic process
GO   GO:0031640; killing of cells of another organism
GO   GO:0042742; defense response to bacterium
HI   Molecular function: Antimicrobial; Bacteriolytic enzyme.
CA   Molecular function.
//
ID   Bait region.
AC   KW-0082
DE   Protein having a peptide stretch which contains specific cleavage
DE   sites for different proteinases, and which enables inhibition of all
DE   four classes of proteinases.
GO   GO:0010466; negative regulation of peptidase activity
GO   GO:0030414; peptidase inhibitor activity
HI   Domain: Bait region.
CA   Domain.
//
ID   Bardet-Biedl syndrome.
AC   KW-0083
DE   Protein which, if defective, causes Bardet-Biedl syndrome (BBS), a
DE   genetically heterogeneous, autosomal recessive disorder. It is
DE   characterized by pigmentary retinopathy, obesity, polydactyly,
DE   hypogenitalism, renal malformation and intellectual disability.
DE   Secondary features include diabetes mellitus, hypertension and
DE   congenital heart disease.
SY   BBS.
HI   Disease: Ciliopathy; Bardet-Biedl syndrome.
CA   Disease.
//
ID   Bartter syndrome.
AC   KW-0910
DE   Protein which, if defective, causes Bartter syndrome (BS). In general,
DE   Bartter syndrome refers to a group of autosomal recessive disorders
DE   characterized by often severe intravascular volume depletion due to
DE   renal salt-wasting associated with low blood pressure, hypokalemic
DE   alkalosis, hypercalciuria, and normal serum magnesium levels. Patients
DE   with Bartter syndrome are often critically ill from birth onwards, and
DE   their long-term clinical course may be complicated by
DE   nephrocalcinosis, leading to renal failure. Clinical disease results
DE   from defective renal reabsorption of sodium chloride in the thick
DE   ascending limb (TAL) of the Henle loop, where only 30% of filtered
DE   salt is normally reabsorbed.
HI   Disease: Bartter syndrome.
CA   Disease.
//
ID   Basement membrane.
AC   KW-0084
DE   Protein which is a component of the basement membrane, an
DE   extracellular matrix found under epithelial cells and around smooth
DE   and striated muscle cells. This matrix contains intrinsic
DE   macromolecular components such as collagen, laminin, and sulfated
DE   proteoglycans.
GO   GO:0005604; basement membrane
HI   Cellular component: Secreted; Extracellular matrix; Basement membrane.
CA   Cellular component.
//
ID   Behavior.
AC   KW-0085
DE   Protein which affects the behavior, the action or reaction, of an
DE   organism to a stimulus or situation.
GO   GO:0007610; behavior
HI   Biological process: Behavior.
CA   Biological process.
//
ID   Bence-Jones protein.
AC   KW-0086
DE   Protein which is a dimer of immunoglobulin light chains synthesized in
DE   large amounts by patients who have myeloma or bone marrow tumor.
DE   Bence-Jones protein is sufficiently small to be excreted by the kidney
DE   into urine.
HI   Molecular function: Bence-Jones protein.
CA   Molecular function.
//
ID   Bernard Soulier syndrome.
AC   KW-0087
DE   Protein which, if defective, causes Bernard Soulier syndrome (BSS), a
DE   familial coagulation disorder characterized by a prolonged bleeding
DE   time, unusually large platelets, and impaired prothrombin consumption.
DE   BSS is caused by a genetic deficiency in platelet membrane
DE   glycoprotein Ib alpha chain and platelet glycoprotein IX, where
DE   platelets aggregate normally but do not stick to collagen of the sub-
DE   endothelial membrane.
SY   BSS.
HI   Disease: Bernard Soulier syndrome.
CA   Disease.
//
ID   Bile acid catabolism.
AC   KW-0088
DE   Protein involved in degradation of bile acids. Bile acids, which exist
DE   mainly as bile salts, are a family of carboxylic acid derivatives of
DE   cholesterol which play an important role in the digestion and
DE   absorption of fat. They are made in the liver, stored in the
DE   gallblader, and secreted as needed into the intestines.
SY   Bile acid breakdown; Bile acid catabolic process;
SY   Bile acid degradation; Bile salt breakdown;
SY   Bile salt catabolic process; Bile salt catabolism;
SY   Bile salt degradation.
GO   GO:0030573; bile acid catabolic process
HI   Biological process: Lipid metabolism; Lipid degradation; Bile acid catabolism.
HI   Biological process: Lipid metabolism; Steroid metabolism; Bile acid catabolism.
CA   Biological process.
//
ID   Bile pigment.
AC   KW-0089
DE   Protein binding covalently at least one linear tetrapyrrole
DE   chromophore, e.g. bilirubin, biliverdin, bilifuscin, biliprasin,
DE   choleprasin, bilihumin, and bilicyanin. Bile pigments are produced by
DE   breaking down protoporphyrin IX derived from hemoglobin and other heme
DE   proteins.
SY   Bilin chromophore.
HI   Ligand: Chromophore; Bile pigment.
CA   Ligand.
//
IC   Biological process.
AC   KW-9999
DE   Keywords assigned to proteins because they are involved in a
DE   particular biological process.
//
ID   Biological rhythms.
AC   KW-0090
DE   Protein involved in the generation of rhythmic pattern of behaviors or
DE   activities, e.g. circadian rhythm which is a metabolic or behavioural
DE   rhythm within a cycle of 24 hours.
SY   Rhythmic process.
GO   GO:0048511; rhythmic process
HI   Biological process: Biological rhythms.
CA   Biological process.
//
ID   Biomineralization.
AC   KW-0091
DE   Protein involved in the process by which mineral crystals are
DE   deposited in an organized fashion in the matrix (either cellular or
DE   extracellular) of living organisms. Such process give rise to
DE   inorganic-based structures such as bone, tooth, ivory, shells,
DE   cuticles, corals or bacterial magnetosomes.
GO   GO:0031214; biomineral tissue development
HI   Biological process: Biomineralization.
CA   Biological process.
//
ID   Biotin.
AC   KW-0092
DE   Protein which contains at least one biotin as prosthetic group or
DE   cofactor (e.g. some carboxylases and decarboxylases, and biotin
DE   carboxyl carrier protein) or which binds biotin, like avidin. Biotin
DE   is a water-soluble vitamin (member of the B complex vitamins)
DE   essential for fatty acid biosynthesis, catabolism, and it acts as a
DE   growth factor for many cells.
SY   Biopeiderm; Coenzyme R; Vitamin B7; Vitamin B8; Vitamin H.
HI   Ligand: Biotin.
CA   Ligand.
//
ID   Biotin biosynthesis.
AC   KW-0093
DE   Protein involved in the synthesis of biotin, a prosthetic group for
DE   some carboxylase and decarboxylase enzymes. This water-soluble vitamin
DE   is essential for fatty acid biosynthesis, catabolism, and it acts as a
DE   growth factor for many cells.
SY   Biopeiderm anabolism; Biopeiderm biosynthesis;
SY   Biopeiderm biosynthetic process; Biopeiderm formation;
SY   Biopeiderm synthesis; Biotin anabolism; Biotin biosynthetic process;
SY   Biotin formation; Biotin synthesis; Coenzyme R anabolism;
SY   Coenzyme R biosynthesis; Coenzyme R biosynthetic process;
SY   Coenzyme R formation; Coenzyme R synthesis; Vitamin B7 anabolism;
SY   Vitamin B7 biosynthetic process; Vitamin B7 formation;
SY   Vitamin B7 synthesis; Vitamin B8 anabolism;
SY   Vitamin B8 biosynthetic process; Vitamin B8 formation;
SY   Vitamin B8 synthesis; Vitamin H anabolism; Vitamin H biosynthesis;
SY   Vitamin H biosynthetic process; Vitamin H formation;
SY   Vitamin H synthesis.
GO   GO:0009102; biotin biosynthetic process
HI   Biological process: Biotin biosynthesis.
CA   Biological process.
//
ID   Blood coagulation.
AC   KW-0094
DE   Protein involved in blood clotting, a complex enzymatic cascade in
DE   which the activated form of one factor catalyzes the activation of the
DE   next factor. Both the extrinsic clotting pathway, induced by a damaged
DE   surface, and the intrinsic pathway, induced by a trauma, converge in a
DE   final common pathway to form cross-linked fibrin clots.
GO   GO:0007596; blood coagulation
HI   Biological process: Hemostasis; Blood coagulation.
CA   Biological process.
//
ID   Blood coagulation cascade activating toxin.
AC   KW-1204
DE   Toxin which activates the blood coagulation cascade, which leads to
DE   the production of fibrin clots. Blood coagulation activating toxins
DE   include a variety of snake venom proteases.
HI   Molecular function: Toxin; Hemostasis impairing toxin; Blood coagulation cascade activating toxin.
CA   Molecular function.
//
ID   Blood coagulation cascade inhibiting toxin.
AC   KW-1203
DE   Toxin which inhibits the blood coagulation cascade, which leads to the
DE   production of fibrin clots. Blood coagulation inhibiting toxins
DE   include a variety of snake venom proteases.
HI   Molecular function: Toxin; Hemostasis impairing toxin; Blood coagulation cascade inhibiting toxin.
CA   Molecular function.
//
ID   Blood group antigen.
AC   KW-0095
DE   Protein belonging to the set of cell surface antigens found chiefly,
DE   but not solely, on blood cells. More than fifteen different blood
DE   group systems are recognised in humans. In most cases the antigenic
DE   determinant resides in the carbohydrate chains of membrane
DE   glycoproteins or glycolipids.
SY   Agglutinogen.
HI   Molecular function: Blood group antigen.
CA   Molecular function.
//
ID   Bradykinin receptor impairing toxin.
AC   KW-1222
DE   Toxin which interferes with the function of the bradykinin receptor
DE   (BDKR). BDKRs are G-protein coupled receptors whose principal ligand
DE   is the 9-amino acid peptide bradykinin.
HI   Molecular function: Toxin; G-protein coupled receptor impairing toxin; Bradykinin receptor impairing toxin.
CA   Molecular function.
//
ID   Bradyzoite.
AC   KW-1136
DE   Protein expressed in the bradyzoite stage, a latent, slowly growing
DE   and cyst-forming stage in the life cycle of coccidians (e.g.
DE   Toxoplasmy). Encysted bradyzoites promote chronic infection and
DE   widespread dissemination of the parasite.
HI   Developmental stage: Bradyzoite.
CA   Developmental stage.
//
ID   Branched-chain amino acid biosynthesis.
AC   KW-0100
DE   Protein involved in the synthesis of the essential aliphatic branched-
DE   chain amino acids leucine (Leu), isoleucine (Ile) and valine (Val).
SY   Branched-chain amino acid anabolism;
SY   Branched-chain amino acid biosynthetic process;
SY   Branched-chain amino acid formation;
SY   Branched-chain amino acid synthesis.
GO   GO:0009082; branched-chain amino acid biosynthetic process
HI   Biological process: Amino-acid biosynthesis; Branched-chain amino acid biosynthesis.
CA   Biological process.
//
ID   Branched-chain amino acid catabolism.
AC   KW-0101
DE   Protein involved in the degradation of the branched-chain amino acids
DE   leucine (Leu), isoleucine (Ile) and valine (Val).
SY   Branched-chain amino acid breakdown;
SY   Branched-chain amino acid catabolic process;
SY   Branched-chain amino acid degradation.
GO   GO:0009083; branched-chain amino acid catabolic process
HI   Biological process: Branched-chain amino acid catabolism.
CA   Biological process.
//
ID   Brassinosteroid biosynthesis.
AC   KW-1069
DE   Protein involved in the synthesis of brassinosteroids, a class of
DE   steroid plant hormones. Brassinosteroids are involved in numerous
DE   plant processes, such as cell expansion and elongation (in association
DE   with auxin), vascular differentiation, pollen elongation and pollen
DE   tube formation and protection to plants during chilling and drought
DE   stress. Brassinolide is the first isolated brassinosteroid.
SY   Brassinosteroid anabolism; Brassinosteroid biosynthetic process;
SY   Brassinosteroid formation; Brassinosteroid synthesis.
GO   GO:0016132; brassinosteroid biosynthetic process
HI   Biological process: Lipid metabolism; Lipid biosynthesis; Steroid biosynthesis; Brassinosteroid biosynthesis.
CA   Biological process.
//
ID   Brassinosteroid signaling pathway.
AC   KW-1070
DE   Protein involved in the brassinosteroid (BR) signaling pathway (e.g.
DE   transport and signal transduction) that regulates many aspects of
DE   plant growth and development including cell expansion and elongation
DE   (in association with auxin), vascular differentiation and pollen
DE   elongation and pollen tube formation. Also involved in plants
DE   protection during chilling and drought stress. BRs are
DE   polyhydroxysteroid phytohormones and over 70 BR compounds have been
DE   isolated in plants. Brassinolide was the first BR isolated from
DE   Brassica napus and remains one of the most active BR.
SY   BR signalling pathway; BR-signalling pathway.
GO   GO:0009742; brassinosteroid mediated signaling pathway
HI   Biological process: Brassinosteroid signaling pathway.
CA   Biological process.
//
ID   Bromination.
AC   KW-0102
DE   Protein which is posttranslationally modified by the attachment of at
DE   least one bromine.
SY   Bromated; Brominated.
HI   PTM: Bromination.
CA   PTM.
//
ID   Bromodomain.
AC   KW-0103
DE   Protein containing at least one bromodomain. The bromodomain is a
DE   conserved region, approximately 70 amino acids, characteristic for a
DE   class of regulatory proteins. It mediates interactions with proteins
DE   that are necessary for transcriptional activation.
HI   Domain: Bromodomain.
CA   Domain.
//
ID   Brugada syndrome.
AC   KW-0992
DE   Protein which, if defective, causes Brugada syndrome, a heart disease
DE   characterized by an electrocardiogram pattern showing ST segment
DE   elevation in right precordial leads (V1 to V3), incomplete or complete
DE   right bundle branch block, and ventricular tachyarrhythmia. In some
DE   cases, tachycardia does not terminate spontaneously and it may
DE   degenerate into ventricular fibrillation and lead to sudden death.
SY   BRS.
HI   Disease: Brugada syndrome.
CA   Disease.
//
ID   c-di-GMP.
AC   KW-0973
DE   Protein whose function is c-di-GMP-dependent or which catalyzes its
DE   hydrolysis. c-di-GMP is the abbreviation for cyclic di-GMP, bis-(3'-
DE   5') cyclic diguanylic acid. It acts as a bacterial second messenger.
SY   3',5'-cyclic di-GMP; 3'-5'-cyclic diguanylic acid;
SY   Bis-(3'-5') cyclic diguanylic acid;
SY   Bis-(3'-5')-cyclic dimeric guanosine monophosphate; c-(Gpgp); cGpGp;
SY   Cyclic-bis(3',5')diguanylic acid; Cyclic diguanylate;
SY   Cyclic diguanylic acid; Cyclic dinucleotide di-GMP;
SY   Guanosine 3',5'-cyclic monophosphate.
HI   Ligand: c-di-GMP.
CA   Ligand.
//
ID   Cadmium.
AC   KW-0104
DE   Protein which binds at least one cadmium atom, or protein whose
DE   function is cadmium-dependent. Cadmium is a heavy metal, chemical
DE   symbol Cd.
SY   Cadmium ion; Cd.
HI   Ligand: Cadmium.
WW   https://www.webelements.com/webelements/elements/text/Cd/
CA   Ligand.
//
ID   Cadmium resistance.
AC   KW-0105
DE   Protein that confers, on bacteria and other microorganisms, the
DE   ability to withstand the transition metal cadmium (Cd).
SY   Cadmium ion resistance; Cd resistance; Resistance to cadmium;
SY   Resistance to cadmium ion; Resistance to Cd.
GO   GO:0046686; response to cadmium ion
HI   Biological process: Cadmium resistance.
CA   Biological process.
//
ID   Calcium.
AC   KW-0106
DE   Protein which binds at least one calcium atom, or protein whose
DE   function is calcium-dependent. Calcium is a metal, chemical symbol Ca.
DE   Calcium is essential for a variety of bodily functions, such as
DE   neurotransmission, muscle contraction and proper heart function.
SY   Ca; Calcium ion.
HI   Ligand: Calcium.
WW   https://www.webelements.com/calcium/
CA   Ligand.
//
ID   Calcium channel.
AC   KW-0107
DE   Cell membrane glycoprotein forming a channel in a biological membrane
DE   selectively permeable to calcium ions. Calcium is essential for a
DE   variety of bodily functions, such as neurotransmission, muscle
DE   contraction and proper heart function.
SY   Ca channel; Calcium ion channel.
GO   GO:0005262; calcium channel activity
GO   GO:0070588; calcium ion transmembrane transport
HI   Ligand: Calcium; Calcium channel.
HI   Biological process: Transport; Ion transport; Calcium transport; Calcium channel.
HI   Molecular function: Ion channel; Calcium channel.
CA   Molecular function.
//
ID   Calcium channel impairing toxin.
AC   KW-0108
DE   Protein which interferes with the function of calcium channels which
DE   are membrane proteins forming a channel in a biological membrane
DE   selectively permeable to calcium ions. They are found in various
DE   venoms from snakes, scorpions and spiders.
SY   Ca channel inhibitor; Calcium ion channel inhibitor.
GO   GO:0005246; calcium channel regulator activity
HI   Molecular function: Toxin; Ion channel impairing toxin; Calcium channel impairing toxin.
CA   Molecular function.
//
ID   Calcium transport.
AC   KW-0109
DE   Protein involved in the transport of calcium ions. Calcium is
DE   essential for a variety of bodily functions, such as
DE   neurotransmission, muscle contraction and proper heart function.
SY   Calcium ion transport; Ca transport.
GO   GO:0006816; calcium ion transport
HI   Ligand: Calcium; Calcium transport.
HI   Biological process: Transport; Ion transport; Calcium transport.
CA   Biological process.
//
ID   Calcium-activated potassium channel impairing toxin.
AC   KW-1221
DE   Protein which interferes with the function of calcium-activated
DE   potassium channels (KCa) which are membrane proteins forming a channel
DE   in a biological membrane selectively permeable to potassium ions and
DE   gated by intracellular calcium. They are mostly found in snake and
DE   scorpion venoms.
HI   Molecular function: Toxin; Ion channel impairing toxin; Potassium channel impairing toxin; Calcium-activated potassium channel impairing toxin.
CA   Molecular function.
//
ID   Calcium/phospholipid-binding.
AC   KW-0111
DE   Protein which contains at least one binding site for calcium and
DE   phospholipid. For example, proteins with annexin repeats, of which a
DE   pair may form one binding site for calcium and phospholipid, or some
DE   proteins with C2 domains.
SY   Calcium-dependent phospholipid binding.
GO   GO:0005544; calcium-dependent phospholipid binding
HI   Ligand: Calcium; Calcium/phospholipid-binding.
CA   Ligand.
//
ID   Calmodulin-binding.
AC   KW-0112
DE   Protein which binds at least one calmodulin, an ubiquitous small
DE   calcium-binding protein. Its binding to proteins may cause a
DE   conformational change which either activates or inactivates their
DE   function.
GO   GO:0005516; calmodulin binding
HI   Molecular function: Calmodulin-binding.
CA   Molecular function.
//
ID   Calvin cycle.
AC   KW-0113
DE   Protein involved in the cycle of biochemical reactions responsible for
DE   photosynthetic CO(2) fixation in many photosynthetic bacteria and in
DE   the stroma of plant chloroplasts. The energy and reducing power for
DE   this reaction are provided by the ATP and NADPH produced during the
DE   light reactions of photosynthesis. The Calvin cycle is the only
DE   photosynthetic pathway in C3 plants. In C4 and CAM plants CO(2) is
DE   initially fixed into other organic acids that are subsequently
DE   decarboxylated to release CO(2) to the Calvin cycle. Non-
DE   photosynthetic organism (e.g. Rhizobium) also use the cycle to fix
DE   CO(2).
SY   Calvin-Benson cycle; Reductive pentose phosphate cycle.
GO   GO:0019253; reductive pentose-phosphate cycle
HI   Biological process: Calvin cycle.
CA   Biological process.
//
ID   cAMP.
AC   KW-0114
DE   Protein whose function is cAMP-dependent or which catalyzes its
DE   hydrolysis. cAMP is the abbreviation for cyclic AMP, adenosine 3',5'-
DE   cyclic monophosphate, the first second messenger hormone signaling
DE   system to be characterised. It is generated from ATP by the action of
DE   adenyl cyclase that is coupled to hormone receptors by G proteins.
DE   cAMP activates a specific protein kinase and is inactivated by
DE   phosphodiesterase action giving 5'AMP.
SY   3',5'-cyclic AMP; Adenosine-3',5'-cyclic-monophosphate;
SY   Adenosine 3',5'-phosphate; Cyclic adenylic acid; Cyclic AMP.
HI   Ligand: cAMP.
CA   Ligand.
//
ID   cAMP biosynthesis.
AC   KW-0115
DE   Protein involved in the synthesis of cAMP. cAMP is the abbreviation
DE   for cyclic AMP, adenosine 3',5'-cyclic monophosphate.
SY   3',5'-cyclic AMP anabolism; 3',5'-cyclic AMP biosynthesis;
SY   3',5'-cyclic AMP biosynthetic process; 3',5'-cyclic AMP formation;
SY   3',5'-cyclic AMP synthesis;
SY   Adenosine-3',5'-cyclic-monophosphate anabolism;
SY   Adenosine-3',5'-cyclic-monophosphate biosynthesis;
SY   Adenosine-3',5'-cyclic-monophosphate biosynthetic process;
SY   Adenosine-3',5'-cyclic-monophosphate formation;
SY   Adenosine-3',5'-cyclic-monophosphate synthesis;
SY   Adenosine 3',5'-phosphate anabolism;
SY   Adenosine 3',5'-phosphate biosynthesis;
SY   Adenosine 3',5'-phosphate biosynthetic process;
SY   Adenosine 3',5'-phosphate formation;
SY   Adenosine 3',5'-phosphate synthesis; cAMP anabolism;
SY   cAMP biosynthetic process; cAMP formation; cAMP synthesis;
SY   Cyclic adenylic acid anabolism; Cyclic adenylic acid biosynthesis;
SY   Cyclic adenylic acid biosynthetic process;
SY   Cyclic adenylic acid formation; Cyclic adenylic acid synthesis;
SY   Cyclic AMP anabolism; Cyclic AMP biosynthesis;
SY   Cyclic AMP biosynthetic process; Cyclic AMP formation;
SY   Cyclic AMP synthesis.
GO   GO:0006171; cAMP biosynthetic process
HI   Biological process: cAMP biosynthesis.
CA   Biological process.
//
ID   cAMP-binding.
AC   KW-0116
DE   Protein which binds at least one cAMP. cAMP is the abbreviation for
DE   cyclic AMP, adenosine 3',5'-cyclic monophosphate.
SY   3',5'-cyclic AMP-binding;
SY   Adenosine-3',5'-cyclic-monophosphate-binding;
SY   Adenosine 3',5'-phosphate-binding; Cyclic adenylic acid-binding;
SY   Cyclic AMP-binding.
GO   GO:0030552; cAMP binding
HI   Ligand: cAMP; cAMP-binding.
HI   Ligand: Nucleotide-binding; cAMP-binding.
CA   Ligand.
//
ID   Cap snatching.
AC   KW-1157
DE   Protein involved in cap snatching, a process in which a cellular mRNA
DE   is cleaved few nucleotides after the 5'cap. The resulting 10- to 13-
DE   nucleotides long capped fragment serve as primer for the initiation of
DE   viral mRNA synthesis. Cap snatching is used by negative stranded RNA
DE   virus which do not encode a guanylyl transferase, like influenza or
DE   hantaviruses.
GO   GO:0075526; cap snatching
HI   Biological process: Cap snatching.
CA   Biological process.
//
ID   Capsid decoration protein.
AC   KW-1232
DE   Viral decoration protein attached to the capsid of some prokaryotic
DE   viruses. Decoration proteins are located on the outermost surface of
DE   the capsid and are involved in stabilizing the head structure.
GO   GO:0098021; viral capsid, decoration
HI   Cellular component: Virion; Capsid protein; Capsid decoration protein.
CA   Cellular component.
//
ID   Capsid inner membrane protein.
AC   KW-1231
DE   Viral protein part of the inner membrane of the capsid, a lipid
DE   bilayer contained inside the virion capsid.
GO   GO:0039641; viral inner membrane
HI   Cellular component: Virion; Capsid inner membrane protein.
CA   Cellular component.
//
ID   Capsid protein.
AC   KW-0167
DE   Structural protein which is part of the complex forming the protective
DE   shell around the nucleic acids of the virus. In prokaryotic viruses,
DE   this closed shell is also referred to as the head.
SY   Coat protein; Head protein.
GO   GO:0019028; viral capsid
HI   Cellular component: Virion; Capsid protein.
CA   Cellular component.
//
ID   Capsule.
AC   KW-0875
DE   Protein which is part of a capsule, the protective structure
DE   surrounding some bacteria or fungi. The bacterial capsule is a layer
DE   of material, usually polysaccharide, attached to the cell wall
DE   possibly via covalent attachments to either phospholipid or lipid-A
DE   molecules. It has several functions: promote bacterial adhesion to
DE   surfaces or interaction with other organisms; act as a permeability
DE   barrier, as a defense mechanism against phagocytosis and/or as a
DE   nutrient reserve. Among pathogens, capsule formation often correlates
DE   with pathogenicity. The fungal capsule is an extracellular layer which
DE   lies outside the cell wall and it is usually composed of
DE   polysaccharides. It protects the cell from different environmental
DE   dangers such as phagocytosis, dessication, etc.
GO   GO:0042603; capsule
HI   Cellular component: Secreted; Capsule.
CA   Cellular component.
//
ID   Capsule biogenesis/degradation.
AC   KW-0972
DE   Protein which is involved in the formation, organization, maintenance
DE   or degradation of the capsule. The capsule is a protective structure
DE   surrounding some bacteria or fungi. The bacterial capsule is a layer
DE   of material, usually polysaccharide, attached to the cell wall
DE   possibly via covalent attachments to either phospholipid or lipid-A
DE   molecules. The fungal capsule is an extracellular layer which lies
DE   outside the cell wall and it is usually composed of polysaccharides.
HI   Biological process: Capsule biogenesis/degradation.
CA   Biological process.
//
ID   Carbohydrate metabolism.
AC   KW-0119
DE   Protein participating in biochemical reactions in which carbohydrates
DE   are involved. Carbohydrate is a general term for sugars and related
DE   compounds with the general formula Cn(H2O)n. The smallest are
DE   monosaccharides (e.g. glucose); polysaccharides (e.g. starch,
DE   cellulose, glycogen) can be large and vary in length.
SY   Carbohydrate metabolic process; Sugar metabolic process;
SY   Sugar metabolism.
GO   GO:0005975; carbohydrate metabolic process
HI   Biological process: Carbohydrate metabolism.
CA   Biological process.
//
ID   Carbon dioxide fixation.
AC   KW-0120
DE   Protein involved in the process of carbon dioxide fixation, e.g.
DE   incorporation of carbon dioxide into carbohydrates by photosynthetic
DE   organisms or formation of oxaloacetate from pyruvate.
SY   Carbon utilization by fixation of carbon dioxide;
SY   Carbon utilization by fixation of CO(2);
SY   Carbon utilization by fixation of CO2; CO(2) fixation; CO2 fixation.
GO   GO:0015977; carbon fixation
HI   Biological process: Carbon dioxide fixation.
CA   Biological process.
//
ID   Carboxypeptidase.
AC   KW-0121
DE   Protein that hydrolyzes a C-terminal peptide bond in polypeptide
DE   chains.
GO   GO:0004180; carboxypeptidase activity
HI   Molecular function: Hydrolase; Protease; Carboxypeptidase.
CA   Molecular function.
//
ID   Carboxysome.
AC   KW-1282
DE   Protein located in or on the carboxysome, bacterial microcompartments
DE   in which ribulose bisphosphate carboxylase (RuBisCO)-mediated CO(2)
DE   fixation occurs. The cytoplasmic polyhedral inclusion bodies are
DE   surrounded by a thin protein coat. Found in cyanobacteria and some
DE   chemoautotrophs, they enhance autotrophic CO(2) fixation in air by
DE   increasing the CO(2) concentration around RuBisCO, thus reducing its
DE   reaction with O(2), a competing substrate. They contain carbonic
DE   anhydrase as part of the CO(2) concentration mechanism.
GO   GO:0031470; carboxysome
HI   Cellular component: Bacterial microcompartment; Carboxysome.
CA   Cellular component.
//
ID   Cardiomyopathy.
AC   KW-0122
DE   Protein which, if defective, causes cardiomyopathy, a chronic disorder
DE   which affects the heart muscle causing a reduced pumping function. It
DE   is a major cause of morbidity and mortality.
HI   Disease: Cardiomyopathy.
CA   Disease.
//
ID   Cardiotoxin.
AC   KW-0123
DE   Protein which has a poisonous or deleterious effect upon the heart or
DE   other parts of the cardiovascular system.
HI   Molecular function: Toxin; Cardiotoxin.
CA   Molecular function.
//
ID   Carnitine biosynthesis.
AC   KW-0124
DE   Protein involved in the biosynthesis of carnitine (L-3-hydroxy-4,
DE   N,N,N-trimethylaminobutyrate), an essential metabolite with a number
DE   of indispensable roles in intermediary metabolism.
SY   3-hydroxy-4-(trimethylammonio)butanoate anabolism;
SY   3-hydroxy-4-(trimethylammonio)butanoate biosynthesis;
SY   3-hydroxy-4-(trimethylammonio)butanoate biosynthetic process;
SY   3-hydroxy-4-(trimethylammonio)butanoate formation;
SY   3-hydroxy-4-(trimethylammonio)butanoate synthesis;
SY   Carnitine anabolism; Carnitine biosynthetic process;
SY   Carnitine formation; Carnitine synthesis;
SY   Gamma-trimethyl-hydroxybutyrobetaine anabolism;
SY   Gamma-trimethyl-hydroxybutyrobetaine biosynthesis;
SY   Gamma-trimethyl-hydroxybutyrobetaine biosynthetic process;
SY   Gamma-trimethyl-hydroxybutyrobetaine formation;
SY   Gamma-trimethyl-hydroxybutyrobetaine synthesis.
GO   GO:0045329; carnitine biosynthetic process
HI   Biological process: Carnitine biosynthesis.
CA   Biological process.
//
ID   Carotenoid biosynthesis.
AC   KW-0125
DE   Protein involved in the synthesis of carotenoids, a group of orange,
DE   yellow, red, purple or brown pigments in plants, bacteria and some
DE   fungi. Carotenoids, which comprise the carotenes and the xanthophylls,
DE   are long polyisoprenoid molecules having conjugated double bonds
DE   enabling light absorbtion.
SY   Carotenoid anabolism; Carotenoid biosynthetic process;
SY   Carotenoid formation; Carotenoid synthesis.
GO   GO:0016117; carotenoid biosynthetic process
HI   Biological process: Carotenoid biosynthesis.
CA   Biological process.
//
ID   Cataract.
AC   KW-0898
DE   Protein which, if defective, causes cataract, a partial or complete
DE   ocular opacity that affects the crystalline lens or its capsule,
DE   leading to impaired vision or blindness. The many types of cataract
DE   are classified by their morphology (size, shape, location) or etiology
DE   (cause and time of occurrence). Cataracts may occur as an isolated
DE   anomaly, as part of generalized ocular developmental defects, or as a
DE   component of a multisystem disorder.
HI   Disease: Cataract.
CA   Disease.
//
ID   Catecholamine biosynthesis.
AC   KW-0127
DE   Protein involved in the synthesis of catecholamines, which are amine
DE   derivatives of catechol (2-hydroxyphenol). They are synthesized from
DE   the amino acid tyrosine (Tyr) in sympathetic-nerve terminals and in
DE   the adrenal gland. Catecholamines act as hormones or neuro-
DE   transmitters, e.g. adrenaline, noradrenaline and dopamine.
SY   Catecholamine anabolism; Catecholamine biosynthetic process;
SY   Catecholamine formation; Catecholamine synthesis.
GO   GO:0042423; catecholamine biosynthetic process
HI   Biological process: Catecholamine biosynthesis.
CA   Biological process.
//
ID   Catecholamine metabolism.
AC   KW-0128
DE   Protein participating the biochemical reactions in which
DE   catecholamines are involved. Catecholamines are amine derivatives of
DE   catechol (2-hydroxyphenol). They are synthesized from the amino acid
DE   tyrosine (Tyr) in sympathetic-nerve terminals and in the adrenal
DE   gland. Catecholamines act as hormones or neuro-transmitters, e.g.
DE   adrenaline, noradrenaline and dopamine.
SY   Catecholamine metabolic process.
GO   GO:0006584; catecholamine metabolic process
HI   Biological process: Catecholamine metabolism.
CA   Biological process.
//
ID   Caveolin-mediated endocytosis of virus by host.
AC   KW-1166
DE   Viral protein involved in virus internalization by the host cell via
DE   caveolae, which are specialized lipid rafts that form 50-70 nm flask-
DE   shaped invaginations of the cell membrane. Caveolins form the
DE   structural backbone of caveolae. Internalization via caveolae is not a
DE   constitutive process but only occurs upon cell stimulation.Endocytic
DE   caveolae deliver their viral content to early endosomes. Caveolae
DE   represent a low capacity but highly regulated pathway. This pathway is
DE   used by viruses including HPV-31, BK virus, NDV, RSV, Coxsackie B
DE   virus, SV40, murine polyomavirus, and Echovirus 1.
SY   Virion endocytosis by caveolin-coated vesicle.
GO   GO:0075513; caveolin-mediated endocytosis of virus by host cell
HI   Biological process: Virus entry into host cell; Viral penetration into host cytoplasm; Virus endocytosis by host; Caveolin-mediated endocytosis of virus by host.
CA   Biological process.
//
ID   CBS domain.
AC   KW-0129
DE   Protein containing at least one CBS domain, a conserved domain found
DE   in a wide range of proteins, which is named after cystathionine beta-
DE   synthase (CBS), an enzyme that contains 2 copies of this domain.
HI   Domain: CBS domain.
CA   Domain.
//
ID   Cell adhesion.
AC   KW-0130
DE   Protein involved in the adherence of cells to other cells or to a
DE   matrix. Cell adhesion is mediated by cell surface proteins.
GO   GO:0007155; cell adhesion
HI   Biological process: Cell adhesion.
CA   Biological process.
//
ID   Cell adhesion impairing toxin.
AC   KW-1217
DE   Toxin which interferes with the adherence of cells to other cells or
DE   to a matrix. Cell adhesion impairing toxins are mostly found in venom
DE   of snakes.
HI   Molecular function: Toxin; Cell adhesion impairing toxin.
CA   Molecular function.
//
ID   Cell cycle.
AC   KW-0131
DE   Protein involved in the complex series of events by which the cell
DE   duplicates its contents and divides into two. The eukaryotic cell
DE   cycle can be divided in four phases termed G1 (first gap period), S
DE   (synthesis, phase during which the DNA is replicated), G2 (second gap
DE   period) and M (mitosis). The prokaryotic cell cycle typically involves
DE   a period of growth followed by DNA replication, partition of
DE   chromosomes, formation of septum and division into two similar or
DE   identical daughter cells.
GO   GO:0007049; cell cycle
HI   Biological process: Cell cycle.
CA   Biological process.
//
ID   Cell division.
AC   KW-0132
DE   Protein involved in the separation of one cell into two daughter
DE   cells. In eukaryotic cells, cell division includes the nuclear
DE   division (mitosis) and the subsequent cytoplasmic division
DE   (cytokinesis).
GO   GO:0051301; cell division
HI   Biological process: Cell cycle; Cell division.
CA   Biological process.
//
ID   Cell inner membrane.
AC   KW-0997
DE   Protein found in or associated with the prokaryotic cell inner
DE   membrane, a selectively permeable membrane which separates the
DE   cytoplasm from the periplasm in prokaryotes with 2 membranes.
SY   Inner membrane.
GO   GO:0005886; plasma membrane
HI   Cellular component: Membrane; Cell membrane; Cell inner membrane.
CA   Cellular component.
//
ID   Cell junction.
AC   KW-0965
DE   Protein found in or associated with a cell junction, a cell-cell or
DE   cell-extracellular matrix contact within a tissue of a multicellular
DE   organism, especially abundant in epithelia. In vertebrates, there are
DE   three major types of cell junctions: anchoring junctions (e.g.
DE   adherens junctions), communicating junctions (e.g. gap junctions) and
DE   occluding junctions (e.g. tight junctions).
GO   GO:0070161; anchoring junction
HI   Cellular component: Cell junction.
WW   https://www.ncbi.nlm.nih.gov/bookshelf/br.fcgi?book=mboc4&part=A3469
CA   Cellular component.
//
ID   Cell membrane.
AC   KW-1003
DE   Protein found in or associated with the cytoplasmic membrane, a
DE   selectively permeable membrane which separates the cytoplasm from its
DE   surroundings. Known as the cell inner membrane in prokaryotes with 2
DE   membranes.
SY   Cytoplasmic membrane; Plasmalemma; Plasma membrane.
GO   GO:0005886; plasma membrane
HI   Cellular component: Membrane; Cell membrane.
CA   Cellular component.
//
ID   Cell outer membrane.
AC   KW-0998
DE   Protein found in or associated with the prokaryotic cell outer
DE   membrane, a selectively permeable membrane which separates the
DE   prokaryotic periplasm from its surroundings. Traditionally only Gram-
DE   negative bacteria were thought of as having an outer membrane, but
DE   recent work has shown some Actinobacteria, including Mycobacterium
DE   tuberculosis, as well as at least 1 archaea (Ignicoccus hospitalis)
DE   have a cell outer membrane.
SY   Outer membrane.
GO   GO:0009279; cell outer membrane
HI   Cellular component: Membrane; Cell outer membrane.
CA   Cellular component.
//
ID   Cell projection.
AC   KW-0966
DE   Protein found in or associated with a cell protrusion such as
DE   pseudopodium, filopodium, lamellipodium, growth cone, flagellum,
DE   acrosome or axon, or bacterial comet tail. These membrane-
DE   cytoskeleton-coupled processes are involved in many biological
DE   functions, such as cell motility, cancer-cell invasion, endocytosis,
DE   phagocytosis, exocytosis, pathogen infection, neurite extension and
DE   cytokinesis.
SY   Cell protrusion.
GO   GO:0042995; cell projection
HI   Cellular component: Cell projection.
CA   Cellular component.
//
ID   Cell shape.
AC   KW-0133
DE   Protein involved in the formation and maintenance of the cell shape,
DE   the physical dimensions of a cell. In most plants, algae, bacteria and
DE   fungi the cell wall is responsible for the shape of the cells.
GO   GO:0008360; regulation of cell shape
HI   Biological process: Cell shape.
CA   Biological process.
//
ID   Cell wall.
AC   KW-0134
DE   Protein found in or associated with a complex and rigid layer
DE   surrounding the cell. Cell walls are found in bacteria, archaea,
DE   fungi, plants, and algae. The cell wall envelopes the inner or plasma
DE   membrane in all bacteria and is surrounded by the outer membrane in
DE   bacteria with 2 membranes (Gram-negative). Bacterial cell walls
DE   contain peptidoglycan whereas those of archaea do not. Some archaea
DE   may contain pseudopeptidoglycan, which is composed of N-
DE   acetyltalosaminuronic acid, instead of N-acetyl muramic acid in
DE   peptidoglycan. The plant cell wall is made of fibrils of cellulose
DE   embedded in a matrix of several other kinds of polymers such as pectin
DE   and lignin. Algal cell walls are usually composed of cellulose,
DE   glycoproteins, sporopollenin, calcium and various polysaccharides such
DE   as manosyl, xylanes, alginic acid. Diatom cell walls (or frustules)
DE   contain silica. The cell wall plays a role in cell shape, cell
DE   stability and development, and protection against environmental
DE   dangers.
GO   GO:0005618; cell wall
HI   Cellular component: Secreted; Cell wall.
CA   Cellular component.
//
ID   Cell wall biogenesis/degradation.
AC   KW-0961
DE   Protein which is involved in the formation, organization, maintenance
DE   or degradation of the cell wall. The cell wall is an extracellular
DE   layer outside the cell membrane which protects the cell against
DE   mechanical damage, osmotic strength and which determines the cell
DE   shape. It is prominent in most plants, algae, bacteria and fungi.
GO   GO:0071555; cell wall organization
HI   Biological process: Cell wall biogenesis/degradation.
CA   Biological process.
//
IC   Cellular component.
AC   KW-9998
DE   Keywords assigned to proteins because they are found in a specific
DE   cellular or extracellular component.
//
ID   Cellulose biosynthesis.
AC   KW-0135
DE   Protein involved in the synthesis of cellulose, a linear polymer of
DE   (1-4)-beta-linked D-glucose subunits. It is the most abundant cell-
DE   wall and structural polysaccharide in plants and it is also found in
DE   some lower invertebrates. Cellulose is the major component of wood and
DE   thus of paper. Cotton is the purest natural form of cellulose. As a
DE   raw material, it forms the basis for many derivatives used in
DE   chromatography, ion exchange materials, explosives manufacturing and
DE   pharmaceutical preparations.
SY   Cellulose anabolism; Cellulose biosynthetic process;
SY   Cellulose formation; Cellulose synthesis.
GO   GO:0030244; cellulose biosynthetic process
HI   Biological process: Cellulose biosynthesis.
CA   Biological process.
//
ID   Cellulose degradation.
AC   KW-0136
DE   Protein involved in the conversion of cellulose into D-glucose.
DE   Cellulose is the most abundant cell-wall and structural polysaccharide
DE   in plants and it is also found in some lower invertebrates. Cellulose
DE   is the major component of wood and thus of paper. Cotton is the purest
DE   natural form of cellulose. As a raw material, it forms the basis for
DE   many derivatives used in chromatography, ion exchange materials,
DE   explosives manufacturing and pharmaceutical preparations.
SY   Cellulose breakdown; Cellulose catabolic process;
SY   Cellulose catabolism.
GO   GO:0030245; cellulose catabolic process
HI   Biological process: Carbohydrate metabolism; Polysaccharide degradation; Cellulose degradation.
CA   Biological process.
//
ID   Centromere.
AC   KW-0137
DE   Protein which binds centromeres or which is required for the assembly
DE   and movement of centromeres. Centromeres are the regions of replicated
DE   eukaryotic chromosomes where the two chromatids are joined together.
SY   Chromosome pericentric region.
GO   GO:0000775; chromosome, centromeric region
HI   Cellular component: Centromere.
CA   Cellular component.
//
ID   CF(0).
AC   KW-0138
DE   Protein component of the F-type ATP synthase complex CF(0) or protein
DE   involved in its assembly. F-type ATPases consist of the two complex
DE   components CF(0), the membrane proton channel, and CF(1), the
DE   catalytic core.
SY   ATPase membrane proton channel;
SY   Proton-transporting ATP synthase complex coupling factor F(0).
GO   GO:0045263; proton-transporting ATP synthase complex, coupling factor F(o)
HI   Biological process: Transport; Ion transport; Hydrogen ion transport; CF(0).
HI   Cellular component: CF(0).
CA   Cellular component.
//
ID   CF(1).
AC   KW-0139
DE   Protein component of the F-type ATP synthase complex CF(1) or protein
DE   involved in its assembly. F-type ATPases consist of the two complex
DE   components CF(0), the membrane proton channel, and CF(1), the
DE   catalytic core.
SY   ATPase catalytic core;
SY   Proton-transporting ATP synthase complex catalytic core F(1).
GO   GO:0045261; proton-transporting ATP synthase complex, catalytic core F(1)
HI   Biological process: ATP synthesis; CF(1).
HI   Cellular component: CF(1).
CA   Cellular component.
//
ID   cGMP.
AC   KW-0140
DE   Protein whose function is cGMP-dependent or which catalyzes its
DE   hydrolysis. cGMP is the abbreviation for cyclic GMP, guanosine 3',5'-
DE   cyclic monophosphate. It acts as a second messenger.
SY   3',5'-cyclic GMP; Cyclic GMP; Cyclic guanylic acid;
SY   Guanosine 3',5'-cyclic monophosphate; Guanosine 3',5'-phosphate.
HI   Ligand: cGMP.
CA   Ligand.
//
ID   cGMP biosynthesis.
AC   KW-0141
DE   Protein involved in the synthesis of cGMP. cGMP is the abbreviation
DE   for cyclic GMP, guanosine 3',5'-cyclic monophosphate.
SY   3',5'-cyclic GMP anabolism; 3',5'-cyclic GMP biosynthesis;
SY   3',5'-cyclic GMP biosynthetic process; 3',5'-cyclic GMP formation;
SY   3',5'-cyclic GMP synthesis; cGMP anabolism; cGMP biosynthetic process;
SY   cGMP formation; cGMP synthesis; Cyclic GMP anabolism;
SY   Cyclic GMP biosynthesis; Cyclic GMP biosynthetic process;
SY   Cyclic GMP formation; Cyclic GMP synthesis;
SY   Cyclic guanylic acid anabolism; Cyclic guanylic acid biosynthesis;
SY   Cyclic guanylic acid biosynthetic process;
SY   Cyclic guanylic acid formation; Cyclic guanylic acid synthesis;
SY   Guanosine-3',5'-cyclic-monophosphate anabolism;
SY   Guanosine-3',5'-cyclic-monophosphate biosynthesis;
SY   Guanosine-3',5'-cyclic-monophosphate biosynthetic process;
SY   Guanosine-3',5'-cyclic-monophosphate formation;
SY   Guanosine-3',5'-cyclic-monophosphate synthesis;
SY   Guanosine 3',5'-phosphate anabolism;
SY   Guanosine 3',5'-phosphate biosynthesis;
SY   Guanosine 3',5'-phosphate biosynthetic process;
SY   Guanosine 3',5'-phosphate formation;
SY   Guanosine 3',5'-phosphate synthesis.
GO   GO:0006182; cGMP biosynthetic process
HI   Biological process: cGMP biosynthesis.
CA   Biological process.
//
ID   cGMP-binding.
AC   KW-0142
DE   Protein which binds at least one cGMP. cGMP is the abbreviation for
DE   cyclic GMP, guanosine 3',5'-cyclic monophosphate.
SY   3',5'-cyclic GMP-binding; Cyclic GMP-binding;
SY   Cyclic guanylic acid-binding;
SY   Guanosine 3',5'-cyclic monophosphate-binding;
SY   Guanosine 3',5'-phosphate-binding.
GO   GO:0030553; cGMP binding
HI   Ligand: cGMP; cGMP-binding.
HI   Ligand: Nucleotide-binding; cGMP-binding.
CA   Ligand.
//
ID   Chaperone.
AC   KW-0143
DE   Protein which is transiently involved in the noncovalent folding,
DE   assembly and/or disassembly of other polypeptides or RNA molecules,
DE   including any transport and oligomerisation processes they may
DE   undergo, and the refolding and reassembly of protein and RNA molecules
DE   denatured by stress. Though involved in these processes, chaperones
DE   are not an integral part of these functioning molecules. Also used for
DE   metallochaperones, which function to provide a metal directly to
DE   target proteins while protecting this metal from scavengers.
HI   Molecular function: Chaperone.
CA   Molecular function.
//
ID   Charcot-Marie-Tooth disease.
AC   KW-0144
DE   Protein which, if defective, causes Charcot-Marie-Tooth disease (CMT),
DE   a heterogeneous group of hereditary motor and sensory neuropathies
DE   (HMSN) characterized by distal muscular atrophy and weakness, hollow
DE   feet, absent or diminished deep-tendon reflexes and impaired
DE   sensation. CMT is classified into two major classes. CMT type 1
DE   includes demyelinating neuropathies that are characterized by nerve
DE   conductance velocities (NCVs) less than 38m/s and segmental
DE   demyelination and remyelination; CMT type 2 includes axonal
DE   neuropathies that are characterized by normal or mildly reduced NCVs
DE   and chronic axonal degeneration and regeneration.
HI   Disease: Neuropathy; Charcot-Marie-Tooth disease.
CA   Disease.
//
ID   Chemotaxis.
AC   KW-0145
DE   Protein involved in the movement of a cell, or organism, along a
DE   concentration gradient of a chemotactic agent, such as a protein which
DE   causes, mediates or responds to chemotaxis. Chemotactic molecules such
DE   as sugars, peptides, cell metabolites, cell-wall or membrane lipids
DE   bind to cell surface receptors and trigger activation of intracellular
DE   signaling pathways, as well as remodeling of the cytoskeleton through
DE   the activation or inhibition of various actin-binding proteins.
GO   GO:0006935; chemotaxis
HI   Biological process: Chemotaxis.
CA   Biological process.
//
ID   Chitin degradation.
AC   KW-0146
DE   Protein involved in the breakdown of chitin, a linear polysaccharide
DE   consisting of (1->4)-beta-linked D-glucosamine residues, most of which
DE   are N-acetylated.
SY   Chitin breakdown; Chitin catabolic process; Chitin catabolism.
GO   GO:0006032; chitin catabolic process
HI   Biological process: Carbohydrate metabolism; Polysaccharide degradation; Chitin degradation.
CA   Biological process.
//
ID   Chitin-binding.
AC   KW-0147
DE   Protein which binds chitin, a linear polysaccharide consisting of
DE   (1->4)-beta-linked D-glucosamine residues, most of which are N-
DE   acetylated. The 30-43 amino acids long chitin-binding domain contains
DE   several conserved glycine and cysteines residues. The conserved
DE   cysteines form disulfide bonds. Chitin-binding domains have been found
DE   in plant, fungal and bacterial proteins.
GO   GO:0008061; chitin binding
HI   Ligand: Chitin-binding.
CA   Ligand.
//
ID   Chloride.
AC   KW-0868
DE   Protein which binds at least one chloride, or protein whose function
DE   is chloride-dependent. Chloride is a negatively-charged ion, which is
DE   abbreviated Cl(-).
SY   Chloride anion; Chloride ion; Cl-.
HI   Ligand: Chloride.
WW   https://www.webelements.com/chlorine/
CA   Ligand.
//
ID   Chloride channel.
AC   KW-0869
DE   Protein which is part of an anion channel found in the plasma membrane
DE   and in intracellular membranes. These channels are permeable for
DE   various anions, such as iodide, bromide, but also for nitrates,
DE   phosphates and even negatively charged amino acids. They are called
DE   chloride channels, because chloride is the most abundant anion and the
DE   predominant permeating species in all organisms. They have been
DE   classified according to their gating mechanisms, which may depend on
DE   changes in the transmembrane electric field (voltage-dependent/gated
DE   chloride channels, e.g. ClC family), on a protein kinase/nucleotide
DE   mediated mechanism (CFTR), an increase in intracellular calcium
DE   (calcium activated chloride channels, e.g. CaCC), cell swelling
DE   (volume-regulated anion channels, e.g. VRAC) or binding of a ligand,
DE   e.g. glycine or - aminobutyric acid (GABA) activated channels. In
DE   contrast with cation channels, they are not involved in the initiation
DE   or spread of excitation, but in the regulation of excitability in
DE   nerve and muscle. They also participate in many housekeeping
DE   processes, such as volume regulation, pH regulation in organelles,
DE   electrogenesis and control of synaptic activity. The chloride channels
DE   are crucial for transepithelial transport and the control of water
DE   flow, and often provide unexpected permeation pathways for a large
DE   variety of anions.
SY   Chloride anion channel; Chloride ion channel; Cl- channel.
GO   GO:0005254; chloride channel activity
GO   GO:0006821; chloride transport
GO   GO:0034707; chloride channel complex
HI   Biological process: Transport; Ion transport; Chloride channel.
HI   Molecular function: Ion channel; Chloride channel.
HI   Ligand: Chloride; Chloride channel.
CA   Molecular function.
//
ID   Chloride channel impairing toxin.
AC   KW-1265
DE   Protein which interferes with the function of chloride channels which
DE   are membrane proteins forming a channel in a biological membrane
DE   selectively permeable to chloride ions. Chloride channels include
DE   voltage-gated chloride channels (ClC), ionotropic GABA receptors
DE   (ligand-gated ion channels activated by GABA) and CFTR ion channels
DE   (ABC transporter-class ion channels). Toxins that target these
DE   channels are found in venom of several species including scorpions and
DE   snakes.
SY   Chloride anion channel inhibitor; Chloride ion channel inhibitor;
SY   Cl- channel inhibitor.
HI   Molecular function: Toxin; Ion channel impairing toxin; Chloride channel impairing toxin.
CA   Molecular function.
//
ID   Chlorophyll.
AC   KW-0148
DE   Protein which interacts with chlorophyll, the major light-absorbing
DE   pigment in most oygenic green organisms. Higher plants contain
DE   chlorophyll a and chlorophyll b which are magnesium-porphyrin
DE   complexes esterified to a long hydrophobic terpenoid side chain (the
DE   alcohol phytol).
GO   GO:0016168; chlorophyll binding
HI   Ligand: Chromophore; Chlorophyll.
CA   Ligand.
//
ID   Chlorophyll biosynthesis.
AC   KW-0149
DE   Protein involved in the synthesis of chlorophylls. These
DE   photosynthetic pigments are magnesium-porphyrin complexes with a long
DE   hydrophobic terpenoid side chain (the alcohol phytol). Angiosperms
DE   have only a light-dependent pathway for chlorophyll biosynthesis,
DE   other oxygenic organisms seem to have both the light-dependent and the
DE   light-independent pathways. Non-oxygenic organisms, which make
DE   bacteriochlorophyll, only have a light-independent pathway.
SY   Chlorophyll anabolism; Chlorophyll biosynthetic process;
SY   Chlorophyll formation; Chlorophyll synthesis.
GO   GO:0015995; chlorophyll biosynthetic process
HI   Biological process: Chlorophyll biosynthesis.
CA   Biological process.
//
ID   Chlorophyll catabolism.
AC   KW-0881
DE   Protein involved in the degradation of chlorophylls. These
DE   photosynthetic pigments are magnesium-porphyrin complexes with a long
DE   hydrophobic terpenoid side chain (the alcohol phytol).
SY   Chlorophyll breakdown; Chlorophyll catabolic process;
SY   Chlorophyll degradation.
GO   GO:0015996; chlorophyll catabolic process
HI   Biological process: Chlorophyll catabolism.
CA   Biological process.
//
ID   Chloroplast.
AC   KW-0150
DE   Protein encoded by or localized in the chloroplast, the most common
DE   form of plastid, found in all photosynthetic organisms except
DE   glaucophyte algae. In green (photosynthesizing) tissue they house the
DE   machinery necessary for photosynthesis and CO(2) fixation. They are
DE   surrounded by between 2 and 4 membranes and contain thylakoids in
DE   green tissue.
GO   GO:0009507; chloroplast
HI   Cellular component: Plastid; Chloroplast.
CA   Cellular component.
//
ID   Chlorosome.
AC   KW-0151
DE   Photosynthetic light-harvesting complexes found in green bacteria.
DE   Chlorosomes are sac-like organelles appressed to the cytoplasmic
DE   membrane of the cell membrane.
GO   GO:0046858; chlorosome
HI   Biological process: Photosynthesis; Chlorosome.
HI   Cellular component: Chlorosome.
CA   Cellular component.
//
ID   Cholesterol biosynthesis.
AC   KW-0152
DE   Protein involved in the synthesis of cholesterol, the major sterol of
DE   higher animals. It is a component of cell membranes, especially of the
DE   plasma membrane.
SY   Cholesterol anabolism; Cholesterol biosynthetic process;
SY   Cholesterol formation; Cholesterol synthesis.
GO   GO:0006695; cholesterol biosynthetic process
HI   Biological process: Lipid metabolism; Steroid metabolism; Sterol metabolism; Cholesterol metabolism; Cholesterol biosynthesis.
HI   Biological process: Lipid metabolism; Lipid biosynthesis; Steroid biosynthesis; Sterol biosynthesis; Cholesterol biosynthesis.
HI   Biological process: Lipid metabolism; Steroid metabolism; Sterol metabolism; Sterol biosynthesis; Cholesterol biosynthesis.
CA   Biological process.
//
ID   Cholesterol metabolism.
AC   KW-0153
DE   Protein which participates in the biochemical reactions where
DE   cholesterol is involved, including transport. Cholesterol is the major
DE   sterol of higher animals and an important component of cell membranes,
DE   especially of the plasma membrane.
SY   Cholesterol metabolic process.
GO   GO:0008203; cholesterol metabolic process
HI   Biological process: Lipid metabolism; Steroid metabolism; Sterol metabolism; Cholesterol metabolism.
CA   Biological process.
//
ID   Chondrogenesis.
AC   KW-0891
DE   Protein involved in chondrogenesis, the mechanism of cartilage
DE   formation. Chondrogenesis proceeds through determination of cells and
DE   their aggregation into prechondrogenic condensations, differentiation
DE   into chondrocytes, and later maturation. The formation of the long
DE   bones requires a cartilage template.
SY   Cartilage biogenesis; Cartilage biosynthesis; Cartilage development;
SY   Cartilage formation.
GO   GO:0051216; cartilage development
HI   Biological process: Chondrogenesis.
CA   Biological process.
//
ID   Chromate resistance.
AC   KW-0155
DE   Protein that enables bacteria and other microorganisms to withstand
DE   chromate, a salt of chromic acid (H2CrO4).
SY   Resistance to chromate.
GO   GO:0046687; response to chromate
HI   Biological process: Chromate resistance.
CA   Biological process.
//
ID   Chromatin regulator.
AC   KW-0156
DE   Protein controlling the opening or closing of chromatin.
GO   GO:0006325; chromatin organization
HI   Molecular function: Chromatin regulator.
CA   Molecular function.
//
ID   Chromophore.
AC   KW-0157
DE   Protein which interacts with one or more chromophores. A chromophore
DE   absorbs and transmits light energy. Originally it was used for visibly
DE   colored molecules, but it applies also to UV- and IR-absorbing
DE   molecules.
HI   Ligand: Chromophore.
CA   Ligand.
//
ID   Chromoplast.
AC   KW-0957
DE   Protein found in or associated with a chromoplast, a plastid
DE   containing pigments other than chlorophyll. Found in flower, petals
DE   and fruit.
GO   GO:0009509; chromoplast
HI   Cellular component: Plastid; Chromoplast.
CA   Cellular component.
//
ID   Chromosomal rearrangement.
AC   KW-0160
DE   Protein which can be altered by a structural chromosomal
DE   rearrangement. Structural rearrangements result from chromosome
DE   breakage, followed by reconstitution in an abnormal combination.
DE   Classes of chromosomal rearrangements include: deletions,
DE   duplications, insertions, inversions, translocations and
DE   transpositions.
HI   Coding sequence diversity: Chromosomal rearrangement.
CA   Coding sequence diversity.
//
ID   Chromosome.
AC   KW-0158
DE   Protein which is associated with chromosomal DNA, including histones,
DE   protamines and high mobility group proteins.
SY   Chromosomal protein.
GO   GO:0005694; chromosome
HI   Cellular component: Chromosome.
CA   Cellular component.
//
ID   Chromosome partition.
AC   KW-0159
DE   Protein involved in chromosome partition, the process by which newly
DE   replicated plasmids and chromosomes are actively segregated prior to
DE   cell division. E.g., par and soj which contribute to efficient
DE   chromosome partitioning by serving functions analogous to centromeres
DE   (i.e. pairing or positioning of sister chromosomes).
SY   Chromosome segregation.
GO   GO:0007059; chromosome segregation
HI   Biological process: Chromosome partition.
CA   Biological process.
//
ID   Chronic granulomatous disease.
AC   KW-0161
DE   Protein which, if defective, causes chronic granulomatous disease
DE   (CGD), a disease characterized by the failure of activated phagocytes
DE   to generate superoxide.
SY   CGD.
HI   Disease: Chronic granulomatous disease.
CA   Disease.
//
ID   Chylomicron.
AC   KW-0162
DE   Protein component of the chylomicrons or involved in their catabolism.
DE   Chylomicrons are the largest lipoprotein complexes with the lowest
DE   protein-to-lipid ratio. They are present in the blood or lymph and
DE   transport exogenous (dietary) cholesterol, triacylglycerols and other
DE   lipids from the intestine to the liver or to the adipose tissue.
GO   GO:0042627; chylomicron
HI   Cellular component: Chylomicron.
CA   Cellular component.
//
ID   Ciliopathy.
AC   KW-1186
DE   Protein which, if defective, causes any one of a group of diseases
DE   associated with either abnormal formation or function of cilia.
DE   Ciliopathies cover a large spectrum of often overlapping phenotypes
DE   ranging from relatively mild, tissue-restricted pathologies to severe
DE   defects in multiple organs. Although cilia play important roles in
DE   many tissues, the predominantly affected organs are kidney, eye, liver
DE   and brain. Clinical features typically include retinal degeneration,
DE   renal disease and cerebral anomalies. Additional manifestations
DE   include congenital fibrocystic diseases of the liver, diabetes,
DE   obesity and skeletal dysplasias. Ciliary dysfunction in the embryo may
DE   cause randomization of left-right body asymmetry or situs inversus, as
DE   well as severe malformations leading to embryonic lethality.
HI   Disease: Ciliopathy.
CA   Disease.
//
ID   Cilium.
AC   KW-0969
DE   Protein found in or associated with a cilium, a cell surface
DE   projection found at the surface of a large proportion of eukaryotic
DE   cells. The two basic types of cilia, motile (alternatively named
DE   flagella) and non-motile, collectively perform a wide variety of
DE   functions broadly encompassing cell/fluid movement and sensory
DE   perception. Their most prominent structural component is the axoneme
DE   which consists of nine doublet microtubules, with all motile cilia
DE   - except those at the embryonic node - containing an additional
DE   central pair of microtubules. The axonemal microtubules of all cilia
DE   nucleate and extend from a basal body, a centriolar structure most
DE   often composed of a radial array of nine triplet microtubules. In most
DE   cells, basal bodies associate with cell membranes and cilia are
DE   assembled as 'extracellular' membrane-enclosed compartments.
SY   Cilia.
GO   GO:0005929; cilium
HI   Cellular component: Cell projection; Cilium.
WW   https://ciliome.com
CA   Cellular component.
//
ID   Cilium biogenesis/degradation.
AC   KW-0970
DE   Protein which is involved in the formation, organization, maintenance
DE   and degradation of the cilium, a cell surface projection found at the
DE   surface of a large proportion of eukaryotic. Their most prominent
DE   structural component is the axoneme which consists of nine doublet
DE   microtubules, with all motile cilia - except those at the embryonic
DE   node - containing an additional central pair of microtubules.
GO   GO:0030030; cell projection organization
HI   Biological process: Cilium biogenesis/degradation.
CA   Biological process.
//
ID   Citrate utilization.
AC   KW-0163
DE   Protein which allows the utilization of the 6-carbon tricarboxylic
DE   acid citrate as a sole source of carbon and energy.
GO   GO:0006101; citrate metabolic process
HI   Biological process: Citrate utilization.
CA   Biological process.
//
ID   Citrullination.
AC   KW-0164
DE   Protein which is posttranslationally modified by the deimination of
DE   one or more arginine residues.
SY   2-amino-5-(carbamoylamino)pentanoic acid; Citrulline;
SY   N5-carbamoylornithine.
HI   PTM: Citrullination.
CA   PTM.
//
ID   Clathrin- and caveolin-independent endocytosis of virus by host.
AC   KW-1167
DE   Viral protein involved in virus internalization into the host cell via
DE   endocytic pathways that involve neither clathrin nor caveolins. These
DE   pathways can be further defined by their dependency on various
DE   molecules such as cholesterol, DNM2/Dynamin-2, small GTPases or
DE   tyrosine kinase and possibly involve non-caveolar lipid rafts.
DE   Clathrin- and caveolin-independent pathways are used by viruses
DE   including poliovirus, human rhinovirus 14, lymphocytic
DE   choriomeningitis virus, murine norovirus-1 and SV40.
SY   Non-clathrin/non caveolin-mediated endocytosis by host.
GO   GO:0019065; receptor-mediated endocytosis of virus by host cell
HI   Biological process: Virus entry into host cell; Viral penetration into host cytoplasm; Virus endocytosis by host; Clathrin- and caveolin-independent endocytosis of virus by host.
CA   Biological process.
//
ID   Clathrin-mediated endocytosis of virus by host.
AC   KW-1165
DE   Viral protein involved in virus internalization by the host cell via
DE   clathrin-mediated endocytosis. In response to an internalization
DE   signal, clathrin is assembled on the inside face of the cell membrane
DE   to form characteristic invaginations or clathrin coated pits that
DE   pinch off through the action of DNM1/Dynamin-1 or DNM2/Dynamin-2. The
DE   virus bound to its host cell receptor is internalized into clathrin-
DE   coated vesicles (CCV). Endocytic CCV deliver their viral content to
DE   early endosomes. The endosomal acidic pH and/or receptor binding
DE   usually induces structural modifications of the virus surface proteins
DE   that lead to penetration of the endosomal membrane via fusion or
DE   permeabilization mechanisms.
SY   Virion endocytosis by clathrin-coated vesicle.
GO   GO:0075512; clathrin-dependent endocytosis of virus by host cell
HI   Biological process: Virus entry into host cell; Viral penetration into host cytoplasm; Virus endocytosis by host; Clathrin-mediated endocytosis of virus by host.
CA   Biological process.
//
ID   Cleavage on pair of basic residues.
AC   KW-0165
DE   Protein which is posttranslationally modified by the cleavage on at
DE   least one pair of basic residues, in order to release one or more
DE   mature active peptides (such as hormones).
HI   PTM: Cleavage on pair of basic residues.
CA   PTM.
//
ID   Coated pit.
AC   KW-0168
DE   Protein which is a component of a coated pit. Coated pits are regions
DE   of the donor membrane where the assembly of the vesicle coat take
DE   place. The coat assembles from soluble protomers such as coat protein
DE   complex-I and coat protein complex-II. The components of the coat
DE   often define the intracellular sorting station, and contribute to both
DE   membrane deformation and local movement of the resulting transport
DE   intermediate following scission. During the first steps of the
DE   vesicle-mediated membrane transport, coated pits are internalized to
DE   form coated vesicles which transport proteins between distinct
DE   membrane-bound organelles.
GO   GO:0005905; clathrin-coated pit
HI   Cellular component: Membrane; Coated pit.
CA   Cellular component.
//
ID   Cobalamin.
AC   KW-0846
DE   Protein which contains at least one cobalamin as cofactor, e.g.
DE   methylmalonyl-CoA mutase, or which binds and/or transports cobalamin,
DE   such as intrinsic factor or transcobalamins. Cobalamin, which is
DE   synthesized by microorganisms, has equatorial sites occupied by a
DE   tetrapyrrol ring structure (corrin ring) with a cobalt(III) ion in the
DE   center, one axial site occupied by an intramolecularly-bound
DE   dimethylbenzimidazole and the other axial site occupied by a number of
DE   different ligands such as water (aquacobalamin), cyanide
DE   (cyanocobalamin=vitamin B12), glutathione (glutathionylcobalamin),
DE   5'deoxyadenosine (adenosylcobalamin=coenzyme B12) or a methyl group
DE   (methylcobalamin). It is a prosthetic group of certain mammalian
DE   enzymes, where it is essential for the normal maturation and
DE   development of erythrocytes. A deficiency in the diet or more
DE   frequently the failure to absorb the vitamin give rise to pernicious
DE   anemia.
SY   Vitamin B12.
GO   GO:0031419; cobalamin binding
HI   Ligand: Cobalt; Cobalamin.
CA   Ligand.
//
ID   Cobalamin biosynthesis.
AC   KW-0169
DE   Protein involved in the synthesis of cobalamin. Cobalamin, which is
DE   synthesized by microorganisms, has equatorial sites occupied by a
DE   modified porphyrin ring system, with two of the four pyrrol rings
DE   fused directly (without an intervening methine bridge). The modified
DE   porphyrin system binds a cobalt(III) ion in the center, and this is
DE   called a corrin ring system. One axial site is occupied usually by an
DE   intramolecularly-bound dimethylbenzimidazole nucleotide and the other
DE   axial site is occupied by a number of different ligands such as water
DE   (aquacobalamin), cyanide (cyanocobalamine=vitamin B12), glutathione
DE   (glutathionylcobalamine), 5'deoxyadenosine
DE   (adenosylcobalamine=coenzyme B12) or a methyl group (methylcobalamin).
DE   Vitamin B12, for instance, is a prosthetic group of certain mammalian
DE   enzymes, where it is essential for the normal maturation and
DE   development of erythrocytes. A deficiency in the diet or more
DE   frequently the failure to absorb the vitamin B12 give rise to
DE   pernicious anemia.
SY   Cobalamin anabolism; Cobalamin biosynthetic process;
SY   Cobalamin formation; Cobalamin synthesis; Vitamin B12 anabolism;
SY   Vitamin B12 biosynthesis; Vitamin B12 biosynthetic process;
SY   Vitamin B12 formation; Vitamin B12 synthesis.
GO   GO:0009236; cobalamin biosynthetic process
HI   Biological process: Cobalamin biosynthesis.
CA   Biological process.
//
ID   Cobalt.
AC   KW-0170
DE   Protein which binds at least one cobalt atom, or protein whose
DE   function is cobalt-dependent. Cobalt is a metallic element, chemical
DE   symbol Co.
SY   Co; Cobalt cation; Cobalt ion; Co cation; Co ion.
HI   Ligand: Cobalt.
WW   https://www.webelements.com/cobalt/
CA   Ligand.
//
ID   Cobalt transport.
AC   KW-0171
DE   Protein involved in the transport of the trace element cobalt, which
DE   is a component of vitamin B12.
SY   Cobalt cation transport; Cobalt ion transport; Co cation transport;
SY   Co ion transport; Co transport.
GO   GO:0006824; cobalt ion transport
HI   Ligand: Cobalt; Cobalt transport.
HI   Biological process: Transport; Ion transport; Cobalt transport.
CA   Biological process.
//
ID   Cockayne syndrome.
AC   KW-0172
DE   Protein which, if defective, causes Cockayne's syndrome (CS), an
DE   autosomal recessive disease characterized by UV-sensitive skin
DE   (without pigmentation abnormalities), neurological dysfunction due to
DE   demyelination of neurons and calcification of basal ganglia
DE   (psychomotor retardation, deafness, optic atrophy, retinal
DE   pigmentation and hyperreflexes) and dysmorphic dwarfism (immature
DE   sexual development and microcephaly).
SY   Cockayne's syndrome; CS.
HI   Disease: Cockayne syndrome.
CA   Disease.
//
IC   Coding sequence diversity.
AC   KW-9997
DE   Keywords assigned to proteins because their sequences can differ, due
DE   to differences in the coding sequences such as polymorphisms, RNA-
DE   editing, alternative splicing.
//
ID   Coenzyme A biosynthesis.
AC   KW-0173
DE   Protein involved in the biosynthetic pathway leading from pantothenate
DE   to coenzyme A (CoA). CoA has two halves in phosphodiester linkage: a
DE   3',5'-ADP residue, and 4-phosphopantetheine. The phosphopantetheine
DE   moiety is itself composed of three structural entities: a branched
DE   chain dihydroxy acid in amide linkage to a beta-alanyl residue, which
DE   is in turn linked to a cysteamide containing the reactive thiol.
DE   Coenzyme A functions as a carrier of acetyl and acyl groups and is
DE   essential for numerous biosynthetic, energy-yielding, and degradative
DE   metabolic pathways. Acetyl-CoA is the common cellular currency for
DE   acetyl transfers.
SY   CoA anabolism; CoA biosynthesis; CoA biosynthetic process;
SY   CoA formation; CoASH anabolism; CoASH biosynthesis;
SY   CoASH biosynthetic process; CoASH formation; CoASH synthesis;
SY   CoA synthesis; Coenzyme A anabolism; Coenzyme A biosynthetic process;
SY   Coenzyme A formation; Coenzyme A synthesis.
GO   GO:0015937; coenzyme A biosynthetic process
HI   Biological process: Coenzyme A biosynthesis.
CA   Biological process.
//
ID   Coenzyme M biosynthesis.
AC   KW-0174
DE   Protein involved in the biosynthesis of coenzyme M. Coenzyme M (2-
DE   mercaptoethanesulfonic acid) is the smallest known organic cofactor.
DE   CoM serves as a methyl group carrier in key reactions within the
DE   pathway of methane formation from C1 precursors. In the alkene
DE   metabolism pathway, it is involved in aliphatic epoxyde carboxylation.
SY   2-mercaptoethanesulfonic acid anabolism;
SY   2-mercaptoethanesulfonic acid biosynthesis;
SY   2-mercaptoethanesulfonic acid biosynthetic process;
SY   2-mercaptoethanesulfonic acid formation;
SY   2-mercaptoethanesulfonic acid synthesis; Coenzyme M anabolism;
SY   Coenzyme M biosynthetic process; Coenzyme M formation;
SY   Coenzyme M synthesis; CoM anabolism; CoM biosynthesis;
SY   CoM biosynthetic process; CoM formation; CoM synthesis.
GO   GO:0019295; coenzyme M biosynthetic process
HI   Biological process: Coenzyme M biosynthesis.
CA   Biological process.
//
ID   Coiled coil.
AC   KW-0175
DE   Protein which contains at least one coiled coil domain, a type of
DE   secondary structure composed of two or more alpha helices which
DE   entwine to form a cable structure. In proteins, the helical cables
DE   serve a mechanical role in forming stiff bundles of fibres.
SY   Heptad repeat pattern.
HI   Domain: Coiled coil.
CA   Domain.
//
ID   Collagen.
AC   KW-0176
DE   Protein which contains one or more collagen-like domain. Collagen is a
DE   fibrous protein found in vertebrates, the major element of skin, bone,
DE   tendon, cartilage, blood vessels and teeth. It forms insoluble fibres
DE   of high tensile strength and which contains the unusual amino acids
DE   hyroxyproline and hydroxylysine. It is rich in glycine but lacks
DE   cysteine and tryptophan, and has an unusually regular amino-acid
DE   domain.
GO   GO:0005581; collagen trimer
HI   Domain: Collagen.
CA   Domain.
//
ID   Collagen degradation.
AC   KW-0177
DE   Protein involved in the degradation of collagen, a family of fibrous
DE   proteins found in skin, bones, teeth, cartilage and other tissues of
DE   vertebrates.
SY   Collagen breakdown; Collagen catabolic process; Collagen catabolism.
GO   GO:0030574; collagen catabolic process
HI   Biological process: Collagen degradation.
CA   Biological process.
//
ID   Competence.
AC   KW-0178
DE   Protein involved in competence, the state in which a cell or organism
DE   is able to take up DNA and become genetically transformed.
GO   GO:0030420; establishment of competence for transformation
HI   Biological process: Competence.
CA   Biological process.
//
ID   Complement activation lectin pathway.
AC   KW-1018
DE   Protein involved in the complement activation lectin pathway which
DE   activates the proteins of the complement system. This pathway can be
DE   activated mainly by mannose-binding lectin (MBL) interacting with
DE   carbohydrate structures on microbial surfaces and by ficolins with
DE   different fine carbohydrate binding specificity.
SY   Lectin complement pathway; Lectin pathway.
GO   GO:0001867; complement activation, lectin pathway
HI   Biological process: Immunity; Innate immunity; Complement activation lectin pathway.
CA   Biological process.
//
ID   Complement alternate pathway.
AC   KW-0179
DE   Protein involved in the complement alternate pathway which activates
DE   the proteins of the complement system. This pathway can be activated
DE   by IgA immune complexes, but also by bacterial endotoxins,
DE   polysaccharides and cell walls, without participation of an antigen-
DE   antibody reaction.
SY   Alternate complement pathway;
SY   Complement activation alternative pathway; Properdin system.
GO   GO:0006957; complement activation, alternative pathway
HI   Biological process: Immunity; Innate immunity; Complement alternate pathway.
CA   Biological process.
//
ID   Complement pathway.
AC   KW-0180
DE   Pathway which activates the proteins of the complement system, a group
DE   of blood proteins of the globulin class involved in the lysis of
DE   foreign cells after they have been coated with antibody, and which
DE   also promote the removal of antibody-coated foreign particles by
DE   phagocytic cells. The pathway proceeds by a cascade reaction of
DE   successive binding and proteolytic cleavage of complement components.
DE   This pathway can be activated by either IgG or IgM binding to an
DE   antigen.
SY   Classical complement pathway; Complement activation classical pathway.
GO   GO:0006958; complement activation, classical pathway
HI   Biological process: Immunity; Innate immunity; Complement pathway.
CA   Biological process.
//
ID   Complement system impairing toxin.
AC   KW-1216
DE   Toxin which interferes with the complement system. These toxins act by
DE   activating, inhibiting, or mimicking proteins of this system. They are
DE   mostly found in snake and spider venoms.
HI   Molecular function: Toxin; Complement system impairing toxin.
CA   Molecular function.
//
ID   Cone-rod dystrophy.
AC   KW-0182
DE   Protein which, if defective, causes cone-rod dystrophy, a disease
DE   where dystrophy of cone-rod cells is characterized by the initial
DE   degeneration of cone photoreceptor cells, thus causing early loss of
DE   visual acuity and color vision, followed by the degeneration of rod
DE   photoreceptor cells and leading to progressive night blindness and
DE   peripheral visual field loss.
HI   Disease: Cone-rod dystrophy.
CA   Disease.
//
ID   Congenital adrenal hyperplasia.
AC   KW-0954
DE   Protein which, if defective, causes congenital adrenal hyperplasia, a
DE   group of inherited disorders of cortisol biosynthesis. Defective
DE   cortisol biosynthesis results in compensatory hypersecretion of
DE   corticotropin with subsequent adrenal hyperplasia and excessive
DE   androgen production. Various clinical types are recognized: "salt
DE   wasting form" is the most severe type, "simple virilizing form" with
DE   normal aldosterone biosynthesis, "non-classic form" or late onset, and
DE   "cryptic form" or asymptomatic.
SY   CAH.
HI   Disease: Congenital adrenal hyperplasia.
CA   Disease.
//
ID   Congenital disorder of glycosylation.
AC   KW-0900
DE   Protein which, if defective, causes a congenital disorder of
DE   glycosylation. In the endoplasmic reticulum (ER) of eukaryotes, N-
DE   linked glycans are first assembled on the lipid carrier dolichyl
DE   pyrophosphate. The GlcNAc(2)Man(9)Glc(3) oligosaccharide is
DE   transferred to selected asparagine residues of nascent polypeptides.
DE   Defects along the biosynthetic pathway of N-glycans are associated
DE   with severe multisystemic syndromes called congenital disorders of
DE   glycosylation (CDG). The characteristic biochemical feature of CDG is
DE   defective glycosylation of glycoproteins due to mutations in genes
DE   required for the biosynthesis of N-linked oligosaccharides. Defects of
DE   the assembly of dolichyl-linked oligosaccharides or their transfer on
DE   to nascent glycoproteins form type I forms of CDG, whereas CDG type II
DE   comprises all defects of the trimming and elongation of N-linked
DE   oligosaccharides.
HI   Disease: Congenital disorder of glycosylation.
CA   Disease.
//
ID   Congenital dyserythropoietic anemia.
AC   KW-1055
DE   Protein which, if defective, causes congenital dyserythropoietic
DE   anemia, a heterogeneous group of disorders characterized by the
DE   occurrence of multinuclear erythroid precursors in the bone marrow,
DE   ineffective erythropoiesis, iron overload and anemia. Various forms
DE   are differentiated mainly by the morphological appearance of the
DE   erythroid precursors.
SY   CDA.
HI   Disease: Hereditary hemolytic anemia; Congenital dyserythropoietic anemia.
CA   Disease.
//
ID   Congenital erythrocytosis.
AC   KW-0985
DE   Protein which, if defective, causes congenital absolute
DE   erythrocytosis, a disorder characterized by expansion of the
DE   erythrocyte compartment in the peripheral blood. Total red cell mass
DE   is increased in the absence of a reduction of plasma volume.
DE   Erythrocytoses are usually divided into primary and secondary forms.
DE   Primary erythrocytoses are due to defects in the erythroid progenitors
DE   and are characterized by low erythropoietin levels. Secondary
DE   erythrocytoses can be due to defects in hypoxia sensing, or to
DE   conditions that cause low tissue oxygen tension with consequent
DE   increase in erythropoietin secretion.
SY   Congenital polycythemia.
HI   Disease: Congenital erythrocytosis.
CA   Disease.
//
ID   Congenital generalized lipodystrophy.
AC   KW-1022
DE   Protein which, if defective, causes congenital generalized
DE   lipodystrophy, a disorder characterized by near complete absence of
DE   adipose tissue from birth. Affected patients manifest insulin
DE   resistance, early onset diabetes mellitus, hypertriglyceridemia,
DE   hepatic steatosis and acanthosis nigricans.
SY   Berardinelli-Seip syndrome; Congenital generalized lipoatrophy.
HI   Disease: Congenital generalized lipodystrophy.
CA   Disease.
//
ID   Congenital hypothyroidism.
AC   KW-0984
DE   Protein which, if defective, causes congenital hypothyroidism, a
DE   condition due to thyroid hormones deficiency, presenting at birth.
DE   Congenital hypothyroidism occurs when the thyroid gland fails to
DE   develop or function properly. In most cases, the thyroid gland is
DE   absent, abnormally located, or severely reduced in size. In the
DE   remaining cases, a normal-sized or enlarged thyroid gland is present,
DE   but production of thyroid hormones is decreased or absent. If
DE   untreated, congenital hypothyroidism can lead to intellectual
DE   disability and growth failure.
HI   Disease: Congenital hypothyroidism.
CA   Disease.
//
ID   Congenital muscular dystrophy.
AC   KW-0912
DE   The congenital muscular dystrophies (CMD) are a heterogeneous group of
DE   disorders characterized by hypotonia, muscle weakness, dystrophic
DE   changes on skeletal muscle biopsy, and joint contractures that present
DE   at birth or during the first 6 months of life. Intellectual disability
DE   with or without structural brain changes is an additional feature of
DE   several CMD syndromes.
HI   Disease: Congenital muscular dystrophy.
CA   Disease.
//
ID   Congenital myasthenic syndrome.
AC   KW-1004
DE   Protein which, if defective, causes congenital myasthenic syndrome.
DE   Congenital myasthenic syndromes constitute a group of inherited
DE   diseases characterized by a congenital defect in neuromuscular
DE   transmission at the neuromuscular junction, including pre-synaptic,
DE   synaptic, and post-synaptic disorders that are not of autoimmune
DE   origin. Congenital myasthenic syndromes are characterized by muscle
DE   weakness affecting the axial and limb muscles (with hypotonia in
DE   early-onset forms), the ocular muscles (leading to ptosis and
DE   ophthalmoplegia), and the facial and bulbar musculature (affecting
DE   sucking and swallowing, and leading to dysphonia). The symptoms
DE   fluctuate and worsen with physical effort.
SY   CMS.
HI   Disease: Congenital myasthenic syndrome.
CA   Disease.
//
ID   Congenital stationary night blindness.
AC   KW-1014
DE   Protein which, if defective, causes congenital stationary night
DE   blindness that is the failure or imperfection of vision at night or in
DE   dim light, with good vision only on bright days.
SY   CSNB.
HI   Disease: Congenital stationary night blindness.
CA   Disease.
//
ID   Conidiation.
AC   KW-0183
DE   Protein involved in conidiation, the production of conidia which are
DE   asexual fungal spores.
SY   Conidia biosynthesis; Conidia formation; Conidium biosynthesis;
SY   Conidium formation.
GO   GO:0048315; conidium formation
HI   Biological process: Sporulation; Conidiation.
CA   Biological process.
//
ID   Conjugation.
AC   KW-0184
DE   Protein involved in the temporary fusion of two gametes or two cells
DE   leading to the transfer of genetic material. This process is seen in
DE   bacteria, ciliate protozoa and certain fungi.
HI   Biological process: Conjugation.
CA   Biological process.
//
ID   Copper.
AC   KW-0186
DE   Protein which binds at least one copper atom, or protein whose
DE   function is copper-dependent. Copper is a trace metallic element,
DE   chemical symbol Cu.
SY   Copper cation; Copper ion; Cu; Cu cation; Cu ion.
HI   Ligand: Copper.
WW   https://www.webelements.com/copper/
CA   Ligand.
//
ID   Copper transport.
AC   KW-0187
DE   Protein involved in the transport of ions of the trace element copper.
SY   Copper cation transport; Copper ion transport; Cu transport.
GO   GO:0006825; copper ion transport
HI   Ligand: Copper; Copper transport.
HI   Biological process: Transport; Ion transport; Copper transport.
CA   Biological process.
//
ID   Copulatory plug.
AC   KW-0188
DE   Protein involded in the formation of the copulatory plug, a plug
DE   composed of a number of proteins which are secreted by the seminal
DE   vesicle under the influence of testosterone. Found in rodents.
GO   GO:0042628; mating plug formation
HI   Cellular component: Copulatory plug.
CA   Cellular component.
//
ID   Corneal dystrophy.
AC   KW-1212
DE   Protein which, if defective, causes corneal dystrophy. The term
DE   corneal dystrophy includes a heterogeneous group of bilateral, primary
DE   alterations of the cornea that are not associated with prior
DE   inflammation or secondary to systemic disease. Most corneal
DE   dystrophies present with variable shaped corneal opacities in a clear
DE   or cloudy cornea and they affect visual acuity to different degrees.
DE   Corneal dystrophies may be present at birth but more frequently
DE   develop during adolescence and progress slowly throughout life.
HI   Disease: Corneal dystrophy.
CA   Disease.
//
ID   Covalent protein-DNA linkage.
AC   KW-0190
DE   Protein covalently attached to a DNA molecule. For example some
DE   viruses contains proteins that are attached to the end of a viral
DE   replicating DNA and which are necessary for DNA replication.
SY   DNA-protein covalent cross-linking.
HI   PTM: Covalent protein-DNA linkage.
CA   PTM.
//
ID   Covalent protein-RNA linkage.
AC   KW-0191
DE   Protein covalently attached to a RNA molecule. For example some
DE   viruses contains proteins that are attached to the end of a viral
DE   replicating RNA and which are necessary for RNA replication.
SY   RNA-protein covalent cross-linking.
GO   GO:0018144; RNA-protein covalent cross-linking
HI   PTM: Covalent protein-RNA linkage.
CA   PTM.
//
ID   Craniosynostosis.
AC   KW-0989
DE   Protein which, if defective, causes craniosynostosis, the premature
DE   closure of one or more cranial sutures which results in an abnormal
DE   head shape. Different types of craniosynostosis are known. All are
DE   characterized by skull deformities, with face and often limb
DE   involvement in the syndromic forms.
SY   Craniostosis.
HI   Disease: Craniosynostosis.
CA   Disease.
//
ID   CRISPR-cas system evasion by virus.
AC   KW-1257
DE   Viral protein that inhibits host defense CRISPR-cas system (Clustered
DE   Regularly Interspaced Short Palindromic Repeats). The CRISPR-cas
DE   system is composed of genomic sensors that allow prokaryotes to
DE   acquire DNA fragments from invading viruses and plasmids into the
DE   CRISPR locus. These stored fragments (called spacers) are transcribed
DE   and processed into small crRNA which are used to destroy matching DNA
DE   in future viral and plasmid invasion. Some prokaryotic viruses express
DE   specific genes that allow them to evade CRISPR-cas system.
GO   GO:0098672; inhibition of host CRISPR-cas system by virus
HI   Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host adaptive immune response by virus; CRISPR-cas system evasion by virus.
CA   Biological process.
//
ID   Crown gall tumor.
AC   KW-0192
DE   Protein involved in crown gall tumor formation, a plant tumor caused
DE   by the bacterium Agrobacterium tumefaciens.
HI   Disease: Crown gall tumor.
CA   Disease.
//
ID   CTQ.
AC   KW-0885
DE   Protein which contains at least one cysteine tryptophylquinone (CTQ)
DE   cross-link modification. CTQ is formed by oxidation of the indole ring
DE   of a tryptophan to form tryptophylquinone followed by covalent cross-
DE   linking with a cysteine residue. In the quinohemoprotein amine
DE   dehydrogenase, CTQ mediates during the catalytic cycle electron
DE   transfer from the substrate to either a copper protein, azurin, or
DE   cytochrome c-550.
SY   Cysteine tryptophylquinone.
HI   PTM: CTQ.
CA   PTM.
//
ID   Cushing syndrome.
AC   KW-1062
DE   Protein which, if defective, causes Cushing syndrome, a condition
DE   caused by prolonged exposure to excess levels of cortisol from
DE   endogenous or exogenous sources. Endogenous Cushing syndrome is due to
DE   excess production of cortisol by the adrenal glands. It may be caused
DE   by pituary hypersecretion of adrenocorticotropic hormone (ACTH),
DE   ectopic ACTH secretion by non-pituary tumors, or may result from
DE   cortisol hypersecretion by adrenal gland tumors (ACTH-independent
DE   Cushing syndrome). Cushing syndrome is clinically characterized by
DE   upper body obesity, osteoporosis, hypertension, diabetes mellitus,
DE   hirsutism, amenorrhea, and excess body fluid.
SY   Cushing's syndrome; Hyperadrenocorticism; Hypercortisolism.
HI   Disease: Cushing syndrome.
CA   Disease.
//
ID   Cuticle.
AC   KW-0193
DE   Protein which is a component of the cuticle, the outer protective
DE   layer produced by epidermal cells that covers the body of many
DE   invertebrates.
GO   GO:0042302; structural constituent of cuticle
HI   Cellular component: Cuticle.
CA   Cellular component.
//
ID   Cyanelle.
AC   KW-0194
DE   Protein encoded by the cyanelle genome or protein located in the
DE   cyanelle. Cyanelles are the plastids of glaucocystophyte algae. They
DE   are surrounded by a double membrane and, in between, a peptidoglycan
DE   wall. The cyanelle genome is of chloroplast size and contains genes
DE   for tRNAs, rRNAs and approx. 150 proteins, which is more than found in
DE   higher plant chloroplast genomes (this feature is also shared by other
DE   primitive plastids). Thylakoid membrane architecture is cyanobacteria-
DE   like. Historically, the term cyanelle is derived from a classification
DE   as endosymbiotic cyanobacteria, and thus is not fully correct.
SY   Cyanoplast; Muroplast.
GO   GO:0009842; cyanelle
HI   Cellular component: Plastid; Cyanelle.
CA   Cellular component.
//
ID   Cyclin.
AC   KW-0195
DE   Protein that belongs to the cyclin family or that contains a cyclin
DE   box-like domain. Cyclins are regulatory subunits of the cyclin-
DE   dependent protein kinases. They form kinase holoenzymes, with distinct
DE   biochemical characteristics and nonredundant biological functions,
DE   which mediate phosphorylation of cellular proteins, including key cell
DE   cycle regulatory molecules. In this way, the kinase holoenzymes
DE   promote the transit of cells through the division cycle. Cyclins
DE   accumulate during interphase of eukaryotic cell cycle and are
DE   destroyed at the end of mitosis.
HI   Molecular function: Cyclin.
CA   Molecular function.
//
ID   Cycloheximide resistance.
AC   KW-0196
DE   Protein that confers, on an organism, the ability to withstand
DE   cycloheximide, an antibiotic produced by Streptomyces griseus, which
DE   inhibits eukaryotic elongation during protein synthesis. The
DE   resistance is often due to mutations that prevent antibiotic binding
DE   to the protein.
SY   Resistance to cycloheximide.
GO   GO:0046898; response to cycloheximide
HI   Biological process: Antibiotic resistance; Cycloheximide resistance.
CA   Biological process.
//
ID   Cysteine biosynthesis.
AC   KW-0198
DE   Protein involved in the synthesis of cysteine, the amino acid with the
DE   highly reactive sulfhydryl group (-SH). It is derived from the amino
DE   acids methionine and serine. Cysteine plays a special role in shaping
DE   some proteins by forming disulfide bonds. In enzymes the unique
DE   reactivity of this group is frequently exploited at the catalytic
DE   site.
SY   Cysteine anabolism; Cysteine biosynthetic process; Cysteine formation;
SY   Cysteine synthesis.
GO   GO:0019344; cysteine biosynthetic process
HI   Biological process: Amino-acid biosynthesis; Cysteine biosynthesis.
CA   Biological process.
//
ID   Cystinuria.
AC   KW-0199
DE   Protein which, if defective, causes cystinuria (CSNU), an autosomal
DE   recessive condition of persistent excessive urinary excretion of
DE   cystine and three other dibasic amino acids: lysine, ornithine, and
DE   arginine. CSNU arises from impaired reabsorption of these amino acids
DE   through the epithelial cells of the renal tubule and gastrointestinal
DE   tract. It is characterized by cystine stones in the kidney, ureter and
DE   bladder. Three clinical types of cystinuria have been described:
DE   cystinuria type-I (CSNU1), type-II (CSNU2) and type-III (CSNU3).
SY   CSNU.
HI   Disease: Cystinuria.
CA   Disease.
//
ID   Cytadherence.
AC   KW-0200
DE   Protein involved in cytadherence, the attachment of mycoplasma to the
DE   epithelium.
GO   GO:0020035; adhesion of symbiont to microvasculature
HI   Biological process: Cytadherence.
CA   Biological process.
//
ID   Cytochrome c-type biogenesis.
AC   KW-0201
DE   Protein involved in the biogenesis of c-type cytochromes. Cytochromes
DE   c are electron-transfer proteins having one or several heme c groups,
DE   bound to the protein by one or, more commonly two, thioether bonds
DE   involving sulphydryl groups of cysteine residues.
SY   Cytochrome c-type formation; Cytochrome c-type synthesis.
GO   GO:0017004; cytochrome complex assembly
HI   Biological process: Cytochrome c-type biogenesis.
CA   Biological process.
//
ID   Cytokine.
AC   KW-0202
DE   Small secreted proteins from higher eukaryotes which affect the
DE   growth, division and functions of other cells, e.g. interleukins,
DE   lymphokines, TNF and interferons. Generally, growth factors are not
DE   classified as cytokines, though TGF is an exception. Chemokines are a
DE   subset of cytokines. They differ from classical hormones in that they
DE   are produced by a number of tissues or cell types rather than by
DE   specialized glands. They generally act locally in a paracrine or
DE   autocrine rather than endocrine manner.
GO   GO:0005125; cytokine activity
GO   GO:0005615; extracellular space
HI   Molecular function: Cytokine.
CA   Molecular function.
//
ID   Cytokinin biosynthesis.
AC   KW-0203
DE   Protein involved in the synthesis of cytokinins, a class of plant
DE   hormones which promote cell division (e.g. kinetin, zeatin, benzyl
DE   adenine). They are also involved in cell growth, cell differentiation
DE   and in other physiological processes.
SY   Cytokinin anabolism; Cytokinin biosynthetic process;
SY   Cytokinin formation; Cytokinin synthesis.
GO   GO:0009691; cytokinin biosynthetic process
HI   Biological process: Cytokinin biosynthesis.
CA   Biological process.
//
ID   Cytokinin signaling pathway.
AC   KW-0932
DE   Protein involved in the cytokinin signaling pathway (i.e. transport or
DE   signal transduction). Cytokinins (i.e. kinetin and zeatin) are defined
DE   more by their biological activity (e.g. inducing cell division in
DE   tissue culture) rather than by structure. These phytohormones are
DE   synthesized in the root apical meristem and transported through the
DE   plant in the xylem sap. Cytokinins are involved in several
DE   physiological processes such as promoting cell division and
DE   chloroplast maturation, regulating cell growth and differentiation,
DE   and monitoring nutrient uptake and senescence. Together with auxin,
DE   they also regulate the cell cycle and tissue morphogenesis.
SY   Cytokinin mediated signaling.
GO   GO:0009736; cytokinin-activated signaling pathway
HI   Biological process: Cytokinin signaling pathway.
CA   Biological process.
//
ID   Cytolysis.
AC   KW-0204
DE   Protein involved in the rupture of cell membranes and loss of
DE   cytoplasm, e.g. exotoxin, cytolysin.
SY   Cell lysis.
GO   GO:0031640; killing of cells of another organism
HI   Biological process: Cytolysis.
CA   Biological process.
//
ID   Cytoplasm.
AC   KW-0963
DE   Protein found in the cytoplasm, the content of a cell within the
DE   plasma membrane and, in eukaryotics cells, surrounding the nucleus.
DE   This three-dimensional, jelly-like lattice interconnects and supports
DE   the other solid structures. The cytosol (the soluble portion of the
DE   cytoplasm outside the organelles) is mostly composed of water and many
DE   low molecular weight compounds. In eukaryotes, the cytoplasm also
DE   contains a network of cytoplasmic filaments (cytoskeleton).
GO   GO:0005737; cytoplasm
HI   Cellular component: Cytoplasm.
CA   Cellular component.
//
ID   Cytoplasmic inwards viral transport.
AC   KW-1176
DE   Viral protein that allows the active transport of viral components
DE   along cytoskeletal filaments toward the intracellular replication
DE   sites during virus entry. Viruses such as adenoviruses, adeno-
DE   associated virus, vaccinia virus, poliovirus, canine parvovirus,
DE   African swine fever virus, rabies virus, human herpes virus 1, foamy
DE   virus are thought to use active intracellular transport of viral
DE   components.
GO   GO:0075606; transport of viral material towards nucleus
HI   Biological process: Virus entry into host cell; Cytoplasmic inwards viral transport.
CA   Biological process.
//
ID   Cytoplasmic vesicle.
AC   KW-0968
DE   Protein found in or associated with cytoplasmic vesicles, which
DE   mediate vesicular transport among the organelles of secretory and
DE   endocytic systems. These transport vesicles are classified by the
DE   identity of the protein coat used in their formation and also by the
DE   cargo they contain, e.g. clathrin-, COPI-, and COPII-coated vesicles,
DE   synaptic vesicles, secretory vesicles, phagosomes, etc.
GO   GO:0031410; cytoplasmic vesicle
HI   Cellular component: Cytoplasmic vesicle.
CA   Cellular component.
//
ID   Cytosine metabolism.
AC   KW-0205
DE   Protein involved in the biochemical reactions with the pyrimidine base
DE   cytosine.
SY   Cytosine metabolic process.
GO   GO:0019858; cytosine metabolic process
HI   Biological process: Cytosine metabolism.
CA   Biological process.
//
ID   Cytoskeleton.
AC   KW-0206
DE   Protein which is a component or which is associated with the
DE   cytoskeleton, a dynamic three-dimensional filamentous structure in the
DE   cytoplasm. The cytoskeleton is both a muscle and a skeleton, and its
DE   roles include maintenance of cell shape, cell movement (in
DE   eukaryotes), cytokinesis, and the organization of the organelles
DE   within the cell. This includes the major components of cytoskeleton;
DE   microfilaments (actin-like proteins), microtubules (tubulin-like
DE   proteins) and intermediate filaments (mostly in eukaryotes) and
DE   prokaryotic MinD-ParA proteins. Originally not thought to exist in
DE   prokaryotes, but now known to have the same functions as in
DE   eukyaryotes.
GO   GO:0005856; cytoskeleton
HI   Cellular component: Cytoplasm; Cytoskeleton.
CA   Cellular component.
//
ID   D-amino acid.
AC   KW-0208
DE   Protein which contains at least one D-amino acid. All of the amino
DE   acids derived from natural proteins are of the L configuration. D-
DE   amino acids are found in nature, especially as components of certain
DE   peptide antibiotics and in walls of certain microorganisms.
HI   PTM: D-amino acid.
CA   PTM.
//
ID   Deafness.
AC   KW-0209
DE   Protein which, if defective, causes a partial or total inability to
DE   hear. The two principal types of deafness are conductive deafness that
DE   results from changes in the middle ear, and nerve or sensorineural
DE   deafness that is caused by damages to the inner ear, the nerve
DE   pathways to the brain, or the area of the brain that receives sound
DE   information.
HI   Disease: Deafness.
CA   Disease.
//
ID   Decarboxylase.
AC   KW-0210
DE   Enzyme that belongs to the lyase family and which catalyzes the
DE   spliting of CO(2) from the carboxylic group of amino acids, beta-keto
DE   acids and alpha-keto acids.
GO   GO:0016831; carboxy-lyase activity
HI   Molecular function: Lyase; Decarboxylase.
CA   Molecular function.
//
ID   Decay of host mRNAs by virus.
AC   KW-1132
DE   Viral protein involved in the degradation of host mRNAs. Viruses have
DE   evolved ways of degrading host mRNAs to inhibit cellular translation.
DE   This global inhibition of cellular protein synthesis serves to ensure
DE   maximal viral gene expression and to evade host immune response. Decay
DE   of host mRNAs can be achieved by endonucleotic RNA cleavage or
DE   associated with PABPC1 nuclear relocalization.
GO   GO:0039595; induction by virus of catabolism of host mRNA
HI   Biological process: Host-virus interaction; Host gene expression shutoff by virus; Eukaryotic host gene expression shutoff by virus; Host mRNA suppression by virus; Decay of host mRNAs by virus.
CA   Biological process.
//
ID   Defensin.
AC   KW-0211
DE   Families of microbicidal and cytotoxic peptides. Defensins have
DE   antibacterial, antifungal and antiviral properties. Defensins kills
DE   cells by forming voltage-regulated multimeric channels in the
DE   susceptible cell's membrane.
GO   GO:0006952; defense response
HI   Molecular function: Antimicrobial; Defensin.
CA   Molecular function.
//
ID   Degradation of host capsule during virus entry.
AC   KW-1238
DE   Virion protein involved in breaking down host cell capsule to reach
DE   the host cell wall, and finally the host cytoplasmic membrane. Many
DE   prokaryotic viruses carry for example glycanase, polysaccharide lyase
DE   or deacetylase activities to specifically digest host capsule.
GO   GO:0098996; disruption of host cell glycocalyx during viral entry
HI   Cellular component: Virion; Degradation of host capsule during virus entry.
HI   Biological process: Virus entry into host cell; Degradation of host cell envelope components during virus entry; Degradation of host capsule during virus entry.
CA   Biological process.
//
ID   Degradation of host cell envelope components during virus entry.
AC   KW-1235
DE   Virion protein involved in breaking down host cell surface components
DE   to reach the host cytoplasmic membrane. Many prokaryotic viruses for
DE   example carry enzymatic activities to degrade the host cell
DE   lipopolysaccharide layer, cell wall, or capsule.
GO   GO:0098994; disruption of host cell envelope during viral entry
HI   Cellular component: Virion; Degradation of host cell envelope components during virus entry.
HI   Biological process: Virus entry into host cell; Degradation of host cell envelope components during virus entry.
CA   Biological process.
//
ID   Degradation of host chromosome by virus.
AC   KW-1247
DE   Viral protein that rapidly degrades the host DNA at the onset of
DE   infection. The breakdown products can be reused to synthesize viral
DE   DNA or can be excreted from the host cell. Degrading host chromosome
DE   provides an advantage during the virus life cycle by reducing or
DE   eliminating competing host macromolecular synthesis. Bacteriophages
DE   such as T4 or T5 for example are known to induce degradation of the
DE   host chromosome and excretion of the host DNA degradation products.
GO   GO:0099015; degradation of host chromosome by virus
HI   Biological process: Host-virus interaction; Host gene expression shutoff by virus; Bacterial host gene expression shutoff by virus; Degradation of host chromosome by virus.
CA   Biological process.
//
ID   Degradation of host lipopolysaccharides during virus entry.
AC   KW-1237
DE   Virion protein involved in breaking down host cell lipopolysaccharides
DE   (LPS) to reach the cytoplasmic membrane of prokaryotes with 2
DE   membranes. Many prokaryotic viruses carry glycanase or deacetylase
DE   activities to digest host LPS.
GO   GO:0098995; disruption by virus of host envelope lipopolysaccharide during virus entry
HI   Biological process: Virus entry into host cell; Degradation of host cell envelope components during virus entry; Degradation of host lipopolysaccharides during virus entry.
CA   Biological process.
//
ID   Degradation of host peptidoglycans during virus entry.
AC   KW-1236
DE   Virion exolysin involved in breaking down host cell peptidoglycans
DE   (e.g. murein, pseudomurein) to reach the host cytoplasmic membrane
DE   during virus entry. Exolysins are usually part of the tail or the base
DE   plate of prokaryotic viruses. Exolysins can display various enzymatic
DE   activities such as lysozyme, transglycosylase, muramidase or even
DE   protease activity. Murein hydrolases for example are widespread in
DE   bacteriophages infecting Gram-positive or Gram-negative bacteria.
GO   GO:0098932; disruption by virus of host cell wall peptidoglycan during virus entry
HI   Cellular component: Virion; Degradation of host peptidoglycans during virus entry.
HI   Biological process: Virus entry into host cell; Degradation of host cell envelope components during virus entry; Degradation of host peptidoglycans during virus entry.
CA   Biological process.
//
ID   Dejerine-Sottas syndrome.
AC   KW-0213
DE   Protein which, if defective, causes Dejerine-Sottas disease. DSS is a
DE   hereditary motor and sensory neuropathy (HMSN) of the Charcot-Marie-
DE   Tooth disease type 1 class. DSS is characterized by severe early
DE   onset, very slow nerve conduction velocities (less than 12m/sec) and
DE   raised cerebrospinal fluid protein concentrations (0.7 g/l). Clinical
DE   signs are delayed age of walking as well as areflexia.
SY   DSS.
HI   Disease: Neuropathy; Dejerine-Sottas syndrome.
CA   Disease.
//
ID   Dental caries.
AC   KW-0214
DE   Protein involved in dental caries or important in the prevention of
DE   dental caries. Dental caries are localized destruction of the tooth
DE   surface, initiated by decalcification of the enamel and followed by
DE   enzymatic lysis of organic structures, the result of which is cavity
DE   formation. The cavity may penetrate the enamel and dentin, and reach
DE   the pulp. The disease may be caused by acids produced by bacteria
DE   which lead to decalcification, or by microorganisms that destroy the
DE   enamel protein, or by keratolytic microorganisms producing chelates
DE   that lead to decalcification.
HI   Disease: Dental caries.
CA   Disease.
//
ID   Deoxyribonucleotide synthesis.
AC   KW-0215
DE   Protein involved in the synthesis of deoxyribonucleotides, the basic
DE   repeating units in DNA. Deoxyribonucleotides consist of a purine or a
DE   pyrimidine base bonded to deoxyribose, which in turn is bound to a
DE   phosphate group. They are synthesised by reduction of ribonucleoside
DE   diphosphates.
SY   Deoxyribonucleotide anabolism; Deoxyribonucleotide biosynthesis;
SY   Deoxyribonucleotide biosynthetic process;
SY   Deoxyribonucleotide formation.
GO   GO:0009263; deoxyribonucleotide biosynthetic process
HI   Biological process: Deoxyribonucleotide synthesis.
CA   Biological process.
//
ID   Dermonecrotic toxin.
AC   KW-1061
DE   Protein involved in the necrosis of the skin.
HI   Molecular function: Toxin; Dermonecrotic toxin.
CA   Molecular function.
//
ID   Desmin-related myopathy.
AC   KW-0911
DE   Protein which, if defective, causes desmin-related myopathy (DRM), a
DE   clinically and genetically heterogeneous group of muscular disorders
DE   defined morphologically by intrasarcoplasmic aggregates of desmin,
DE   usually accompanied by other protein aggregates. Both autosomal
DE   dominant and autosomal recessive inheritance have been reported.
DE   Approximately one-third of DRMs are thought to be caused by mutations
DE   in the desmin gene.
HI   Disease: Myofibrillar myopathy; Desmin-related myopathy.
CA   Disease.
//
ID   Detoxification.
AC   KW-0216
DE   Protein involved in degrading toxic compounds. Detoxification
DE   generally takes place in the liver or kidney and inactivates toxins,
DE   either by degradation or by conjugation of residues to a hydrophilic
DE   moiety in order to promote excretion.
GO   GO:0009636; response to toxic substance
HI   Biological process: Detoxification.
CA   Biological process.
//
ID   Developmental protein.
AC   KW-0217
DE   Protein involved in development, the process whereby a multicellular
DE   organism develops from its early immature forms, e.g., zygote, larva,
DE   embryo, into an adult.
GO   GO:0007275; multicellular organism development
HI   Molecular function: Developmental protein.
CA   Molecular function.
//
IC   Developmental stage.
AC   KW-9996
DE   Keywords assigned to proteins because they are expressed specifically
DE   in a given developmental stage.
//
ID   Diabetes insipidus.
AC   KW-0218
DE   Protein which, if defective, causes diabetes insipidus, a rare form of
DE   diabetes in which the kidney tubules do not reabsorb enough water
DE   resulting in excessive urine excretion (polyuria). Two types of
DE   diabetes insipidus are recognized: central or neurohypophyseal
DE   diabetes insipidus which is due to defects in the neurohypophyseal
DE   system and results in a deficient quantity of anti-diuretic hormone
DE   being produced or released; nephrogenic diabetes insipidus, a
DE   vasopressin unresponsive condition of polyuria and hyposthenuria.
HI   Disease: Diabetes insipidus.
CA   Disease.
//
ID   Diabetes mellitus.
AC   KW-0219
DE   Protein which, if defective, causes diabetes mellitus, a disorder of
DE   impaired carbohydrate, protein, and fat metabolism due to insufficient
DE   secretion of insulin or to target tissue insulin resistance. Diabetes
DE   mellitus can be divided into two main types, type I or insulin-
DE   dependent diabetes mellitus (IDDM), and type II, or non insulin-
DE   dependent diabetes mellitus (NIDDM). Type I diabetes mellitus normally
DE   starts in childhood or adolescence and is caused by the body's own
DE   immune system which destroys the insulin-producing beta cells in the
DE   pancreas. Classical features are polydipsia, polyphagia and polyuria,
DE   due to hyperglycemia-induced osmotic diuresis. Type II diabetes
DE   mellitus normally starts in adulthood and is caused by a lack of
DE   sensitivity to the body's own insulin. It is usually characterized by
DE   a gradual onset with minimal or no symptoms of metabolic disturbance.
DE   Both forms of diabetes mellitus lead to secondary complications
DE   (notably cardiovascular, nephropathy, retinopathy, neuropathy). Two
DE   other major subcategories of diabetes mellitus are gestational
DE   diabetes and diabetes secondary to other medical conditions. In common
DE   usage, the term diabetes, when used alone, refers to diabetes mellitus
DE   and not diabetes insipidus.
HI   Disease: Diabetes mellitus.
CA   Disease.
//
ID   Diaminopimelate biosynthesis.
AC   KW-0220
DE   Protein involved in the synthesis of diaminopimelate, the ionic form
DE   of the amino acid diaminopimelic acid (DAP) which is found in the
DE   murein peptidoglycans of bacterial cell walls. Diaminopimelic acid is
DE   synthesised from aspartate.
SY   Diaminopimelate anabolism; Diaminopimelate biosynthetic process;
SY   Diaminopimelate formation; Diaminopimelate synthesis.
GO   GO:0019877; diaminopimelate biosynthetic process
HI   Biological process: Diaminopimelate biosynthesis.
CA   Biological process.
//
ID   Diamond-Blackfan anemia.
AC   KW-1024
DE   Protein which, if defective, causes Diamond-Blackfan anemia, a rare
DE   congenital non-regenerative hypoplastic anemia that usually presents
DE   early in infancy. The disease is characterized by a moderate to severe
DE   macrocytic anemia, erythroblastopenia, and an increased risk of
DE   developing leukemia. 30 to 40% of Diamond-Blackfan anemia patients
DE   present with short stature and congenital anomalies, the most frequent
DE   being craniofacial (Pierre-Robin syndrome and cleft palate), thumb and
DE   urogenital anomalies.
SY   Aase-Smith syndrome II; Aase syndrome; BDS; Blackfan-Diamond disease;
SY   Blackfan-Diamond syndrome; Chronic congenital aregenerative anemia;
SY   Congenital erythroid hypoplastic anemia;
SY   Congenital hypoplastic anemia of Blackfan and Diamond; DBA;
SY   Erythrogenesis imperfecta; Pure red cell aplasia.
HI   Disease: Diamond-Blackfan anemia.
CA   Disease.
//
ID   Differentiation.
AC   KW-0221
DE   Protein involved in differentiation, the developmental process of a
DE   multicellular organism by which cells become specialized for
DE   particular functions. Differentiation requires selective expression of
DE   the genome; the fully differentiated state may be preceded by a stage
DE   in which the cell is already programmed for differentiation but is not
DE   yet expressing the characteristic phenotype determination. Also used
DE   for fungal conidiation proteins, and for some bacteria that present
DE   specialization of function in cell types, such as Caulobacter
DE   crescentus.
SY   Cell differentiation.
GO   GO:0030154; cell differentiation
HI   Biological process: Differentiation.
CA   Biological process.
//
ID   Digestion.
AC   KW-0222
DE   Protein involved in the process whereby nutrients are rendered soluble
DE   and capable of being absorbed by the organism or cell, by action of
DE   various hydrolytic enzymes that break down proteins, carbohydrates,
DE   fats, etc.
GO   GO:0007586; digestion
HI   Biological process: Digestion.
CA   Biological process.
//
ID   Dioxygenase.
AC   KW-0223
DE   Enzyme that reduces molecular oxygen by incorporating both atoms into
DE   its substrate(s).
GO   GO:0051213; dioxygenase activity
HI   Molecular function: Oxidoreductase; Dioxygenase.
CA   Molecular function.
//
ID   Dipeptidase.
AC   KW-0224
DE   Enzyme that hydrolyzes a dipeptide into its constituent amino acids.
GO   GO:0016805; dipeptidase activity
HI   Molecular function: Hydrolase; Protease; Dipeptidase.
CA   Molecular function.
//
ID   Direct protein sequencing.
AC   KW-0903
DE   Protein, whose amino acid sequence has been partially (more than one
DE   residue) or completely determined experimentally by Edman degradation
DE   or by mass spectrometry.
HI   Technical term: Direct protein sequencing.
CA   Technical term.
//
IC   Disease.
AC   KW-9995
DE   Keywords assigned to proteins because they are involved in a specific
DE   disease.
//
ID   Disease variant.
AC   KW-0225
DE   Protein for which at least one genetic variant involved in a disease
DE   is reported in the feature table of the UniProtKB/Swiss-Prot entry.
HI   Disease: Disease variant.
HI   Coding sequence diversity: Disease variant.
CA   Disease.
//
ID   Disulfide bond.
AC   KW-1015
DE   Protein which is modified by the formation of a bond between the thiol
DE   groups of two peptidyl-cysteine residues. The process of chemical
DE   oxidation that forms interchain disulfide bonds can produce stable,
DE   covalently linked protein dimers, multimers or complexes, whereas
DE   intrachain disulfide bonds can contribute to protein folding and
DE   stability. Depending on the protein environment, some disulfide bonds
DE   are more labile, forming transient redox-active disulfide bonds that
DE   are alternately reduced and oxidized in the course of an enzymatic
DE   reaction.
HI   PTM: Disulfide bond.
CA   PTM.
//
ID   DNA condensation.
AC   KW-0226
DE   Protein involved in DNA condensation. In most eukaryotes, the
DE   chromosomal packing involves the wrapping of DNA around a core of
DE   histones to form nucleosomes. Adjacent nucleosomes are packaged
DE   together via Histone 1 and nucleosomes are organised into a 30 nm
DE   chromatin fibre. DNA condensation takes place as cells enter mitosis
DE   or when germ cells enter meiosis.
GO   GO:0030261; chromosome condensation
HI   Biological process: DNA condensation.
CA   Biological process.
//
ID   DNA damage.
AC   KW-0227
DE   Protein induced by DNA damage or protein involved in the response to
DE   DNA damage. Drug- or radiation-induced injuries in DNA introduce
DE   deviations from its normal double-helical conformation. These changes
DE   include structural distortions which interfere with replication and
DE   transcription, as well as point mutations which disrupt base pairs and
DE   exert damaging effects on future generations through changes in DNA
DE   sequence. Response to DNA damage results in either repair or
DE   tolerance.
SY   DNA damage response; Response to DNA damage stimulus.
GO   GO:0006974; DNA damage response
HI   Biological process: DNA damage.
CA   Biological process.
//
ID   DNA end degradation evasion by virus.
AC   KW-1256
DE   Viral protein that inhibits or counteracts prokaryotic host
DE   helicase/nuclease proteins in order to escape the antiviral activity
DE   of the latter. When functioning in their exonuclease mode,
DE   helicase/nuclease proteins such as bacterial RecBCD or AddAB degrade
DE   any free DNA end as well as the linear dsDNA products resulting from
DE   restriction Type II cleavage. Any prokaryotic virus that exposes free
DE   dsDNA ends as part of its life cycle must find the means to evade
DE   destruction by these host enzymes. Prokaryotic viruses escape this
DE   host defense by expressing inhibitors or by protecting the ends of
DE   their linear genomes from digestion.
GO   GO:0099016; evasion by virus of DNA end degradation
HI   Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; DNA end degradation evasion by virus.
CA   Biological process.
//
ID   DNA excision.
AC   KW-0228
DE   Protein involved in the repair of damages to one strand of DNA (loss
DE   of purines due to thermal fluctuations, formation of pyrimidine dimers
DE   by UV irradiation, for instance). The site of damage is recognized,
DE   excised by an endonuclease, the correct sequence is copied from the
DE   complementary strand by a polymerase and the ends of this correct
DE   sequence are joined to the rest of the strand by a ligase. In
DE   bacterial systems, the polymerase also acts as endonuclease. Excisase
DE   A and other proteins involved in recombination mediate DNA excision; a
DE   process whereby abnormal or mismatched nucleotides are enzymatically
DE   cut out of a strand of a DNA molecule.
GO   GO:0006281; DNA repair
HI   Biological process: DNA excision.
CA   Biological process.
//
ID   DNA integration.
AC   KW-0229
DE   Protein involved in DNA integration, a process that mediates the
DE   insertion of foreign genetic material, or other duplex DNA, into a
DE   chromosome, or another replicon, in order to form a covalently linked
DE   DNA continuous with the host DNA.
GO   GO:0015074; DNA integration
HI   Biological process: DNA integration.
CA   Biological process.
//
ID   DNA invertase.
AC   KW-0230
DE   Specific recombinases which catalyze the inversion of a DNA segment
DE   within a nucleoprotein structure termed invertasome.
GO   GO:0000150; DNA strand exchange activity
GO   GO:0003677; DNA binding
GO   GO:0006310; DNA recombination
HI   Biological process: DNA recombination; DNA invertase.
HI   Molecular function: DNA-binding; DNA invertase.
HI   Molecular function: DNA invertase.
CA   Molecular function.
//
ID   DNA recombination.
AC   KW-0233
DE   Protein involved in DNA recombination, i.e. any process in which DNA
DE   molecules are cleaved and the fragments are rejoined to give a new
DE   combination.
GO   GO:0006310; DNA recombination
HI   Biological process: DNA recombination.
CA   Biological process.
//
ID   DNA repair.
AC   KW-0234
DE   Protein involved in the repair of DNA, the various biochemical
DE   processes by which damaged DNA can be restored. DNA repair embraces,
DE   for instance, not only the direct reversal of some types of damage
DE   (such as the enzymatic photoreactivation of thymine dimers), but also
DE   multiple distinct mechanisms for excising damaged base; termed
DE   nucleotide excision repair (NER), base excision repair (BER) and
DE   mismatch repair (MMR); or mechanisms for repairing double-strand
DE   breaks.
GO   GO:0006281; DNA repair
HI   Biological process: DNA damage; DNA repair.
CA   Biological process.
//
ID   DNA replication.
AC   KW-0235
DE   Protein involved in DNA replication, i.e. the duplication of DNA by
DE   making a new copy of an existing molecule. The parental double-
DE   stranded DNA molecule is replicated semi conservatively, i.e. each
DE   copy contains one of the original strands paired with a newly
DE   synthesized strand that is complementary in terms of AT and GC base
DE   pairing.
GO   GO:0006260; DNA replication
HI   Biological process: DNA replication.
CA   Biological process.
//
ID   DNA replication inhibitor.
AC   KW-0236
DE   Protein involved in the inhibition of DNA replication.
SY   Negative regulation of DNA replication.
GO   GO:0008156; negative regulation of DNA replication
HI   Molecular function: DNA replication inhibitor.
CA   Molecular function.
//
ID   DNA synthesis.
AC   KW-0237
DE   Protein involved in the synthesis of DNA from deoxyribonucleic acid
DE   monomers.
SY   DNA biosynthesis; DNA biosynthetic process.
GO   GO:0071897; DNA biosynthetic process
HI   Biological process: DNA synthesis.
CA   Biological process.
//
ID   DNA-binding.
AC   KW-0238
DE   Protein which binds to DNA, typically to pack or modify the DNA, or to
DE   regulate gene expression. Among those proteins that recognize specific
DE   DNA sequences, there are a number of characteristic conserved motifs
DE   believed to be essential for specificity. Many DNA-binding domains are
DE   described in PROSITE.
GO   GO:0003677; DNA binding
HI   Molecular function: DNA-binding.
CA   Molecular function.
//
ID   DNA-directed DNA polymerase.
AC   KW-0239
DE   Enzyme that catalyzes DNA synthesis by addition of deoxyribonucleotide
DE   units to a DNA chain using DNA as a template. They can also possess
DE   exonuclease activity and therefore function in DNA repair.
GO   GO:0003887; DNA-directed DNA polymerase activity
HI   Molecular function: Transferase; Nucleotidyltransferase; DNA-directed DNA polymerase.
CA   Molecular function.
//
ID   DNA-directed RNA polymerase.
AC   KW-0240
DE   Protein of the DNA-directed RNA polymerase complexes, which catalyze
DE   RNA synthesis the by addition of ribonucleotide units to a RNA chain
DE   using DNA as a template. They can initiate a chain de novo.
DE   Prokaryotes have a single enzyme for the three RNA types that is
DE   subject to stringent regulatory mechanisms. Eukaryotes have type I
DE   that synthesizes all rRNA except the 5S component, type II that
DE   synthesizes mRNA and hnRNA and type III that synthesizes tRNA and the
DE   5S component of rRNA.
GO   GO:0000428; DNA-directed RNA polymerase complex
HI   Biological process: Transcription; DNA-directed RNA polymerase.
HI   Cellular component: DNA-directed RNA polymerase.
CA   Cellular component.
//
IC   Domain.
AC   KW-9994
DE   Keywords assigned to proteins because they have at least one specimen
DE   of a specific domain.
//
ID   Down syndrome.
AC   KW-0241
DE   Protein which, if defective, causes Down's syndrome, a condition due
DE   to the presence of three copies of chromosome 21 (trisomy 21),
DE   characterized by some degree of intellectual disability, short stature
DE   and poor muscle tone. Common (1 in 700 live births); incidence
DE   increases with maternal age. The cause is usually non-disjunction at
DE   meiosis but occasionally a translocation of fused chromosomes 21 and
DE   14.
SY   Down's syndrome.
HI   Disease: Down syndrome.
CA   Disease.
//
ID   Dwarfism.
AC   KW-0242
DE   Protein which, if defective, causes dwarfism, a skeletal growth defect
DE   resulting in the condition of being undersized.
HI   Disease: Dwarfism.
CA   Disease.
//
ID   Dynein.
AC   KW-0243
DE   Large multimeric complex with ATPase activity, responsible for the
DE   movement of eukaryotic cilia and flagella (axonemal dynein) and for
DE   the intracellular retrograde motility of vesicles, organelles and
DE   chromosomes along microtubules (cytosolic dynein). Constitutes the
DE   side arms of the outer microtubule doublets in the ciliary axoneme and
DE   is responsible for the sliding. Also used for the dynein-associated
DE   microtubule-binding proteins (MTBs), e.g. dynactin.
GO   GO:0030286; dynein complex
HI   Cellular component: Dynein.
CA   Cellular component.
//
ID   Dyskeratosis congenita.
AC   KW-1011
DE   Protein which, if defective, causes dyskeratosis congenita, a
DE   clinically and genetically heterogeneous disorder characterized by
DE   abnormal skin pigmentation, mucosal leukoplakia, nail dystrophy,
DE   progressive bone marrow failure, and increased predisposition to
DE   cancer.
SY   DKC.
HI   Disease: Dyskeratosis congenita.
CA   Disease.
//
ID   Dystonia.
AC   KW-1023
DE   Protein which, if defective, causes dystonia or dystonic conditions
DE   that feature persistent or recurrent episodes of dystonia as a major
DE   manifestation of disease. Dystonia is a movement disorder with a
DE   neurological basis, due to disordered tonicity of muscle. It is
DE   characterized by sustained involuntary muscle contractions that cause
DE   abnormal postures, twisting, repetitive and patterned movements. It
DE   may affect muscles throughout the body (generalized), in certain parts
DE   of the body (segmental), or may be confined to particular muscles or
DE   muscle groups (focal).
HI   Disease: Dystonia.
CA   Disease.
//
ID   Dystroglycanopathy.
AC   KW-1215
DE   Protein which, if defective, causes any of the muscular disorders
DE   caused by aberrant glycosylation of dystroglycan. These genetically
DE   heterogeneous diseases include a range of conditions with different
DE   degrees of severity. At the most severe end of the clinical spectrum,
DE   Walker-Warburg syndrome (WWS), muscle-eye-brain disease (MEB) and
DE   Fukuyama congenital muscular dystrophy (FCMD) are characterized by
DE   congenital muscular dystrophy and severe structural brain and eye
DE   abnormalities, which in WWS result in early infantile death. At the
DE   mildest end of the clinical spectrum, affected individuals present
DE   with limb girdle muscular dystrophy (LGMD), without brain and eye
DE   involvement.
HI   Disease: Dystroglycanopathy.
CA   Disease.
//
ID   Early protein.
AC   KW-0244
DE   Bacteriophage or viral protein expressed in the first phase of the
DE   infectious cycle.
HI   Developmental stage: Early protein.
CA   Developmental stage.
//
ID   Ectodermal dysplasia.
AC   KW-0038
DE   Protein which, if defective, causes ectodermal dysplasia, a
DE   heterogeneous group of developmental disorders affecting tissues of
DE   ectodermal origin. Ectodermal dysplasias are characterized by abnormal
DE   development of two or more ectodermal structures such as hair, teeth,
DE   nails and sweat glands, with or without any additional clinical sign.
DE   Each combination of clinical features represents a different type of
DE   ectodermal dysplasia.
SY   ED.
HI   Disease: Ectodermal dysplasia.
CA   Disease.
//
ID   EGF-like domain.
AC   KW-0245
DE   Protein containing at least one EGF-like domain, a sequence of about
DE   thirty to forty amino-acid residues long found in the sequence of
DE   epidermal growth factor (EGF). It has been shown to be present, in a
DE   more or less conserved form, in a large number of proteins. The EGF-
DE   like domain contains six cysteines which form disulfide bonds within
DE   the domain (C1-C3, C2-C4, C5-C6).
HI   Domain: EGF-like domain.
CA   Domain.
//
ID   Ehlers-Danlos syndrome.
AC   KW-0248
DE   Protein which, if defective, causes Ehlers-Danlos syndrome (EDS), a
DE   genetically and phenotypically heterogeneous group of connective-
DE   tissue disorders. It affects primarily the skin, ligaments, joints,
DE   and blood vessels. Typical features include skin hyperextensibility,
DE   joint hypermobility, easy bruisability, friability of tissues with
DE   bleeding and poor wound healing. Inheritance can be autosomal
DE   dominant, autosomal recessive, or X-linked recessive.
SY   EDS.
HI   Disease: Ehlers-Danlos syndrome.
CA   Disease.
//
ID   Electron transport.
AC   KW-0249
DE   Protein involved in the transport of electrons, a process by which
DE   electrons are transported through a series of reactions from the
DE   reductant, or electron donor, to the oxidant, or electron acceptor,
DE   with concomitant energy conversion. Necessary for both photosynthesis
DE   and aerobic respiration.
HI   Biological process: Transport; Electron transport.
CA   Biological process.
//
ID   Elliptocytosis.
AC   KW-0250
DE   Protein which, if defective, causes elliptocytosis, a disorder
DE   characterized by variable haemolytic anaemia and elliptical red blood
DE   cell shape. Caused by deficiency/dysfunction of red blood cell
DE   membrane proteins.
HI   Disease: Hereditary hemolytic anemia; Elliptocytosis.
CA   Disease.
//
ID   Elongation factor.
AC   KW-0251
DE   Protein that associates with ribosomes cyclically during the
DE   elongation phase of protein synthesis, and catalyze formation of the
DE   acyl bond between the incoming amino-acid residue and the peptide
DE   chain.
SY   Translation elongation factor activity.
GO   GO:0003746; translation elongation factor activity
GO   GO:0006414; translational elongation
HI   Biological process: Protein biosynthesis; Elongation factor.
HI   Molecular function: Elongation factor.
CA   Molecular function.
//
ID   Emery-Dreifuss muscular dystrophy.
AC   KW-1067
DE   Protein which, if defective, causes Emery-Dreifuss muscular dystrophy,
DE   a heterogenous group of inherited muscular dystrophy without the
DE   involvement of nervous system. The disease is characterized by slowly
DE   progressive muscle weakness, contracture of the elbows, Achilles
DE   tendon and posterior cervical muscles, and cardiac features.
SY   Scapuloperoneal muscular dystrophy.
HI   Disease: Emery-Dreifuss muscular dystrophy.
CA   Disease.
//
ID   Encapsulin nanocompartment.
AC   KW-1284
DE   Protein located in or on an encapsulin nanocompartment, proteinaceous
DE   shells that encapsulate enzymes. The selectively permeable, self-
DE   assembling 25-42 nm shell is made of only 1 protein, unlike the larger
DE   bacterial microcompartment. The shell protein has an HK97-like fold
DE   and probably evolved from a viral protein. Artificial encapsulin
DE   nanocompartments can be expressed and filled with cargo proteins for
DE   biotechnological uses. They are found in many bacterial and a few
DE   archaeal phyla.
HI   Cellular component: Encapsulin nanocompartment.
CA   Cellular component.
//
ID   Endocytosis.
AC   KW-0254
DE   Protein involved in endocytosis, a process by which extracellular
DE   materials are taken up into a cell by invagination of the plasma
DE   membrane to form vesicles enclosing these materials.
GO   GO:0006897; endocytosis
HI   Biological process: Endocytosis.
CA   Biological process.
//
ID   Endonuclease.
AC   KW-0255
DE   Phosphodiesterase capable of cleaving at phosphodiester internal bonds
DE   within a DNA or RNA substrate.
GO   GO:0004519; endonuclease activity
HI   Molecular function: Hydrolase; Nuclease; Endonuclease.
CA   Molecular function.
//
ID   Endoplasmic reticulum.
AC   KW-0256
DE   Protein whose subcellular location is the endoplasmic reticulum, a
DE   membrane system continuous with the outer nuclear membrane. It
DE   consists of flattened, single-membrane vesicles whose inner
DE   compartments, the cisternae, interconnect to form channels throughout
DE   the cytoplasm. The rough-surface portion is studded with ribosomes.
GO   GO:0005783; endoplasmic reticulum
HI   Cellular component: Endoplasmic reticulum.
CA   Cellular component.
//
ID   Endorphin.
AC   KW-0257
DE   Morphine-like peptides produced by the brain in response to
DE   neurotransmitters. They bind to neuron receptors that mediate the
DE   action of opiates and induce analgesia and sedation.
GO   GO:0007218; neuropeptide signaling pathway
HI   Molecular function: Endorphin.
CA   Molecular function.
//
ID   Endosome.
AC   KW-0967
DE   Protein found in or associated with endosomes. Endosomes are highly
DE   dynamic membrane systems involved in transport within the cell, they
DE   receive endocytosed cell membrane molecules and sort them for either
DE   degradation or recycling back to the cell surface. They also receive
DE   newly synthesised proteins destined for vacuolar/lysosomal
DE   compartments. In certain cell types, endosomal multivesicular bodies
DE   may fuse with the cell surface in an exocytic manner. These released
DE   vesicles are called exosomes.
GO   GO:0005768; endosome
HI   Cellular component: Endosome.
CA   Cellular component.
//
ID   Enterobactin biosynthesis.
AC   KW-0259
DE   Protein involved in the synthesis of enterobactin, a compound that
DE   transports iron from the bacterial environment into the cell
DE   cytoplasm.
SY   Enterobactin anabolism; Enterobactin biosynthetic process;
SY   Enterobactin formation; Enterobactin synthesis;
SY   Enterochelin anabolism; Enterochelin biosynthesis;
SY   Enterochelin biosynthetic process; Enterochelin formation;
SY   Enterochelin synthesis.
GO   GO:0009239; enterobactin biosynthetic process
HI   Biological process: Enterobactin biosynthesis.
CA   Biological process.
//
ID   Enterotoxin.
AC   KW-0260
DE   Toxin which, either when ingested or when produced by enterobacteria
DE   within the intestine, acts on the intestinal mucosa and induces
DE   diarrhea by perturbing ion and water transport systems.
HI   Molecular function: Toxin; Enterotoxin.
CA   Molecular function.
//
ID   Epidermolysis bullosa.
AC   KW-0263
DE   Protein which, if defective, causes epidermolysis bullosa, any of a
DE   group of mechano-bullous disorders characterized by blistering and/or
DE   erosion of the skin and mucous membranes which occur spontaneously or
DE   as a result of mild physical trauma. Traditionally, epidermolysis
DE   bullosa is divided into three broad categories based on the level of
DE   tissue separation: in epidermolysis bullosa simplex (EBS), tissue
DE   separation is intraepidermal and occurs within the basal keratinocytes
DE   at the bottom layer of epidermis; the junctional forms (JEB) display
DE   tissue separation within the dermo-epidermal basement membrane
DE   (basement membrane zone, BMZ), primarily within the lamina lucida; in
DE   the dystrophic forms (DEB), tissue separation occurs below the lamina
DE   densa within the upper papillary dermis. Some forms of epidermolysis
DE   bullosa display tissue separation at the basal cell/lamina lucida
DE   interface, at the level of the hemidesmosomes (hemidesmosomal
DE   variants). The hemidesmosomal variants overlap with the traditional
DE   subtypes, particularly the simplex and junctional forms. In addition
DE   to skin involvement, various extracutaneous manifestations can be
DE   associated with distinct subtypes of epidermolysis bullosa.
HI   Disease: Epidermolysis bullosa.
CA   Disease.
//
ID   Epilepsy.
AC   KW-0887
DE   Protein which, if defective, causes epilepsy, any of a group of
DE   disorders characterized by paroxysmal transient disturbances of the
DE   electrical activity of the brain that may be manifested as episodic
DE   impairment or loss of consciousness, abnormal motor phenomena, psychic
DE   or sensory disturbances, or perturbation of the autonomic nervous
DE   system. Epilepsy is classified as either symptomatic or idiopathic
DE   according to whether the cause is known or unknown. Both of these
DE   types can be classified into partial and generalized epilepsy,
DE   depending on whether the seizures are due to limited or to widespread
DE   brain lesions, respectively.
HI   Disease: Epilepsy.
CA   Disease.
//
ID   ER-Golgi transport.
AC   KW-0931
DE   Protein involved in the 'ER-to-Golgi' transport, a bidirectional
DE   membrane traffic between the endoplasmic reticulum and the Golgi
DE   apparatus which mediates the transfer of cargo molecules by means of
DE   small vesicles or tubular-saccular extensions.
SY   ER/Golgi transport; ER to Golgi transport; Golgi-to-ER transport.
GO   GO:0016192; vesicle-mediated transport
HI   Biological process: Transport; ER-Golgi transport.
CA   Biological process.
//
ID   ERV.
AC   KW-0895
DE   Protein encoded by proviral genes of endogenous retroviruses. When a
DE   retrovirus infects a host cell, viral reverse transcriptase (RT) makes
DE   a DNA copy of the RNA viral genome. The integrated DNA form of a
DE   retrovirus is referred to as a provirus. Proviral genes are expressed
DE   by cellular mechanisms. Retroviruses that enter the germline are
DE   referred to as endogenous retroviruses (ERVs) to distinguish them from
DE   horizontally transmitted, not passed on to host progeny, "exogenous"
DE   retroviruses. Amplification of ERV copy number via retrotransposition
DE   or reinfection has given rise to numerous ERV sequences in the
DE   vertebrate genomes. As much as 8% of the human genome, and 10% of the
DE   mouse genome, consists of sequences derived from ERV insertions.
SY   Endogenous retrovirus; Fossil virus.
HI   Technical term: ERV.
CA   Technical term.
//
ID   Erythrocyte maturation.
AC   KW-0265
DE   Protein involved in the maturation of erythrocytes, the predominant
DE   type of cells present in vertebrate blood and which contain the gas-
DE   transporting protein, hemoglobin.
SY   RBC maturation; Red blood cell maturation;
SY   Red blood corpuscle maturation.
GO   GO:0043249; erythrocyte maturation
HI   Biological process: Erythrocyte maturation.
CA   Biological process.
//
ID   Ethylene biosynthesis.
AC   KW-0266
DE   Protein involved in the synthesis of ethylene (C2H4), an unsaturated
DE   hydrocarbon gas mainly produced in plants. It has developmental
DE   effects as a hormone, including growth inhibition, regulation of fruit
DE   development, leaf abscission and aging.
SY   Ethylene anabolism; Ethylene biosynthetic process; Ethylene formation;
SY   Ethylene synthesis.
GO   GO:0009693; ethylene biosynthetic process
HI   Biological process: Ethylene biosynthesis.
CA   Biological process.
//
ID   Ethylene signaling pathway.
AC   KW-0936
DE   Protein involved in the ethylene signaling pathway (e.g. transport and
DE   signal transduction) that regulates many aspects of plant growth and
DE   development (e.g. seed germination, root and shoot growth, flower
DE   development, plant defense, senescence, abscission and ripening). This
DE   phytohormone can be synthesized from methionin.
SY   Ethylene mediated signaling pathway.
GO   GO:0009873; ethylene-activated signaling pathway
HI   Biological process: Ethylene signaling pathway.
CA   Biological process.
//
ID   Eukaryotic host gene expression shutoff by virus.
AC   KW-1262
DE   Viral protein which prevents host gene expression by blocking host
DE   transcription, mRNA export or translation. This gives viral
DE   transcripts a competitive edge to use the hijacked translation
DE   machinery. Preventing the expression of host proteins is also a
DE   strategy to counteract the antiviral response.
HI   Biological process: Host-virus interaction; Host gene expression shutoff by virus; Eukaryotic host gene expression shutoff by virus.
CA   Biological process.
//
ID   Eukaryotic host transcription shutoff by virus.
AC   KW-1191
DE   Viral protein involved in inhibiting host transcription to ensure the
DE   shutoff of cellular proteins expression and give virus transcripts a
DE   competitive edge for access to the cellular translation machinery.
DE   Preventing the expression of host proteins is also a strategy to
DE   counteract the antiviral response. Inhibition of transcription can be
DE   performed by interfering with host RNA pol-II function or interfering
DE   with general transcription factors.
GO   GO:0039653; suppression by virus of host transcription
HI   Biological process: Host-virus interaction; Host gene expression shutoff by virus; Eukaryotic host gene expression shutoff by virus; Eukaryotic host transcription shutoff by virus.
CA   Biological process.
//
ID   Eukaryotic host translation shutoff by virus.
AC   KW-1193
DE   Viral protein involved in inhibiting the host translational machinery
DE   to shutoff cellular gene expression. This gives virus transcripts a
DE   competitive edge to use the hijacked translation machinery. Preventing
DE   the expression of host proteins is also a strategy to counteract the
DE   antiviral response. Several virus are known to inhibit host
DE   translation mostly by inactivating translation factors.
GO   GO:0039604; suppression by virus of host translation
HI   Biological process: Host-virus interaction; Host gene expression shutoff by virus; Eukaryotic host gene expression shutoff by virus; Eukaryotic host translation shutoff by virus.
CA   Biological process.
//
ID   Evasion of bacteria-mediated translation shutoff by virus.
AC   KW-1259
DE   Viral protein that counteracts the translation shutoff set up by the
DE   bacterial host in order to inhibit viral replication. This antiviral
DE   defense system alters a crucial cellular process thereby blocking
DE   virus multiplication and ending up with host dormancy or even cell
DE   death. For example, some E.coli strains infected by bacteriophage T4
DE   activate an anticodon nuclease which causes depletion of tRNA(Lys)
DE   and, consequently, abolishes T4 protein synthesis and causes cell
DE   death. However, this effect is counteracted by the repair of tRNA(Lys)
DE   in consecutive reactions catalyzed by the viral enzymes polynucleotide
DE   kinase and RNA ligase. The ToxIN system functions as a toxin-antitoxin
DE   (TA) tandem which is used as a antiviral defense mechanism.
HI   Biological process: Host-virus interaction; Evasion of bacteria-mediated translation shutoff by virus.
CA   Biological process.
//
ID   Evasion of host immunity by viral interleukin-like protein.
AC   KW-1125
DE   Viral protein sharing sequence homology with host interleukins.
DE   Interleukins are produced by immune system cells such as lymphocytes,
DE   macrophages and monocytes, and modulate inflammation and immunity by
DE   regulating growth, mobility and differentiation of lymphoid and other
DE   cells. Several viruses encode interleukin-like proteins playing a role
DE   in immune evasion. Additionally, viral interleukins have been shown to
DE   activate cellular signaling cascades that enhance virus replication.
GO   GO:0019049; mitigation of host antiviral defense response
HI   Biological process: Host-virus interaction; Viral immunoevasion; Evasion of host immunity by viral interleukin-like protein.
CA   Biological process.
//
ID   Excision nuclease.
AC   KW-0267
DE   Enzyme which excises abnormal or mismatched nucleotides from a DNA
DE   strand.
GO   GO:0004518; nuclease activity
HI   Biological process: DNA damage; DNA repair; Excision nuclease.
HI   Molecular function: Excision nuclease.
CA   Molecular function.
//
ID   Exocytosis.
AC   KW-0268
DE   Protein involved in exocytosis, a process by which a material is
DE   transported out of a cell using a vesicle that first engulfs the
DE   material and then is extruded through an opening in the cell membrane.
DE   The exocyst protein complex plays an important role in exocytosis by
DE   directing exocytic vesicles to their precise sites of fusion in the
DE   plasma membrane.
SY   Vesicle exocytosis.
GO   GO:0006887; exocytosis
HI   Biological process: Exocytosis.
CA   Biological process.
//
ID   Exonuclease.
AC   KW-0269
DE   Enzyme that degrades DNA or RNA by progressively splitting off single
DE   nucleotides from one end of the chain.
GO   GO:0004527; exonuclease activity
HI   Molecular function: Hydrolase; Nuclease; Exonuclease.
CA   Molecular function.
//
ID   Exopolysaccharide synthesis.
AC   KW-0270
DE   Protein involved in the synthesis of exopolysaccharide (EPS), a high
DE   molecular-weight polymer composed of saccharide subunits. An example
DE   is succinoglycan (EPS I) of Rhizobium meliloti, that is important for
DE   invasion of the nodules that it elicits on its host, Medicago sativa.
SY   EPS anabolism; EPS biosynthesis; EPS biosynthetic process;
SY   EPS formation; EPS synthesis; Exopolysaccharide anabolism;
SY   Exopolysaccharide biosynthesis;
SY   Exopolysaccharide biosynthetic process; Exopolysaccharide formation.
GO   GO:0000271; polysaccharide biosynthetic process
HI   Biological process: Exopolysaccharide synthesis.
CA   Biological process.
//
ID   Exosome.
AC   KW-0271
DE   Protein which is a component of the exosome, a complex of proteins
DE   that includes 3->5 exoribonucleases and that plays a major role in
DE   diverse RNA processing and degradation pathways in eukaryotes and
DE   archaea.
GO   GO:0000178; exosome (RNase complex)
HI   Cellular component: Exosome.
CA   Cellular component.
//
ID   Extinct organism protein.
AC   KW-0952
DE   Protein originating from a species thought to be extinct, i.e. from a
DE   species for which no known surviving specimens are known to exist. Eg.
DE   Dodo, Mammoth or Neanderthal.
HI   Technical term: Extinct organism protein.
CA   Technical term.
//
ID   Extracellular matrix.
AC   KW-0272
DE   Protein found in the extracellular matrix. The extracellular matrix
DE   consists of any material produced by cells and secreted into the
DE   surrounding medium, but this term generally applies to the non-
DE   cellular components of animal tissues. The extracellular matrix forms
DE   a supportive meshwork around cells and is largely composed of
DE   collagen, laminin, fibronectin and glycosaminoglycans. It can
DE   influence the properties of the cells that it supports. In certain
DE   tissues, specific modifications to the extracellular matrix occur. For
DE   instance, the matrix of bone is mineralized to resist compression.
GO   GO:0031012; extracellular matrix
HI   Cellular component: Secreted; Extracellular matrix.
CA   Cellular component.
//
ID   Eye lens protein.
AC   KW-0273
DE   Protein found in the lens, a transparent body at the front of the
DE   vertebrate eye.
GO   GO:0005212; structural constituent of eye lens
HI   Molecular function: Eye lens protein.
CA   Molecular function.
//
ID   FAD.
AC   KW-0274
DE   Protein involved in flavin adenine dinucleotide synthesis or protein
DE   which contains at least one FAD as prosthetic group, cofactor
DE   (flavoprotein) or cosubstrate such as many oxidation-reduction
DE   enzymes. FAD is an electron carrier molecule that functions as a
DE   hydrogen acceptor. The generic term "flavin" derives from the Latin
DE   word flavius ("yellow") because of the brilliant yellow color they
DE   exhibit as solids and in neutral aqueous solutions.
SY   Flavin adenine dinucleotide.
HI   Ligand: Flavoprotein; FAD.
CA   Ligand.
//
ID   Familial hemophagocytic lymphohistiocytosis.
AC   KW-0951
DE   Protein which, if defective, causes familial hemophagocytic
DE   lymphohistiocytosis. FHL is a genetically heterogeneous, autosomal
DE   recessive disorder characterized by immune dysregulation with
DE   hypercytokinemia and defective natural killer cell function. The
DE   clinical features of the disease include fever, hepatosplenomegaly,
DE   cytopenia, hypertriglyceridemia, hypofibrinogenemia, and neurological
DE   abnormalities ranging from irritability and hypotonia to seizures,
DE   cranial nerve deficits and ataxia. Hemophagocytosis is a prominent
DE   feature of the disease, and non-malignant infiltration of macrophages
DE   and activated T lymphocytes in lymph nodes, spleen and other organs is
DE   also found.
SY   FHL; Hemophagocytic lymphohistiocytosis; HPLH.
HI   Disease: Familial hemophagocytic lymphohistiocytosis.
CA   Disease.
//
ID   Fanconi anemia.
AC   KW-0923
DE   Protein which, if defective, causes Fanconi anemia. Fanconi anemia is
DE   a rare recessive disorder characterized by progressive pancytopenia,
DE   hypoplasia of the bone marrow and patchy brown discoloration of the
DE   skin, due to melanin deposition. It is associated with multiple
DE   congenital anomalies of the musculoskeletal and genitourinary systems.
SY   Fanconi pancytopenia.
HI   Disease: Fanconi anemia.
CA   Disease.
//
ID   Fatty acid biosynthesis.
AC   KW-0275
DE   Protein involved in the synthesis of fatty acids, long chain organic
DE   acids of the general formula CH3(CnHx)COOH. They are constituents of
DE   lipids and can be saturated or unsaturated. The esterified forms are
DE   important both as energy storage molecules and structural molecules.
SY   Fatty acid anabolism; Fatty acid biosynthetic process;
SY   Fatty acid formation; Fatty acid synthesis.
GO   GO:0006633; fatty acid biosynthetic process
HI   Biological process: Lipid metabolism; Fatty acid metabolism; Fatty acid biosynthesis.
HI   Biological process: Lipid metabolism; Lipid biosynthesis; Fatty acid biosynthesis.
CA   Biological process.
//
ID   Fatty acid metabolism.
AC   KW-0276
DE   Protein involved in the biochemical reactions with fatty acids. Fatty
DE   acids are long chain organic acids of the general formula
DE   CH3(CnHx)COOH. They are constituents of lipids and can be saturated or
DE   unsaturated. The esterified forms are important both as energy storage
DE   molecules and structural molecules.
SY   Fatty acid metabolic process.
GO   GO:0006631; fatty acid metabolic process
HI   Biological process: Lipid metabolism; Fatty acid metabolism.
CA   Biological process.
//
ID   Fertilization.
AC   KW-0278
DE   Protein involved in fertilization, the union of two haploid cells, the
DE   gametes, to form a diploid cell, the zygote.
GO   GO:0007338; single fertilization
HI   Biological process: Fertilization.
CA   Biological process.
//
ID   Fibrinogenolytic toxin.
AC   KW-1206
DE   Toxin involved in fibrinogen degradation leading to a decrease of
DE   plasma fibrinogen concentration. Fibrinogenolytic toxins are mostly
DE   snake venom proteases.
HI   Molecular function: Toxin; Hemostasis impairing toxin; Fibrinogenolytic toxin.
CA   Molecular function.
//
ID   Fibrinolysis.
AC   KW-0280
DE   Protein involved in fibrin degradation leading to the dissolving of
DE   blood clots.
GO   GO:0042730; fibrinolysis
HI   Biological process: Hemostasis; Blood coagulation; Fibrinolysis.
CA   Biological process.
//
ID   Fibrinolytic toxin.
AC   KW-1205
DE   Toxin involved in fibrin degradation leading to the dissolution of
DE   fibrin clots. Fibrinolytic toxins are mostly snake venom proteases.
HI   Molecular function: Toxin; Hemostasis impairing toxin; Fibrinolytic toxin.
CA   Molecular function.
//
ID   Fimbrium.
AC   KW-0281
DE   Protein found in a fimbrium or pilus. A fimbrium or pilus is a hair-
DE   like, non-flagellar, polymeric filamentous appendage that extend from
DE   the bacterial or archaeal cell surface, such as type 1 pili, P-pili,
DE   type IV pili or curli. Pili perform a variety of functions, including
DE   surface adhesion, motility, cell-cell interactions, biofilm formation,
DE   conjugation, DNA uptake, and twitching motility.
SY   Fimbria; Pili; Pilus.
GO   GO:0009289; pilus
HI   Cellular component: Fimbrium.
CA   Cellular component.
//
ID   Fimbrium biogenesis.
AC   KW-1029
DE   Protein which is involved in the formation, organization or
DE   maintenance of the fimbrium, a long hair-like cell surface appendage.
DE   The flagellar apparatus consists of the flagellar filament made of
DE   polymerized flagellin, the hook-like structure near the cell surface
DE   and a system of rings embedded in the cell enveloppe (the basal body
DE   or flagellar motor). The basal body and the hook anchor the whip-like
DE   filament to the cell surface. The flagellum is a rotating structure
DE   whose switches propels the cell through a liquid medium.
SY   Fimbria biogenesis; Pili biogenesis; Pilus biogenesis.
HI   Biological process: Fimbrium biogenesis.
CA   Biological process.
//
ID   Flagellar rotation.
AC   KW-0283
DE   Protein involved in the movement of the flagella.
SY   Flagella motility; Flagellar motility; Flagella rotation;
SY   Flagellum motility; Flagellum rotation.
GO   GO:0097588; archaeal or bacterial-type flagellum-dependent cell motility
HI   Biological process: Flagellar rotation.
CA   Biological process.
//
ID   Flagellum.
AC   KW-0282
DE   Protein present in the flagellum, a long whip-like or feathery
DE   structure which propels the cell through a liquid medium. This motile
DE   cilium is produced by unicellular eukaryotes and by the motile male
DE   gametes of many eukaryotic organisms. The flagella commonly have a
DE   characteristic axial '9+2' microtubular array (axoneme) and bends are
DE   generated along the length of the flagellum by restricted sliding of
DE   the nine outer doublets.
SY   Flagella; Motile cilia; Motile cilium; Undulipodia; Undulipodium.
GO   GO:0031514; motile cilium
HI   Cellular component: Cell projection; Cilium; Flagellum.
CA   Cellular component.
//
ID   Flavonoid biosynthesis.
AC   KW-0284
DE   Protein involved in the synthesis of flavonoids, polyphenolic
DE   compounds possessing 15 carbon atoms; two benzene rings joined by a
DE   linear three carbon chain, a C6-C3-C6 skeleton. C6 presents a benzene
DE   ring, C3 often is part of of an oxygen-containing ring. Flavonoids are
DE   coloured phenolic pigments originally considered vitamins (Vitamins P,
DE   C2) but not shown to have any nutritional role. They are responsible
DE   for the red/purple colours of many higher plants.
SY   Flavonoid anabolism; Flavonoid biosynthetic process;
SY   Flavonoid formation; Flavonoid synthesis.
GO   GO:0009813; flavonoid biosynthetic process
HI   Biological process: Flavonoid biosynthesis.
CA   Biological process.
//
ID   Flavoprotein.
AC   KW-0285
DE   Enzymes which contain one or more flavin nucleotides (FAD or FMN) as
DE   redox cofactors or cosubstrates. Flavoproteins are involved, for
DE   example, in the oxidative degradation of pyruvate, fatty acids and
DE   amino acids, and in the process of electron transport.
HI   Ligand: Flavoprotein.
CA   Ligand.
//
ID   Flight.
AC   KW-0286
DE   Protein which stimulates or which is involved in flight, the act of
DE   passing through the air by the use of wings.
SY   Flight behavior.
GO   GO:0007629; flight behavior
HI   Biological process: Flight.
CA   Biological process.
//
ID   Flowering.
AC   KW-0287
DE   Protein involved in the transition from vegetative to reproductive
DE   development in plants.
SY   Flower development.
GO   GO:0009908; flower development
HI   Biological process: Flowering.
CA   Biological process.
//
ID   FMN.
AC   KW-0288
DE   Protein involved in flavin adenine mononucleotide synthesis or protein
DE   which contains at least one FMN as prosthetic group/cofactor
DE   (flavoproteins) or cosubstrate, such as many oxidation-reduction
DE   enzymes. FMN is an electron carrier molecule that functions as a
DE   hydrogen acceptor. The generic term "flavin" derives from the Latin
DE   word flavius ("yellow") because of the brilliant yellow color they
DE   exhibit as solids and in neutral aqueous solutions.
SY   Flavin adenine mononucleotide; Flavin mononucleotide;
SY   Riboflavin 5'-phosphate.
HI   Ligand: Flavoprotein; FMN.
CA   Ligand.
//
ID   Folate biosynthesis.
AC   KW-0289
DE   Protein involved in the synthesis of folate, the ionic form of folic
DE   acid (Latin folium, 'leaf'), first found in spinach leaves. Folate is
DE   converted in a two-step reduction into its coenzyme form
DE   tetrahydrofolate, often abbreviated FH4 or THF, which acts as a
DE   carrier of one-carbon units at several oxidation levels in a variety
DE   of biosyntheses.
SY   Folacin anabolism; Folacin biosynthesis; Folacin biosynthetic process;
SY   Folacin formation; Folacin synthesis; Folate anabolism;
SY   Folate biosynthetic process; Folate formation; Folate synthesis;
SY   Folic acid anabolism; Folic acid biosynthesis;
SY   Folic acid biosynthetic process; Folic acid formation;
SY   Folic acid synthesis; Pteroylglutamic acid anabolism;
SY   Pteroylglutamic acid biosynthesis;
SY   Pteroylglutamic acid biosynthetic process;
SY   Pteroylglutamic acid formation; Pteroylglutamic acid synthesis.
GO   GO:0046656; folic acid biosynthetic process
HI   Biological process: Folate biosynthesis.
CA   Biological process.
//
ID   Folate-binding.
AC   KW-0290
DE   Protein that binds folate, the ionic form of folic acid.
SY   Folacin-binding; Folic acid-binding; Pteroylglutamic acid-binding.
GO   GO:0005542; folic acid binding
HI   Ligand: Folate-binding.
CA   Ligand.
//
ID   Formylation.
AC   KW-0291
DE   A protein in which either the N-terminal N-formylmethionine has not
DE   been processed by the methionyl-tRNA formyltransferase or which is
DE   posttranslationally modified by the attachment of at least one formyl
DE   group.
SY   N-Formylated.
HI   PTM: Formylation.
CA   PTM.
//
ID   Fruit ripening.
AC   KW-0292
DE   Protein involved in fruit ripening. The fruit is the matured ovary of
DE   a plant, enclosing the seed(s). The plant hormone ethylene stimulates
DE   fruit ripening.
GO   GO:0009835; fruit ripening
HI   Biological process: Fruit ripening.
CA   Biological process.
//
ID   Fruiting body.
AC   KW-0293
DE   Protein involved in fruiting body formation or expressed in fruiting
DE   bodies, any specialized reproductive structure that produces spores or
DE   gametes in fungi, slime molds, algae, etc. Fruiting bodies are
DE   distinct in size, shape and coloration for each species.
HI   Developmental stage: Fruiting body.
CA   Developmental stage.
//
ID   Fucose metabolism.
AC   KW-0294
DE   Protein involved in the biochemical reactions with fucose. L-fucose
DE   (6-deoxy-L-galactose) is present in some algae and identified in the
DE   chains of glycoproteins; it is the only polysaccharides of certain
DE   bacterias.
SY   Fucose metabolic process.
GO   GO:0006004; fucose metabolic process
HI   Biological process: Carbohydrate metabolism; Fucose metabolism.
CA   Biological process.
//
ID   Fungicide.
AC   KW-0295
DE   Protein capable of killing or inhibiting growth of fungi.
SY   Anti-fungal.
GO   GO:0031640; killing of cells of another organism
GO   GO:0050832; defense response to fungus
HI   Molecular function: Antimicrobial; Fungicide.
CA   Molecular function.
//
ID   Fusion of virus membrane with host cell membrane.
AC   KW-1169
DE   Viral protein involved in the merging of the virus envelope with host
DE   cytoplasmic membrane during viral penetration into host cell. Virus
DE   fusion proteins drive this fusion reaction by undergoing a major
DE   conformational change that is triggered by interactions with the
DE   target cell. This pathway is used by viruses whose fusion protein is
DE   usually pH independent such as most paramyxoviruses, herpesviruses and
DE   retroviruses. MHV-JHM coronavirus has been shown to fuse directly with
DE   the host cytoplasmic membrane. Prokaryotic viruses such as
DE   Tectiviridae fuse their inner membrane with the host cytoplasmic
DE   membrane whereas Cystoviridae fuse their outer membrane with the host
DE   cytoplasmic membrane.
SY   Viral entry into host cell via plasma membrane fusion.
GO   GO:0019064; fusion of virus membrane with host plasma membrane
HI   Biological process: Virus entry into host cell; Viral penetration into host cytoplasm; Fusion of virus membrane with host membrane; Fusion of virus membrane with host cell membrane.
CA   Biological process.
//
ID   Fusion of virus membrane with host endosomal membrane.
AC   KW-1170
DE   Viral protein involved in the merging of the virus envelope with host
DE   endosomal membrane during viral penetration into host cell. Viral
DE   fusion proteins drive this fusion reaction by undergoing a major
DE   conformational change that is triggered by interactions with the
DE   target cell. The specific trigger is mainly endosome acidification
DE   which induce activation of the fusion protein by conformational
DE   change. This pathway is used by enveloped viruses which are
DE   endocytosed and whose fusion protein is usually pH-dependent like
DE   influenza A virus, rhabdoviruses, bornaviruses, filoviruses,
DE   asfarviridae, flaviviridae, alphaviruses, HIV-1, avian leukosis virus,
DE   SARS, 229E, and MHV-2 coronaviruses.
SY   Viral entry into host cell via plasma membrane fusion.
GO   GO:0039654; fusion of virus membrane with host endosome membrane
HI   Biological process: Virus entry into host cell; Viral penetration into host cytoplasm; Fusion of virus membrane with host membrane; Fusion of virus membrane with host endosomal membrane.
CA   Biological process.
//
ID   Fusion of virus membrane with host membrane.
AC   KW-1168
DE   Viral protein involved in the merging of the virion membrane with a
DE   host membrane during viral penetration into host cell. Viral fusion
DE   proteins drive this fusion reaction by undergoing a major
DE   conformational change that is triggered by interactions with the
DE   target cell. The specific trigger depends on the virus and can be
DE   exposure to low pH in the endocytic pathway or interaction of the
DE   virion with the host receptor(s). In prokaryotic viruses, host-virus
DE   membrane fusion can occur either at the host outer membrane or plasma
DE   membrane. Bacteriophages such as cystoviridae fuse their external
DE   envelope with the host outer membrane, whereas others like
DE   tectiviridae fuse their inner envelope with the host plasma membrane.
SY   Viral entry into host cell via membrane fusion.
GO   GO:0039663; membrane fusion involved in viral entry into host cell
HI   Biological process: Virus entry into host cell; Viral penetration into host cytoplasm; Fusion of virus membrane with host membrane.
CA   Biological process.
//
ID   Fusion of virus membrane with host outer membrane.
AC   KW-1239
DE   Viral protein involved in the merging of the virion external lipidic
DE   membrane (envelope) with the prokaryotic host outer membrane during
DE   viral penetration into host cell. Bacteriophages such as Cystoviridae
DE   for example fuse their membrane with the host outer membrane.
SY   Viral entry into host cell via outer membrane fusion.
GO   GO:0098997; fusion of virus membrane with host outer membrane
HI   Cellular component: Virion; Fusion of virus membrane with host outer membrane.
HI   Biological process: Virus entry into host cell; Viral penetration into host cytoplasm; Fusion of virus membrane with host membrane; Fusion of virus membrane with host outer membrane.
CA   Biological process.
//
ID   G-protein coupled acetylcholine receptor impairing toxin.
AC   KW-1214
DE   Toxin which interferes with the function of the muscarinic
DE   acetylcholine receptor (mAChR). The mAChR is a specific class of G-
DE   protein coupled receptor (GPCR) that binds acetylcholine. These toxins
DE   are mostly found in snake venoms.
SY   mAChR regulator; Muscarinic acetylcholine receptor regulator.
HI   Molecular function: Toxin; G-protein coupled receptor impairing toxin; G-protein coupled acetylcholine receptor impairing toxin.
CA   Molecular function.
//
ID   G-protein coupled receptor.
AC   KW-0297
DE   Receptors which transduce extracellular signals across the cell
DE   membrane. At the external side they receive a ligand (a photon in case
DE   of opsins), and at the cytosolic side they activate a guanine
DE   nucleotide-binding (G) protein. These receptors are hydrophobic
DE   proteins that cross the membrane seven times.
SY   7TM receptor; GPCR.
GO   GO:0004930; G protein-coupled receptor activity
GO   GO:0007186; G protein-coupled receptor signaling pathway
HI   Molecular function: Receptor; G-protein coupled receptor.
HI   Molecular function: Transducer; G-protein coupled receptor.
CA   Molecular function.
//
ID   G-protein coupled receptor impairing toxin.
AC   KW-1213
DE   Toxin which interferes with the function of G-protein coupled
DE   receptors (GPCRs). These toxins are mostly found in snake and scorpion
DE   venoms.
SY   GPCR regulator.
HI   Molecular function: Toxin; G-protein coupled receptor impairing toxin.
CA   Molecular function.
//
ID   G0/G1 host cell cycle checkpoint dysregulation by virus.
AC   KW-1077
DE   Viral protein involved in the modulation of host cell cycle
DE   progression by dysregulating the G0/G1 transition. Some viruses
DE   benefit from keeping cells in resting state (G0), while others favor
DE   entry through G1 and subsequent cell division to replicate more
DE   efficiently.
GO   GO:0039646; perturbation by virus of host G0/G1 transition checkpoint
HI   Biological process: Host-virus interaction; Modulation of host cell cycle by virus; G0/G1 host cell cycle checkpoint dysregulation by virus.
CA   Biological process.
//
ID   G1/S host cell cycle checkpoint dysregulation by virus.
AC   KW-1078
DE   Viral protein involved in the modulation of host cell cycle
DE   progression by dysregulating the G1/S transition. Some viruses benefit
DE   from an arrest in G1 to S phase transition, while others force through
DE   S phase to favor their own replication.
GO   GO:0039645; perturbation by virus of host G1/S transition checkpoint
HI   Biological process: Host-virus interaction; Modulation of host cell cycle by virus; G1/S host cell cycle checkpoint dysregulation by virus.
CA   Biological process.
//
ID   Galactitol metabolism.
AC   KW-0298
DE   Protein involved in the biochemical reactions with galactitol. This
DE   sugar alcohol is derived from galactose. It can be found in certain
DE   bacteria, yeasts, fungi and plants. In humans, the congenital
DE   galactosemic cataracts are due to an accumulation of galactitol within
DE   the lens.
SY   Dulcitol metabolic process; Dulcitol metabolism;
SY   Galactitol metabolic process.
GO   GO:0019402; galactitol metabolic process
HI   Biological process: Galactitol metabolism.
CA   Biological process.
//
ID   Galactose metabolism.
AC   KW-0299
DE   Protein involved in the biochemical reactions with the monosaccharide
DE   galactose. This optical isomer (epimer) of glucose is a constituent of
DE   various oligosaccharides (e.g. lactose, raffinose), polysaccharides
DE   (e.g. galactans, agar, gum arabic) and also of sphingolipids
DE   (galactocerebrosides).
SY   Galactose metabolic process.
GO   GO:0006012; galactose metabolic process
HI   Biological process: Carbohydrate metabolism; Galactose metabolism.
CA   Biological process.
//
ID   Gamma-carboxyglutamic acid.
AC   KW-0301
DE   Protein which possesses at least one gamma-carboxyglutamic acid, a
DE   vitamin K dependent post-translational modification of a glutamate
DE   residue found in blood coagulation proteins and in the proteins of
DE   calcified tissues. Gamma-carboxyglutamyl residues are good chelators
DE   of calcium ions. There are two natural forms of vitamin K, which are
DE   phylloquinone (vitamin K1 or phytylmenaquinone) in green vegetables
DE   and menaquinone (vitamin K2 or menaquinone-n, depending of the number
DE   of isoprene units of the side-chain or MK-n) in intestinal bacteria,
DE   as well as one synthetic provitamin form, menadione (vitamin K3). In
DE   infants, the primary symptom of a deficiency of this fat-soluble
DE   vitamin is a hemorrhagic syndrome.
SY   1-carboxyglutamic acid.
HI   PTM: Gamma-carboxyglutamic acid.
CA   PTM.
//
ID   Gangliosidosis.
AC   KW-0331
DE   Protein which, if defective, causes gangliosidosis. Gangliosidosis
DE   defines any of a group of autosomal recessive lysosomal storage
DE   diseases characterized by the accumulation of gangliosides GM1 or GM2
DE   and related glycoconiugates, and by progressive psychomotor
DE   deterioration. Subtypes include GM1-gangliosidoses and GM2-
DE   gangliosidoses.
HI   Disease: Gangliosidosis.
CA   Disease.
//
ID   Gap junction.
AC   KW-0303
DE   Protein component of gap junctions which are specialized regions of
DE   the plasma membrane formed by a cluster of channels allowing small
DE   molecules to diffuse from the cytosol of one cell to that of an
DE   adjacent cell. A current model of the gap junction consists of a
DE   cluster of gap-junction channels. Both membranes contain connexon
DE   hemichannels, composed of a hexamer of an integral membrane protein
DE   which is often referred to as connexin. The junction of two adjacent
DE   connexons forms a gap-junction channel.
GO   GO:0005921; gap junction
HI   Cellular component: Cell junction; Gap junction.
CA   Cellular component.
//
ID   Gap protein.
AC   KW-0302
DE   A group of insect proteins which are crucial for the development of
DE   proper embryonic segmentation. These are the first proteins that
DE   define the coarsest subdivisions. Generally, gap gene mutations are
DE   lethal and eliminate a large block of contiguous segments from the
DE   embryo.
GO   GO:0035282; segmentation
HI   Molecular function: Developmental protein; Gap protein.
CA   Molecular function.
//
ID   Gas vesicle.
AC   KW-0304
DE   Protein of, or involved in synthesis of, gas vesicles. Gas vesicles
DE   (GV) are hollow, watertight, gas-permeable proteinaceous
DE   nanostructures found in some microorganisms. During planktonic growth
DE   they allow positioning of the organism at a favorable depth for light
DE   or nutrient acquisition. By regulating their relative GV content,
DE   aquatic microbes can perform vertical migrations. The GV is
DE   impermeable to liquid water but is highly permeable to gases and is
DE   normally filled with air. As they scatter light, they may also protect
DE   against UV light. Two main proteins are present in the gas vesicle:
DE   GvpA, an extremely hydrophobic protein which makes the ribs that form
DE   the structure, and GvpC, which binds to the outside of the ribs, helps
DE   shape GVs and stiffens the structure against collapse.
GO   GO:0031411; gas vesicle
HI   Cellular component: Gas vesicle.
CA   Cellular component.
//
ID   Gaseous exchange.
AC   KW-0305
DE   Protein involved in the exchange of gases.
GO   GO:0007585; respiratory gaseous exchange by respiratory system
HI   Biological process: Gaseous exchange.
CA   Biological process.
//
ID   Gastrulation.
AC   KW-0306
DE   Protein involved in gastrulation, a stage in early embryogenesis in
DE   which cell movements result in a massive reorganization of the embryo
DE   from an initially unstructured group of cells, the blastula, into a
DE   multi-layered organism. During gastrulation, the primary germ layers
DE   (endoderm, mesoderm, and ectoderm) are formed and organized in their
DE   proper locations for further development.
GO   GO:0007369; gastrulation
HI   Molecular function: Developmental protein; Gastrulation.
HI   Biological process: Gastrulation.
CA   Biological process.
//
ID   Gaucher disease.
AC   KW-0307
DE   Protein which, if defective, causes Gaucher disease, the most
DE   prevalent sphingolipid storage disorder caused by a recessively
DE   inherited deficiency of the enzyme glucocerebrosidase. Most common in
DE   Ashkenazi Jews, it is associated with hepatosplenomegaly (enlargement
DE   of liver and spleen) and, in severe early onset forms of the disease,
DE   with neurological dysfunction.
HI   Disease: Gaucher disease.
CA   Disease.
//
ID   Genetically modified food.
AC   KW-0308
DE   Any protein used in a biotechnological process that results in the
DE   modification of a naturally occurring food (crop or livestock).
DE   Examples include proteins introduced to enable herbicide or insect
DE   resistance or proteins that act in fruit ripening.
HI   Technical term: Genetically modified food.
CA   Technical term.
//
ID   Germination.
AC   KW-0309
DE   Protein involved in germination, the physiological and developmental
DE   changes by a seed, spore, pollen grain (microspore), or zygote that
DE   occur after release from dormancy, and encompassing events prior to
DE   and including the first visible indications of growth.
HI   Biological process: Germination.
CA   Biological process.
//
ID   Gibberellin signaling pathway.
AC   KW-0939
DE   Protein involved in the gibberellin (GA) signaling pathway (e.g.
DE   transport and signal transduction) that regulates many aspects of
DE   plant growth including seed germination, hypocotyl elongation, stem
DE   elongation, leaf expansion, trichome development, pollen maturation
DE   and flower and fruit development. GAs are tetracyclic diterpenoid
DE   phytohormones found in plants, fungi and bacteria. They are named
DE   GA1....GAn in order of discovery. The term "gibberellin" was first
DE   given to a substance, produced by the fungus Gibberella fujikuroi,
DE   which caused overgrowth symptoms in rice. This substance was later
DE   proven to be a mixture of GAs, with GA1 and GA3 being the active
DE   factors.
SY   GA signalling pathway; GA-signalling pathway;
SY   Gibberellic acid signaling pathway.
GO   GO:0009740; gibberellic acid mediated signaling pathway
HI   Biological process: Gibberellin signaling pathway.
CA   Biological process.
//
ID   Glaucoma.
AC   KW-0955
DE   Protein which, if defective, causes glaucoma, a group of eye diseases
DE   characterized by pathological changes in the optic disk, progressive
DE   loss of optic nerve axons and visual field defects. Most of the
DE   patients with glaucoma have an increased intraocular pressure. The
DE   disease is painless and often diagnosed at a late stage, when visual
DE   field defects are severe. Glaucoma is one of the leading causes of
DE   blindness worldwide.
HI   Disease: Glaucoma.
CA   Disease.
//
ID   Gluconate utilization.
AC   KW-0311
DE   Protein involved in the biochemical pathway(s) in which gluconate is
DE   the carbon source.
GO   GO:0019521; D-gluconate metabolic process
HI   Biological process: Gluconate utilization.
CA   Biological process.
//
ID   Gluconeogenesis.
AC   KW-0312
DE   Protein involved in the biosynthesis of "new" glucose from such
DE   noncarbohydrate precursors as pyruvate, lactate, certain amino acids
DE   and intermediates of the tricarboxylic acid cycle.
SY   Glucose biosynthesis; Glucose biosynthetic process.
GO   GO:0006094; gluconeogenesis
HI   Biological process: Gluconeogenesis.
CA   Biological process.
//
ID   Glucose metabolism.
AC   KW-0313
DE   Protein involved in the biochemical reactions with the 6-carbon aldose
DE   sugar glucose.
SY   Glucose metabolic process.
GO   GO:0006006; glucose metabolic process
HI   Biological process: Carbohydrate metabolism; Glucose metabolism.
CA   Biological process.
//
ID   Glutamate biosynthesis.
AC   KW-0314
DE   Protein involved in the synthesis of the acidic amino acid glutamate.
DE   Glutamate is a component of proteins and can also act as a
DE   neurotransmitter in the central nervous system.
SY   Glutamate anabolism; Glutamate biosynthetic process;
SY   Glutamate formation; Glutamate synthesis; Glutamic acid anabolism;
SY   Glutamic acid biosynthesis; Glutamic acid biosynthetic process;
SY   Glutamic acid formation; Glutamic acid synthesis.
GO   GO:0006537; glutamate biosynthetic process
HI   Biological process: Amino-acid biosynthesis; Glutamate biosynthesis.
CA   Biological process.
//
ID   Glutamine amidotransferase.
AC   KW-0315
DE   Enzyme that catalyzes the removal of the ammonia group from glutamine
DE   and transfers it to a substrate to form a new carbon-nitrogen group.
DE   Glutamine amidotransferase (GATase) domains can occur either as single
DE   polypeptides or as domains in larger multifunctional proteins. There
DE   exist two classes of glutamine amidotransferases domains: I and II.
SY   Glutamine metabolic process.
GO   GO:0006541; glutamine metabolic process
HI   Domain: Glutamine amidotransferase.
CA   Domain.
//
ID   Glutaricaciduria.
AC   KW-0316
DE   Protein which, if defective, causes glutaricaciduria (GA), a metabolic
DE   disorder characterized by the excretion of glutaric acid in the urine.
DE   Type I GA is caused by the deficiency of glutaryl-CoA dehydrogenase, a
DE   mitochondrial enzyme involved in the metabolism of lysine,
DE   hydroxylysine and tryptophan. Type II GA differs from type I in that
DE   multiple acyl-CoA dehydrogenase deficiencies result in a large
DE   excretion not only of glutaric acid but also of lactic, ethylmalonic,
DE   butyric, isobutyric, 2-methyl-butyric, and isovaleric acids. GA II can
DE   result from a deficiency of any one of 3 mitochondrial molecules: the
DE   alpha and beta subunits of electron transfer flavoprotein and electron
DE   transfer flavoprotein-ubiquinone oxidoreductase.
SY   GA; Glutaric aciduria.
HI   Disease: Glutaricaciduria.
CA   Disease.
//
ID   Glutathione biosynthesis.
AC   KW-0317
DE   Protein involved in the synthesis of the tripeptide glutathione
DE   (Gamma-Glu-Cys-Gly). Glutathione sulphydryl group is kept largely in
DE   the reduced state; this allows it to act as a sulphydryl buffer,
DE   reducing any disulphide bonds formed within cytoplasmic proteins to
DE   cysteines. Glutathione is also important as a cofactor for the enzyme
DE   glutathione peroxidase, in the uptake of amino acids and participates
DE   in leucotriene synthesis. Glutathione contains an unusual peptide
DE   linkage between the carboxyl group of the glutamate side chain and the
DE   amine group of cysteine.
SY   Glutathione anabolism; Glutathione biosynthetic process;
SY   Glutathione formation; Glutathione synthesis.
GO   GO:0006750; glutathione biosynthetic process
HI   Biological process: Glutathione biosynthesis.
CA   Biological process.
//
ID   Glutathionylation.
AC   KW-0318
DE   Protein which is posttranslationally modified by the attachment of a
DE   glutathione molecule by a disulfide bond.
SY   Glutathionylated.
HI   PTM: Glutathionylation.
CA   PTM.
//
ID   Glycation.
AC   KW-0971
DE   Protein containing one or more covalently linked glucose residues,
DE   resulting from a non-enzymatic spontaneous reaction. The carbohydrate
DE   is attached to an amino-acid nitrogen atom (e.g. from a lysine side
DE   chain, or the amino-terminal group). This modification is a side
DE   effect of diabetes and aging. Glycation is the first step toward the
DE   formation of advanced glycation endproducts (AGEs). Some AGEs are
DE   benign, but others are implicated in age-related chronic diseases such
DE   as: type II diabetes mellitus, cardiovascular diseases, Alzheimer's
DE   disease, etc.
SY   Glycated.
HI   PTM: Glycoprotein; Glycation.
CA   PTM.
//
ID   Glycerol metabolism.
AC   KW-0319
DE   Protein involved in the biochemical reactions with the 3-carbon sugar
DE   alcohol glycerol. Glycerol is primarily of interest as the central
DE   structural component of the major classes of biological lipids,
DE   triglycerides and phosphatidyl phospholipids. It is also an important
DE   intermediate in carbohydrate and lipid metabolism.
SY   Glycerol metabolic process.
GO   GO:0006071; glycerol metabolic process
HI   Biological process: Glycerol metabolism.
CA   Biological process.
//
ID   Glycogen biosynthesis.
AC   KW-0320
DE   Protein involved in the synthesis of glycogen, a branched polymer of
DE   D-glucose (mostly -(1-4) linked, but with some -(1-6) linked residues
DE   at branch points). Glycogen is the major short term storage polymer of
DE   animal cells and is particularly abundant in liver and to a lesser
DE   extent in muscles.
SY   Glycogen anabolism; Glycogen biosynthetic process; Glycogen formation;
SY   Glycogen synthesis.
GO   GO:0005978; glycogen biosynthetic process
HI   Biological process: Glycogen biosynthesis.
CA   Biological process.
//
ID   Glycogen metabolism.
AC   KW-0321
DE   Protein involved in the biochemical reactions with glycogen, a
DE   branched polymer of D-glucose (mostly -(1-4) linked, but with some
DE   - (1-6) linked residues at branch points). Glycogen is the major short
DE   term storage polymer of animal cells and is particularly abundant in
DE   liver and to a lesser extent in muscles.
SY   Glycogen metabolic process.
GO   GO:0005977; glycogen metabolic process
HI   Biological process: Carbohydrate metabolism; Glycogen metabolism.
CA   Biological process.
//
ID   Glycogen storage disease.
AC   KW-0322
DE   Protein which, if defective, causes glycogen storage disease, a group
DE   of inherited metabolic disorders involving the enzymes responsible for
DE   the synthesis and degradation of glycogen. At least thirteen types of
DE   this disease have been described.
HI   Disease: Glycogen storage disease.
CA   Disease.
//
ID   Glycolate pathway.
AC   KW-0323
DE   Protein involved in the glycolate pathway, synthesis of the amino
DE   acids serine and glycine from glycolate via a glyoxylate intermediate.
SY   C2 cycle; Oxidative photosynthetic carbon pathway;
SY   Photorespiration pathway; Photosynthetic carbon oxydation cycle.
GO   GO:0009854; oxidative photosynthetic carbon pathway
HI   Biological process: Glycolate pathway.
CA   Biological process.
//
ID   Glycolysis.
AC   KW-0324
DE   Protein involved in the anaerobic enzymatic conversion of glucose to
DE   lactate or pyruvate, resulting in energy stored in the form of
DE   adenosine triphosphate (ATP), as occurs in skeletal muscle and in
DE   embryonic tissue.
GO   GO:0006096; glycolytic process
HI   Biological process: Glycolysis.
CA   Biological process.
//
ID   Glycoprotein.
AC   KW-0325
DE   Protein containing one or more covalently linked carbohydrates of
DE   various types, i.e. from monosaccharides to branched polysaccharides,
DE   including glycosylphosphatidylinositol (GPI), glycosaminoglycans
DE   (GAG).
SY   Glycosylated.
HI   PTM: Glycoprotein.
CA   PTM.
//
ID   Glycosidase.
AC   KW-0326
DE   Hydrolases which attack glycosidic bonds in carbohydrates,
DE   glycoproteins and glycolipids. The glycosidases are not highly
DE   specific. Usually they distinguish only the type of bond, e.g. O- or
DE   N-glycosidic, and its configuration (alpha or beta).
GO   GO:0008152; metabolic process
GO   GO:0016798; hydrolase activity, acting on glycosyl bonds
HI   Molecular function: Hydrolase; Glycosidase.
CA   Molecular function.
//
ID   Glycosome.
AC   KW-0327
DE   Protein present in the glycosome, a microbody-like organelle found in
DE   all members of the protist order Kinetoplastida examined. Nine enzymes
DE   involved in glucose and glycerol metabolism are associated with these
DE   organelles. These enzymes are involved in pathways which, in other
DE   organisms, are usually located in the cytosol.
GO   GO:0020015; glycosome
HI   Cellular component: Glycosome.
CA   Cellular component.
//
ID   Glycosyltransferase.
AC   KW-0328
DE   Enzymes that catalyze the transfer of glycosyl (sugar) residues to an
DE   acceptor, both during degradation (cosubstrates= water or inorganic
DE   phosphate) and during biosynthesis of polysaccharides, glycoproteins
DE   and glycolipids. In biosynthetic glycosyl transfers, the common
DE   activated monomeric sugar intermediate is a nucleoside diphosphate
DE   sugar.
GO   GO:0016757; glycosyltransferase activity
HI   Molecular function: Transferase; Glycosyltransferase.
CA   Molecular function.
//
ID   Glyoxylate bypass.
AC   KW-0329
DE   Protein involved in the glyoxylate bypass, an alternate route in
DE   bacteria, plants, and fungi which bypasses the CO2-evolving steps of
DE   the tricarboxylic acid cycle, thus permiting the utilization of fatty
DE   acids or acetate, in the form of acetyl-CoA, as sole carbon source,
DE   particularly for the net biosynthesis of carbohydrate from fatty
DE   acids. The glyoxylate bypass is especially prominent in plant seeds.
SY   Glyoxylate cycle.
GO   GO:0006097; glyoxylate cycle
HI   Biological process: Glyoxylate bypass.
CA   Biological process.
//
ID   Glyoxysome.
AC   KW-0330
DE   Protein present in the glyoxysome, a membrane-surrounded plant cell
DE   organelle, especially found in germinating seeds, and involved in the
DE   breakdown and conversion of fatty acids to acetyl-CoA for the
DE   glyoxylate bypass. Since it is also rich in catalase, the glyoxysome
DE   may be related to the microbodies or peroxisomes or derived from them.
GO   GO:0009514; glyoxysome
HI   Cellular component: Glyoxysome.
CA   Cellular component.
//
ID   GMP biosynthesis.
AC   KW-0332
DE   Protein involved in the synthesis of GMP. GMP is the abbreviation for
DE   the nucleotide guanosine 5'-monophosphate.
SY   GMP anabolism; GMP biosynthetic process; GMP formation; GMP synthesis;
SY   Guanosine 5'-monophosphate anabolism;
SY   Guanosine 5'-monophosphate biosynthetic process;
SY   Guanosine 5'-monophosphate formation;
SY   Guanosine 5'-monophosphate synthesis; Guanylic acid anabolism;
SY   Guanylic acid biosynthetic process; Guanylic acid formation;
SY   Guanylic acid synthesis.
GO   GO:0006177; GMP biosynthetic process
HI   Biological process: Purine biosynthesis; GMP biosynthesis.
CA   Biological process.
//
ID   Golgi apparatus.
AC   KW-0333
DE   Protein found in the Golgi apparatus, an organelle present in
DE   eukaryotic cells that appears as a stack of 6-8 plate-like membranous
DE   compartments and associated vesicles and vacuoles, often located near
DE   the centrosome. It has four functionally distinct compartments: cis,
DE   medial and trans Golgi stacks, and the trans Golgi network (TGN). The
DE   first three are involved in posttranslational modifications of
DE   proteins (e.g., N- or O-glycosylation, sulfation, processing of acid
DE   hydrolases), while the TGN is involved in sorting the proteins to
DE   their final destination (e.g., to lysosomes, to secretory vesicles, or
DE   to plasma membrane).
SY   Golgi complex; Golgi stack.
GO   GO:0005794; Golgi apparatus
HI   Cellular component: Golgi apparatus.
CA   Cellular component.
//
ID   Gonadal differentiation.
AC   KW-0334
DE   Protein involved in gonadal differentiation, the progressive
DE   restriction of the developmental potential and increasing
DE   specialization of function which takes place during the embryonic
DE   development and leads to the formation of gamete-producing glands,
DE   such as ovary or testis.
GO   GO:0007506; gonadal mesoderm development
HI   Biological process: Differentiation; Gonadal differentiation.
CA   Biological process.
//
ID   Gout.
AC   KW-0335
DE   Protein which, if defective, causes gout, a recurrent acute arthritis
DE   of peripheral joints caused by the precipitation of monosodium urate
DE   crystals in articular cartilage. Gout is usually due to overproduction
DE   of uric acid secondary to an inherited abnormality of purine
DE   metabolism, but may be a result of urate under-excretion.
HI   Disease: Gout.
CA   Disease.
//
ID   GPI-anchor.
AC   KW-0336
DE   Protein bound to the lipid bilayer of a membrane through either a GPI-
DE   anchor (glycosylphosphatidylinositol anchor), a complex oligoglycan
DE   linked to a phosphatidylinositol group, or a GPI-like-anchor, a
DE   similar complex oligoglycan linked to a sphingolipidinositol group,
DE   resulting in the attachment of the C-terminus of the protein to the
DE   membrane.
SY   Glycosylphosphatidylinositol anchor;
SY   Glycosylsphingolipidinositol anchor.
GO   GO:0098552; side of membrane
HI   PTM: Glycoprotein; GPI-anchor.
HI   PTM: Lipoprotein; GPI-anchor.
HI   Cellular component: Membrane; GPI-anchor.
CA   PTM.
//
ID   GPI-anchor biosynthesis.
AC   KW-0337
DE   Protein involved in the synthesis or the attachment to a protein of a
DE   GPI-anchor (glycosylphosphatidylinositol anchor) or a GPI-like-anchor
DE   (glycosylsphingolipidinositol anchor), both of which have complex
DE   oligoglycan linked to a phospholipidinositol molecule that serves to
DE   attach the C-terminus of some extracellular membrane proteins to the
DE   lipid bilayer of a membrane. The core glycolipid is composed of a
DE   tetraglycan: three mannose units and one glucosamine linked to a
DE   phospholipidinositol. The terminal mannose is linked to the protein
DE   via an ethanolamine attached to the C-terminal of the mature protein.
DE   The core structure is conserved from protozoa to humans. There are,
DE   however, marked differences in the glycosyl side chains attached to
DE   the core glycolipid. The phospholipid component may be either a
DE   phosphatide (two long chain fatty acids attached by ester linkage to
DE   glycerol phosphate) or a sphingolipid (a long chain fatty acid
DE   attached by amide linkage to a ceramide phosphate). Some yeast and
DE   Dictyosteliida synthesize the GPI-like anchor de novo, whereas other
DE   organisms may interconvert the lipid components by a "resculpting"
DE   process after the anchor is attached to the protein.
SY   Glycosylphosphatidylinositol anchor anabolism;
SY   Glycosylphosphatidylinositol anchor biosynthesis;
SY   Glycosylphosphatidylinositol anchor biosynthetic process;
SY   Glycosylphosphatidylinositol anchor formation;
SY   Glycosylphosphatidylinositol anchor synthesis; GPI-anchor anabolism;
SY   GPI-anchor biosynthetic process; GPI-anchor formation;
SY   GPI-anchor synthesis.
GO   GO:0006506; GPI anchor biosynthetic process
HI   Biological process: GPI-anchor biosynthesis.
CA   Biological process.
//
ID   Growth arrest.
AC   KW-0338
DE   Protein involved in growth arrest, a phenomenon occurring when a cell
DE   does not proceed through the cell cycle.
SY   Cell cycle arrest; Cellular quiescence.
GO   GO:0051726; regulation of cell cycle
HI   Biological process: Cell cycle; Growth arrest.
CA   Biological process.
//
ID   Growth factor.
AC   KW-0339
DE   Protein which, by binding to a cell-surface receptor, triggers an
DE   intracellular signal-transduction pathway leading to differentiation,
DE   proliferation, or other cellular response.
GO   GO:0008083; growth factor activity
HI   Molecular function: Growth factor.
CA   Molecular function.
//
ID   Growth factor binding.
AC   KW-0340
DE   Protein other than a receptor that binds to a cell's growth factor.
GO   GO:0019838; growth factor binding
HI   Molecular function: Growth factor binding.
CA   Molecular function.
//
ID   Growth regulation.
AC   KW-0341
DE   Protein involved in growth regulation, which usually implies the
DE   control of the rate of division rather than that of the size of an
DE   individual cell.
SY   Regulation of cell growth.
HI   Biological process: Growth regulation.
CA   Biological process.
//
ID   GTP-binding.
AC   KW-0342
DE   Protein which binds guanosine 5'-triphosphate (GTP), a ribonucleotide
DE   guanosine (a purine base guanine linked to the sugar D-ribofuranose)
DE   that carries three phosphate groups esterified to the sugar moiety.
SY   Guanosine 5'-triphosphate-binding; Guanosine triphosphate-binding.
GO   GO:0005525; GTP binding
HI   Ligand: Nucleotide-binding; GTP-binding.
CA   Ligand.
//
ID   GTPase activation.
AC   KW-0343
DE   GTPase-activating protein (GAP) by itself does not hydrolyze GTP but,
DE   by binding to a GTPase, accelerates its intrinsic GTPase activity.
GO   GO:0005096; GTPase activator activity
HI   Molecular function: GTPase activation.
CA   Molecular function.
//
ID   Guanine-nucleotide releasing factor.
AC   KW-0344
DE   Protein which catalyzes the release of GDP (guanosine 5'-diphosphate).
GO   GO:0005085; guanyl-nucleotide exchange factor activity
HI   Molecular function: Guanine-nucleotide releasing factor.
CA   Molecular function.
//
ID   HDL.
AC   KW-0345
DE   Protein or apolipoprotein associated with High-Density Lipoproteins
DE   (HDL), a class of proteins involved in lipid (cholesterol,
DE   phospholipids and triacylglycerol) metabolism in the body fluids. HDL
DE   are formed in the liver and are involved in reverse cholesterol
DE   transport, the transport of cholesterol from peripherical tissues to
DE   the liver. Apolipoproteins are proteins which are specifically
DE   associated with lipoproteins, which is not the case for all the
DE   proteins associated with HDL or with the other lipoprotein classes.
GO   GO:0034364; high-density lipoprotein particle
HI   Cellular component: HDL.
CA   Cellular component.
//
ID   Hearing.
AC   KW-1009
DE   Protein involved in hearing, the special sense by which an organism is
DE   able to receive an auditory stimulus, convert it to a molecular
DE   signal, and recognize and characterize the signal. Sonic stimuli are
DE   detected in the form of vibrations and are processed to form a sound.
GO   GO:0007605; sensory perception of sound
HI   Biological process: Hearing.
CA   Biological process.
//
ID   Helical capsid protein.
AC   KW-1139
DE   Viral protein that forms a helical capsid to protect the viral genome.
DE   Viral helical capsids are about 7-30 nm in diameter and 200-2000 nm
DE   long.
GO   GO:0019029; helical viral capsid
HI   Cellular component: Virion; Capsid protein; Helical capsid protein.
HI   Cellular component: Virion; Helical capsid protein.
CA   Cellular component.
//
ID   Helicase.
AC   KW-0347
DE   Protein with an helicase activity. Helicases are ATPases that catalyze
DE   the unwinding of double-stranded nucleic acids. They are tightly
DE   integrated (or coupled) components of various macromolecular complexes
DE   which are involved in processes such as DNA replication,
DE   recombination, and nucleotide excision repair, as well as RNA
DE   transcription and splicing.
GO   GO:0004386; helicase activity
HI   Ligand: Nucleotide-binding; ATP-binding; Helicase.
HI   Molecular function: Hydrolase; Helicase.
CA   Molecular function.
//
ID   Hemagglutinin.
AC   KW-0348
DE   Protein which causes agglutination of erythrocytes or other cell
DE   types: In viruses, a protein which is responsible for attaching the
DE   virus to cell receptors and for initiating infection.
HI   Molecular function: Hemagglutinin.
CA   Molecular function.
//
ID   Heme.
AC   KW-0349
DE   Protein containing at least one heme, an iron atom coordinated to a
DE   protoporphyrin IX. In myoglobin and hemoglobin, one of the
DE   coordination positions of iron is occupied by oxygen or other ligands,
DE   such as carbon monoxide. Hemes are also found in cytochromes of the
DE   electron-transport chain where they bind electrons, in reducing
DE   peroxides (catalases and peroxidases), and act as terminal components
DE   in multienzyme systems involved in hydroxylation. Cytochrome c is the
DE   only common heme protein in which the heme is covalently bound.
SY   Haeme.
HI   Ligand: Iron; Heme.
HI   Ligand: Metal-binding; Heme.
CA   Ligand.
//
ID   Heme biosynthesis.
AC   KW-0350
DE   Protein involved in the synthesis of heme, an iron atom coordinated to
DE   a protoporphyrin IX.
SY   Haeme anabolism; Haeme biosynthesis; Haeme biosynthetic process;
SY   Haeme formation; Haeme synthesis; Heme anabolism;
SY   Heme biosynthetic process; Heme formation; Heme synthesis.
GO   GO:0006783; heme biosynthetic process
HI   Biological process: Heme biosynthesis.
CA   Biological process.
//
ID   Hemoglobin-binding.
AC   KW-0351
DE   Protein which binds hemoglobin, a gas-carrying protein found in red
DE   blood cells.
SY   Haemoglobin-binding.
GO   GO:0030492; hemoglobin binding
HI   Ligand: Hemoglobin-binding.
CA   Ligand.
//
ID   Hemolymph clotting.
AC   KW-0353
DE   Protein involved in the coagulation of hemolymph, the circulatory
DE   fluid of invertebrate animals which is functionally comparable to the
DE   blood and lymph of vertebrates.
SY   Haemolymph clotting; Hemolymph coagulation.
GO   GO:0042381; hemolymph coagulation
HI   Biological process: Hemolymph clotting.
CA   Biological process.
//
ID   Hemolysis.
AC   KW-0354
DE   Protein involved in hemolysis, the disruption of the integrity of the
DE   red cell membrane, thus causing the release of hemoglobin.
SY   Haemolysis.
GO   GO:0031640; killing of cells of another organism
HI   Biological process: Cytolysis; Hemolysis.
CA   Biological process.
//
ID   Hemolytic uremic syndrome.
AC   KW-1068
DE   Protein which, if defective, causes hemolytic uremic syndrome, a
DE   disorder characterized by non-immune hemolytic anemia,
DE   thrombocytopenia and renal failure. The vast majority of cases are
DE   sporadic, occur in young children and are associated with epidemics of
DE   diarrhea due to bacterial infections. This typical form of the disease
DE   has a good prognosis and death rate is very low. In contrast to
DE   typical hemolytic uremic syndrome, atypical forms present without a
DE   prodrome of enterocolitis and diarrhea and have a poor prognosis, with
DE   frequent development of end-stage renal disease or death.
SY   Hemolytic-uremic syndrome; HUS.
HI   Disease: Hemolytic uremic syndrome.
CA   Disease.
//
ID   Hemophilia.
AC   KW-0355
DE   Protein which, if defective, causes hemophilia, a genetic disease
DE   characterized by uncontrollable bleeding due to a sex-linked recessive
DE   deficiency of blood-clotting factor (usually of Factor VIII).
SY   Haemophilia.
HI   Biological process: Hemostasis; Blood coagulation; Hemophilia.
HI   Disease: Hemophilia.
CA   Disease.
//
ID   Hemorrhagic toxin.
AC   KW-1200
DE   Toxin which induces the leakage of blood components into tissues by
DE   damaging endothelial cells or disturbing endothelial cell interactions
DE   with the basement membrane. Hemorrhagic toxins are mostly found in
DE   snake venoms.
SY   Hemorrhagin.
HI   Molecular function: Toxin; Hemostasis impairing toxin; Hemorrhagic toxin.
CA   Molecular function.
//
ID   Hemostasis.
AC   KW-0356
DE   Protein involved in the arrest of bleeding through blood clotting and
DE   contraction of blood vessels.
GO   GO:0007599; hemostasis
HI   Biological process: Hemostasis.
CA   Biological process.
//
ID   Hemostasis impairing toxin.
AC   KW-1199
DE   Toxin which interferes with hemostasis regrouping all mechanisms
DE   implicated in the cessation of blood loss through damaged vessels.
DE   Hence, hemostasis impairing toxins not only interfere with platelet
DE   aggregation, the coagulation cascade, fibrinogen depletion, and fibrin
DE   clot degradation (fibrinolysis), but also provoke hemorrhage by
DE   damaging endothelial cells or disturbing their interaction with the
DE   basement membrane. Numerous snake venom families have the capacity to
DE   interfere with hemostasis.
HI   Molecular function: Toxin; Hemostasis impairing toxin.
CA   Molecular function.
//
ID   Heparan sulfate.
AC   KW-0357
DE   Protein containing at least one heparan sulfate, a highly sulfated
DE   glycosaminoglycan, closely related to heparin, which consists of
DE   repeating units of disaccharides composed of iduronic acid,
DE   glucosamine and N-acetylglucosamine.
HI   PTM: Glycoprotein; Proteoglycan; Heparan sulfate.
CA   PTM.
//
ID   Heparin-binding.
AC   KW-0358
DE   Protein which binds heparin, a highly sulfated glycosaminoglycan which
DE   consists of repeating units of disaccharides composed of D-
DE   glucosamine, D-glucuronic acid or L-iduronic acid. This anticoagulant
DE   is found in the granules of mast cells.
GO   GO:0008201; heparin binding
HI   Molecular function: Heparin-binding.
CA   Molecular function.
//
ID   Herbicide resistance.
AC   KW-0359
DE   Protein that confers, on plants, bacteria or other microorganisms, the
DE   ability to withstand herbicide action. Herbicides are chemicals that
DE   selectively kill plants. Herbicide resistance occurs usually as a
DE   result of mutation or amplification of a gene, e.g. 3-phosphoshikimate
DE   1-carboxyvinyltransferase.
SY   Resistance to herbicide.
GO   GO:0009635; response to herbicide
HI   Biological process: Herbicide resistance.
CA   Biological process.
//
ID   Hereditary hemolytic anemia.
AC   KW-0360
DE   Protein which, if defective, causes hereditary hemolytic anemia, a
DE   hereditary disease characterized by the premature destruction of red
DE   blood cells.
SY   Hereditary haemolytic anemia.
HI   Disease: Hereditary hemolytic anemia.
CA   Disease.
//
ID   Hereditary multiple exostoses.
AC   KW-0361
DE   Protein which, if defective, causes hereditary multiple exostoses
DE   (EXT). It is an autosomal dominant disease characterized by the
DE   formation of cartilage-capped benign tumors (exostoses), developing
DE   from the juxtaepiphyseal regions of the long bones and often
DE   accompanied by skeletal deformities and short stature.
HI   Disease: Hereditary multiple exostoses.
CA   Disease.
//
ID   Hereditary nonpolyposis colorectal cancer.
AC   KW-0362
DE   Protein which, if defective, causes hereditary non-polyposis
DE   colorectal cancer (HNPCC), also known as Lynch's syndrome. It is an
DE   autosomal dominant syndrome which confers an increased risk for
DE   colorectal and endometrial cancers as well as others tumors.
DE   Clinically, HNPCC is often divided into two subgroups: type I,
DE   characterized by a hereditary predisposition to colorectal cancer, a
DE   young age of onset, and carcinoma observed in the proximal colon; type
DE   II, characterized by an increased risk for cancers in certain tissues
DE   such as the uterus, ovary, breast, stomach, small intestine, skin, and
DE   larynx in addition to the colon.
SY   HNPCC; Lynch's syndrome.
HI   Disease: Hereditary nonpolyposis colorectal cancer.
CA   Disease.
//
ID   Hereditary spastic paraplegia.
AC   KW-0890
DE   Protein which, if defective, causes hereditary spastic paraplegias
DE   (HSPs). HSPs are a diverse class of hereditary degenerative spinal
DE   cord disorders characterized by a slow, gradual, progressive weakness
DE   and spasticity (stiffness) of the legs. Initial symptoms may include
DE   difficulty with balance, weakness and stiffness in the legs, muscle
DE   spasms, and dragging the toes when walking. In some forms of the
DE   disorder, bladder symptoms (such as incontinence) may appear, or the
DE   weakness and stiffness may spread to other parts of the body. Rate of
DE   progression and the severity of symptoms are quite variable.
SY   HSP.
HI   Disease: Neurodegeneration; Hereditary spastic paraplegia.
CA   Disease.
//
ID   Hermansky-Pudlak syndrome.
AC   KW-0363
DE   Protein which, if defective, causes Hermansky-Pudlak syndrome, a rare
DE   autosomal recessive disorder characterized by oculocutaneous albinism
DE   and storage pool deficiency due to an absence of platelet dense
DE   bodies. Lysosomal ceroid lipofuscinosis, pulmonary fibrosis and
DE   granulomatous colitis are occasional manifestations of the disease.
SY   HPS.
HI   Disease: Albinism; Hermansky-Pudlak syndrome.
CA   Disease.
//
ID   Heterocyst.
AC   KW-0364
DE   Protein which is implicated in heterocyst formation. A heterocyst is a
DE   differentiated cyanobacterial cell that carries out nitrogen fixation.
DE   The heterocysts function as the sites for nitrogen fixation under
DE   aerobic conditions. They are formed in response to a lack of fixed
DE   nitrogen (NH4 or NO3). The morphological differentiation is
DE   accompanied by biochemical alterations. The mature heterocysts contain
DE   no functional photosystem II and cannot produce oxygen. Instead, they
DE   contain only photosystem I, which enables them to carry out cyclic
DE   photophosphorylation and ATP regeneration. These changes provide the
DE   appropriate conditions for the functioning of the oxygen-sensitive
DE   nitrogenase.
GO   GO:0043158; heterocyst development
HI   Developmental stage: Heterocyst.
CA   Developmental stage.
//
ID   Heterotaxy.
AC   KW-1056
DE   Protein which, if defective, causes heterotaxy, a broad group of
DE   disorders caused by failure to correctly establish left-right
DE   patterning during embryogenesis with consequent abnormal segmental
DE   arrangements of cardiac chambers, vessels, lungs, and/or abdominal
DE   organs. Heterotaxy include complex cardiac malformations, situs
DE   inversus, situs ambiguus, isomerism. Situs inversus indicates complete
DE   left-right reversal of organ position and is not usually associated
DE   with structural anomalies. Situs ambiguus is an abnormal arrangement
DE   of viscera almost invariably associated with complex cardiovascular
DE   malformations as well as anomalies of the spleen and the
DE   gastrointestinal system. Isomerism is a defect in asymmetry of paired
DE   organs that usually have distinct right and left forms, but in this
DE   condition, are mirror images.
SY   Heterotaxia; Situs ambiguous; Situs ambiguus; Visceral heterotaxy.
HI   Disease: Heterotaxy.
CA   Disease.
//
ID   Hibernation.
AC   KW-0909
DE   Protein involved in the process of hibernation. Hibernation is a state
DE   of inactivity in an animal brought about by short day lengths, cold
DE   temperatures and limitations of food.
GO   GO:0042750; hibernation
HI   Biological process: Hibernation.
CA   Biological process.
//
ID   Hirschsprung disease.
AC   KW-0367
DE   Hirschsprung's disease (HSCR); a genetic disorder of neural crest
DE   development characterized by the absence of intramural ganglion cells
DE   in the hindgut; often resulting in intestinal obstruction.
SY   HSCR.
HI   Disease: Hirschsprung disease.
CA   Disease.
//
ID   Histidine biosynthesis.
AC   KW-0368
DE   Protein involved in the synthesis of the weakly basic amino acid
DE   histidine.
SY   Histidine anabolism; Histidine biosynthetic process;
SY   Histidine formation; Histidine synthesis.
GO   GO:0000105; histidine biosynthetic process
HI   Biological process: Amino-acid biosynthesis; Histidine biosynthesis.
CA   Biological process.
//
ID   Histidine metabolism.
AC   KW-0369
DE   Protein involved in the biochemical reactions with the weakly basic
DE   amino acid histidine.
SY   Histidine metabolic process.
GO   GO:0006547; histidine metabolic process
HI   Biological process: Histidine metabolism.
CA   Biological process.
//
ID   Holoprosencephaly.
AC   KW-0370
DE   A clinically variable and genetically heterogeneous malformation in
DE   which the developing forebrain fails to correctly separate into right
DE   and left hemispheres. In its most severe form (alobar
DE   holoprosencephaly), the forebrain consists of a single ventricle, and
DE   midbrain structures may be malformed as well. In the most extreme
DE   cases, anophthalmia or cyclopia is evident along with a congenital
DE   absence of the mature nose. In milder forms (semilobar or lobar
DE   holoprosencephaly), rudimentary midline structures are present. The
DE   less severe form features facial dysmorphia characterized by ocular
DE   hypertelorism, defects of the upper lip and/or nose, and absence of
DE   the olfactory nerves or corpus callosum. The majority of cases are
DE   sporadic, although families with both autosomal dominant and autosomal
DE   recessive holoprosencephaly have been described.
HI   Disease: Holoprosencephaly.
CA   Disease.
//
ID   Homeobox.
AC   KW-0371
DE   Protein which contains at least one homeobox, a conserved sequence
DE   originally detected, on the nucleotide level, in many of the genes
DE   which give rise to homeotic and segmentation mutants in Drosophila.
DE   The homeobox, also termed homeodomain, consists of about 60 amino
DE   acids and is involved in DNA-binding.
SY   Homeodomain.
GO   GO:0003677; DNA binding
HI   Domain: Homeobox.
CA   Domain.
//
ID   Hormone.
AC   KW-0372
DE   Protein which functions as a hormone, a biochemical substance secreted
DE   by specialized cells that affects the metabolism or behavior of other
DE   cells which possess functional receptors for the hormone. Hormones may
DE   be hydrophilic, like insulin, in which case the receptors are on the
DE   cell surface, or lipophilic, like the steroids, where the receptor can
DE   be intracellular.
GO   GO:0005179; hormone activity
HI   Molecular function: Hormone.
CA   Molecular function.
//
ID   Host cell inner membrane.
AC   KW-1030
DE   Protein found in or associated with the prokaryotic host cell inner
DE   membrane, a selectively permeable membrane which separates the host
DE   cytoplasm from the host periplasm in prokaryotes with 2 membranes.
SY   Host inner membrane.
GO   GO:0020002; host cell plasma membrane
HI   Cellular component: Membrane; Host membrane; Host cell membrane; Host cell inner membrane.
CA   Cellular component.
//
ID   Host cell junction.
AC   KW-1031
DE   Protein found in or associated with a host cell junction, a host cell-
DE   host cell or host cell-host extracellular matrix contact within a
DE   tissue of a host multicellular organism, especially abundant in host
DE   epithelia. In vertebrates, there are three major types of cell
DE   junctions: anchoring junctions (e.g. adherens junctions),
DE   communicating junctions (e.g. gap junctions) and occluding junctions
DE   (e.g. tight junctions).
GO   GO:0044156; host cell junction
HI   Cellular component: Host cell junction.
CA   Cellular component.
//
ID   Host cell lysis by virus.
AC   KW-0578
DE   Viral protein involved in the lysis of the host cell allowing the
DE   release of mature, newly formed virions. Viruses use different way to
DE   lyse their host cell. They can express viroporins as Adenoviridae or
DE   Picornaviridae do in the late phase of infection. Phycodnaviridae for
DE   their part seem to express lytic phospholipids. In dsDNA prokaryotic
DE   viruses, lysis-specific proteins are expressed: a holin, which
DE   permeabilizes the inner membrane and an endolysin which then gains
DE   access to and degrades the host peptidoglycans. Some bacterioviruses
DE   express a signal-containing endolysin and thus do not need the holin
DE   function.
GO   GO:0044659; viral release from host cell by cytolysis
HI   Biological process: Cytolysis; Host cell lysis by virus.
HI   Biological process: Viral release from host cell; Host cell lysis by virus.
CA   Biological process.
//
ID   Host cell membrane.
AC   KW-1032
DE   Protein found in or associated with the host cytoplasmic membrane, a
DE   selectively permeable membrane which separates the cytoplasm from its
DE   surroundings. Known as the host cell inner membrane in prokaryotes
DE   with 2 membranes.
SY   Host cytoplasmic membrane; Host plasmalemma; Host plasma membrane.
GO   GO:0020002; host cell plasma membrane
HI   Cellular component: Membrane; Host membrane; Host cell membrane.
CA   Cellular component.
//
ID   Host cell outer membrane.
AC   KW-1033
DE   Protein found in or associated with the prokaryotic cell outer
DE   membrane, a selectively permeable membrane which separates the
DE   prokaryotic periplasm from its surroundings in prokaryotes with 2
DE   membranes. Traditionally only Gram-negative bacteria were thought of
DE   as having an outer membrane, but recent work has shown some
DE   Actinobacteria, including Mycobacterium tuberculosis, as well as at
DE   least 1 archaea (Ignicoccus hospitalis) have a cell outer membrane.
SY   Host outer membrane.
GO   GO:0020002; host cell plasma membrane
HI   Cellular component: Membrane; Host membrane; Host cell outer membrane.
CA   Cellular component.
//
ID   Host cell projection.
AC   KW-1034
DE   Protein found in or associated with a host cell projection, a host
DE   cell protrusion such as pseudopodium, filopodium, lamellipodium,
DE   growth cone, flagellum, acrosome, axon, pili or bacterial comet tail.
DE   These membrane-cytoskeleton-coupled processes are involved in many
DE   biological functions, such as host cell motility, cancer-cell
DE   invasion, endocytosis, phagocytosis, exocytosis, pathogen infection,
DE   neurite extension and cytokinesis.
SY   Host cell protrusion.
GO   GO:0044157; host cell projection
HI   Cellular component: Host cell projection.
CA   Cellular component.
//
ID   Host cell receptor for virus entry.
AC   KW-1183
DE   Cell surface protein used by a virus as an attachment and entry
DE   receptor. In some cases, binding to a cellular receptor is not
DE   sufficient for infection: an additional cell surface molecule, or
DE   coreceptor, is required for entry. Some viruses are able to use
DE   different receptors depending on the target cell type. In prokaryotic
DE   viruses, cell receptor for virus entry can also be localized on host
DE   outer membrane, pilus or flagellum.
SY   Viral receptor activity.
GO   GO:0001618; virus receptor activity
HI   Molecular function: Receptor; Host cell receptor for virus entry.
CA   Molecular function.
//
ID   Host cytoplasm.
AC   KW-1035
DE   Protein found in the host cytoplasm, the content of a host cell within
DE   the plasma membrane and, in eukaryotics cells, surrounds the host
DE   nucleus.
GO   GO:0030430; host cell cytoplasm
HI   Cellular component: Host cytoplasm.
CA   Cellular component.
//
ID   Host cytoplasmic vesicle.
AC   KW-1036
DE   Protein found in or associated with host cytoplasmic vesicles, which
DE   mediate vesicular transport among the organelles of host secretory and
DE   endocytic systems.
GO   GO:0044161; host cell cytoplasmic vesicle
HI   Cellular component: Host cytoplasmic vesicle.
CA   Cellular component.
//
ID   Host cytoskeleton.
AC   KW-1037
DE   Protein which is a component or which is associated with the host
DE   cytoskeleton, a dynamic three-dimensional structure that fills the
DE   host cytoplasm of eukaryotic cells. It is responsible for cell
DE   movement, cytokinesis, and the organization of the organelles or
DE   organelle-like structures within the host cell.
GO   GO:0044163; host cytoskeleton
HI   Cellular component: Host cytoplasm; Host cytoskeleton.
CA   Cellular component.
//
ID   Host endoplasmic reticulum.
AC   KW-1038
DE   Protein whose subcellular location is the host endoplasmic reticulum
DE   (ER), which is an extensive network of membrane tubules, vesicles and
DE   flattened cisternae (sac-like structures) found throughout the
DE   eukaryotic host cell, especially those responsible for the production
DE   of hormones and other secretory products.
GO   GO:0044165; host cell endoplasmic reticulum
HI   Cellular component: Host endoplasmic reticulum.
CA   Cellular component.
//
ID   Host endosome.
AC   KW-1039
DE   Protein found in or associated with host endosomes, which are highly
DE   dynamic membrane systems involved in transport within the host cell,
DE   they receive endocytosed host cell membrane molecules and sort them
DE   for either degradation or recycling back to the host cell surface.
DE   They also receive newly synthesised proteins destined for host
DE   vacuolar/lysosomal compartments.
GO   GO:0044174; host cell endosome
HI   Cellular component: Host endosome.
CA   Cellular component.
//
ID   Host G2/M cell cycle arrest by virus.
AC   KW-1079
DE   Viral protein involved in the modulation of host cell cycle by
DE   inhibiting the G2/M transition. A variety of viruses have been
DE   associated with G2/M arrest, including some DNA viruses, some RNA
DE   viruses and retroviruses but the mechanisms by which arrest is
DE   achieved greatly differs between those viruses.
GO   GO:0039592; perturbation by virus of G2/M transition of host mitotic cell cycle
HI   Biological process: Host-virus interaction; Modulation of host cell cycle by virus; Host G2/M cell cycle arrest by virus.
CA   Biological process.
//
ID   Host gene expression shutoff by virus.
AC   KW-1190
DE   Viral protein which prevents host gene expression by blocking for
DE   example host transcription, mRNA export or translation. This gives
DE   virus transcripts a competitive edge to use the hijacked translation
DE   machinery. Preventing the expression of host proteins is also a
DE   strategy to counteract the antiviral response.
GO   GO:0039657; suppression by virus of host gene expression
HI   Biological process: Host-virus interaction; Host gene expression shutoff by virus.
CA   Biological process.
//
ID   Host Golgi apparatus.
AC   KW-1040
DE   Protein found in the host Golgi apparatus, a series of flattened,
DE   cisternal membranes and similar vesicles usually arranged in close
DE   apposition to each other to form stacks. In mammalian cells, the host
DE   Golgi apparatus is juxtanuclear, often pericentriolar. The stacks are
DE   connected laterally by tubules to create a perinuclear ribbon
DE   structure, the 'Golgi ribbon'. In plants and lower animal cells, the
DE   host Golgi exists as many copies of discrete stacks dispersed
DE   throughout the host cytoplasm. It is a polarized structure with, in
DE   most higher eukaryotic cells, a cis-face associated with a tubular
DE   reticular network of membranes facing the endoplasmic reticulum, the
DE   cis-Golgi network (CGN), a medial area of disk-shaped flattened
DE   cisternae, and a trans-face associated with another tubular reticular
DE   membrane network, the trans-Golgi network (TGN) directed toward the
DE   host plasma membrane and compartments of the host endocytic pathway.
SY   Host apparatus golgiensis; Host complexus golgiensis; Host Golgi;
SY   Host Golgi complex.
GO   GO:0044177; host cell Golgi apparatus
HI   Cellular component: Host Golgi apparatus.
CA   Cellular component.
//
ID   Host lipid droplet.
AC   KW-1041
DE   Protein characteristic of host lipid droplet, a dynamic cytoplasmic
DE   host organelle which consists of an heterogeneous macromolecular
DE   assembly of lipids and proteins covered by a unique phospholipid
DE   monolayer. They may play a role in host lipid metabolism and storage,
DE   and they may be involved in the regulation of intracellular
DE   trafficking and signal transduction.
SY   Host adiposome; Host lipid bodies; Host lipid body;
SY   Host lipid particle; Host monolayer-surrounded lipid storage body;
SY   Host oil bodies; Host oil body; Host oleosome; Host spherosome.
GO   GO:0044186; host cell lipid droplet
HI   Cellular component: Host lipid droplet.
CA   Cellular component.
//
ID   Host lysosome.
AC   KW-1042
DE   Protein found in the host lysosome, a membrane-limited organelle
DE   present in all eukaryotic cells, which contains a large number of
DE   hydrolytic enzymes that are used for degrading almost any kind of
DE   cellular constituent, including entire organelles. The mechanisms
DE   responsible for delivering cytoplasmic cargo to the host
DE   lysosome/vacuole are known collectively as autophagy and play an
DE   important role in the maintenance of homeostasis.
GO   GO:0044187; host cell lysosome
HI   Cellular component: Host lysosome.
CA   Cellular component.
//
ID   Host membrane.
AC   KW-1043
DE   Protein which is membrane-bound or membrane-associated with the host
DE   membrane, a lipid bilayer which surrounds host enclosed spaces and
DE   compartments. This selectively permeable structure is essential for
DE   effective separation of a host cell or organelle from its
DE   surroundings.
GO   GO:0033644; host cell membrane
HI   Cellular component: Membrane; Host membrane.
CA   Cellular component.
//
ID   Host microsome.
AC   KW-1044
DE   Protein found in host microsomes, which are a heterogenous set of
DE   vesicles 20-200 nm in diameter and formed from the host endoplasmic
DE   reticulum when host cells are disrupted.
GO   GO:0033648; host intracellular membrane-bounded organelle
HI   Cellular component: Host endoplasmic reticulum; Host microsome.
CA   Cellular component.
//
ID   Host mitochondrion.
AC   KW-1045
DE   Protein encoded by or localized in the host mitochondrion, a
DE   semiautonomous, self-reproducing organelle that occurs in the
DE   cytoplasm of all cells of most, but not all, host eukaryotes. Each
DE   host mitochondrion is surrounded by a double limiting membrane. The
DE   inner membrane is highly invaginated, and its projections are called
DE   cristae. They are the sites of the reactions of oxidative
DE   phosphorylation, which result in the formation of ATP.
GO   GO:0033650; host cell mitochondrion
HI   Cellular component: Host mitochondrion.
CA   Cellular component.
//
ID   Host mitochondrion inner membrane.
AC   KW-1046
DE   Protein found in or associated with the host mitochondrion inner
DE   membrane, the membrane which separates the host mitochondrial matrix
DE   from the host mitochondrial intermembrane space.
SY   Host inner mitochondrial membrane; Host mitochondrial inner membrane.
GO   GO:0044192; host cell mitochondrial inner membrane
HI   Cellular component: Membrane; Host membrane; Host mitochondrion inner membrane.
HI   Cellular component: Host mitochondrion; Host mitochondrion inner membrane.
CA   Cellular component.
//
ID   Host mitochondrion outer membrane.
AC   KW-1047
DE   Protein found in or associated with the host mitochondrion outer
DE   membrane, the host mitochondrial membrane facing the host cytoplasm.
SY   Host mitochondrial outer membrane; Host outer mitochondrial membrane.
GO   GO:0044193; host cell mitochondrial outer membrane
HI   Cellular component: Membrane; Host membrane; Host mitochondrion outer membrane.
HI   Cellular component: Host mitochondrion; Host mitochondrion outer membrane.
CA   Cellular component.
//
ID   Host mRNA suppression by virus.
AC   KW-1192
DE   Viral protein involved in suppressing host mRNAs expression to
DE   maximize expression of viral mRNAs. Decimating cellular mRNAs
DE   eventually leads to shutoff of host proteins expression and gives
DE   virus transcripts a competitive edge for access to the cellular
DE   translation machinery. Preventing the expression of host proteins is
DE   also a strategy to counteract the antiviral response. Suppression of
DE   host mRNA can be performed by interfering with host pre-mRNA
DE   processing function (splicing or polyadenylation), by degrading mRNAs
DE   or blocking their export from the nucleus to the cytoplasm.
HI   Biological process: Host-virus interaction; Host gene expression shutoff by virus; Eukaryotic host gene expression shutoff by virus; Host mRNA suppression by virus.
CA   Biological process.
//
ID   Host nucleus.
AC   KW-1048
DE   Protein located in the host nucleus, which is the most obvious
DE   organelle in any host eukaryotic cell. It is a membrane-bound
DE   organelle and is surrounded by double membranes. It communicates with
DE   the surrounding cytosol via numerous nuclear pores.
GO   GO:0042025; host cell nucleus
HI   Cellular component: Host nucleus.
CA   Cellular component.
//
ID   Host periplasm.
AC   KW-1049
DE   Protein located in the host periplasm, the space between the inner and
DE   outer membrane in host Gram-negative bacteria. In Gram-positive
DE   bacteria a smaller periplasmic space is found between the inner
DE   membrane and the peptidoglycan layer. Also used for the host
DE   intermembrane spaces of host fungi and host organelles.
SY   Host periplasmic space.
GO   GO:0044229; host cell periplasmic space
HI   Cellular component: Host periplasm.
CA   Cellular component.
//
ID   Host synapse.
AC   KW-1051
DE   Protein located in the host synapse, the communicating cell-cell
DE   junctions that allow signals to pass from a host nerve cell to a host
DE   target cell. In a chemical synapse, the signal is carried by a
DE   neurotransmitter which diffuses across a narrow synaptic cleft and
DE   activates a receptor on the postsynaptic membrane of the target cell.
GO   GO:0044221; host cell synapse
HI   Cellular component: Host synapse.
CA   Cellular component.
//
ID   Host thylakoid.
AC   KW-1050
DE   Protein located in or on the host thylakoid, a membranous cellular
DE   structure containing the photosynthetic pigments, reaction centers and
DE   electron-transport chain. In host chloroplast, thylakoids stack up to
DE   form the grana or stay as single cisternae and interconnect the grana.
DE   Thylakoid, where photosynthesis occurs, are found in chloroplasts,
DE   cyanelles and in photosynthetic bacteria where they are the extensive
DE   invaginations of the plasma membrane.
GO   GO:0044159; host thylakoid
HI   Cellular component: Host thylakoid.
CA   Cellular component.
//
ID   Host-virus interaction.
AC   KW-0945
DE   Viral or cellular protein involved in a host-virus interaction.
DE   Viruses interact with many cellular pathways to achieve their
DE   replication cycle. Entry into the host cell, transport to the viral
DE   replication sites or viral exit from the host cell are all steps that
DE   require specific interactions between the virus and its host.
DE   Additionally, the evasion from the host immune response requires a lot
DE   of viral proteins to associate with and inhibit cellular proteins with
DE   antiviral functions.
HI   Biological process: Host-virus interaction.
CA   Biological process.
//
ID   Hyaluronic acid.
AC   KW-0373
DE   Protein which binds hyaluronic acic, an acidic glycosaminoglycan which
DE   consists of repeating units of the disaccharide composed of D-
DE   glucuronic acid and N-acetyl-D-glucosamine. This linear polymer is
DE   present in cell coats and in the extracellular ground substance of the
DE   connective tissues of vertebrates; it also occurs in the synovial
DE   fluid in joints and in the vitreous humor of the eye.
GO   GO:0005540; hyaluronic acid binding
HI   Ligand: Hyaluronic acid.
CA   Ligand.
//
ID   Hybridoma.
AC   KW-0374
DE   Protein sequenced from a hybridoma, an artificially produced hybrid
DE   cell line created by fusion of a lymphocyte and a myeloma cell. These
DE   cells can multiply indefinitely in culture and produce monoclonal
DE   antibodies.
HI   Technical term: Hybridoma.
CA   Technical term.
//
ID   Hydrogen ion transport.
AC   KW-0375
DE   Protein involved in the transport of hydrogen ions across a membrane.
DE   Used to power processes such as ATP synthesis and bacterial flagellar
DE   rotation.
SY   Hydrogen cation transport; Proton transport.
GO   GO:1902600; proton transmembrane transport
HI   Biological process: Transport; Ion transport; Hydrogen ion transport.
CA   Biological process.
//
ID   Hydrogen peroxide.
AC   KW-0376
DE   Protein involved in hydrogen peroxide (H(2)O(2)) decomposition, e.g.,
DE   catalase. H(2)O(2) is generated by the body as a byproduct of aerobic
DE   cellular respiration.
GO   GO:0042744; hydrogen peroxide catabolic process
HI   Molecular function: Oxidoreductase; Peroxidase; Hydrogen peroxide.
HI   Biological process: Hydrogen peroxide.
CA   Biological process.
//
ID   Hydrogenosome.
AC   KW-0377
DE   Protein characteristic of the hydrogenosome, a redox organelle of
DE   anaerobic unicellular eukaryotes which contains hydrogenase and
DE   produces hydrogen and ATP by glycolysis. They are found in various
DE   unrelated eukaryotes, such as anaerobic flagellates, chytridiomycete
DE   fungi and ciliates. Most hydrogenosomes lack a genome, but some like
DE   that of the anaerobic ciliate Nyctotherus ovalis, have retained a
DE   rudimentary genome.
GO   GO:0042566; hydrogenosome
HI   Cellular component: Hydrogenosome.
CA   Cellular component.
//
ID   Hydrolase.
AC   KW-0378
DE   Enzyme which catalyzes hydrolysis reaction, i.e. the addition of the
DE   hydrogen and hydroxyl ions of water to a molecule with its consequent
DE   splitting into two or more simpler molecules.
GO   GO:0016787; hydrolase activity
HI   Molecular function: Hydrolase.
CA   Molecular function.
//
ID   Hydroxylation.
AC   KW-0379
DE   Protein which is posttranslationally modified by the attachment of at
DE   least one hydroxyl (-OH) group.
SY   Hydroxylated.
HI   PTM: Hydroxylation.
CA   PTM.
//
ID   Hyperlipidemia.
AC   KW-0380
DE   Protein which, if defective, causes hyperlipidemia, a condition
DE   characterized by the elevation of lipids in the bloodstream. There are
DE   different types of hyperlipidemias: type I (lipoprotein lipase
DE   deficiency), IIa (hypercholesterolemia; LDL receptor deficiency), IIb
DE   (combined hyperlipidemia), III (dysbetalipoproteinemia), IV
DE   (hypertriglyceridemia) and V (mixed hyperlipidemia).
HI   Disease: Hyperlipidemia.
CA   Disease.
//
ID   Hypersensitive response.
AC   KW-0381
DE   Protein involved in hypersensitive response, a complex and early
DE   defense response that causes necrosis and cell death to restrict the
DE   growth of a pathogen. Local and systemic biochemical changes include
DE   generation of active oxygen species (oxidative burst), cell death,
DE   overproduction of lignin-related materials, and the induction of
DE   certain proteins such as pathogen related (PR) proteins.
SY   HR.
GO   GO:0009626; plant-type hypersensitive response
HI   Biological process: Plant defense; Hypersensitive response.
CA   Biological process.
//
ID   Hypersensitive response elicitation.
AC   KW-0928
DE   Proteins involved in hypersensitive response (HR) elicitation. HR is a
DE   rapid defense-associated programmed cell death of plant cells at the
DE   site of invasion.
GO   GO:0034053; symbiont-mediated perturbation of host defense-related programmed cell death
HI   Biological process: Hypersensitive response elicitation.
CA   Biological process.
//
ID   Hypogonadotropic hypogonadism.
AC   KW-1016
DE   Protein which, if defective, causes hypogonadotropic hypogonadism, a
DE   disorder characterized by a deficiency of the pituitary secretion of
DE   follicle-stimulating hormone (FSH) and luteinizing hormone (LH).
DE   Affected individuals present with absent or impaired sexual
DE   development due to sex-steroid-hormone deficiency, low serum levels of
DE   the pituitary gonadotropins FSH and LH, and infertility.
SY   HH; Idiopathic hypogonadotropic hypogonadism; IHH;
SY   Isolated hypogonadotropic hypogonadism.
HI   Disease: Hypogonadotropic hypogonadism.
CA   Disease.
//
ID   Hypotensive agent.
AC   KW-0382
DE   Protein which can cause hypotension, i.e. low blood pressure or a
DE   sudden drop in blood pressure.
SY   Antihypertensive agents.
GO   GO:0008217; regulation of blood pressure
HI   Molecular function: Hypotensive agent.
CA   Molecular function.
//
ID   Hypotrichosis.
AC   KW-1063
DE   Protein which, if defective, causes hypotrichosis, a condition
DE   characterized by reduced pilosity over the body and scalp (with
DE   sparse, thin, and short hair).
HI   Disease: Hypotrichosis.
CA   Disease.
//
ID   Hypusine.
AC   KW-0385
DE   Protein which is posttranslationally modified on at least one lysine
DE   residue to form hypusine (N-epsilon-(4-aminobutyl)lysine). This
DE   spermidine-dependent reaction is catalyzed by deoxyhypusine synthase
DE   and deoxyhypusine hydroxylase. eIF-5A is the only protein in
DE   eukaryotes and archaebacteria known to contain hypusine.
HI   PTM: Hypusine.
CA   PTM.
//
ID   Hypusine biosynthesis.
AC   KW-0386
DE   Protein involved in the synthesis of hypusine, an amino acid formed by
DE   the two posttranslational steps in the modification of a lysine: (i)
DE   deoxyhypusine synthase catalyzes the transfer of a 4-aminobutyl moiety
DE   from spermidine to a specific lysine residue to form a deoxyhypusine
DE   residue, N-epsilon-(4-aminobutyl)lysine, and (ii) deoxyhypusine
DE   hydroxylase catalyzes the hydroxylation of the deoxyhypusine residue
DE   to form hypusine (N-epsilon-(4-amino-2-hydroxybutyl)lysine).
SY   Hypusine anabolism; Hypusine biosynthetic process; Hypusine formation;
SY   Hypusine synthesis.
GO   GO:0008612; peptidyl-lysine modification to peptidyl-hypusine
HI   Biological process: Hypusine biosynthesis.
CA   Biological process.
//
ID   Ice nucleation.
AC   KW-0387
DE   Protein which promotes the nucleation of ice. The proteins catalyzes
DE   the formation of ice crystals in extracellular fluid at relatively
DE   high temperatures (up to -2 degrees Celsius) to protect the organism
DE   from damage by intracellular ice formation.
GO   GO:0050825; ice binding
HI   Molecular function: Ice nucleation.
CA   Molecular function.
//
ID   Ichthyosis.
AC   KW-0977
DE   Protein which, if defective, causes ichthyosis, any of a group of
DE   cutaneous disorders characterized by increased or aberrant
DE   keratinization and resulting in non-inflammatory scaling of the skin.
DE   Most ichthyoses are genetically determined, while some may be acquired
DE   and develop in association with various systemic diseases or be a
DE   prominent feature in certain genetic syndromes.
HI   Disease: Ichthyosis.
CA   Disease.
//
ID   IFIT mRNA restriction evasion by virus.
AC   KW-1196
DE   Viral protein allowing host innate defense evasion by methylating the
DE   first and second ribonucleotide of viral mRNAs (cap1 and cap2). These
DE   methylations allow viral RNA to escape cellular antiviral process
DE   mediated by host IFIT proteins which degrade non cap1-methylated
DE   mRNAs. Also prevents IFIH1/MDA5 sensor activation by cap0 mRNAs, which
DE   would trigger interferon beta synthesis.
GO   GO:0039699; viral mRNA cap methylation
HI   Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; IFIT mRNA restriction evasion by virus.
CA   Biological process.
//
ID   IgA-binding protein.
AC   KW-0388
DE   Protein binding to immunoglobulin A, the major class of antibodies
DE   found in external secretions such as saliva, tears, gastric fluid,
DE   milk and mucosal secretions.
GO   GO:0019862; IgA binding
HI   Molecular function: IgA-binding protein.
CA   Molecular function.
//
ID   IgE-binding protein.
AC   KW-0389
DE   Protein binding to immunoglobulin E, the antibody class involved in
DE   local inflammatory reactions, reactions to parasites, and also in
DE   allergic responses.
GO   GO:0019863; IgE binding
HI   Molecular function: IgE-binding protein.
CA   Molecular function.
//
ID   IgG-binding protein.
AC   KW-0390
DE   Protein binding to immunoglobulin G, the main type of immunoglobulin
DE   produced towards the end of a primary immune response and in a
DE   secondary response.
GO   GO:0019864; IgG binding
HI   Molecular function: IgG-binding protein.
CA   Molecular function.
//
ID   Immunity.
AC   KW-0391
DE   Protein involved in immunity, any immune system process that functions
DE   in the response of an organism to a potential internal or invasive
DE   threat. The vertebrate immune system is formed by the innate immune
DE   system (composed of phagocytes, complement, antimicrobial peptides,
DE   etc) and by the adaptive immune system which consists of T- and B-
DE   lymphocytes.
SY   Immune response.
GO   GO:0002376; immune system process
HI   Biological process: Immunity.
CA   Biological process.
//
ID   Immunoglobulin.
AC   KW-1280
DE   A glycoprotein produced in membrane-bound or secreted form by B
DE   lymphocytes. The basic structural unit of an immunoglobulin (Ig) is
DE   composed of two identical covalently linked heavy chains and two
DE   identical light chains. Both the heavy chains and light chains contain
DE   a series of repeating homologous structural units called Ig domains.
DE   The N-terminal variable regions of the heavy and light chains form the
DE   antigen binding sites, whereas the C-terminal constant regions of the
DE   heavy chains interact with other molecules in the immune system. The
DE   membrane-bound antibodies serve as receptors that mediate the antigen-
DE   triggered activation of B cells. Secreted antibodies function as
DE   mediators of specific humoral immunity by engaging various effector
DE   mechanisms that serve to eliminate the bound antigen.
SY   Antibody.
GO   GO:0019814; immunoglobulin complex
HI   Biological process: Immunity; Adaptive immunity; Immunoglobulin.
HI   Cellular component: Immunoglobulin.
CA   Cellular component.
//
ID   Immunoglobulin domain.
AC   KW-0393
DE   A globular structural motif found in many proteins of the immune
DE   system, including immunoglobulins (Igs), T cell receptors (TCRs) and
DE   major histocompatibility complex (MHC) molecules. Ig domains are
DE   approximately 110 amino acid residues in length, include an internal
DE   disulfide bond, and contain two layers of beta-pleated sheets, each
DE   layer composed of three to five strands of antiparallel polypeptide
DE   chains. Ig domains are classified as V-like or C-like on the basis of
DE   closest homology to either Ig V or C domains.
SY   Immunoglobulin fold.
HI   Domain: Immunoglobulin domain.
CA   Domain.
//
ID   Inflammasome.
AC   KW-1271
DE   Component of the inflammasome complex involved in innate immunity and
DE   inflammation. Inflammasomes are supramolecular micron-sized complexes
DE   that assemble in the cytosol adjacent to the nucleus in response to
DE   pathogens and other damage-associated signals. The core of
DE   inflammasomes consists of at least 2 components: a signal sensor and
DE   an effector inflammatory caspase (mostly CASP1). However, most
DE   inflammasomes contain a third element, an adaptor (often ASC/PYCARD).
DE   In response to a danger signal, the sensor homooligomerizes and
DE   interacts with the adaptor that polymerizes and forms a platform to
DE   recruit caspase precursors. This results in increased local
DE   concentration of the enzyme, leading to trans-autocleavage and
DE   activation. Active caspases process proinflammatory IL1B and IL18
DE   cytokine precursors, which are then secreted in the extracellular
DE   milieu and induce inflammatory responses. In adaptor-independent
DE   inflammasomes, the sensor directly recruits the caspase. Additional
DE   proteins may interaction with the core complex. Inflammasomes also
DE   induce pyroptosis, an inflammatory form of programmed cell death.
SY   ASC focus; ASC speck.
GO   GO:0061702; canonical inflammasome complex
HI   Cellular component: Cytoplasm; Inflammasome.
CA   Cellular component.
//
ID   Inflammatory response.
AC   KW-0395
DE   Protein involved in the localized protective response to tissue
DE   damage, microbial infection, or the presence of foreign matter. It is
DE   characterized by swelling, redness, heat and pain and involves a
DE   complex series of events including vascular changes and accumulation
DE   of blood cells, such as neutrophil leucocytes and mononuclear
DE   phagocytes, at the site of injury.
SY   Response to inflammation.
GO   GO:0006954; inflammatory response
HI   Biological process: Inflammatory response.
CA   Biological process.
//
ID   Inhibition of eukaryotic host transcription initiation by virus.
AC   KW-1111
DE   Viral protein involved in the disruption of the host transcriptional
DE   machinery. Viruses have evolved ways of interacting with the cellular
DE   preinitiation complex (PIC) to shutoff host transcription initiation.
DE   For example, the TATA binding protein and TFIIH are targeted by some
DE   viral proteins and thus cannot assemble properly to form a functional
DE   PIC.
GO   GO:0039602; suppression by virus of host transcription initiation from RNA polymerase II promoter
HI   Biological process: Host-virus interaction; Host gene expression shutoff by virus; Eukaryotic host gene expression shutoff by virus; Eukaryotic host transcription shutoff by virus; Inhibition of eukaryotic host transcription initiation by virus.
CA   Biological process.
//
ID   Inhibition of eukaryotic host translation factors by virus.
AC   KW-1075
DE   Viral protein that inhibits or degrades host translation initiation
DE   factor(s). Viruses have evolved ways of interacting with the cellular
DE   translational machinery to shutoff host gene expression. This global
DE   inhibition of cellular protein synthesis serves to ensure maximal
DE   viral gene expression and to evade host immune response. Some viruses
DE   are known to cleave host translation initiation factors like EIF3 or
DE   EIF4G, while others achieve translation inhibition by promoting
DE   dephosphorylation of some host translation initiation factors or their
DE   binding partners.
GO   GO:0039606; suppression by virus of host translation initiation
HI   Biological process: Host-virus interaction; Host gene expression shutoff by virus; Eukaryotic host gene expression shutoff by virus; Eukaryotic host translation shutoff by virus; Inhibition of eukaryotic host translation factors by virus.
CA   Biological process.
//
ID   Inhibition of host adaptive immune response by virus.
AC   KW-1080
DE   Viral protein involved in the evasion of host adaptive immune
DE   response. Upon infection, the innate immune system provides mechanisms
DE   for the rapid sensing and elimination of viruses. Adaptive immunity
DE   has evolved to provide a broader and more finely tuned repertoire of
DE   recognition for both self- and nonself-antigens. In vertebrates, the
DE   adaptive immune response is mediated by T and B lymphocytes expressing
DE   specific receptors. A lot of viruses escape the adaptive immune
DE   response by different mechanisms including interference with the
DE   presentation of antigenic peptides at the surface of infected cells.
DE   Bacteria and archaea have adaptive immunity, the CRISPR-Cas system.
GO   GO:0039504; suppression by virus of host adaptive immune response
HI   Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host adaptive immune response by virus.
CA   Biological process.
//
ID   Inhibition of host apoptosis by viral BCL2-like protein.
AC   KW-1081
DE   Viral protein sharing sequence similarity with host BCL2 protein.
DE   Cellular BCL2 family members are divided in two groups, some having
DE   anti-apoptotic activity (such as BCL2 itself) while others have pro-
DE   apoptotic function (such as BAX). If the level of proapoptotic members
DE   are higher than inhibitors, then the cell undergoes apoptosis. So far,
DE   all viral homologues display anti-apoptotic activity.
GO   GO:0019050; suppression by virus of host apoptotic process
HI   Biological process: Host-virus interaction; Modulation of host cell apoptosis by virus; Inhibition of host apoptosis by viral BCL2-like protein.
CA   Biological process.
//
ID   Inhibition of host apoptosis by viral FLIP-like protein.
AC   KW-1082
DE   Viral protein sharing sequence similarity with host FLIPs (FLICE-
DE   inhibitory proteins). Cellular FLIPs play an essential role in
DE   apoptosis functioning as a link between cell survival and cell death
DE   pathways . Viral FLIPs inhibit apoptosis by interfering with death
DE   receptor signaling.
GO   GO:0019050; suppression by virus of host apoptotic process
HI   Biological process: Host-virus interaction; Modulation of host cell apoptosis by virus; Inhibition of host apoptosis by viral FLIP-like protein.
CA   Biological process.
//
ID   Inhibition of host autophagy by virus.
AC   KW-1083
DE   Viral protein involved in the inhibition of host autophagy. Autophagy
DE   is a major intracellular pathway in the delivery of cytoplasmic
DE   material to lysosomes for degradation. It is also essential for the
DE   removal of pathogenic protein aggregates from the cell during
DE   infection. Several viruses including influenza and HIV-1 block
DE   autophagosome maturation by interacting with and inhibiting host
DE   Beclin-1, an essential protein playing a central role in autophagy.
GO   GO:0039521; suppression by virus of host autophagy
HI   Biological process: Host-virus interaction; Inhibition of host autophagy by virus.
CA   Biological process.
//
ID   Inhibition of host caspases by virus.
AC   KW-1085
DE   Viral protein involved in the evasion of host cell apoptosis by
DE   inhibiting host caspases. Many viruses from diverse families have
DE   evolved mechanisms to evade or delay cell death by suppressing the
DE   activity of cytoplasmic proteases termed caspases which have a central
DE   role in apoptosis induction.
GO   GO:0019050; suppression by virus of host apoptotic process
HI   Biological process: Host-virus interaction; Modulation of host cell apoptosis by virus; Inhibition of host caspases by virus.
CA   Biological process.
//
ID   Inhibition of host chemokines by virus.
AC   KW-1086
DE   Viral protein involved in the evasion of host immune response by
DE   inhibiting chemokines. Chemokines have several roles including Th1/Th2
DE   differentiation, T_cell costimulation, or promotion of leukocyte
DE   migration. Due to the importance of chemokines in immunity, viruses
DE   have evolved mechanisms to counter the chemokine network. They encode
DE   chemokine-like proteins, chemokine receptors, or chemokine-binding
DE   proteins to inhibit cellular chemokines.
GO   GO:0042785; evasion of host immune response via modulation of host cytokine network
HI   Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host chemokines by virus.
CA   Biological process.
//
ID   Inhibition of host complement factors by virus.
AC   KW-1087
DE   Viral protein involved in the evasion of host humoral response by
DE   inhibiting the complement factors. The activation of complement
DE   involves the sequential proteolyis of proteins to generate enzymes
DE   with catalytic activities. The biological functions of the complement
DE   include opsonization, inflammation, lysis of immune complexes, or
DE   enhancement of the humoral immune response. Some herpesviruses,
DE   poxviruses and retroviruses mimic or interact with complement
DE   regulatory proteins to block complement activation and neutralization
DE   of virus particles.
GO   GO:0039573; suppression by virus of host complement activation
HI   Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host complement factors by virus.
CA   Biological process.
//
ID   Inhibition of host DNA replication by virus.
AC   KW-1248
DE   Viral protein that blocks host DNA replication without inhibiting host
DE   transcription or translation. Inhibiting host replication provides an
DE   advantage during the virus life cycle by reducing or eliminating
DE   competing host macromolecular synthesis. Bacteriophage N4 for example
DE   is known to shut off the host DNA replication while the host genome
DE   remains structurally intact. Bacteriophage lambda prevents host DNA
DE   replication initiation and Staphylococcus bacteriophages target the
DE   replicative DNA polymerase processivity clamp and the helicase.
GO   GO:0098673; inhibition of host DNA replication by virus
HI   Biological process: Host-virus interaction; Modulation of host cell cycle by virus; Inhibition of host DNA replication by virus.
CA   Biological process.
//
ID   Inhibition of host IKBKE by virus.
AC   KW-1224
DE   Viral protein involved in the evasion of host innate defenses by
DE   inhibiting the IKBKE/IKK-epsilon kinase. Upon viral infection, the
DE   DDX58/RIG-I or IFIH1/MDA5 receptors recognize foreign material and
DE   transmit the signal to downstream components MAVS and IKBKE. In turn,
DE   the IKBKE kinase phosphorylates and activates IRF3 and/or IRF7. Once
DE   phosphorylated, IRF3 and IRF7 translocate into the nucleus to drive
DE   transcription of interferons. Several viruses including arenaviruses
DE   or ebola virus interact directly with and inhibit IKBKE/IKK-epsilon to
DE   prevent IRFs activation.
GO   GO:0039724; suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IKBKE activity
HI   Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; Inhibition of host RLR pathway by virus; Inhibition of host IKBKE by virus.
CA   Biological process.
//
ID   Inhibition of host innate immune response by virus.
AC   KW-1090
DE   Viral protein involved in the evasion of host innate immune response.
DE   Upon viral infection, the innate immune system initially defends the
DE   host in a non-specific manner. Many viral proteins interact with and
DE   inhibit components the host innate system to replicate more
DE   efficiently. In metazoans and plants, the innate immune system
DE   includes the intracellular pattern recognition receptors (PRRs) that
DE   detect pathogen-associated molecular patterns (PAMPs). In plants and
DE   invertebrates, it includes the RNA interference (RNAi) system. Plants
DE   also have effector-triggered immunity (ETI). In metazoans, it includes
DE   the cell-dependent mechanisms (e.g. phagocytes) or secreted factors.
DE   Bacteria and archaea have an innate immune system relying on various
DE   systems (e.g. the restriction-modification system, Pycsar).
GO   GO:0039503; suppression by virus of host innate immune response
HI   Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus.
CA   Biological process.
//
ID   Inhibition of host interferon receptors by virus.
AC   KW-1091
DE   Viral protein involved in the evasion of the interferon pathway by
DE   inhibiting interferon receptors. Interferon signaling exerts antiviral
DE   effects through cell surface receptors termed interferon receptors. In
DE   response to binding of extracellular interferons, they activate the
DE   JAK/STAT pathway causing transcriptional activation of IFN-regulated
DE   genes. To avoid this antiviral response, several viruses target the
DE   interferon receptors and send them to degradation via the proteasome.
GO   GO:0140886; suppression by virus of host interferon-mediated signaling pathway
HI   Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; Interferon antiviral system evasion; Inhibition of host interferon signaling pathway by virus; Inhibition of host interferon receptors by virus.
CA   Biological process.
//
ID   Inhibition of host interferon signaling pathway by virus.
AC   KW-1114
DE   Viral protein involved in the evasion of host innate defense by
DE   inhibiting the interferon signaling pathway leading to the production
DE   of interferon-induced genes. Interferons bind to the IFN receptors
DE   (IFNAR) on the cell surface and activate Jak/Tyk kinases. These
DE   kinases phosphorylate STAT1 and STAT2 that translocate to the nucleus
DE   and induce the expression of interferon stimulated genes (ISGs). Many
DE   viruses interact with components of this pathway to prevent expression
DE   of ISGs and inhibit the host immune response.
GO   GO:0039502; suppression by virus of host type I interferon-mediated signaling pathway
HI   Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; Interferon antiviral system evasion; Inhibition of host interferon signaling pathway by virus.
CA   Biological process.
//
ID   Inhibition of host IRF3 by virus.
AC   KW-1092
DE   Viral protein involved in the evasion of host innate defense by
DE   inhibiting the interferon regulatory factor-3 (IRF3) protein. Viral
DE   infection triggers the phosphorylation and activation of IRF3. The
DE   activated IRF3 migrates to the nucleus, where it complexes with the
DE   transcription coactivator CREBBP/EP300, leading to the transcriptional
DE   activation of the IFN-alpha and IFN-beta genes. Several viral proteins
DE   directly bind to IRF3 and inhibit its transcriptional activity while
DE   others target it to the proteasome for degradation.
GO   GO:0039548; suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity
HI   Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; Inhibition of host RLR pathway by virus; Inhibition of host IRF3 by virus.
CA   Biological process.
//
ID   Inhibition of host IRF7 by virus.
AC   KW-1093
DE   Viral protein involved in the evasion of host innate defense by
DE   inhibiting the interferon regulatory factor-7 (IRF7) protein. Viral
DE   infection triggers the phosphorylation and activation of IRF7. The
DE   activated IRF7 migrates to the nucleus leading to the transcriptional
DE   activation of the IFN-alpha and IFN-beta genes. Some viral proteins
DE   prevent IRF7 phosphorylation and nuclear activation. Ebola virus VP35
DE   interacts with IRF7 and hijacks the cellular SUMOylation machinery for
DE   its advantage to increase IRF7 SUMOylation thereby disabling its
DE   activity.
GO   GO:0039557; suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF7 activity
HI   Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; Inhibition of host RLR pathway by virus; Inhibition of host IRF7 by virus.
CA   Biological process.
//
ID   Inhibition of host IRF9 by virus.
AC   KW-1094
DE   Viral protein involved in the evasion of the type I and III interferon
DE   pathway by inhibiting the interferon regulatory factor-9 (IRF9)
DE   protein. Viral infection triggers the phosphorylation and activation
DE   of IRF9. The activated IRF9 migrates to the nucleus leading to the
DE   transcriptional activation of several hundred IFN-responsive genes.
DE   Some viral proteins inhibit IRF9 activation by preventing its nuclear
DE   localization upon infection or by sending it to the nucleus in an
DE   inactive state.
GO   GO:0039560; disruption by virus of host JAK-STAT cascade via inhibition of host IRF9 activity
HI   Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; Interferon antiviral system evasion; Inhibition of host interferon signaling pathway by virus; Inhibition of host IRF9 by virus.
CA   Biological process.
//
ID   Inhibition of host ISG15 by virus.
AC   KW-1095
DE   Viral protein involved in the evasion of host immune defense by
DE   inhibiting the ISG15 protein, an ubiquitin-like modifier playing
DE   important roles in the innate immune response. Like ubiquitin, ISG15
DE   is conjugated to lysines on numerous target proteins through its
DE   conserved C-terminal region. Viruses escape from the antiviral
DE   activity of ISG15 by direct interaction or by cleavage of ISG15
DE   derivatives.
GO   GO:0039579; suppression by virus of host ISG15-protein conjugation
HI   Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; Interferon antiviral system evasion; Inhibition of host interferon signaling pathway by virus; Inhibition of host ISG15 by virus.
CA   Biological process.
//
ID   Inhibition of host JAK1 by virus.
AC   KW-1096
DE   Viral protein involved in the evasion of the type I, II and III
DE   interferon pathways by inhibiting the JAK1 protein. Upon viral
DE   infection, JAK1 is activated by the interferon-alpha/beta, -gamma, and
DE   -lambda signal transduction pathways. Several viral proteins can
DE   directly interact with JAK1 to prevent its ability to phosphorylate
DE   the downstream partners STAT1 or STAT2.
GO   GO:0039576; disruption by virus of host JAK-STAT cascade via inhibition of JAK1 activity
HI   Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; Interferon antiviral system evasion; Inhibition of host interferon signaling pathway by virus; Inhibition of host JAK1 by virus.
CA   Biological process.
//
ID   Inhibition of host MAVS by virus.
AC   KW-1097
DE   Viral protein involved in the evasion of host innate defense by
DE   inhibiting the MAVS protein. During viral replication, dsRNA is
DE   produced and detected by DDX58/RIG-I or IFIH1/MDA5 that will activate
DE   MAVS to coordinate pathways leading to induction of antiviral
DE   cytokines. Several viral proteins including NS3/4A from Hepatitis C,
DE   or protease 3C from hepatitis A virus, cleave MAVS to abrogate its
DE   activity.
GO   GO:0039545; suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity
HI   Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; Inhibition of host RLR pathway by virus; Inhibition of host MAVS by virus.
CA   Biological process.
//
ID   Inhibition of host MDA5 by virus.
AC   KW-1089
DE   Viral protein involved in the evasion of host innate defense by
DE   inhibiting the IFIH1/MDA5 protein. Upon recognition of long viral
DE   dsRNAs, IFIH1/MDA5 initiates an antiviral signaling cascade by
DE   interacting with downstream partners. Some viral proteins including
DE   paramyxovirus V proteins interact with IFIH1/MDA5 and blocks its
DE   binding with its downstream partner MAVS.
GO   GO:0039554; suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of host MDA-5 activity
HI   Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; Inhibition of host RLR pathway by virus; Inhibition of host MDA5 by virus.
CA   Biological process.
//
ID   Inhibition of host MHC class I molecule presentation by virus.
AC   KW-1115
DE   Viral protein involved in the evasion of host adaptive immune response
DE   by inhibiting the presentation of loaded MHC class I molecules at the
DE   cell surface. Many viruses 'intercept' the loaded MHC class I
DE   molecules and retain them in the endoplasmic reticulum or target them
DE   to degradation in order to prevent presentation of the peptides at the
DE   cell surface.
GO   GO:0046776; suppression by virus of host antigen processing and presentation of peptide antigen via MHC class I
HI   Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host adaptive immune response by virus; Inhibition of host MHC class I molecule presentation by virus.
CA   Biological process.
//
ID   Inhibition of host MHC class II molecule presentation by virus.
AC   KW-1116
DE   Viral protein involved in the evasion of host adaptive immune response
DE   by inhibiting the presentation of loaded MHC class II molecules at the
DE   cell surface. MHC class II molecules are found only on a few
DE   specialized cells termed professional antigen-presenting cells (APCs).
DE   This group includes macrophages, dendritic cells and B-cells. Many
DE   viruses 'intercept' the loaded MHC class II molecules and retain them
DE   in the endoplasmic reticulum or target them to degradation in order to
DE   prevent presentation of the peptides at the cell surface.
GO   GO:0039505; suppression by virus of host antigen processing and presentation of peptide antigen via MHC class II
HI   Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host adaptive immune response by virus; Inhibition of host MHC class II molecule presentation by virus.
CA   Biological process.
//
ID   Inhibition of host mitotic exit by virus.
AC   KW-1098
DE   Viral protein involved in the inhibition of host cell cycle
DE   progression by preventing cells to exit mitosis.
GO   GO:0039593; peturbation by virus of host exit from mitosis
HI   Biological process: Host-virus interaction; Modulation of host cell cycle by virus; Inhibition of host mitotic exit by virus.
CA   Biological process.
//
ID   Inhibition of host mRNA nuclear export by virus.
AC   KW-1099
DE   Viral protein involved in the disruption of the mRNA nuclear export
DE   machinery. Viruses have evolved ways of interacting with the nuclear
DE   export machinery to inhibit cellular translation and maximize the
DE   expression of their own mRNAs. This global inhibition of cellular
DE   protein synthesis serves to ensure maximal viral gene expression and
DE   to evade host immune response.
GO   GO:0039522; suppression by virus of host mRNA export from nucleus
HI   Biological process: Host-virus interaction; Host gene expression shutoff by virus; Eukaryotic host gene expression shutoff by virus; Host mRNA suppression by virus; Inhibition of host mRNA nuclear export by virus.
CA   Biological process.
//
ID   Inhibition of host NF-kappa-B by virus.
AC   KW-1100
DE   Viral protein involved in the inhibition of host NF-kappa-B. This
DE   protein is a pleiotropic transcription factor which is present in
DE   almost all cell types and is involved in many biological processes
DE   such as inflammation, immunity, differentiation, cell growth,
DE   tumorigenesis and apoptosis. Many viruses have developed strategies to
DE   inhibit the NF-kappa-B pathway in order to evade host immunity and
DE   inhibit production of proinflammatory cytokines.
GO   GO:0039644; suppression by virus of host NF-kappaB cascade
HI   Biological process: Host-virus interaction; Inhibition of host NF-kappa-B by virus.
CA   Biological process.
//
ID   Inhibition of host PKR by virus.
AC   KW-1102
DE   Viral protein involved in the evasion of the interferon pathway by
DE   inhibiting the interferon induced PKR/EIF2AK2 protein. During viral
DE   replication of RNA viruses, dsRNA is produced leading to the
DE   activation of the PKR/EIF2AK2 kinase. Once activated, PKR/EIF2AK2
DE   autophosphorylates and catalyzes the phosphorylation of many
DE   substrates including the translation initiation factor EIF2S1, leading
DE   to the inhibition of the initiation of protein synthesis. Several
DE   viral proteins prevent PKR/EIF2AK2 activation by direct interaction
DE   while others target PKR/EIF2AK2 to degradation.
GO   GO:0030291; protein serine/threonine kinase inhibitor activity
GO   GO:0039580; suppression by virus of host PKR signaling
HI   Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; Interferon antiviral system evasion; Inhibition of host interferon signaling pathway by virus; Inhibition of host PKR by virus.
CA   Biological process.
//
ID   Inhibition of host poly(A)-binding protein by virus.
AC   KW-1101
DE   Viral protein involved in the inhibition of host translation by
DE   inhibiting the poly(A)-binding protein PABPC1. Viruses have evolved
DE   ways of interacting with the host translational machinery to shutoff
DE   host gene expression. This global inhibition of cellular protein
DE   synthesis serves to ensure maximal viral gene expression and to evade
DE   host immune response. One common target is the translation initiation
DE   factor PABPC1. Some viruses proteolytically cleave PABPC1, while
DE   others displace PABPC1 from EIF4G1.
GO   GO:0039604; suppression by virus of host translation
HI   Biological process: Host-virus interaction; Host gene expression shutoff by virus; Eukaryotic host gene expression shutoff by virus; Eukaryotic host translation shutoff by virus; Inhibition of host poly(A)-binding protein by virus.
CA   Biological process.
//
ID   Inhibition of host pre-mRNA processing by virus.
AC   KW-1103
DE   Viral protein involved in the disruption of host pre-mRNA processing.
DE   Viruses have evolved ways of interacting with the cellular RNA
DE   splicing machinery and regulate splicing of cellular pre-mRNAs as a
DE   part of the mechanism for shutting down the synthesis of host
DE   proteins. This global inhibition of cellular protein synthesis serves
DE   to ensure maximal viral gene expression and to evade host immune
DE   response.
GO   GO:0039524; suppression by virus of host mRNA processing
HI   Biological process: Host-virus interaction; Host gene expression shutoff by virus; Eukaryotic host gene expression shutoff by virus; Host mRNA suppression by virus; Inhibition of host pre-mRNA processing by virus.
CA   Biological process.
//
ID   Inhibition of host proteasome antigen processing by virus.
AC   KW-1117
DE   Viral protein involved in the evasion of host adaptive immune response
DE   by inhibiting MHC class I peptide antigen generation by the
DE   proteasome. The processing of foreign proteins leads to the
DE   presentation of viral peptides by MHC class I molecules to cytotoxic T
DE   lymphocytes and triggers immune response. Several viral proteins have
DE   evolved mechanisms to avoid synthesis of antigenic peptide by the
DE   proteasome. Epstein-Barr virus EBNA-1 for example contains an internal
DE   repeat exclusively composed of glycines and alanines that inhibits its
DE   proteasomal degradation.
GO   GO:0039588; suppression by virus of host antigen processing and presentation
HI   Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host adaptive immune response by virus; Inhibition of host proteasome antigen processing by virus.
CA   Biological process.
//
ID   Inhibition of host RIG-I by virus.
AC   KW-1088
DE   Viral protein involved in the evasion of host innate defense by
DE   inhibiting the DDX58/RIG-I protein. Upon recognition of viral RNA, the
DE   cytosolic receptor DDX58/RIG-I initiates an antiviral signaling
DE   cascade by interacting with downstream partners. Several viral
DE   proteins inhibit DDX58/RIG-I via direct interaction while others via
DE   proteolytic cleavage.
GO   GO:0039540; suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of host RIG-I activity
HI   Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; Inhibition of host RLR pathway by virus; Inhibition of host RIG-I by virus.
CA   Biological process.
//
ID   Inhibition of host RLR pathway by virus.
AC   KW-1113
DE   Viral protein involved in the evasion of host innate defense by
DE   inhibiting the DDX58/RIG-I-like receptor (RLR) pathway leading to the
DE   triggering of interferon-mediated response. This pathway starts with
DE   the recognition of viral RNA by host proteins including DDX58/RIG-I or
DE   IFIH1. Then, the signal is transmitted through MAVS and TRAFs leading
DE   to the activation and nuclear localization of transcription factors
DE   IRF3 and IRF7 to induce IFNalpha/beta transcription and protein
DE   production. Many viruses interact with components of this pathway to
DE   inhibit production of interferons and establishment of the antiviral
DE   state.
GO   GO:0039532; negative regulation of viral-induced cytoplasmic pattern recognition receptor signaling pathway
HI   Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; Inhibition of host RLR pathway by virus.
CA   Biological process.
//
ID   Inhibition of host RNA polymerase II by virus.
AC   KW-1104
DE   Viral protein involved in the disruption of the host RNA polymerase
DE   II. Many viruses induce alterations in the cellular gene expression.
DE   Among these, shutoff of host transcription by targeting RNA polymerase
DE   II is commonly used. Indeed, many viruses are able to modify RNAP II
DE   CTD including Herpes virus, HIV, Epstein-Barr virus or Bunyamwera
DE   virus.
GO   GO:0039523; suppression by virus of host mRNA transcription via inhibition of RNA polymerase II activity
HI   Biological process: Host-virus interaction; Host gene expression shutoff by virus; Eukaryotic host gene expression shutoff by virus; Eukaryotic host transcription shutoff by virus; Inhibition of host RNA polymerase II by virus.
CA   Biological process.
//
ID   Inhibition of host STAT1 by virus.
AC   KW-1105
DE   Viral protein involved in the evasion of the type I, II and III
DE   interferon pathways by inhibiting the STAT1 protein. Upon viral
DE   infection, STAT1 is activated by IFN-gamma, IFN-alpha/beta, or IFN-
DE   lambda that bind to specific cell surface receptors. While IFN-gamma
DE   induces STAT1 homodimerization, IFN-alpha/beta and IFN-lambda
DE   stimulate heterodimerization of STAT1 and STAT2, both leading to STAT1
DE   nuclear localization and subsequent induction of IFN-stimulated genes.
DE   Many viruses interfere with STAT1 activation, often by preventing
DE   STAT1 phosphorylation and nuclear localization.
GO   GO:0039563; disruption by virus of host JAK-STAT cascade via inhibition of STAT1 activity
HI   Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; Interferon antiviral system evasion; Inhibition of host interferon signaling pathway by virus; Inhibition of host STAT1 by virus.
CA   Biological process.
//
ID   Inhibition of host STAT2 by virus.
AC   KW-1106
DE   Viral protein involved in the evasion of type I and III interferon
DE   pathways by inhibiting STAT2 protein. Upon viral infection, STAT2 is
DE   activated by IFN-alpha/beta or IFN-lambda that bind to specific cell
DE   surface receptors. In turn, IFN-alpha/beta (or IFN-lambda) induces
DE   heterodimerization of STAT1 and STAT2 by phosphorylation, leading to
DE   STAT2 nuclear localization and subsequent induction of IFN-stimulated
DE   genes. Many viruses interfere with STAT2 activation, often by
DE   preventing STAT2 phosphorylation and nuclear localization.
GO   GO:0039564; disruption by virus of host JAK-STAT cascade via inhibition of STAT2 activity
HI   Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; Interferon antiviral system evasion; Inhibition of host interferon signaling pathway by virus; Inhibition of host STAT2 by virus.
CA   Biological process.
//
ID   Inhibition of host TAP by virus.
AC   KW-1107
DE   Viral protein involved in the evasion of host adaptive immune response
DE   by inhibiting the TAP complex. Transporter associated with antigen
DE   (TAP), composed of two subunits TAP1 and TAP2, is required for the
DE   translocation of peptides into the ER, where they are loaded onto MHC
DE   class I. Thereafter, the viral peptides are presented to cytotoxic T
DE   lymphocytes at the cell surface and trigger immune response. The
DE   loading of peptide on MHC by TAP is targeted by several viruses
DE   including herpesviruses and retroviruses.
GO   GO:0039588; suppression by virus of host antigen processing and presentation
HI   Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host adaptive immune response by virus; Inhibition of host TAP by virus.
CA   Biological process.
//
ID   Inhibition of host tapasin by virus.
AC   KW-1108
DE   Viral protein involved in the evasion of host adaptive immune response
DE   by inhibiting the tapasin/TAPBP protein. tapasin/TAPBP is a type I
DE   transmembrane protein essential for the optimal expression of stable
DE   MHC class I molecules on host cell surface. Its helps the MHC class I
DE   molecules to remain in a peptide receptive state, avoiding
DE   irreversible denaturation. Several retroviruses and DNA viruses encode
DE   proteins interacting with tapasin/TAPBP and inhibiting its activity.
GO   GO:0046776; suppression by virus of host antigen processing and presentation of peptide antigen via MHC class I
HI   Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host adaptive immune response by virus; Inhibition of host tapasin by virus.
CA   Biological process.
//
ID   Inhibition of host TBK1 by virus.
AC   KW-1223
DE   Viral protein involved in the evasion of host innate defenses by
DE   inhibiting the TBK1 kinase. Upon viral infection, Toll-like receptors
DE   (TLRs) or DNA recognition receptors recognize foreign material and
DE   transmit the signal to TBK1 that in turn phosphorylates and activates
DE   IRF3 and IRF7. Once phosphorylated, IRF3 and/or IRF7 translocate into
DE   the nucleus to drive transcription of interferons. Several viruses
DE   including herpes simplex virus 1 or vaccinia virus interact directly
DE   with and inhibit TBK1 to prevent IRFs activation.
GO   GO:0039723; suppression by virus of host viral-induced cytoplasmic pattern recognition receptor signaling pathway via inhibition of TBK1 activity
HI   Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; Inhibition of host TLR pathway by virus; Inhibition of host TBK1 by virus.
CA   Biological process.
//
ID   Inhibition of host tetherin by virus.
AC   KW-1084
DE   Viral protein involved in the evasion of host immune defense by
DE   inhibiting the BST2/tetherin protein. BST2/tetherin is an alpha
DE   interferon-inducible cellular factor that impairs the release of many
DE   enveloped viruses, including human immunodeficiency virus type 1 (HIV-
DE   1), HIV-2, as well as other retroviruses. Several viruses manage to
DE   circumvent the antiviral activity of BST2/tetherin either by sending
DE   BST2/tetherin to degradation (HIV-1) or by lowering the presence of
DE   BST2 on cell surfaces (HIV-2).
GO   GO:0039587; suppression by virus of host tetherin activity
HI   Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; Inhibition of host tetherin by virus.
CA   Biological process.
//
ID   Inhibition of host TLR pathway by virus.
AC   KW-1225
DE   Viral protein involved in the evasion of host innate defenses by
DE   inhibiting the Toll-like recognition receptor (TLR) pathway. This
DE   pathway usually starts with the recognition of viruses by host TLRs
DE   including TLR3 or TLR4. Then, the signal is transmitted through MYD88
DE   (or TRIF) and then to TBK1 leading to the activation and nuclear
DE   localization of transcription factors IRF3 and/or IRF7 to induce
DE   IFNalpha/beta transcription and production of proinflammatory
DE   cytokines through activation of the NF-kappaB signaling pathway. Many
DE   viruses interact with components of this pathway to inhibit production
DE   of interferons and establishment of the antiviral state.
GO   GO:0039722; suppression by virus of host toll-like receptor signaling pathway
HI   Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; Inhibition of host TLR pathway by virus.
CA   Biological process.
//
ID   Inhibition of host TRAFs by virus.
AC   KW-1110
DE   Viral protein involved in the evasion of host innate defense by
DE   inhibiting TRAF proteins. After viral infection, the cellular
DE   signaling pathway leading to production of interferons is activated
DE   and several TRAF family members including TRAF2, TRAF3, and TRAF5
DE   participate in this cascade. Many viruses encode protein able to
DE   interact with TRAF members to inhibit their antiviral activity.
GO   GO:0039527; disruption by virus of host TRAF-mediated signal transduction
HI   Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; Inhibition of host RLR pathway by virus; Inhibition of host TRAFs by virus.
CA   Biological process.
//
ID   Inhibition of host TYK2 by virus.
AC   KW-1112
DE   Viral protein involved in the evasion of the type I and III interferon
DE   pathways by inhibiting the host TYK2 protein. Upon viral infection,
DE   the TYK2 protein is activated by IFNalpha/beta or IFN-lambda
DE   stimulation leading to a series of phosphorylation events that induce
DE   transcription of several hundred IFN-responsive genes. Several viruses
DE   have evolved mechanisms to inhibit TYK2 activity thereby preventing
DE   the subsequent activation of downstream partners STAT1 and STAT2.
GO   GO:0039574; disruption by virus of host JAK-STAT cascade via inhibition of host TYK2 activity
HI   Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; Interferon antiviral system evasion; Inhibition of host interferon signaling pathway by virus; Inhibition of host TYK2 by virus.
CA   Biological process.
//
ID   Initiation factor.
AC   KW-0396
DE   Protein which plays an important role in initiating the translation of
DE   a mRNA molecule into a polypeptide. Initiation factors help to form
DE   the complex between the mRNA and a ribosome.
SY   Translation initiation factor.
GO   GO:0003743; translation initiation factor activity
GO   GO:0006413; translational initiation
HI   Biological process: Protein biosynthesis; Initiation factor.
HI   Molecular function: Initiation factor.
CA   Molecular function.
//
ID   Innate immunity.
AC   KW-0399
DE   Protein involved in innate immunity, an inborn defense mechanism used
DE   by organisms to defend themselves against invasion by pathogens
DE   (bacteria, fungi, viruses, etc.). Initially discovered in insects
DE   which are devoid of an adaptive immune system and rely only on innate
DE   immune reactions for their defense, this immediate response
DE   accomplishes many activities including recognition and effector
DE   functions. Recognition is mediated by broad specificity, pattern
DE   recognition, receptors which recognize many related molecular
DE   structures (e.g. polysaccharides, polynucleotides) present in
DE   microorganisms but not found in the host. The innate responses include
DE   the release of antimicrobial peptides, production of cytokines, acute-
DE   phase proteins, complement. Although many different innate immune
DE   mechanisms are deployed for host defence, a unifying theme of innate
DE   immunity is the use of germline-encoded pattern recognition receptors
DE   for pathogens or damaged self components, such as the Toll-like
DE   receptors, nucleotide-binding domain leucine-rich repeat (LRR)-
DE   containing receptors, retinoic acid-inducible gene I-like RNA
DE   helicases and C-type lectin receptors.
GO   GO:0045087; innate immune response
HI   Biological process: Immunity; Innate immunity.
WW   http://users.rcn.com/jkimball.ma.ultranet/BiologyPages/I/Innate.html
WW   https://www.nature.com/articles/nri2686
CA   Biological process.
//
ID   Inner capsid protein.
AC   KW-1153
DE   Viral protein that is a component of the inner layer of a double or
DE   triple concentric icosahedral capsid. Inner capsids are part of
DE   reoviridae and cystoviridae virions.
GO   GO:0039625; viral inner capsid
HI   Cellular component: Virion; Capsid protein; Inner capsid protein.
CA   Cellular component.
//
ID   Inositol biosynthesis.
AC   KW-0398
DE   Protein involved in the synthesis of inositol, a cyclic hexahydric
DE   alcohol. It occurs in various forms, of which myo-inositol, a
DE   constituent of phospholipids, is the most important.
SY   Inositol anabolism; Inositol biosynthetic process; Inositol formation;
SY   Inositol synthesis.
GO   GO:0006021; inositol biosynthetic process
HI   Biological process: Inositol biosynthesis.
CA   Biological process.
//
ID   Insecticide resistance.
AC   KW-0978
DE   Protein that confers, on insect vectors and pests, the ability to
DE   withstand insecticide action. Insecticides are chemicals that
DE   selectively kill insects. Insecticide resistance usually occurs by two
DE   broad mechanisms. The first is where the insect may produce large
DE   amounts of enzymes, such as esterases which either break down the
DE   insecticide molecule or bind to it so tightly that it cannot function
DE   (a process known as sequestration). The second mechanism involves
DE   mutation of the insecticide target site, such as the
DE   acetylcholinesterase enzyme in the nervous system. This effectively
DE   blocks the action of the insecticide.
SY   Resistance to insecticide.
HI   Biological process: Insecticide resistance.
CA   Biological process.
//
ID   Integrin.
AC   KW-0401
DE   Protein of the integrin family of cell surface heterodimeric receptors
DE   that mediates dynamic cell-to-cell as well as cell-to-matrix adhesion.
DE   Integrins function as mechanochemical sensors and transducers able to
DE   change rapidly and reversibly their adhesive functions by modulating
DE   their ligand-binding affinity. Each subunit has a large N-terminal
DE   extracellular domain followed by a transmembrane domain and a short C-
DE   terminal cytoplasmic region. Some subclasses of integrins share a
DE   common beta chain while having different alpha chains.
GO   GO:0007229; integrin-mediated signaling pathway
HI   Molecular function: Integrin.
CA   Molecular function.
//
ID   Intellectual disability.
AC   KW-0991
DE   Protein which, if defective, is involved in intellectual disability, a
DE   disorder appearing during development and characterized by subnormal
DE   intellectual functioning and impaired adaptive behavior.
SY   Mental deficiency; Mental retardation; Mental subnormality.
HI   Disease: Intellectual disability.
CA   Disease.
//
ID   Interferon antiviral system evasion.
AC   KW-0922
DE   Viral protein which prevents the activation of the antiviral state
DE   induced by interferon (IFN) in the host cell, thereby allowing the
DE   virus to replicate optimally. The antiviral state is the result of a
DE   signaling pathway induced by IFN-alpha or IFN-beta following viral
DE   infection. It leads to the transcription of various cellular antiviral
DE   genes coding for host defense proteins.
SY   Antiviral state evasion; Interferon response evasion.
GO   GO:0019049; mitigation of host antiviral defense response
HI   Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; Interferon antiviral system evasion.
CA   Biological process.
//
ID   Intermediate capsid protein.
AC   KW-1154
DE   Viral protein that is a component of the intermediate layer of a
DE   triple concentric icosahedral capsid. Intermediate capsids are part of
DE   reoviridae virions.
GO   GO:0039626; viral intermediate capsid
HI   Cellular component: Virion; Capsid protein; Intermediate capsid protein.
CA   Cellular component.
//
ID   Intermediate filament.
AC   KW-0403
DE   Intermediate filaments (IF) are proteins which are primordial
DE   components of the cytoskeleton and the nuclear envelope. They
DE   generally form filamentous structures 8 to 14 nm wide and intermediate
DE   in size between microtubules and microfilaments. This family of
DE   protein includes cytokeratins, vimentin, desmin, glial fibrillary
DE   acidic protein, neurofilament proteins and nestin. All IF proteins are
DE   structurally similar in that they consist of: a central rod domain
DE   which is arranged in coiled-coiled alpha-helices, with at least two
DE   short characteristic interruptions; an N-terminal non-helical domain
DE   (head) of variable length; and an C-terminal domain (tail) which is
DE   also non-helical and shows extreme length variation between different
DE   IF proteins.
GO   GO:0005882; intermediate filament
HI   Cellular component: Intermediate filament.
CA   Cellular component.
//
ID   Intrahepatic cholestasis.
AC   KW-0988
DE   Protein which, if defective, causes intrahepatic cholestasis, a
DE   condition characterized by stoppage or suppression of the bile flow
DE   from the liver to the duodenum without extrahepatic bile duct
DE   obstruction.
HI   Disease: Intrahepatic cholestasis.
CA   Disease.
//
ID   Intron homing.
AC   KW-0404
DE   Endonucleases involved in intron homing, a genetic event leading to
DE   the transfer of an intron DNA sequence. This type of intron mobility
DE   depends on site-specific restriction endonucleases encoded by the
DE   mobile introns.
SY   Intron transposition.
GO   GO:0006314; intron homing
HI   Molecular function: Hydrolase; Nuclease; Endonuclease; Intron homing.
HI   Biological process: Intron homing.
CA   Biological process.
//
ID   Iodination.
AC   KW-0405
DE   Protein which is posttranslationally modified by the replacement of at
DE   least one hydrogen by iodine.
SY   Iodinated.
HI   PTM: Iodination.
CA   PTM.
//
ID   Ion channel.
AC   KW-0407
DE   Protein which is part of a transmembrane protein complex that forms a
DE   hydrophilic channel across the lipid bilayer through which specific
DE   inorganic ions can diffuse down their electrochemical gradients. The
DE   channels are usually gated and only open in response to a specific
DE   stimulus, such as a change in membrane potential (voltage-gated) or
DE   the binding of a ligand (ligand-gated channel).
GO   GO:0034220; monoatomic ion transmembrane transport
GO   GO:0034702; monoatomic ion channel complex
HI   Biological process: Transport; Ion transport; Ion channel.
HI   Molecular function: Ion channel.
CA   Molecular function.
//
ID   Ion channel impairing toxin.
AC   KW-0872
DE   Protein which interferes with the function of ion channels, which are
DE   hydrophilic channels across the lipid bilayer through which specific
DE   inorganic ions can diffuse down their electrochemical gradients.
GO   GO:0099106; ion channel regulator activity
HI   Molecular function: Toxin; Ion channel impairing toxin.
CA   Molecular function.
//
ID   Ion transport.
AC   KW-0406
DE   Protein involved in the transport of ions. Such proteins are usually
DE   transmembrane and mediate a movement of ions across cell membranes.
DE   Transport may be passive (facilitated diffusion; down the
DE   electrochemical gradient), or active (against the electrochemical
DE   gradient). Active transport requires energy which may come from light,
DE   oxidation reactions, ATP hydrolysis, or cotransport of other ions or
DE   molecules.
GO   GO:0006811; monoatomic ion transport
HI   Biological process: Transport; Ion transport.
CA   Biological process.
//
ID   Ionotropic glutamate receptor inhibitor.
AC   KW-1028
DE   Protein that inhibits ionotropic glutamate receptor (iGluR). iGluRs
DE   are glutamate-gated ion channels that mediate excitatory
DE   neurotransmission in the central nervous system. Based on both
DE   molecular and pharmacological criteria, iGluRs have been divided into
DE   two major classes, the non-NMDA class, which includes both AMPA and
DE   kainate subtypes of receptors, and the NMDA class.
HI   Molecular function: Toxin; Neurotoxin; Postsynaptic neurotoxin; Ionotropic glutamate receptor inhibitor.
HI   Molecular function: Toxin; Ion channel impairing toxin; Ionotropic glutamate receptor inhibitor.
CA   Molecular function.
//
ID   Iron.
AC   KW-0408
DE   Protein which binds at least one iron atom, or protein whose function
DE   is iron-dependent. Iron is a metal, chemical symbol Fe.
SY   Fe; Fe cation; Fe ion; Iron cation; Iron ion.
HI   Ligand: Iron.
WW   https://www.webelements.com/iron/
CA   Ligand.
//
ID   Iron storage.
AC   KW-0409
DE   Protein involved in the storage of iron.
GO   GO:0006879; intracellular iron ion homeostasis
HI   Ligand: Iron; Iron storage.
HI   Biological process: Iron storage.
CA   Biological process.
//
ID   Iron transport.
AC   KW-0410
DE   Protein involved in the transport of iron.
SY   Fe transport; Iron cation transport; Iron ion transport.
GO   GO:0006826; iron ion transport
HI   Biological process: Transport; Ion transport; Iron transport.
HI   Ligand: Iron; Iron transport.
CA   Biological process.
//
ID   Iron-sulfur.
AC   KW-0411
DE   Protein which binds at least one iron-sulfur cluster, e.g. 2Fe-2S,
DE   3Fe-4S, 4Fe-4S.
SY   Iron-sulfur cluster.
GO   GO:0051536; iron-sulfur cluster binding
HI   Ligand: Iron; Iron-sulfur.
HI   Ligand: Metal-binding; Iron-sulfur.
CA   Ligand.
//
ID   Isoleucine biosynthesis.
AC   KW-0412
DE   Protein involved in the synthesis of the hydrophobic amino acid
DE   isoleucine.
SY   Isoleucine anabolism; Isoleucine biosynthetic process;
SY   Isoleucine formation; Isoleucine synthesis.
GO   GO:0009097; isoleucine biosynthetic process
HI   Biological process: Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Isoleucine biosynthesis.
CA   Biological process.
//
ID   Isomerase.
AC   KW-0413
DE   Enzyme that catalyzes the 1,1-, 1,2- or 1,3-hydrogen shift. The 1,1-
DE   hydrogen shift is an inversion at an asymmetric carbon center
DE   (racemases, epimerases). The 1,2-hydrogen shift involved a hydrogen
DE   transfer between two adjacent carbon atoms, one undergoing oxidation,
DE   the other reduction (aldose-ketose isomerases). The 1,3-hydrogen
DE   shifts are allylic or azaallylic (when nitrogen is one of the three
DE   atoms) isomerizations.
GO   GO:0016853; isomerase activity
HI   Molecular function: Isomerase.
CA   Molecular function.
//
ID   Isopeptide bond.
AC   KW-1017
DE   Protein which is posttranslationally modified by the formation of an
DE   amide bond between an amino-group and a carboxyl-group at least one of
DE   which is not an alpha group. An isopeptide bond involves the side
DE   chain of one or two amino acid residues. Because there are few enzymes
DE   that hydrolyze isopeptide bonds, the formation of interchain
DE   isopeptide bonds can produce stably linked protein dimers, multimers
DE   or complexes, such as blood clots.
HI   PTM: Isopeptide bond.
CA   PTM.
//
ID   Isoprene biosynthesis.
AC   KW-0414
DE   Protein involved in the synthesis of isoprene, an important organic
DE   unit of 5 carbons in plants. It is used to build up isoprenoids,
DE   including carotenoids, terpenes and natural rubber.
SY   Isoprene anabolism; Isoprene biosynthetic process; Isoprene formation;
SY   Isoprene synthesis.
GO   GO:0008299; isoprenoid biosynthetic process
HI   Biological process: Isoprene biosynthesis.
CA   Biological process.
//
ID   Jasmonic acid signaling pathway.
AC   KW-1184
DE   Protein involved in the jasmonic acid (jasmonate, JA) signaling
DE   pathway (e.g. transport and signal transduction) that regulates many
DE   aspects of plant growth, development and cellular signaling (e.g.
DE   growth inhibition, senescence, tuber formation, response to wounding,
DE   plant defense, and leaf abscission). This phytohormone and its
DE   derivatives such as methyl jasmonate (MeJA) can be synthesized from
DE   the fatty acid linolenic acid in the oxylipin octadecanoid pathway.
SY   JA mediated signaling; JA signaling pathway;
SY   Jasmonate mediated signaling; Jasmonate signaling pathway;
SY   Jasmonic acid mediated signaling.
HI   Biological process: Jasmonic acid signaling pathway.
CA   Biological process.
//
ID   Joubert syndrome.
AC   KW-0979
DE   Protein which, if defective, causes Joubert syndrome, an autosomal
DE   recessive multisystem disorder characterized by cerebellar ataxia,
DE   developmental delay, hypotonia, neonatal breathing abnormalities and
DE   oculomotor apraxia. Neuroradiologically, it is characterized by
DE   cerebellar vermis hypoplasia/aplasia, thickened and reoriented
DE   superior cerebellar peduncles, and an abnormally large interpeduncular
DE   fossa, giving the appearance of the 'molar tooth sign' on transaxial
DE   slices. A wide clinical variability with a marked variation in
DE   severity and inconsistent presence of the following features is
DE   observed: episodic apnea-hyperpnea, abnormal eye movements, occipital
DE   meningoencephalocele, polydactyly, nephronophthisis or cystic
DE   dysplasia of the kidney, chorioretinal coloboma and retinal dysplasia.
DE   The variable association of ocular and renal abnormalities with
DE   cerebellar features typical of Joubert syndrome defines the cerebello-
DE   oculo-renal syndromes (CORSs).
SY   Cerebellar vermis agenesis; Cerebelloparenchymal disorder IV; CPD IV;
SY   JBTS; Joubert-Boltshauser syndrome; JS.
HI   Disease: Ciliopathy; Joubert syndrome.
CA   Disease.
//
ID   Kallmann syndrome.
AC   KW-0956
DE   Protein which, if defective, causes Kallmann syndrome, a disorder
DE   characterized by the association of hypogonadotropic hypogonadism with
DE   anosmia or hyposmia. Kallmann syndrome is caused by impaired embryonic
DE   development of the olfactory system and the GnRH-synthesizing neurons.
DE   The main clinical features consist of the association of micropenis
DE   and cryptorchidism in young boys, the absence of spontaneous puberty,
DE   and a partial or total loss of the sense of smell (anosmia). In some
DE   patients other developmental anomalies can be present such as renal
DE   agenesis, cleft lip/palate, selective tooth agenesis and bimanual
DE   synkinesis.
SY   Dysplasia olfactogenitalis of De Morsier; HHA;
SY   Hypogonadotropic hypogonadism and anosmia; Kallmann's syndrome;
SY   Kallmann de Morsier syndrome; KMS.
HI   Disease: Kallmann syndrome.
CA   Disease.
//
ID   Kartagener syndrome.
AC   KW-1012
DE   Protein which, if defective, causes Kartagener syndrome, a rare and
DE   genetically heterogeneous disorder characterized by the combination of
DE   primary ciliary dyskinesia and situs inversus viscerum.
SY   Dextrocardia-bronchiectasis-sinusitis syndrome; KTGS;
SY   Siewert syndrome.
HI   Disease: Ciliopathy; Primary ciliary dyskinesia; Kartagener syndrome.
CA   Disease.
//
ID   Karyogamy.
AC   KW-0415
DE   Protein involved in the fusion of the nuclei of two gametes after
DE   cytoplasmic fusion.
GO   GO:0000741; karyogamy
HI   Biological process: Karyogamy.
CA   Biological process.
//
ID   Kelch repeat.
AC   KW-0880
DE   Protein containing at least one Kelch repeat.
HI   Domain: Kelch repeat.
CA   Domain.
//
ID   Keratin.
AC   KW-0416
DE   Fibrous proteins rich in cysteine and the chief constituent of horn,
DE   nails, hair, epidermis and feathers. Two major conformational groups
DE   have been characterized, alpha-keratin, whose peptide backbone forms
DE   an alpha-helix, and beta-keratin, whose backbone forms a zigzag or
DE   pleated sheet structure.
GO   GO:0005882; intermediate filament
HI   Cellular component: Keratin.
CA   Cellular component.
//
ID   Keratinization.
AC   KW-0417
DE   Protein involved in keratinization, the process in which the cytoplasm
DE   of the outermost cells of the vertebrate epidermis is replaced by
DE   keratin. Keratinization occurs in the stratum corneum, feathers, hair,
DE   claws, nails, hooves, and horns.
GO   GO:0031424; keratinization
HI   Biological process: Keratinization.
CA   Biological process.
//
ID   Kinase.
AC   KW-0418
DE   Enzyme that catalyzes the transfer of phosphate (phosphoryl or
DE   pyrophosphoryl transfer) usually from ATP to a second substrate.
SY   Phosphotransferase.
GO   GO:0016301; kinase activity
GO   GO:0016310; phosphorylation
HI   Molecular function: Transferase; Kinase.
CA   Molecular function.
//
ID   Kinetochore.
AC   KW-0995
DE   The kinetochore is a complex assembled at centromeric region of DNA,
DE   which provides the major attachment point for the spindle
DE   microtubules. In monocentric chromosomes, the kinetochores of point
DE   centromeres bind a single microtubule and the larger kinetochores of
DE   regional centromeres interact with a number of microtubules. In
DE   holocentric chromosomes, the kinetochores bind the diffuse centromere
DE   along the length of the chromosomes.
GO   GO:0000776; kinetochore
HI   Cellular component: Kinetochore.
CA   Cellular component.
//
ID   Kinetoplast.
AC   KW-0419
DE   Protein associated with the kinetoplast DNA (kDNA), the mitochondrial
DE   DNA of trypanosomatid protozoa. kDNA is a massive network, composed of
DE   thousands of topologically interlocked DNA circles. Each cell contains
DE   one network condensed into a disk-shaped structure within the matrix
DE   of its single mitochondrion. The kDNA circles are of two types,
DE   maxicircles present in a few dozen copies and minicircles present in
DE   several thousand copies.
GO   GO:0020023; kinetoplast
HI   Cellular component: Mitochondrion; Kinetoplast.
CA   Cellular component.
//
ID   Knottin.
AC   KW-0960
DE   Small disulfide-rich protein characterized by a special 'disulfide
DE   through disulfide knot'. This knot is obtained when one disulfide
DE   bridge crosses the macrocycle formed by two other disulfides and the
DE   interconnecting backbone (disulfide III-VI goes through disulfides I-
DE   IV and II-V). The knottin structure is found in some plant protease
DE   inhibitors, cyclotides, toxins from cone snails, spiders, insects,
DE   horseshoe crabs and scorpions, gurmarin-like peptides, agouti-related
DE   proteins, and some antimicrobial peptides.
SY   ICK; Inhibitor Cystine Knot.
HI   Domain: Knottin.
WW   http://knottin.cbs.cnrs.fr
CA   Domain.
//
ID   Kringle.
AC   KW-0420
DE   Protein containing at least one kringle domain, a triple-looped,
DE   disulfide cross-linked domain of approximately 80 amino acids in
DE   length and involved in protein-protein interactions.
HI   Domain: Kringle.
CA   Domain.
//
ID   Lacrimo-auriculo-dento-digital syndrome.
AC   KW-0953
DE   Protein which, if defective, causes lacrimo-auriculo-dento-digital
DE   syndrome. Lacrimo-auriculo-dento-digital syndrome, a form of
DE   ectodermal dysplasia, is an autosomal dominant multiple congenital
DE   anomaly. It is characterized by aplastic/hypoplastic lacrimal and
DE   salivary glands and ducts, cup-shaped ears, hearing loss, hypodontia
DE   and enamel hypoplasia, and distal limb segments anomalies. In addition
DE   to these cardinal features, facial dysmorphism, malformations of the
DE   kidney and respiratory system and abnormal genitalia have been
DE   reported. Craniosynostosis and severe syndactyly are not observed.
SY   Lacrimoauriculodentodigital syndrome; LADD syndrome;
SY   Levy-Hollister syndrome.
HI   Disease: Ectodermal dysplasia; Lacrimo-auriculo-dento-digital syndrome.
CA   Disease.
//
ID   Lactation.
AC   KW-0421
DE   Protein involved in lactation, the secretion of milk by mammary
DE   glands.
GO   GO:0007595; lactation
HI   Biological process: Lactation.
CA   Biological process.
//
ID   Lactose biosynthesis.
AC   KW-0422
DE   Protein involved in the synthesis of lactose, a disaccharide of
DE   glucose and galactose present in milk.
SY   Lactose anabolism; Lactose biosynthetic process; Lactose formation;
SY   Lactose synthesis.
GO   GO:0005989; lactose biosynthetic process
HI   Biological process: Lactose biosynthesis.
CA   Biological process.
//
ID   Lactose metabolism.
AC   KW-0423
DE   Protein involved in the biochemical reactions with lactose, a
DE   disaccharide of glucose and galactose, found in milk.
SY   Lactose metabolic process.
GO   GO:0005988; lactose metabolic process
HI   Biological process: Lactose metabolism.
CA   Biological process.
//
ID   Laminin EGF-like domain.
AC   KW-0424
DE   Protein containing at least one laminin EGF-like domain. Laminins are
DE   the major noncollagenous components of basement membranes. Their
DE   subunits contain consecutive repeats of about 60 amino acids, which
DE   include 8 conserved cysteines that form disulfide bonds (C1-C3, C2-C4,
DE   C5-C6, C7-C8). The tertiary structure of this domain is remotely
DE   similar, in its N-terminal, to that of the EGF-like module.
HI   Domain: Laminin EGF-like domain.
CA   Domain.
//
ID   Lantibiotic.
AC   KW-0425
DE   Lanthionine-containing peptide antibiotics are peptides produced by
DE   Gram-positive bacteria which cause cell death of other Gram-positive
DE   bacteria.
GO   GO:0005102; signaling receptor binding
GO   GO:0031640; killing of cells of another organism
HI   Molecular function: Antimicrobial; Antibiotic; Bacteriocin; Lantibiotic.
CA   Molecular function.
//
ID   Late protein.
AC   KW-0426
DE   Bacteriophage or viral protein expressed in a later phase of the
DE   infectious cycle.
HI   Developmental stage: Late protein.
CA   Developmental stage.
//
ID   Latency-replication decision.
AC   KW-1252
DE   Viral protein part of a genetic system that takes part in the decision
DE   of the outcome of the infection: latency or replication. Expression of
DE   genetic switch proteins control the expression of viral genes that act
DE   as effectors in either the establishment of latency (lysogeny) or in
DE   promoting productive replication (lytic cycle). Interactions between
DE   proteins involved in switch regulatory processes and host proteins
DE   often influence the decision.
GO   GO:0098689; latency-replication decision
HI   Biological process: Latency-replication decision.
CA   Biological process.
//
ID   LDL.
AC   KW-0427
DE   Protein constituent of the low-density lipoproteins or protein which
DE   binds LDLs. LDLs are plasma lipoproteins rich in cholesterol esters,
DE   synthesized from the very low-density lipoprotein (VLDL), and which
DE   transport cholesterol to peripheral tissue and regulate de novo
DE   cholesterol synthesis.
GO   GO:0034362; low-density lipoprotein particle
HI   Cellular component: LDL.
CA   Cellular component.
//
ID   Lead.
AC   KW-1027
DE   Protein which binds at least one lead atom, or protein whose function
DE   is lead-dependent. Lead is a metal, chemical symbol Pb.
SY   Lead cation; Lead ion; Pb; Pb cation; Pb ion.
HI   Ligand: Lead.
WW   https://www.webelements.com/lead/
CA   Ligand.
//
ID   Leader peptide.
AC   KW-0428
DE   Short peptide sequences translated from bacterial leader RNA sequences
DE   which are involved in transcriptional or translation attenuation,
DE   mechanisms that modulate mRNA transcription or translation.
HI   Molecular function: Leader peptide.
CA   Molecular function.
//
ID   Leber congenital amaurosis.
AC   KW-0901
DE   Protein which, if defective, causes Leber congenital amaurosis, a
DE   clinically and genetically heterogeneous type of blindness transmitted
DE   as an autosomal recessive trait and occurring at or shortly after
DE   birth. It is associated with an atypical form of diffuse pigmentation
DE   and commonly with optic atrophy and attenuation of the retinal
DE   vessels.
HI   Disease: Leber congenital amaurosis.
CA   Disease.
//
ID   Leber hereditary optic neuropathy.
AC   KW-0429
DE   Protein which, if defective, causes Leber hereditary optic neuropathy,
DE   a mitochondrial disease leading to bilateral, painless loss of central
DE   vision due to selective degeneration of the retinal ganglion cells and
DE   their axons. The disease arises during young adult life and displays
DE   sex-dependent incomplete penetrance and male predominance.
HI   Disease: Primary mitochondrial disease; Leber hereditary optic neuropathy.
CA   Disease.
//
ID   Lectin.
AC   KW-0430
DE   Protein which specifically binds carbohydrates. Lectins are obtained
DE   particularly from seeds of leguminous plants but also from other plant
DE   and animal sources. They contain binding sites for specific mono-and
DE   oligosaccharides. They agglutinate cells by binding to specific sugar
DE   residues in membrane glycoproteins.
GO   GO:0030246; carbohydrate binding
HI   Ligand: Lectin.
CA   Ligand.
//
ID   Leigh syndrome.
AC   KW-0431
DE   Protein which, if defective, causes Leigh syndrome, a
DE   neurodegenerative disorder characterized by the subacute onset of
DE   psychomotor retardation, hypotonia, ataxia, weakness, vision loss, eye
DE   movement abnormalities, seizures, dysphagia, and lactic acidosis.
DE   Pathological features include spongy degeneration of the neuropile of
DE   the basal ganglia, thalamus, brain stem, and spinal cord. The syndrome
DE   is caused by a variety of defects of enzymes involved in energy
DE   metabolism, including cytochrome c oxidase (COX), the mitochondrial
DE   encoded ATP6 subunit of ATP synthase, and the X-linked E1-alpha
DE   subunit of pyruvate dehydrogenase.
HI   Disease: Primary mitochondrial disease; Leigh syndrome.
CA   Disease.
//
ID   Leucine biosynthesis.
AC   KW-0432
DE   Protein involved in the synthesis of the hydrophobic amino acid
DE   leucine.
SY   Leucine anabolism; Leucine biosynthetic process; Leucine formation;
SY   Leucine synthesis.
GO   GO:0009098; leucine biosynthetic process
HI   Biological process: Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Leucine biosynthesis.
CA   Biological process.
//
ID   Leucine-rich repeat.
AC   KW-0433
DE   Protein containing at least one leucine-rich repeat (LRR).
SY   LRR.
HI   Domain: Leucine-rich repeat.
CA   Domain.
//
ID   Leukodystrophy.
AC   KW-1026
DE   Protein which, if defective, causes leukodystrophy, any of a group of
DE   diseases that affect the formation or maintenance of myelin in the
DE   central nervous system.
HI   Disease: Leukodystrophy.
CA   Disease.
//
ID   Leukotriene biosynthesis.
AC   KW-0434
DE   Protein involved in the synthesis of leukotrienes, eicosanoid hormones
DE   first isolated from leukocytes. They are thought to mediate the
DE   allergic response that causes lung constriction and muscle contraction
DE   in asthma.
SY   Leukotriene anabolism; Leukotriene biosynthetic process;
SY   Leukotriene formation; Leukotriene synthesis.
GO   GO:0019370; leukotriene biosynthetic process
HI   Biological process: Leukotriene biosynthesis.
CA   Biological process.
//
ID   Li-Fraumeni syndrome.
AC   KW-0435
DE   Protein which, if defective, causes Li-Fraumeni syndrome (LFS), an
DE   autosomal dominant familial cancer predisposition syndrome associated
DE   with soft-tissue sarcoma, breast cancer, leukemia, osteosarcoma,
DE   melanoma, and cancer of the colon, pancreas, adrenal cortex and brain.
DE   Individuals with LFS are at increased risk for developing multiple
DE   primary cancers.
SY   LFS; Sarcoma family syndrome of Li and Fraumeni; SBLA syndrome.
HI   Disease: Li-Fraumeni syndrome.
CA   Disease.
//
IC   Ligand.
AC   KW-9993
DE   Keywords assigned to proteins because they bind, are associated with,
DE   or whose activity is dependent of some molecule.
//
ID   Ligand-gated ion channel.
AC   KW-1071
DE   Protein which forms or is a component of a ligand-gated channel.
DE   Ligand-gated channels are transmembrane ion channels whose
DE   permeability is increased by the binding of a specific ligand, such as
DE   neurotransmitters, ionositol triphosphates, and cyclic nucleotides.
SY   LGIC; Ligand-gated channel.
HI   Biological process: Transport; Ion transport; Ligand-gated ion channel.
HI   Molecular function: Ion channel; Ligand-gated ion channel.
CA   Molecular function.
//
ID   Ligase.
AC   KW-0436
DE   Enzyme that catalyzes the joining of two molecules coupled with the
DE   breakdown of a pyrophosphate bond in ATP or a similar triphosphate.
DE   Sometimes the terms "synthase", "synthetase" or "carboxylase" are also
DE   used for this class of enzymes.
GO   GO:0016874; ligase activity
HI   Molecular function: Ligase.
CA   Molecular function.
//
ID   Light-harvesting polypeptide.
AC   KW-0437
DE   Proteins which form part of the antenna complex, a light-harvesting
DE   system found in photosynthetic bacteria which absorb light radiation
DE   and transfer the excitation energy to the reaction centres.
GO   GO:0030076; light-harvesting complex
HI   Molecular function: Light-harvesting polypeptide.
CA   Molecular function.
//
ID   Lignin biosynthesis.
AC   KW-0438
DE   Protein involved in the synthesis of lignin, a polymer of
DE   phenylpropanoid subunits found in the walls of plant cells such as
DE   xylem and sclerenchyma fibres. Lignin imparts strength to the wall and
DE   protects against degradation by microorganisms.
SY   Lignin anabolism; Lignin biosynthetic process; Lignin formation;
SY   Lignin synthesis.
GO   GO:0009809; lignin biosynthetic process
HI   Biological process: Lignin biosynthesis.
CA   Biological process.
//
ID   Lignin degradation.
AC   KW-0439
DE   Protein involved in the breakdown of lignin, a polymer of
DE   phenylpropanoid subunits found in the walls of plant cells such as
DE   xylem and sclerenchyma fibres. It imparts strength to the wall and
DE   protects against degradation by microorganisms.
SY   Lignin breakdown; Lignin catabolic process; Lignin catabolism.
GO   GO:0046274; lignin catabolic process
HI   Biological process: Lignin degradation.
CA   Biological process.
//
ID   LIM domain.
AC   KW-0440
DE   Protein which contains at least one LIM domain, a conserved cysteine-
DE   rich domain of approximately 60 amino acids with seven conserved
DE   cysteines and a histidine. The LIM domain binds two zinc ions and
DE   seems to be involved in protein-protein interactions.
SY   LIM motif.
HI   Ligand: Metal-binding; LIM domain.
HI   Ligand: Zinc; LIM domain.
HI   Domain: LIM domain.
CA   Domain.
//
ID   Limb-girdle muscular dystrophy.
AC   KW-0947
DE   Protein which, if defective, causes limb-girdle muscular dystrophy, a
DE   degenerative myopathy without nervous system involvement. The disease
DE   is characterized by slowly progressive wasting and weakness of the
DE   proximal muscles of arms and legs around the pelvic or shoulder
DE   girdles, elevated creatine kinase levels and dystrophic features on
DE   muscle biopsy. Onset of symptoms is in late childhood, adolescence or
DE   even adult life. Limb-girdle muscular dystrophy is a genetically
DE   heterogeneous disorder. Inheritance can be autosomal dominant or
DE   autosomal recessive.
SY   LGMD; Muscular dystrophy limb-girdle type.
HI   Disease: Limb-girdle muscular dystrophy.
CA   Disease.
//
ID   Lipid A biosynthesis.
AC   KW-0441
DE   Protein involved in the synthesis of lipid A (endotoxin), the
DE   hydrophobic anchor of lipopolysaccharide (LPS). Lipid A is a
DE   glucosamine-based phospholipid that makes up the outer monolayer of
DE   the outer membranes of most Gram-negative bacteria.
SY   Lipid A anabolism; Lipid A biosynthetic process; Lipid A formation;
SY   Lipid A synthesis.
GO   GO:0009245; lipid A biosynthetic process
HI   Biological process: Lipid metabolism; Lipid biosynthesis; Lipid A biosynthesis.
CA   Biological process.
//
ID   Lipid biosynthesis.
AC   KW-0444
DE   Protein involved in the synthesis of lipids, a diverse class of
DE   compounds which are insoluble in water but soluble in organic
DE   solvents. They include fats, oils, triacylglycerols, fatty acids,
DE   glycolipids, phospholipids and steroids.
SY   Lipid anabolism; Lipid biosynthetic process; Lipid formation.
GO   GO:0008610; lipid biosynthetic process
HI   Biological process: Lipid metabolism; Lipid biosynthesis.
CA   Biological process.
//
ID   Lipid degradation.
AC   KW-0442
DE   Protein involved in the breakdown of lipids, a diverse class of
DE   compounds, insoluble in water but soluble in organic solvents, and
DE   which include fats, oils, triacylglycerols, fatty acids, glycolipids,
DE   phospholipids and steroids.
SY   Lipid breakdown; Lipid catabolic process; Lipid catabolism.
GO   GO:0016042; lipid catabolic process
HI   Biological process: Lipid metabolism; Lipid degradation.
CA   Biological process.
//
ID   Lipid droplet.
AC   KW-0551
DE   Protein characteristic of a lipid droplet, a dynamic cytoplasmic
DE   organelle which consists of an heterogeneous macromolecular assembly
DE   of lipids and proteins covered by a unique phospholipid monolayer.
DE   Lipid droplets may play a role in lipid metabolism and storage, and
DE   they may be involved in the regulation of intracellular trafficking
DE   and signal transduction.
SY   Adiposome; Lipid bodies; Lipid body; Lipid particle;
SY   Monolayer-surrounded lipid storage body; Oil bodies; Oil body;
SY   Oleosome; Spherosome.
GO   GO:0005811; lipid droplet
HI   Cellular component: Lipid droplet.
CA   Cellular component.
//
ID   Lipid metabolism.
AC   KW-0443
DE   Protein involved in the biochemical reactions of lipids. Lipids are a
DE   diverse class of compounds which are insoluble in water but soluble in
DE   organic solvents. They include fats, oils, triacylglycerols, fatty
DE   acids, glycolipids, phospholipids and steroids.
SY   Lipid metabolic process.
GO   GO:0006629; lipid metabolic process
HI   Biological process: Lipid metabolism.
CA   Biological process.
//
ID   Lipid transport.
AC   KW-0445
DE   Protein involved in the transport of lipids, a diverse class of
DE   compounds which are insoluble in water but soluble in organic
DE   solvents. They include fats, oils, triacylglycerols, fatty acids,
DE   glycolipids, phospholipids and steroids.
GO   GO:0006869; lipid transport
HI   Biological process: Transport; Lipid transport.
CA   Biological process.
//
ID   Lipid-binding.
AC   KW-0446
DE   Protein which binds one or more lipids.
GO   GO:0008289; lipid binding
HI   Ligand: Lipid-binding.
CA   Ligand.
//
ID   Lipopolysaccharide biosynthesis.
AC   KW-0448
DE   Protein involved in the synthesis of lipopolysaccharides (LPS), the
DE   main constituents of the outer cell wall of Gram-negative bacteria.
DE   LPS are composed of lipid molecules joined to polysaccharides and are
DE   highly immunogenic.
SY   Lipopolysaccharide anabolism; Lipopolysaccharide biosynthetic process;
SY   Lipopolysaccharide formation; Lipopolysaccharide synthesis.
GO   GO:0009103; lipopolysaccharide biosynthetic process
HI   Biological process: Lipopolysaccharide biosynthesis.
CA   Biological process.
//
ID   Lipoprotein.
AC   KW-0449
DE   Protein which is posttranslationally modified by the attachment of at
DE   least one lipid or fatty acid, e.g. farnesyl, palmitate and myristate.
SY   Lipidated.
HI   PTM: Lipoprotein.
CA   PTM.
//
ID   Lipoyl.
AC   KW-0450
DE   Protein which contains at least one lipoyl-binding domain. Lipoic acid
DE   is an essential cofactor for E2 acyltransferases and some other
DE   proteins.
HI   Domain: Lipoyl.
CA   Domain.
//
ID   Lissencephaly.
AC   KW-0451
DE   Protein which, if defective, causes lissencephaly, a brain
DE   malformation characterized by the absence (agyria) or reduction
DE   (pachygyria) of brain surface convolutions (gyri), in association with
DE   abnormal organisation of the cortical layers. It results from neuronal
DE   migration defects during embryogenesis. Two large groups can be
DE   distinguished: classical lissencephaly (and its variants) and
DE   cobblestone lissencephaly. Lissencephaly means "smooth brain".
HI   Disease: Lissencephaly.
CA   Disease.
//
ID   Lithium.
AC   KW-0452
DE   Protein whose function is lithium-dependent. Lithium is an alkali
DE   metal, chemical symbol Li.
SY   Li; Li cation; Li ion; Lithium cation; Lithium ion.
HI   Ligand: Lithium.
WW   https://www.webelements.com/lithium/
CA   Ligand.
//
ID   Long QT syndrome.
AC   KW-0454
DE   Protein which, if defective, causes the long QT syndrome, a heart
DE   disease which manifests itself by a prolonged QT interval on the ECG
DE   and, clinically, by a propensity for tachyarrhythmias, causing
DE   syncopes and sudden cardiac death. LQTS may be drug-induced, but
DE   mutations in genes coding for cardiac ion-channels are the cause of
DE   the hereditary forms: Romano-Ward syndrome (RWS), and Jervell and
DE   Lange-Nielsen Syndrome (JLNS).
SY   LQTS.
HI   Disease: Long QT syndrome.
CA   Disease.
//
ID   LTQ.
AC   KW-0886
DE   Protein which contains at least one lysine tyrosylquinone (LTQ) cross-
DE   link modification. LTQ is formed by oxidation of the phenol ring of a
DE   tyrosine to form tyrosylquinone (topaquinone) followed by covalent
DE   cross-linking with a lysine residue.
SY   Lysine topaquinone; Lysine tyrosylquinone.
HI   PTM: LTQ.
CA   PTM.
//
ID   Luminescence.
AC   KW-0455
DE   Protein involved in luminescence, the property of giving off light
DE   without emitting a corresponding degree of heat.
SY   Bioluminescence.
GO   GO:0008218; bioluminescence
HI   Biological process: Luminescence.
CA   Biological process.
//
ID   Lyase.
AC   KW-0456
DE   Enzyme that catalyzes the cleavage of C-C, C-O, C-S, C-N or other
DE   bonds by other means than by hydrolysis or oxidation, with two
DE   substrates in one reaction direction, and one in the other. In the
DE   latter direction, a molecule (of carbon dioxide, water, etc) is
DE   eliminated, thus creating a new double bond or a new ring.
GO   GO:0016829; lyase activity
HI   Molecular function: Lyase.
CA   Molecular function.
//
ID   Lysine biosynthesis.
AC   KW-0457
DE   Protein involved in the synthesis of the essential basic amino acid
DE   lysine.
SY   Lysine anabolism; Lysine biosynthetic process; Lysine formation;
SY   Lysine synthesis.
GO   GO:0009085; lysine biosynthetic process
HI   Biological process: Amino-acid biosynthesis; Lysine biosynthesis.
CA   Biological process.
//
ID   Lysosome.
AC   KW-0458
DE   Protein found in the lysosome, a membrane-limited organelle present in
DE   all eukaryotic cells, which contains a large number of hydrolytic
DE   enzymes that are used for the intracellular degradation of
DE   macromolecules.
GO   GO:0005764; lysosome
HI   Cellular component: Lysosome.
CA   Cellular component.
//
ID   Magnesium.
AC   KW-0460
DE   Protein which binds at least one magnesium atom, or protein whose
DE   function is magnesium-dependent. Magnesium is a metallic element,
DE   chemical symbol Mg.
SY   Magnesium cation; Magnesium ion; Mg; Mg cation; Mg ion.
HI   Ligand: Magnesium.
WW   https://www.webelements.com/magnesium/
CA   Ligand.
//
ID   Magnetosome.
AC   KW-1281
DE   Protein located in or on the magnetosome, a membrane-bound bacterial
DE   organelle that envelops crystals of magnetic iron minerals in
DE   magnetotactic bacteria. Magnetosomes form linear chains that align
DE   along the cellular motility axis at midcell and function in bacterial
DE   navigation along the Earth's magnetic field. They are formed by
DE   invagination of the cell inner membrane; in some species they remain
DE   connected to the inner membrane, in others they pinch off to form
DE   independent intracellular vesicles.
GO   GO:0110143; magnetosome
HI   Cellular component: Magnetosome.
CA   Cellular component.
//
ID   Malaria.
AC   KW-0461
DE   Protein involved in malaria, a human disease caused by Plasmodium, a
DE   parasitic protozoan that grows by sexual reproduction in the Anopheles
DE   mosquito.
HI   Disease: Malaria.
CA   Disease.
//
ID   Maltose metabolism.
AC   KW-0462
DE   Protein involved in the biochemical reactions with maltose, a
DE   disaccharide of glucose. Maltose is produced by the hydrolysis of
DE   starch.
SY   Maltose metabolic process.
GO   GO:0000023; maltose metabolic process
HI   Biological process: Maltose metabolism.
CA   Biological process.
//
ID   Mandelate pathway.
AC   KW-0463
DE   Enzyme involved in the mandelate pathway. These enzymes enable various
DE   microorganisms to grow using D(-)-, L(+)- or DL-mandelate (2-hydroxy-
DE   2-phenylacetate) as the sole source of carbon and energy.
GO   GO:0018924; mandelate metabolic process
HI   Biological process: Mandelate pathway.
CA   Biological process.
//
ID   Manganese.
AC   KW-0464
DE   Protein which binds at least one manganese atom, or protein whose
DE   function is manganese-dependent. Manganese is a metallic element,
DE   chemical symbol Mn.
SY   Manganese cation; Manganese ion; Mn; Mn cation; Mn ion.
HI   Ligand: Manganese.
WW   https://www.webelements.com/manganese/
CA   Ligand.
//
ID   Mannose-binding.
AC   KW-0465
DE   Protein which binds mannose, a 6-carbon aldose sugar, that is found in
DE   many glycoproteins and polysaccharides.
GO   GO:0005537; mannose binding
HI   Ligand: Lectin; Mannose-binding.
CA   Ligand.
//
ID   Maple syrup urine disease.
AC   KW-0466
DE   Protein which, if defective, causes maple syrup urine disease, an
DE   autosomal recessive disorder characterized by mental and physical
DE   retardation, feeding problems and a maple syrup odour to the urine.
HI   Disease: Maple syrup urine disease.
CA   Disease.
//
ID   Mast cell degranulation.
AC   KW-0467
DE   Protein involved in mast cell degranulation. Mast cell is a large,
DE   ovoid cell of hematopoietic lineage, with a centrally located nucleus
DE   and numerous large, intensely basophilic granules. The binding of an
DE   antigen to its specific immunoglobulin-E antibody on the mast cell
DE   surface triggers the release of the MC granules. Mast cells are
DE   involved in hypersensitivity reactions.
GO   GO:0043303; mast cell degranulation
HI   Biological process: Mast cell degranulation.
CA   Biological process.
//
ID   Meckel syndrome.
AC   KW-0981
DE   Protein which, if defective, causes Meckel syndrome, an autosomal
DE   recessive disorder characterized by a combination of renal cysts and
DE   variably associated features, including developmental anomalies of the
DE   central nervous system (usually occipital encephalocele), hepatic
DE   ductal dysplasia and cysts, and polydactyly.
SY   Dysencephalia splanchnocystica; Gruber syndrome;
SY   Meckel-Gruber syndrome; MKS.
HI   Disease: Ciliopathy; Meckel syndrome.
CA   Disease.
//
ID   Meiosis.
AC   KW-0469
DE   Protein involved in meiotic processes or in regulation of meiosis.
DE   Meiosis is the nuclear division which results in the daughter nuclei
DE   each containing half the number of chromosomes of the parent. It
DE   comprises two distinct nuclear divisions, the first and second meiotic
DE   divisions (which may be separated by cell division), the actual
DE   reduction in chromosome number takes place during the first division.
GO   GO:0051321; meiotic cell cycle
HI   Biological process: Meiosis.
CA   Biological process.
//
ID   Melanin biosynthesis.
AC   KW-0470
DE   Protein involved in the synthesis of melanin. Melanins are brown or
DE   black pigments found in skin, hair, feathers, etc. They are irregular
DE   polymeric structures produced from tyrosine. Melanins can be divided
DE   into 3 groups: allomelanins in the plant kingdom, and eumelanins and
DE   phaeomelanins in the animal kingdom.
SY   Melanin anabolism; Melanin biosynthetic process; Melanin formation;
SY   Melanin synthesis.
GO   GO:0042438; melanin biosynthetic process
HI   Biological process: Melanin biosynthesis.
CA   Biological process.
//
ID   MELAS syndrome.
AC   KW-0867
DE   Protein which, if defective, causes mitochondrial encephalomyopathy
DE   with lactic acidosis and stroke-like episodes (MELAS) syndrome, a
DE   genetically heterogeneous disorder, characterized by episodic
DE   vomiting, seizures, and recurrent cerebral insults resembling strokes
DE   and causing hemiparesis, hemianopsia, or cortical blindness.
HI   Disease: Primary mitochondrial disease; MELAS syndrome.
CA   Disease.
//
ID   Melatonin biosynthesis.
AC   KW-0471
DE   Protein involved in the synthesis of melatonin (N-acetyl 5-
DE   methoxytryptamine), a neurohormone synthesized by lower plants and in
DE   the pineal gland in animals. In humans, it is involved in the
DE   regulation of sleep, mood, puberty, ovarian cycles and in the
DE   establishment of circadian rhythms. In lower vertebrates, it causes
DE   aggregation of pigment in melanophores, and thus lightens skin.
SY   Melatonin anabolism; Melatonin biosynthetic process;
SY   Melatonin formation; Melatonin synthesis.
GO   GO:0030187; melatonin biosynthetic process
HI   Biological process: Melatonin biosynthesis.
CA   Biological process.
//
ID   Membrane.
AC   KW-0472
DE   Protein which is membrane-bound or membrane-associated. A membrane is
DE   the layer which forms the boundary of cells and intracellular
DE   organelles. It is composed of two oriented lipid layers in which
DE   proteins are embedded and acts as a selective permeability barrier.
GO   GO:0016020; membrane
HI   Cellular component: Membrane.
CA   Cellular component.
//
ID   Membrane attack complex.
AC   KW-0473
DE   Component of the membrane attack complex which groups the complement
DE   plasma glycoproteins C5b, C6, C7, C8 and polymeric C9 on biological
DE   membranes. The complex forms transmembrane channels which displace
DE   lipid molecules and other constituents, thus disrupting the
DE   phospholipid bilayer of target cells leading to cell lysis by osmotic
DE   leakage. The formation of the membrane attack complex is the terminal
DE   step in the complement cascade.
GO   GO:0005579; membrane attack complex
HI   Biological process: Immunity; Innate immunity; Complement pathway; Membrane attack complex.
HI   Biological process: Cytolysis; Membrane attack complex.
HI   Cellular component: Membrane attack complex.
CA   Cellular component.
//
ID   Menaquinone biosynthesis.
AC   KW-0474
DE   Protein involved in the synthesis of menaquinone, a derivative of 2-
DE   methyl-1,4-naphthoquinone in which the 3-position is substituted with
DE   a variable-length polyisoprene chain. In mammals, menaquinone is an
DE   important component of the blood coagulation system. Mammals need to
DE   obtain this vitamin by their diet or from the bacterial flora of the
DE   gut.
SY   Menaquinone anabolism; Menaquinone biosynthetic process;
SY   Menaquinone formation; Menaquinone synthesis; Vitamin K2 anabolism;
SY   Vitamin K2 biosynthesis; Vitamin K2 biosynthetic process;
SY   Vitamin K2 formation; Vitamin K2 synthesis.
GO   GO:0009234; menaquinone biosynthetic process
HI   Biological process: Menaquinone biosynthesis.
CA   Biological process.
//
ID   Mercuric resistance.
AC   KW-0475
DE   Protein that confers bacteria or other microorganisms the ability to
DE   withstand mercury salts.
SY   Mercuric cation resistance; Mercuric ion resistance;
SY   Resistance to mercury ion.
GO   GO:0046689; response to mercury ion
HI   Biological process: Mercuric resistance.
CA   Biological process.
//
ID   Mercury.
AC   KW-0476
DE   Protein which binds mercury and/or is involved in the cleavage of
DE   carbon-mercury bonds. Mercury is the only liquid metallic element,
DE   chemical symbol is Hg.
SY   Hg; Hg cation; Hg ion; Mercury cation; Mercury ion.
HI   Ligand: Mercury.
WW   https://www.webelements.com/mercury/
CA   Ligand.
//
ID   Merozoite.
AC   KW-0477
DE   Protein expressed in the merozoite stage of sporozoite parasites, an
DE   invasive stage in the life cycle produced by schizogony or asexual
DE   reproduction in which the nucleus of a cell undergoes division several
DE   times. This results in a multinucleate schizont which subsequently
DE   gives rise to a number of uninucleate cells called merozoites.
HI   Developmental stage: Merozoite.
CA   Developmental stage.
//
ID   Metachromatic leukodystrophy.
AC   KW-0478
DE   Protein which, if defective, causes metachromatic leukodystrophy, a
DE   disease characterized by intralysosomal or myelin membrane storage of
DE   cerebroside-3-sulfate. Whereas storage occurs in many cells, the
DE   disease almost exclusively affects oligodendrocytes. Patients suffer
DE   from a progressive demyelination, which causes a variety of
DE   neurological symptoms, including gait disturbances, ataxias, optical
DE   atrophy, dementia, seizures and spastic tetraparesis.
SY   Metachromatic leucodystrophy.
HI   Disease: Leukodystrophy; Metachromatic leukodystrophy.
CA   Disease.
//
ID   Metal-binding.
AC   KW-0479
DE   Protein which binds metals.
GO   GO:0046872; metal ion binding
HI   Ligand: Metal-binding.
CA   Ligand.
//
ID   Metal-thiolate cluster.
AC   KW-0480
DE   Protein which binds at least a cluster composed of metal coordinated
DE   via cysteinyl thiolate bridges to cysteine ligands.
GO   GO:0046872; metal ion binding
HI   Ligand: Metal-binding; Metal-thiolate cluster.
CA   Ligand.
//
ID   Metalloenzyme inhibitor.
AC   KW-0481
DE   Protein that inhibits metalloenzymes, enzymes which contains metal
DE   ions.
GO   GO:0004857; enzyme inhibitor activity
HI   Molecular function: Metalloenzyme inhibitor.
CA   Molecular function.
//
ID   Metalloprotease.
AC   KW-0482
DE   Proteolytic enzyme which use a metal for its catalytic mechanism. Most
DE   metalloproteases are zinc-dependent, some use cobalt.
SY   Metallopeptidase.
GO   GO:0008237; metallopeptidase activity
HI   Molecular function: Hydrolase; Protease; Metalloprotease.
CA   Molecular function.
//
ID   Metalloprotease inhibitor.
AC   KW-0483
DE   Protein that inhibits metalloproteases, which are peptide hydrolases
DE   that use a metal in the catalytic mechanism.
SY   Metallopeptidase inhibitor.
GO   GO:0008191; metalloendopeptidase inhibitor activity
HI   Molecular function: Metalloenzyme inhibitor; Metalloprotease inhibitor.
HI   Molecular function: Protease inhibitor; Metalloprotease inhibitor.
CA   Molecular function.
//
ID   Methanogenesis.
AC   KW-0484
DE   Protein involved in methanogenesis, the energy yielding formation of
DE   methane by methanogenic bacteria.
SY   Methane biosynthesis; Methane biosynthetic process; Methane synthesis.
GO   GO:0015948; methanogenesis
HI   Biological process: Methanogenesis.
CA   Biological process.
//
ID   Methanol utilization.
AC   KW-0485
DE   Protein involved in the utilization of methanol.
GO   GO:0015945; methanol metabolic process
HI   Biological process: Methanol utilization.
CA   Biological process.
//
ID   Methionine biosynthesis.
AC   KW-0486
DE   Protein involved in the synthesis of the hydrophobic amino acid
DE   methionine, an essential amino acid in human diets which contains a
DE   thioether linkage.
SY   Methionine anabolism; Methionine biosynthetic process;
SY   Methionine formation; Methionine synthesis.
GO   GO:0009086; methionine biosynthetic process
HI   Biological process: Amino-acid biosynthesis; Methionine biosynthesis.
CA   Biological process.
//
ID   Methotrexate resistance.
AC   KW-0487
DE   Protein that confers the ability to withstand methotrexate, an
DE   inhibitor of dehydrofolate reductase (DHFR). Methotrexate resistance
DE   occurs usually as a result of mutation or amplification of the DHFR
DE   gene.
SY   Resistance to methotrexate.
GO   GO:0031427; response to methotrexate
HI   Biological process: Methotrexate resistance.
CA   Biological process.
//
ID   Methylation.
AC   KW-0488
DE   Protein which is posttranslationally modified by the attachment of at
DE   least one methyl group.
SY   Methylated.
HI   PTM: Methylation.
CA   PTM.
//
ID   Methyltransferase.
AC   KW-0489
DE   Enzyme that transfers methyl groups from one compound to another.
GO   GO:0008168; methyltransferase activity
GO   GO:0032259; methylation
HI   Molecular function: Transferase; Methyltransferase.
CA   Molecular function.
//
ID   MHC I.
AC   KW-0490
DE   A heterodimeric membrane protein composed of two non-covalently linked
DE   polypeptide chains, a major histocompatibility complex (MHC)-encoded
DE   alpha chain and a non-MHC-encoded subunit B2M/beta2-microglobulin.
DE   Each MHC molecule consists of an extracellular peptide-binding cleft,
DE   followed by an immunoglobulin (Ig)-like domain and transmembrane and
DE   cytoplasmic domains. The amino-terminal alpha-1 and alpha-2 segments
DE   of the alpha chain form the peptide-binding cleft. Expressed on all
DE   nucleated cells, displays peptides derived from cytosolic proteins for
DE   recognition by CD8-positive T cells. By scanning MHC I molecules, CD8-
DE   positive T cells can detect infected or tumor cells and eliminate
DE   them.
GO   GO:0002474; antigen processing and presentation of peptide antigen via MHC class I
GO   GO:0042612; MHC class I protein complex
HI   Biological process: Immunity; MHC I.
HI   Cellular component: MHC I.
CA   Cellular component.
//
ID   MHC II.
AC   KW-0491
DE   A heterodimeric membrane protein composed of two non-covalently linked
DE   alpha and beta polypeptide chains, both major histocompatibility
DE   complex (MHC)-encoded. Each MHC molecule consists of an extracellular
DE   peptide-binding cleft followed by an immunoglobulin (Ig)-like domain
DE   and transmembrane and cytoplasmic domains. The amino-terminal alpha-1
DE   and beta-1 segments interact to form the peptide-binding cleft.
DE   Expressed on professional antigen presenting cells, displays peptides
DE   derived from endocytosed proteins for recognition by CD4-positive
DE   helper T cells. By scanning MHC II molecules, CD4-positive T cells
DE   activate effector mechanisms that eliminate extracellular microbes.
GO   GO:0002504; antigen processing and presentation of peptide or polysaccharide antigen via MHC class II
GO   GO:0042613; MHC class II protein complex
HI   Biological process: Immunity; Adaptive immunity; MHC II.
HI   Cellular component: MHC II.
CA   Cellular component.
//
ID   Microphthalmia.
AC   KW-1013
DE   Protein which, if defective, causes microphthalmia, a developmental
DE   anomaly in which the eyeballs are abnormally small. Disease severity
DE   ranges from moderate reduction of the size of a single eye to complete
DE   bilateral absence of ocular tissues. Microphthalmia can occur in
DE   isolation or as part of a syndrome.
SY   Microphthalmos.
HI   Disease: Microphthalmia.
CA   Disease.
//
ID   Microsome.
AC   KW-0492
DE   Protein found in microsomes, a heterogenous set of vesicles 20-200 nm
DE   in diameter and formed from the endoplasmic reticulum when cells are
DE   disrupted. The vesicles are isolated by differential centrifugation
DE   and are composed of three structural features: rough vesicles, smooth
DE   vesicles and ribosomes. Numerous enzyme activities are associated with
DE   the microsomal fraction.
GO   GO:0043231; intracellular membrane-bounded organelle
HI   Cellular component: Endoplasmic reticulum; Microsome.
CA   Cellular component.
//
ID   Microtubular inwards viral transport.
AC   KW-1177
DE   Viral protein that allows the active transport of complete particles
DE   and viral components along microtubules toward the intracellular
DE   replication sites during virus entry. This transport, which usually
DE   involves motor proteins like dynein or polymerization/depolymerization
DE   reactions as a driving force, is mostly used by viruses that replicate
DE   their genome near or in the nucleus. Neurotropic viruses for example,
DE   often enter neurons at the terminal axon and their viral genome must
DE   be moved retrogradely to cell bodies. Viruses such as adenovirus,
DE   Adeno-associated virus, rabies virus, canine parvovirus, vaccinia,
DE   foamy virus, human papillomavirus 16 and herpes virus utilize this
DE   type of intracellular transport.
GO   GO:0075521; microtubule-dependent intracellular transport of viral material towards nucleus
HI   Biological process: Host-virus interaction; Microtubular inwards viral transport.
HI   Biological process: Virus entry into host cell; Cytoplasmic inwards viral transport; Microtubular inwards viral transport.
CA   Biological process.
//
ID   Microtubular outwards viral transport.
AC   KW-1189
DE   Viral protein that allows the active transport of viral components and
DE   assembled, complete particles along microtubules toward the cell
DE   periphery during virus egress. This transport, which usually involves
DE   interaction with motor proteins like kinesin or
DE   polymerization/depolymerization reactions as a driving force, is
DE   mostly used by viruses that replicate their genome near or in the
DE   nucleus and allows newly assembled viral progeny to reach the plasma
DE   membrane. Herpes simplex virus for example is transported
DE   anterogradely along the axon.
GO   GO:0039701; microtubule-dependent intracellular transport of viral material towards cell periphery
HI   Biological process: Host-virus interaction; Microtubular outwards viral transport.
HI   Biological process: Viral release from host cell; Microtubular outwards viral transport.
CA   Biological process.
//
ID   Microtubule.
AC   KW-0493
DE   Protein associated with or component of the microtubule. The
DE   microtubule is formed by the arrangement of 13 parallel protofilaments
DE   arising from end-to-end aggregation of the tubulin alpha/beta-dimers.
DE   Microtubules are associated with various other proteins (MAPs, dynein,
DE   kinesin) and are involved in structures responsible for cellular
DE   movement such as flagella or cilia. Microtubules of the ciliary
DE   axoneme are more permanent than cytoplasmic and spindle microtubules.
DE   Microtubule formation is inhibited by agents such as colchicine,
DE   vinblastine or vincristine.
GO   GO:0005874; microtubule
HI   Cellular component: Microtubule.
CA   Cellular component.
//
ID   Milk protein.
AC   KW-0494
DE   Protein found in milk, a fluid secreted by female mammals to provide
DE   food for their offspring. It consists of water, proteins, soluble
DE   carbohydrates, electrolytes, lipids and vitamins.
HI   Molecular function: Milk protein.
CA   Molecular function.
//
ID   Mineral balance.
AC   KW-0495
DE   Protein that influences the equilibrium of minerals present in bone,
DE   e.g., fetuin.
SY   Regulation of bone mineralization.
GO   GO:0030500; regulation of bone mineralization
HI   Biological process: Mineral balance.
CA   Biological process.
//
ID   Mitochondrion.
AC   KW-0496
DE   Protein encoded by or localized in the mitochondrion, a
DE   semiautonomous, self-reproducing organelle that occurs in the
DE   cytoplasm of all cells of most, but not all, eukaryotes. Each
DE   mitochondrion is surrounded by a double limiting membrane. The inner
DE   membrane is highly invaginated, and its projections are called
DE   cristae. Mitochondria are the sites of the reactions of oxidative
DE   phosphorylation, which result in the formation of ATP. The size and
DE   coding capacity of the mitochondrial DNA varies considerably in
DE   different organisms, and encodes rRNAs, tRNAs and essential
DE   mitochondrial proteins.
GO   GO:0005739; mitochondrion
HI   Cellular component: Mitochondrion.
CA   Cellular component.
//
ID   Mitochondrion inner membrane.
AC   KW-0999
DE   Protein found in or associated with the inner membrane of a
DE   mitochondrion, the membrane which separates the mitochondrial matrix
DE   from the intermembrane space.
SY   Inner mitochondrial membrane; Mitochondrial inner membrane.
GO   GO:0005743; mitochondrial inner membrane
HI   Cellular component: Membrane; Mitochondrion inner membrane.
HI   Cellular component: Mitochondrion; Mitochondrion inner membrane.
CA   Cellular component.
//
ID   Mitochondrion nucleoid.
AC   KW-1135
DE   Protein found associated with the mitochondrial nucleoid, the
DE   mitochondrial pseudocompartment formed by the chromatin-dense area.
DE   This region, which is functionally equivalent to the eukaryotic
DE   nucleus, is not surrounded by a membrane.
SY   Mitochondrial nucleoid; Mitochromosome.
GO   GO:0042645; mitochondrial nucleoid
HI   Cellular component: Mitochondrion; Mitochondrion nucleoid.
CA   Cellular component.
//
ID   Mitochondrion outer membrane.
AC   KW-1000
DE   Protein found in or associated with the outer membrane of a
DE   mitochondrion, the mitochondrial membrane facing the cytoplasm.
SY   Mitochondrial outer membrane; Outer mitochondrial membrane.
GO   GO:0005741; mitochondrial outer membrane
HI   Cellular component: Membrane; Mitochondrion outer membrane.
HI   Cellular component: Mitochondrion; Mitochondrion outer membrane.
CA   Cellular component.
//
ID   Mitogen.
AC   KW-0497
DE   Protein which can induce mitosis of certain eukaryotic cells, i.e. it
DE   stimulates cellular proliferation.
GO   GO:0051781; positive regulation of cell division
HI   Molecular function: Mitogen.
CA   Molecular function.
//
ID   Mitosis.
AC   KW-0498
DE   Protein involved in mitosis, the nuclear division in eukaryotic cells
DE   involving the exact duplication and separation of the chromosome
DE   threads so that each daughter nucleus carries a chromosome complement
DE   identical to that of the parent nucleus. Mitosis is divided into four
DE   substages: prophase, metaphase, anaphase and telophase.
HI   Biological process: Cell cycle; Cell division; Mitosis.
CA   Biological process.
//
ID   Mitosome.
AC   KW-1025
DE   Protein localized in the mitosome, an organelle found in
DE   "amitochondrial" unicellular organisms which do not have the
DE   capability of gaining energy from oxidative phosphorylation. Mitosomes
DE   are almost certainly derived from mitochondria, they have a double
DE   membrane and most proteins are delivered to them by a targeting
DE   sequence. Unlike mitochondria, mitosomes do not contain any DNA. The
DE   mitosome functions in iron-sulphur cluster assembly.
GO   GO:0032047; mitosome
HI   Cellular component: Mitosome.
CA   Cellular component.
//
ID   Mobility protein.
AC   KW-0499
DE   Protein involved in the conjugative transfer of plasmid DNA. These
DE   proteins provide the function of nicking the DNA at a certain point,
DE   guiding the 5' end of the nicked strand into the recipient cell,
DE   recircularization, and perhaps the priming of complementary strand
DE   synthesis in the recipient.
HI   Biological process: Conjugation; Mobility protein.
HI   Molecular function: Mobility protein.
CA   Molecular function.
//
ID   Modulation of host cell apoptosis by virus.
AC   KW-1119
DE   Viral protein involved in the modulation of host cell apoptosis by
DE   acting different steps of the process. Several viruses encode proteins
DE   that inhibit apoptosis while other viruses use apoptosis to their
DE   advantage to suppress immune response or to disseminate.
GO   GO:0039526; perturbation by virus of host apoptosis
HI   Biological process: Host-virus interaction; Modulation of host cell apoptosis by virus.
CA   Biological process.
//
ID   Modulation of host cell cycle by viral cyclin-like protein.
AC   KW-1120
DE   Viral protein sharing sequence homology with cellular cyclins. Most
DE   viral cyclin homologues are closely related in sequence to the
DE   cellular D-type cyclins, which are implicated in regulating the
DE   transit of cells from G1 into S and are thought to operate via the
DE   inactivation of the retinoblastoma tumour suppressor protein.
GO   GO:0060153; perturbation by virus of host cell cycle progression
HI   Biological process: Host-virus interaction; Modulation of host cell cycle by virus; Modulation of host cell cycle by viral cyclin-like protein.
CA   Biological process.
//
ID   Modulation of host cell cycle by virus.
AC   KW-1121
DE   Viral protein involved in the modulation of host cell cycle. The cell
DE   cycle can be divided into four stages: G1, S, G2 and mitosis, while
DE   cells resting are termed quiescent cells (G0). Viruses have evolved
DE   strategies to modulate cell cycle progression including stimulation of
DE   S phase entry from G1 or G0 or cell cycle arrest at G2/M for example.
DE   This regulation allows viruses to maximize their own replication.
GO   GO:0060153; perturbation by virus of host cell cycle progression
HI   Biological process: Host-virus interaction; Modulation of host cell cycle by virus.
CA   Biological process.
//
ID   Modulation of host chromatin by virus.
AC   KW-1122
DE   Viral protein involved in the regulation of host chromatin structure.
DE   Chromatin has a major role in life cycle of many viruses, and a lot of
DE   them have evolved mechanisms to modulate chromatin-related processes.
DE   For example, histone acetyltransferases, histone deacetylases or
DE   histones are common targets of viruses.
GO   GO:0039525; modulation by virus of host chromatin organization
HI   Biological process: Host-virus interaction; Modulation of host chromatin by virus.
CA   Biological process.
//
ID   Modulation of host dendritic cell activity by virus.
AC   KW-1118
DE   Viral protein involved in the modulation of host dendritic cell
DE   activity. Dendritic cells operate at the interface between the innate
DE   and adaptive immune response by their ability to sample their
DE   environment for pathogenic products, to process them, and to present
DE   viral antigens to T-cells. This results in T cell proliferation and
DE   the induction of virus-specific adaptive immune responses. Therefore
DE   impairing dendritic cell function by viruses is an effective strategy
DE   to disrupt the host immune response.
GO   GO:0039673; evasion by virus of host dendritic cell activity
HI   Biological process: Host-virus interaction; Viral immunoevasion; Modulation of host dendritic cell activity by virus.
CA   Biological process.
//
ID   Modulation of host E3 ubiquitin ligases by virus.
AC   KW-1123
DE   Viral protein involved in the modulation of cellular E3 ubiquitin
DE   ligases. In general, viral proteins redirect cellular E3 ubiquitin
DE   ligases to select specific host proteins for proteasomal degradation.
DE   The aim of this subversion is the creation of a favorable environment
DE   for virus replication and dissemination.
GO   GO:0039648; modulation by symbiont of host protein ubiquitination
HI   Biological process: Host-virus interaction; Modulation of host ubiquitin pathway by virus; Modulation of host E3 ubiquitin ligases by virus.
CA   Biological process.
//
ID   Modulation of host immunity by viral IgG Fc receptor-like protein.
AC   KW-1124
DE   Viral protein acting as an IgG Fc receptors, able to bind IgG and
DE   inhibit host Fc-dependent immune activation. Fc receptors are proteins
DE   found at the surface of certain cells of the immune system including
DE   macrophages, monocytes, natural killer cells or B-cells. They allow
DE   these cells to bind to antibodies that are attached to the surface of
DE   infected cells or pathogens, helping these cells to identify and
DE   eliminate pathogens.
GO   GO:0075528; perturbation by virus of host immune response
HI   Biological process: Host-virus interaction; Viral immunoevasion; Modulation of host immunity by viral IgG Fc receptor-like protein.
CA   Biological process.
//
ID   Modulation of host NK-cell activity by virus.
AC   KW-1131
DE   Viral protein involved in the modulation of host NK-cell activity.
DE   Natural killer (NK) cells are critical in defense against viral
DE   infections, since they provide host protection by releasing cytokines
DE   such as IFN-gamma or by direct lysis of infected targets. Therefore,
DE   during viral infections, viruses and NK cells are in a constant battle
DE   and many viruses have developed a variety of strategies to modulate NK
DE   cell activity.
GO   GO:0039671; evasion by virus of host natural killer cell activity
HI   Biological process: Host-virus interaction; Viral immunoevasion; Modulation of host NK-cell activity by virus.
CA   Biological process.
//
ID   Modulation of host PP1 activity by virus.
AC   KW-1126
DE   Protein phosphatase-1 (PP1) is a member of the Serine/Threonine
DE   phosphatases. The enzyme regulates many important physiological
DE   processes, including gene transcription, translation, metabolism, cell
DE   growth and division. Different viruses including asfivirus, herpes
DE   simplex virus or papillomavirus interact with and modulate PPP1
DE   phosphatase activity to dephosphorylate specific cellular substrates
DE   including EIF2S1. Upon viral infection, the host PKR/EIF2AK2 triggers
DE   the phosphorylation of EIF2S1 leading to a complete translational
DE   shut-off. By dephosphroylating EIF2S1 with PPP1CA, viruses manage to
DE   circumvent this antiviral response and prevent translational shut-off.
GO   GO:0004865; protein serine/threonine phosphatase inhibitor activity
GO   GO:0039606; suppression by virus of host translation initiation
HI   Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; Interferon antiviral system evasion; Inhibition of host interferon signaling pathway by virus; Modulation of host PP1 activity by virus.
CA   Biological process.
//
ID   Modulation of host ubiquitin pathway by viral deubiquitinase.
AC   KW-1127
DE   Viral protein possessing deubiquitinating activity. Hijacking the
DE   ubiquitin system plays an essential role during viral replication.
DE   Therefore, several viruses including EBV or HCMV encode for proteins
DE   able to remove ubiquitin or ubiquitin-like proteins from their
DE   substrate.
GO   GO:0039648; modulation by symbiont of host protein ubiquitination
HI   Biological process: Host-virus interaction; Modulation of host ubiquitin pathway by virus; Modulation of host ubiquitin pathway by viral deubiquitinase.
CA   Biological process.
//
ID   Modulation of host ubiquitin pathway by viral E3 ligase.
AC   KW-1128
DE   Viral protein functioning as a cellular E3 ubiquitin ligase. These
DE   viral proteins usually target several host proteins for proteasomal
DE   degradation.
GO   GO:0039648; modulation by symbiont of host protein ubiquitination
HI   Biological process: Host-virus interaction; Modulation of host ubiquitin pathway by virus; Modulation of host ubiquitin pathway by viral E3 ligase.
CA   Biological process.
//
ID   Modulation of host ubiquitin pathway by viral ubl.
AC   KW-1129
DE   Viral protein sharing sequence similarity with host ubiquitin. Several
DE   of these homologues are present in large DNA viruses such as
DE   entomopoxvirus or canarypoxvirus and are thought to modulate host
DE   ubiquitin pathway.
GO   GO:0039648; modulation by symbiont of host protein ubiquitination
HI   Biological process: Host-virus interaction; Modulation of host ubiquitin pathway by virus; Modulation of host ubiquitin pathway by viral ubl.
CA   Biological process.
//
ID   Modulation of host ubiquitin pathway by virus.
AC   KW-1130
DE   Viral protein involved in the modulation of the host ubiquitin
DE   pathway. The ubiquitination pathway comprises E1, E2, and E3 ligases
DE   that conjugate ubiquitin to protein substrate. Usually, the host E3
DE   ligase determines the substrate specificity. Some viruses encode E3
DE   ligases that modulate the substrate specificity of host E3 ligases.
DE   Alternatively, some viruses encode deubiquitinases able to remove
DE   ubiquitin or ubiquitin-like proteins from their substrate.
GO   GO:0039648; modulation by symbiont of host protein ubiquitination
HI   Biological process: Host-virus interaction; Modulation of host ubiquitin pathway by virus.
CA   Biological process.
//
ID   Modulation of host virulence by virus.
AC   KW-1254
DE   Viral factor that modulates its bacterial host's virulence against a
DE   third organism. These virulence factors are mostly expressed from
DE   integrated viral genomes and have diverse functions. Bacterial host,
DE   and populations, and the encoding (pro)virus probably benefit from the
DE   expression of such factors. For example, Bor and Lom outer membrane
DE   proteins encoded by bacteriophage lambda modify the virulence of the
DE   host bacteria against a eukaryotic target. Some enteric
DE   bacterioviruses direct alterations in lipopolysaccharide biosynthesis,
DE   resulting in bacterial immune evasion of its eukaryotic target. Other
DE   prokaryotic viruses encode exotoxins changing their host bacteria into
DE   serious pathogens. A well-known bacterial exotoxin encoded by a
DE   provirus is the diphtheria toxin.
GO   GO:0098676; modulation of host virulence by virus
HI   Biological process: Virulence; Modulation of host virulence by virus.
CA   Biological process.
//
IC   Molecular function.
AC   KW-9992
DE   Keywords assigned to proteins due to their particular molecular
DE   function.
//
ID   Molybdenum.
AC   KW-0500
DE   Protein which binds molybdenum (or molybdopterin) or protein involved
DE   in the transport of molybdenum, a metallic element, chemical symbol
DE   Mo. It plays an essential role in the active site of all eukaryotic
DE   Mo-containing enzymes. In plants, Mo enzymes are important for nitrate
DE   assimilation, phytohormone synthesis, and purine catabolism. Mo is
DE   often coordinated to the sulfur atoms of a pterin derivative
DE   (molybdopterin [MPT]), thereby forming the active Molybdenum cofactor
DE   (Moco), which is highly conserved in eukaryotes, eubacteria, and
DE   archaebacteria.
SY   Mo; Mo cation; Mo ion; Molybdenum cation; Molybdenum ion.
HI   Ligand: Molybdenum.
WW   https://www.webelements.com/molybdenum/
CA   Ligand.
//
ID   Molybdenum cofactor biosynthesis.
AC   KW-0501
DE   Protein involved in the synthesis of the molybdenum cofactor (Moco), a
DE   molybdenum atom coordinated to the sulfur atoms of a pterin derivative
DE   (molybdopterin [MPT]). It is highly conserved in eukaryotes,
DE   eubacteria, and archaebacteria. In prokaryotes, two operons are
DE   directly associated with biosynthesis of the pterin moiety and its
DE   side chain while additional loci play a role in the acquisition of
DE   molybdenum and/or activation of the cofactor.
SY   Moco anabolism; Moco biosynthesis; Moco biosynthetic process;
SY   Moco formation; Moco synthesis; Molybdenum cofactor anabolism;
SY   Molybdenum cofactor biosynthetic process;
SY   Molybdenum cofactor formation; Molybdenum cofactor synthesis;
SY   Molybdopterin anabolism; Molybdopterin biosynthesis;
SY   Molybdopterin biosynthetic process; Molybdopterin formation;
SY   Molybdopterin synthesis.
GO   GO:0006777; Mo-molybdopterin cofactor biosynthetic process
HI   Biological process: Molybdenum cofactor biosynthesis.
CA   Biological process.
//
ID   Monoclonal antibody.
AC   KW-0502
DE   Antibody produced by a single clone of B cells and thus consisting of
DE   a population of identical antibody molecules all specicfic for a
DE   single antigenic determinant. They are produced from cultured
DE   hybridoma cell lines for research and commercial purposes.
GO   GO:0003823; antigen binding
HI   Molecular function: Monoclonal antibody.
CA   Molecular function.
//
ID   Monooxygenase.
AC   KW-0503
DE   Enzymes that reduce molecular oxygen by incorporating one oxygen atom
DE   into its substrate and the other one in water.
GO   GO:0004497; monooxygenase activity
HI   Molecular function: Oxidoreductase; Monooxygenase.
CA   Molecular function.
//
ID   Morphogen.
AC   KW-0504
DE   Diffusible protein that influence morphogenesis or embryonic
DE   development. These proteins carry information relating, for example,
DE   to a position in the embryo, and thus, determine the differentiation
DE   that cells perceiving this information will undergo. They are thought
DE   to act as a function of a threshold of their concentration.
GO   GO:0009653; anatomical structure morphogenesis
GO   GO:0016015; morphogen activity
HI   Molecular function: Morphogen.
CA   Molecular function.
//
ID   Motor protein.
AC   KW-0505
DE   Protein that walks or slides along microtubules or microfilaments
DE   using the energy provided by ATP or GTP hydrolysis, e.g. dyneins,
DE   myosins and kinesins. Or protein which mediates motility by other non
DE   enzymatic processes, e.g. prestin, a bidirectional voltage-to-force
DE   converter.
HI   Molecular function: Motor protein.
CA   Molecular function.
//
ID   mRNA capping.
AC   KW-0506
DE   Protein involved in the modification (capping) of the 5' end of
DE   eukaryotic mRNAs. This modification occurs after the beginning of
DE   transcription in the nucleus, and consists of adding a guanosine
DE   nucleotide to the 5'-end of mRNAs and then, methylating the guanosine.
DE   Capping protects mRNAs at their termini against attack by phosphatases
DE   and other nucleases and promotes mRNA function at the level of
DE   initiation of translation.
SY   Messenger RNA capping.
GO   GO:0006370; 7-methylguanosine mRNA capping
HI   Biological process: mRNA processing; mRNA capping.
CA   Biological process.
//
ID   mRNA processing.
AC   KW-0507
DE   Protein involved in the processing of the primary mRNA transcript to
DE   yield a functional mRNA. This includes 5' capping, 3' cleavage and
DE   polyadenylation, as well as mRNA splicing and RNA editing.
SY   Messenger RNA processing.
GO   GO:0006397; mRNA processing
HI   Biological process: mRNA processing.
CA   Biological process.
//
ID   mRNA splicing.
AC   KW-0508
DE   Protein involved in the process by which nonsense sequences or
DE   intervening sequences (introns) are removed from pre-mRNA to generate
DE   a functional mRNA (messenger RNA) that contains only exons.
SY   Messenger RNA splicing.
GO   GO:0008380; RNA splicing
HI   Biological process: mRNA processing; mRNA splicing.
CA   Biological process.
//
ID   mRNA transport.
AC   KW-0509
DE   Protein which is involved in the mechanism of export of mRNAs from the
DE   nucleus to the cytoplasm.
SY   Messenger RNA transport.
GO   GO:0051028; mRNA transport
HI   Biological process: Transport; mRNA transport.
CA   Biological process.
//
ID   Mucolipidosis.
AC   KW-0942
DE   Protein which, if defective, causes mucolipidosis, a group of
DE   inherited metabolic diseases characterised by the accumulation of
DE   excessive amounts of acid mucopolysaccharides, sphingolipids, and/or
DE   glycolipids in visceral and mesenchymal cells. Abnormal amounts of
DE   sphingolipids or glycolipids are present in neural tissue. Mental
DE   retardation and skeletal changes are common. All mucolipidosis are
DE   lysosomal disorders and are inherited in an autosomal recessive
DE   manner.
HI   Disease: Mucolipidosis.
CA   Disease.
//
ID   Mucopolysaccharidosis.
AC   KW-0510
DE   Protein which, if defective, causes mucopolysaccharidosis. These
DE   inherited diseases are characterized by excessive accumulation and
DE   secretion of oligomucopoloysaccharide due to the deficiency of enzymes
DE   involved in the degradation of glycosaminoglycans
DE   (mucopolysaccharides). They are progressive and often display a wide
DE   spectrum of clinical severity within one enzyme deficiency.
HI   Disease: Mucopolysaccharidosis.
CA   Disease.
//
ID   Multifunctional enzyme.
AC   KW-0511
DE   Protein that contains at least two distinct enzymatic activities and
DE   two distinct active sites.
GO   GO:0003824; catalytic activity
GO   GO:0008152; metabolic process
HI   Molecular function: Multifunctional enzyme.
CA   Molecular function.
//
ID   Muscle protein.
AC   KW-0514
DE   Characteristic protein of a muscle cell. The major ones are myosin and
DE   actin, which are responsible for the contraction and relaxation of
DE   muscles.
HI   Molecular function: Muscle protein.
CA   Molecular function.
//
ID   Mutator protein.
AC   KW-0515
DE   Protein which is encoded by a mutator gene (mutator). Generally, these
DE   are genes within which certain mutations cause an increase in
DE   frequency of spontaneous mutations in other genes. Mutator proteins
DE   are therefore thought to be responsible for inaccurate DNA
DE   replication.
HI   Molecular function: Mutator protein.
CA   Molecular function.
//
ID   Myofibrillar myopathy.
AC   KW-1060
DE   Protein which, if defective, causes myofibrillar myopathy, a group of
DE   morphologically homogeneous, but genetically heterogeneous
DE   neuromuscular disorders. The morphologic changes in skeletal muscle
DE   result from disintegration of the sarcomeric Z disc and the
DE   myofibrils, followed by abnormal ectopic accumulation of multiple
DE   proteins involved in the structure of the Z disc. Clinical
DE   manifestations are variable and can involve the skeletal, cardiac and
DE   smooth muscle.
HI   Disease: Myofibrillar myopathy.
CA   Disease.
//
ID   Myogenesis.
AC   KW-0517
DE   Protein involved in the differentiation and development of the muscle.
DE   Myogenesis is controlled by myogenic factors, a family of muscle-
DE   specific transcription factors that contain a conserved helix-loop-
DE   helix domain which is homologous to the myc family of proteins.
SY   Muscle development; Muscle formation.
GO   GO:0007517; muscle organ development
HI   Biological process: Myogenesis.
CA   Biological process.
//
ID   Myosin.
AC   KW-0518
DE   A motor protein which uses the energy provided by the hydrolysis of
DE   ATP to drive movements along actin filaments. Different types of
DE   myosin are found in eukaryotic cells.
GO   GO:0016459; myosin complex
HI   Molecular function: Motor protein; Myosin.
CA   Molecular function.
//
ID   Myotoxin.
AC   KW-0959
DE   Protein which causes muscle necrosis. Myotoxins are principally found
DE   in snake venoms. The myotoxic activity can be monitored by
DE   morphological analysis and by the increase of plasma creatine kinase
DE   (CK) activity. The increase in plasma CK levels results from
DE   sarcolemmal damage due to myotoxic components of the venom.
HI   Molecular function: Toxin; Myotoxin.
CA   Molecular function.
//
ID   Myristate.
AC   KW-0519
DE   Protein which is posttranslationally modified by the attachment of at
DE   least one myristate group. The myristate (14-carbon saturated fatty
DE   acid) group is attached through an amide bond to the N-terminal
DE   glycine residue of the mature form of a protein or to an internal
DE   lysine residue. Myristoylproteins may be cytoplasmic or membrane-
DE   associated.
SY   Myristylated; n-tetradecanoate.
HI   PTM: Lipoprotein; Myristate.
CA   PTM.
//
ID   NAD.
AC   KW-0520
DE   Enzymes which use NAD(H) as an electron acceptor or as a cofactor.
DE   Nicotinamide adenine dinucleotide, an important redox coenzyme that
DE   participates in a variety of enzymatic reactions in which it serves as
DE   an electron carrier by being alternately oxidized (NAD+) and reduced
DE   (NADH). NAD also functions as an ADP-ribose donor in ADP-ribosylation
DE   reactions.
SY   Nicotinamide adenine dinucleotide; Nicotinic adenine dinucleotide.
HI   Ligand: NAD.
CA   Ligand.
//
ID   NADP.
AC   KW-0521
DE   Enzymes which use NADP(H) as an electron acceptor or as a cofactor.
DE   Nicotinamide adenine dinucleotide phosphate, a redox coenzyme that
DE   participates in a variety of enzymatic reactions in which it serves as
DE   an electron carrier by being alternately oxidized (NADP+) and reduced
DE   (NADPH). Analogue of NAD, but NADPH is used extensively in
DE   biosynthetic, rather than catabolic pathways as well as in
DE   photosynthesis.
SY   Nicotinamide adenine dinucleotide phosphate;
SY   Nicotinic adenine dinucleotide phosphate.
HI   Ligand: NADP.
CA   Ligand.
//
ID   Necrosis.
AC   KW-1210
DE   Protein involved in necrotic programmed cell death. Necrosis is a form
DE   of traumatic cell death that results from acute cellular injury due
DE   infection, toxins, trauma, etc. Necrosis is characterized by blebbing,
DE   mitochondrial fission, loss of cell membrane integrity and an
DE   uncontrolled release of products of cell death into the intracellular
DE   space. This initiates an inflammatory response in the surrounding
DE   tissue often resulting is a build-up of dead tissue and cell debris
DE   at, or near, the site of the cell death.
SY   Necroptosis; Necrotic cell death; Necrotic programmed cell death.
GO   GO:0012501; programmed cell death
HI   Biological process: Necrosis.
CA   Biological process.
//
ID   Nemaline myopathy.
AC   KW-1057
DE   Protein which, if defective, causes nemaline myopathy, a hereditary
DE   neuromuscular disorder characterized by generally non-progressive
DE   muscle weakness of varying severity, and abnormal thread- or rod-like
DE   structures in muscle fibers on histologic examination. The age of
DE   onset varies from birth to adulthood. The main clinical manifestations
DE   include weakness (usually most severe in the face, the neck flexors,
DE   and the proximal limb muscles), hypotonia, and depressed or absent
DE   deep tendon reflexes. Nemaline myopathy is divided into several broad
DE   groups classified by onset and severity of motor and respiratory
DE   involvement.
SY   NEM; NM; Rod body myopathy; Rod myopathy.
HI   Disease: Nemaline myopathy.
CA   Disease.
//
ID   Nematocyst.
AC   KW-0166
DE   Protein localized in the nematocyst, an organelle found in nematoblast
DE   (cnidoblast) cells. When matured, these stinging organelles store
DE   toxins and can deliver them when the cnidocil (a short extension of
DE   the nematocyst) is stimulated by a prey or another stimulus. These
DE   proteins are principally found in anemones and jellyfishes.
SY   Cnidocyst.
GO   GO:0042151; nematocyst
HI   Cellular component: Nematocyst.
CA   Cellular component.
//
ID   Nephronophthisis.
AC   KW-0983
DE   Protein which, if defective, causes nephronophthisis, a chronic
DE   tubulo-interstitial nephritis that progresses to end-stage renal
DE   failure. Clinical features include anemia, polyuria, polydipsia,
DE   isosthenuria, and death in uremia. Some children present with
DE   extrarenal symptoms such as tapeto-retinal degeneration, mental
DE   retardation, cerebellar ataxia, bone anomalies or liver involvement.
SY   NPHP.
HI   Disease: Nephronophthisis.
CA   Disease.
//
ID   Neurodegeneration.
AC   KW-0523
DE   Protein which, if defective, causes neurodegeneration.
HI   Disease: Neurodegeneration.
CA   Disease.
//
ID   Neurogenesis.
AC   KW-0524
DE   Protein involved in neurogenesis, which involves the differentiation
DE   and development of the nervous system.
SY   Nervous system development; Nervous system formation.
GO   GO:0007399; nervous system development
HI   Biological process: Neurogenesis.
CA   Biological process.
//
ID   Neuronal ceroid lipofuscinosis.
AC   KW-0525
DE   Protein which, if defective, causes neuronal ceroid lipofuscinosis, a
DE   group of neurodegenerative, lysosome storage disorders characterized
DE   by intracellular accumulation of autofluorescent wax-like lipid
DE   materials in brain and other tissues. Neuronal ceroid lipofuscinoses
DE   are associated with variable yet progressive symptoms including
DE   seizures, dementia, visual loss, and/or cerebral atrophy.
SY   CLN; NCL.
HI   Disease: Neurodegeneration; Neuronal ceroid lipofuscinosis.
CA   Disease.
//
ID   Neuropathy.
AC   KW-0622
DE   Protein which, if defective, causes neuropathy, a functional
DE   disturbance or pathological change in the peripheral nervous system,
DE   sometimes limited to non-inflammatory lesions as opposed to those of
DE   neuritis. Neuropathies affecting a specific nerve may be named for the
DE   nerve. The terms mononeuropathy and polyneuropathy may be used to
DE   denote whether one or several nerves are involved.
HI   Disease: Neuropathy.
CA   Disease.
//
ID   Neuropeptide.
AC   KW-0527
DE   Peptides released by neurons as intercellular messengers. Many
DE   neuropeptides are also hormones released by non-neuronal cells. They
DE   have direct synaptic effects (peptide neurotransmitters) or indirect
DE   modulatory effects on the nervous system (peptide neuromodulators).
GO   GO:0007218; neuropeptide signaling pathway
HI   Molecular function: Neuropeptide.
CA   Molecular function.
//
ID   Neurotoxin.
AC   KW-0528
DE   Proteins, often exquisitely toxic, that inhibit neuronal function.
DE   Neurotoxins act typically against sodium channels or block or enhance
DE   synaptic transmission. Most venoms contain neurotoxic substances.
HI   Molecular function: Toxin; Neurotoxin.
CA   Molecular function.
//
ID   Neurotransmitter.
AC   KW-0529
DE   Protein, released by the axon terminal in response to an electrical
DE   impulse, which travels across the synapse to either excite or inhibit
DE   the target cell.
GO   GO:0007268; chemical synaptic transmission
HI   Molecular function: Neurotransmitter.
CA   Molecular function.
//
ID   Neurotransmitter biosynthesis.
AC   KW-0530
DE   Protein involved in the synthesis of neurotransmitters. The proteins
DE   are released by the axon terminal in response to an electrical impulse
DE   and travel across the synapse to either excite or inhibit the target
DE   cell.
SY   Neurotransmitter anabolism; Neurotransmitter biosynthetic process;
SY   Neurotransmitter formation; Neurotransmitter synthesis.
HI   Biological process: Neurotransmitter biosynthesis.
CA   Biological process.
//
ID   Neurotransmitter degradation.
AC   KW-0531
DE   Protein involved in the breakdown of neurotransmitters. The proteins
DE   are released by the axon terminal in response to an electrical impulse
DE   and travel across the synapse to either excite or inhibit the target
DE   cell.
SY   Neurotransmitter breakdown; Neurotransmitter catabolic process;
SY   Neurotransmitter catabolism.
HI   Biological process: Neurotransmitter degradation.
CA   Biological process.
//
ID   Neurotransmitter transport.
AC   KW-0532
DE   Protein involved in the transport of neurotransmitters. The proteins
DE   are released by the axon terminal in response to an electrical impulse
DE   and travel across the synapse to either excite or inhibit the target
DE   cell.
GO   GO:0006836; neurotransmitter transport
HI   Biological process: Transport; Neurotransmitter transport.
CA   Biological process.
//
ID   Nickel.
AC   KW-0533
DE   Protein which binds at least one nickel atom, or protein whose
DE   function is nickel-dependent. Nickel is a metal, chemical symbol Ni.
SY   Ni; Ni cation; Nickel cation; Nickel ion; Ni ion.
HI   Ligand: Nickel.
WW   https://www.webelements.com/nickel/
CA   Ligand.
//
ID   Nickel insertion.
AC   KW-0996
DE   Protein which is involved in the creation and/or insertion of a nickel
DE   metallocenter into another protein, without necessarily binding the
DE   metal itself.
SY   Ni insertion.
HI   Biological process: Nickel insertion.
CA   Biological process.
//
ID   Nickel transport.
AC   KW-0921
DE   Protein involved in the transport of nickel.
SY   Nickel cation transport; Nickel ion transport; Ni transport.
GO   GO:0015675; nickel cation transport
HI   Biological process: Transport; Ion transport; Nickel transport.
HI   Ligand: Nickel; Nickel transport.
CA   Biological process.
//
ID   Niemann-Pick disease.
AC   KW-1054
DE   Protein which, if defective, causes Niemann-Pick disease. Niemann-Pick
DE   disease comprises an inherited group of congenital lipidoses in which
DE   sphingolipids accumulate in cells, especially in the
DE   reticuloendothelial system, due to defective lysosomal storage. The
DE   disease is clinically characterized by progressive degeneration of the
DE   central nervous system with visceral accumulation of cholesterol and
DE   sphingomyelin. The clinical phenotype is highly variable and different
DE   types are distinguished by age of onset, degree of central nervous
DE   system involvement and by the amount of sphingomyelin
DE   phosphodiesterase activity.
SY   Niemann's disease; NPD.
HI   Disease: Niemann-Pick disease.
CA   Disease.
//
ID   Nitrate assimilation.
AC   KW-0534
DE   Protein involved in the uptake, from the environment, of nitrates,
DE   inorganic or organic salts and esters of nitric acid. This includes
DE   the uptake and transport into cells by nitrate transporters, with the
DE   sequential reduction to nitrite and ammonium, catalyzed by the enzymes
DE   nitrate reductase and nitrite reductase, respectively.
GO   GO:0042128; nitrate assimilation
HI   Biological process: Nitrate assimilation.
CA   Biological process.
//
ID   Nitration.
AC   KW-0944
DE   Protein which is posttranslationally modified by replacement of a
DE   hydrogen on an aromatic ring of one or more tyrosine or tryptophan
DE   residues by a nitro (NO2) group.
SY   Nitrated.
HI   PTM: Nitration.
CA   PTM.
//
ID   Nitrogen fixation.
AC   KW-0535
DE   Protein involved in nitrogen fixation, the reduction of gaseous
DE   nitrogen to ammonia. This process is carried out only by prokaryotes
DE   who are either free-living or form symbiotic associations with plants
DE   or other organisms (e.g. termites, protozoa).
GO   GO:0009399; nitrogen fixation
HI   Biological process: Nitrogen fixation.
CA   Biological process.
//
ID   Nodulation.
AC   KW-0536
DE   Protein involved in nodulation, the formation of nitrogen-fixing
DE   nodules on roots of both leguminous plants and the Parasponia genus.
GO   GO:0009877; nodulation
HI   Biological process: Nodulation.
CA   Biological process.
//
ID   Non-syndromic deafness.
AC   KW-1010
DE   Protein which, if defective, causes inability to hear in the absence
DE   of other clinical signs and symptoms. Most forms of non-syndromic
DE   deafness are associated with permanent hearing loss caused by damage
DE   to structures in the inner ear.
SY   Isolated deafness.
HI   Disease: Deafness; Non-syndromic deafness.
CA   Disease.
//
ID   Nonsense-mediated mRNA decay.
AC   KW-0866
DE   Protein involved in nonsense-mediated messenger RNA (mRNA) decay, a
DE   critical process of selective degradation of mRNAs that contain
DE   premature stop codons.
SY   NMD.
GO   GO:0000184; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay
HI   Biological process: Nonsense-mediated mRNA decay.
CA   Biological process.
//
ID   Notch signaling pathway.
AC   KW-0914
DE   Protein involved in the Notch signaling, a signaling pathway involved
DE   in cell-cell communications that regulates a broad spectrum of cell-
DE   fate determinations. Notch proteins are transmembrane receptors, which
DE   are cleaved by the gamma-secretase complex upon activation and
DE   released from the cell membrane and turn into transcriptional
DE   activators after their association with SU(H) proteins.
GO   GO:0007219; Notch signaling pathway
HI   Biological process: Notch signaling pathway.
CA   Biological process.
//
ID   Nuclear pore complex.
AC   KW-0906
DE   Protein associated predominantly with the nuclear pore complex (NPC).
DE   NPCs constitute the exclusive means of nucleocytoplasmic transport in
DE   eukaryotes during interphase. NPCs allow the passive diffusion of ions
DE   and small molecules (up to about 20 kDa or 5 nm) and the active,
DE   nuclear transport receptor (karyopherin: importin and exportin)-
DE   mediated bidirectional transport of macromolecules such as proteins,
DE   RNAs, ribonucleoprotein (RNPs), and ribosomal subunits (up to about 10
DE   MDa) across the double-membrane nuclear envelope. NPC components,
DE   collectively referred to as nucleoporins (NUPs), can play the role of
DE   both NPC structural components and of docking or interaction partners
DE   for transiently associated nuclear transport factors. The NPC is
DE   composed of at least 30 distinct subunits, shows 8-fold rotational
DE   symmetry with specialized structures on the cyto- and nucleoplasmic
DE   side and in the nuclear envelope embedded core. The MW varies from
DE   about 44-60 MDa in S. cerevisiae to 60-120 MDa in vertebrates, yet the
DE   overall architecture is conserved.
SY   NPC; Nuclear pore.
GO   GO:0005643; nuclear pore
HI   Biological process: Transport; mRNA transport; Nuclear pore complex.
HI   Cellular component: Nucleus; Nuclear pore complex.
HI   Biological process: Transport; Protein transport; Translocation; Nuclear pore complex.
WW   http://npd.hgu.mrc.ac.uk/user/compartment?page=nuc_pore
CA   Cellular component.
//
ID   Nuclease.
AC   KW-0540
DE   Enzyme that degrades nucleic acids into shorter oligonucleotides or
DE   single nucleotide subunits by hydrolyzing sugar-phosphate bonds in the
DE   nucleic acid backbone.
GO   GO:0004518; nuclease activity
HI   Molecular function: Hydrolase; Nuclease.
CA   Molecular function.
//
ID   Nucleomorph.
AC   KW-0542
DE   Protein associated with the nucleomorph. A nucleomorph is a remnant
DE   nucleus found between the outer two and inner two membranes of the
DE   plastid in cryptomonads and chlorarachniophyte algae.
GO   GO:0033009; nucleomorph
HI   Cellular component: Nucleomorph.
CA   Cellular component.
//
ID   Nucleosome core.
AC   KW-0544
DE   Protein characteristic of the nucleosome, a repeating structural unit
DE   in chromatin that packages DNA to give the chromatin a 'beads-on-a-
DE   string' appearance. Each repeat consists of approximately 146 base
DE   pairs of DNA wound around a disk-shaped protein core which is composed
DE   of two of each of the nucleosomal histones H2A, H2B, H3 and H4.
GO   GO:0000786; nucleosome
HI   Cellular component: Chromosome; Nucleosome core.
HI   Molecular function: DNA-binding; Nucleosome core.
CA   Cellular component.
//
ID   Nucleotide biosynthesis.
AC   KW-0545
DE   Protein involved in the synthesis of a nucleotide, a phosphate ester
DE   of a nucleoside consisting of a purine or pyrimidine base linked to
DE   ribose or deoxyribose phosphates.
SY   Nucleotide anabolism; Nucleotide biosynthetic process;
SY   Nucleotide formation; Nucleotide synthesis.
GO   GO:0009165; nucleotide biosynthetic process
HI   Biological process: Nucleotide biosynthesis.
CA   Biological process.
//
ID   Nucleotide metabolism.
AC   KW-0546
DE   Protein involved in the biochemical reactions of nucleotides.
DE   Nucleotides are phosphate esters of a nucleoside consisting of a
DE   purine or pyrimidine base linked to ribose or deoxyribose phosphates.
SY   Nucleotide metabolic process.
GO   GO:0009117; nucleotide metabolic process
HI   Biological process: Nucleotide metabolism.
CA   Biological process.
//
ID   Nucleotide-binding.
AC   KW-0547
DE   Protein which binds a nucleotide, a phosphate ester of a nucleoside
DE   consisting of a purine or pyrimidine base linked to ribose or
DE   deoxyribose phosphates.
GO   GO:0000166; nucleotide binding
HI   Ligand: Nucleotide-binding.
CA   Ligand.
//
ID   Nucleotidyltransferase.
AC   KW-0548
DE   Enzyme which transfers a nucleotide from one compound to another.
GO   GO:0016779; nucleotidyltransferase activity
HI   Molecular function: Transferase; Nucleotidyltransferase.
CA   Molecular function.
//
ID   Nucleus.
AC   KW-0539
DE   Protein located in the nucleus of a cell.
GO   GO:0005634; nucleus
HI   Cellular component: Nucleus.
CA   Cellular component.
//
ID   Nylon degradation.
AC   KW-0549
DE   Protein involved in the degradation of nylon, a polymer whose main
DE   chain comprises recurrent amide groups. These compounds are generally
DE   formed from combinations of diamines, diacids and amino acids.
SY   Nylon breakdown; Nylon catabolic process; Nylon catabolism.
GO   GO:0019876; nylon catabolic process
HI   Biological process: Nylon degradation.
CA   Biological process.
//
ID   Obesity.
AC   KW-0550
DE   Protein which, if defective, causes obesity, a disorder characterized
DE   by excessive deposition of fat.
HI   Disease: Obesity.
CA   Disease.
//
ID   Olfaction.
AC   KW-0552
DE   Protein involved in olfaction, the process of smelling.
GO   GO:0007608; sensory perception of smell
HI   Biological process: Sensory transduction; Olfaction.
CA   Biological process.
//
ID   Oncogene.
AC   KW-0553
DE   Protein encoded by an oncogene, which promotes cell transformation.
DE   Examples include viral homologs of cellular proto-oncogenes such as
DE   the transcription factors v-myc and v-jun, the growth factor v-fgr,
DE   the regulatory GTPase v-ras, and papillomavirus protein E6.
SY   Oncoprotein.
HI   Disease: Oncogene.
CA   Disease.
//
ID   One-carbon metabolism.
AC   KW-0554
DE   Protein involved in the biochemical reactions with one-carbon groups,
DE   e.g., methyl and formyl groups.
SY   One-carbon compound metabolic process.
GO   GO:0006730; one-carbon metabolic process
HI   Biological process: One-carbon metabolism.
CA   Biological process.
//
ID   Oogenesis.
AC   KW-0896
DE   Protein involved in egg development and maturation. A process whereby
DE   primordial germ cells form mature ova.
GO   GO:0048477; oogenesis
HI   Biological process: Differentiation; Oogenesis.
CA   Biological process.
//
ID   Opioid peptide.
AC   KW-0555
DE   Endogenous peptides with opiate-like activity.
GO   GO:0001515; opioid peptide activity
HI   Molecular function: Opioid peptide.
CA   Molecular function.
//
ID   Organellar chromatophore.
AC   KW-0994
DE   Protein encoded by the organellar chromatophore genome or a protein
DE   targeted to the organellar chromatophore. The organellar chromatophore
DE   is the photosynthetic inclusion found in Paulinella species, which are
DE   photosynthetic thecate amoeba. It probably derives from a different
DE   endosymbiotic event than that which led to all other plastids. Houses
DE   the machinery necessary for photosynthesis and CO(2) fixation; it also
DE   has the genetic capacity to synthesize some amino acids, some fatty
DE   acids and a few cofactors. It contains thylakoid membranes, and a
DE   residual peptidoglycan wall between the 2 envelope membranes. There
DE   are 1 or 2 chromatophores per cell.
GO   GO:0070111; organellar chromatophore
HI   Cellular component: Plastid; Organellar chromatophore.
CA   Cellular component.
//
ID   Organic radical.
AC   KW-0556
DE   Protein which is posttranslationally modified by the formation of a
DE   stable radical. E.g., P09373 is posttranslationally interconverted,
DE   under anaerobic conditions, from an inactive to an active form that
DE   carries a stable radical localized to a specific glycine at the C-
DE   terminal region of the polypeptidic chain.
HI   PTM: Organic radical.
CA   PTM.
//
ID   Osteogenesis.
AC   KW-0892
DE   Protein involved in osteogenesis, the mechanism of bone formation
DE   wether intramembranous or endochondral. In intramembranous
DE   ossification, bone is formed by differentiation of mesenchymal cells
DE   into osteoblasts with absence of a cartilaginous model. The flat bones
DE   of the skull, the sternum, and the scapula are examples of bones that
DE   develop by intramembranous ossification. The term endochondral refers
DE   to the close association of the developing bone with the pre-existing
DE   hyaline cartilage model of that bone. The long bones of the limbs
DE   (including the phalanges) and the ribs develop by endochondral
DE   ossification.
SY   Bone formation; Ossification.
GO   GO:0001503; ossification
HI   Biological process: Osteogenesis.
CA   Biological process.
//
ID   Osteogenesis imperfecta.
AC   KW-1065
DE   Protein which, if defective, causes osteogenesis imperfecta, a bone
DE   disorder characterized by low bone mass, and brittle, osteoporotic and
DE   easily fractured bones. It may also present with blue sclerae, loose
DE   joints, and imperfect dentin formation.
SY   Brittle bone disease; Fragilitas ostium; Glass bone disease;
SY   Lobstein's disease; Lobstein disease.
HI   Disease: Osteogenesis imperfecta.
CA   Disease.
//
ID   Osteopetrosis.
AC   KW-0987
DE   Protein which, if defective, causes osteopetrosis, an hereditary
DE   disorder characterized by abnormally dense bone due to reduced bone
DE   resorption, and by the common occurrence of fractures of affected
DE   bones.
HI   Disease: Osteopetrosis.
CA   Disease.
//
ID   Outer capsid protein.
AC   KW-1152
DE   Viral protein that is a component of the outer layer of a double or
DE   triple concentric icosahedral capsid. Outer capsids are part of
DE   reoviridae and cystoviridae virions.
GO   GO:0039624; viral outer capsid
HI   Cellular component: Virion; Capsid protein; Outer capsid protein.
CA   Cellular component.
//
ID   Oxidation.
AC   KW-0558
DE   Protein which is posttranslationally modified by oxidation of a
DE   residue.
HI   PTM: Oxidation.
CA   PTM.
//
ID   Oxidoreductase.
AC   KW-0560
DE   Enzyme that catalyzes the oxidation of one compound with the reduction
DE   of another.
GO   GO:0016491; oxidoreductase activity
HI   Molecular function: Oxidoreductase.
CA   Molecular function.
//
ID   Oxygen transport.
AC   KW-0561
DE   Protein involved in the transport of oxygen (e.g. hemoglobin and
DE   myoglobin).
GO   GO:0005344; oxygen carrier activity
GO   GO:0015671; oxygen transport
HI   Biological process: Transport; Oxygen transport.
CA   Biological process.
//
ID   Oxylipin biosynthesis.
AC   KW-0925
DE   Protein involved in the synthesis of oxygenated fatty acids
DE   (oxylipins), including jasmonic acid (jasmonate) (JA) and its
DE   derivatives. Oxylipins regulate many defense and developmental
DE   pathways in plants. JA is involved in wound-mediated signaling
DE   pathways, plant defense, and reproductive development. It acts as a
DE   growth inhibitor and promotes senescence.
SY   Oxylipin anabolism; Oxylipin biosynthetic process; Oxylipin formation;
SY   Oxylipin synthesis.
GO   GO:0031408; oxylipin biosynthetic process
HI   Biological process: Lipid metabolism; Fatty acid metabolism; Fatty acid biosynthesis; Oxylipin biosynthesis.
HI   Biological process: Lipid metabolism; Lipid biosynthesis; Fatty acid biosynthesis; Oxylipin biosynthesis.
CA   Biological process.
//
ID   Pair-rule protein.
AC   KW-0562
DE   A protein encoded by a pair-rule gene. These are developmental genes
DE   in Drosophila involved in delimiting segments in the early embryos.
DE   Mutations in pair rule genes affect every alternate segment.
GO   GO:0007275; multicellular organism development
GO   GO:0007366; periodic partitioning by pair rule gene
HI   Molecular function: Developmental protein; Pair-rule protein.
CA   Molecular function.
//
ID   Paired box.
AC   KW-0563
DE   Protein which contains a paired box domain, a conserved domain of
DE   about 120 amino acids, which is generally located in the N-terminal
DE   section of various proteins.
HI   Domain: Paired box.
CA   Domain.
//
ID   Palmitate.
AC   KW-0564
DE   Protein which is posttranslationally modified by the attachment of at
DE   least one palmitate group. The palmitate (16-carbon saturated fatty
DE   acid) group is usually attached to cysteine via a thioester bond.
DE   Lysine, serine and threonine may also serve as palmitate acceptors.
DE   Many palmitoylproteins are membrane associated either directly through
DE   the palmitate moiety or as transmembrane proteins anchored by the
DE   fatty acid. However, a few are actually secreted from cells.
SY   n-hexadecanoate; Palmitoylated.
HI   PTM: Lipoprotein; Palmitate.
CA   PTM.
//
ID   Palmoplantar keratoderma.
AC   KW-1007
DE   Protein which, if defective, causes hereditary palmoplantar
DE   keratoderma (PPK), a genetically and clinically diverse group of
DE   cutaneous disorders characterized by abnormal thickening of the skin
DE   on the palms and soles. It results from excessive keratin formation
DE   leading to hypertrophy of the stratum corneum (hyperkeratosis). PPKs
DE   are distinguished from each other on the basis of mode of inheritance,
DE   presence of transgrediens (defined as contiguous extension of
DE   hyperkeratosis beyond the palmar and/or plantar skin), association
DE   with other skin findings and/or abnormalities of other organs, and
DE   extent of epidermal involvement (diffuse, focal, punctate). Diffuse
DE   PPK is characterized by uniform involvement of the palmoplantar
DE   surface; focal PPK consists of localized areas of hyperkeratosis
DE   located mainly on pressure points and sites of recurrent friction;
DE   punctate PPK shows multiple small, hyperkeratotic papules or nodules
DE   on the palms and soles.
SY   Hyperkeratosis palmaris et plantaris;
SY   Keratoderma palmaris et plantaris; Keratosis palmoplantaris;
SY   Palmoplantar keratosis; PPK.
HI   Disease: Palmoplantar keratoderma.
CA   Disease.
//
ID   Pantothenate biosynthesis.
AC   KW-0566
DE   Protein involved in the synthesis of pantothenate.
SY   Pantothenate anabolism; Pantothenate biosynthetic process;
SY   Pantothenate formation; Pantothenate synthesis.
GO   GO:0015940; pantothenate biosynthetic process
HI   Biological process: Pantothenate biosynthesis.
CA   Biological process.
//
ID   Parkinson disease.
AC   KW-0907
DE   Protein which, if defective, causes classic Parkinson disease.
DE   Parkinson disease is a complex multifactorial neurodegenerative
DE   disorder, usually occurring in late life, although an early onset and
DE   a juvenile form are known. Typical features are masklike facies,
DE   tremor of resting muscles, a slowing of voluntary movements
DE   (bradykinesia), festinating gait and postural instability. The signs
DE   and symptoms of the disease are the consequence of a striatal
DE   deficiency of dopamine, resulting from neuronal death in the
DE   substantia nigra. Parkinson disease is characterized by the presence
DE   of Lewy bodies, intraneuronal inclusions found in many brain regions
DE   which are not entirely specific to, but are a highly sensitive marker
DE   for, Parkinson disease.
SY   Paralysis agitans; Parkinson's disease; PD.
HI   Disease: Parkinson disease.
CA   Disease.
//
ID   Parkinsonism.
AC   KW-0908
DE   Protein which, if defective, causes parkinsonism. Parkinsonism refers
DE   to disorders, both genetic and non-genetic, characterized by four
DE   primary parkinsonian symptoms: tremor, rigidity, postural instability
DE   and bradykinesia, resulting from the loss or dysfunction of dopamine-
DE   producing neurons in the substantia nigra. Lewy bodies, intraneuronal
DE   accumulations of aggregated proteins, may or may not be present in the
DE   brain of the patients.
HI   Disease: Parkinsonism.
CA   Disease.
//
ID   Pathogenesis-related protein.
AC   KW-0568
DE   Protein induced in several plant species when they are infected by
DE   viruses, viroids, fungi or bacteria. The occurrence of these proteins
DE   is not pathogen-specific, but determined by the type of reaction of
DE   the host plant. They form a protective barrier against pathogens by
DE   collecting at infection sites and act to decrease susceptibility of
DE   plants. They may have anti-fungal or anti-bacterial activity.
SY   PR protein.
GO   GO:0009607; response to biotic stimulus
HI   Biological process: Plant defense; Pathogenesis-related protein.
HI   Molecular function: Pathogenesis-related protein.
CA   Molecular function.
//
ID   Pentose shunt.
AC   KW-0570
DE   Protein involved in the pentose shunt, the biochemical pathway in
DE   which glucose-6-phosphate is oxidized to 6-phosphogluconate with the
DE   production of NADPH. Then 6-phosphogluconate is converted to ribulose-
DE   5-phosphate and CO2 and a second molecule of NADH. This pathway is an
DE   important source of NADPH and ribose-5-phosphate.
SY   Hexose monophosphate pathway; Pentose phosphate pathway;
SY   Phosphogluconate oxidative pathway.
GO   GO:0006098; pentose-phosphate shunt
HI   Biological process: Pentose shunt.
CA   Biological process.
//
ID   Peptide transport.
AC   KW-0571
DE   Protein involved in the transport of peptides.
GO   GO:0015833; peptide transport
HI   Biological process: Transport; Protein transport; Peptide transport.
CA   Biological process.
//
ID   Peptidoglycan synthesis.
AC   KW-0573
DE   Protein involved in the synthesis of peptidoglycan which consists of a
DE   glycosaminoglycan formed by alternating residues of D-glucosamine and
DE   either muramic acid {2-amino-3-O-[(R)-1-carboxyethyl]-2-deoxy-D-
DE   glucose} or L-talosaminuronic acid (2-amino-2-deoxy-L-taluronic acid),
DE   which are usually N-acetylated or N-glycoloylated. The carboxyl group
DE   of the muramic acid is commonly substituted by a peptide containing
DE   residues of both L- and D-amino acids, whereas that of L-
DE   talosaminuronic acid is substituted by a peptide consisting of L-amino
DE   acids only. These peptide units may be cross-linked by a peptide bond,
DE   thereby giving rise to a giant macromolecule that forms the rigid cell
DE   wall (sacculus or murein sacculus). This macromolecule is known to
DE   occur as a monomolecular layer between the inner and outer membrane in
DE   Gram-negative bacteria and as a multimolecular layer, often associated
DE   covalently or non-covalently with various additional compounds
DE   (teichoic acids, neutral polysaccharides. etc.) in Gram-positive
DE   bacteria. In the archaebacteria, several organisms contain a
DE   peptidoglycan, also called pseudomurein, which differs in certain
DE   respects from those of the eubacteria.
SY   Murein anabolism; Murein biosynthesis; Murein biosynthetic process;
SY   Murein formation; Murein synthesis; Peptidoglycan anabolism;
SY   Peptidoglycan biosynthesis; Peptidoglycan biosynthetic process;
SY   Peptidoglycan formation; Pseudomurein anabolism;
SY   Pseudomurein biosynthesis; Pseudomurein biosynthetic process;
SY   Pseudomurein formation; Pseudomurein synthesis.
GO   GO:0009252; peptidoglycan biosynthetic process
HI   Biological process: Cell shape; Peptidoglycan synthesis.
HI   Biological process: Peptidoglycan synthesis.
CA   Biological process.
//
ID   Peptidoglycan-anchor.
AC   KW-0572
DE   Protein that is covalently anchored to the peptidoglycan of a cell
DE   wall envelope. In Gram-positive bacteria, binding proceeds through a
DE   transpeptidation mechanism which requires a C-terminal sorting signal
DE   with a conserved LPXTG or LPXAG motif; an amide bond is created
DE   between the alpha-carboxyl group of the conserved threonine,
DE   alternatively alanine, and the amino group of peptidoglycan cross-
DE   bridges. In Gram-negative bacteria, binding proceeds through the
DE   formation of an isopeptide bond between the epsilon-amino group of a
DE   lysine and the alpha-carboxyl group of a peptidoglycan diaminopimelic
DE   acid.
HI   PTM: Peptidoglycan-anchor.
CA   PTM.
//
ID   Periplasm.
AC   KW-0574
DE   Protein located in the space between the inner membrane and the outer
DE   membrane (cell wall) of Gram negative bacteria and some eukaryotic
DE   algae. Also used for proteins located in the region between the plasma
DE   membrane and the cell wall in fungi.
GO   GO:0042597; periplasmic space
HI   Cellular component: Periplasm.
CA   Cellular component.
//
ID   Peroxidase.
AC   KW-0575
DE   Enzyme that catalyzes the oxidation of a substrate by reducing
DE   peroxide to water. These enzymes are often located in peroxisomes.
GO   GO:0004601; peroxidase activity
HI   Molecular function: Oxidoreductase; Peroxidase.
CA   Molecular function.
//
ID   Peroxisome.
AC   KW-0576
DE   Protein found in or associated with the peroxisome, a small eukaryotic
DE   organelle limited by a single membrane, specialized for carrying out
DE   oxidative reactions. Contains mainly peroxidases, several other
DE   oxidases and catalase. The catalase regulates the contents of the
DE   produced toxic hydrogen peroxide thus protecting the cell. Beta-
DE   oxidation of fatty acids is another major function of peroxisomes. In
DE   plants and fungi this degradation occurs only in this cellular
DE   compartment.
GO   GO:0005777; peroxisome
HI   Cellular component: Peroxisome.
CA   Cellular component.
//
ID   Peroxisome biogenesis.
AC   KW-0962
DE   Protein which is involved in the formation, organization and
DE   maintenance of the peroxisome. The peroxisome is a small eukaryotic
DE   organelle limited by a single membrane, specialized for carrying out
DE   oxidative reactions.
SY   Peroxisome assembly; Peroxisome formation.
GO   GO:0007031; peroxisome organization
HI   Biological process: Peroxisome biogenesis.
CA   Biological process.
//
ID   Peroxisome biogenesis disorder.
AC   KW-0958
DE   Protein which, if defective, causes peroxisome biogenesis disorder, a
DE   group of peroxisomal disorders arising from a failure of protein
DE   import into the peroxisomal membrane or matrix. The PBD group is
DE   comprised of four disorders: Zellweger syndrome (ZWS), neonatal
DE   adrenoleukodystrophy (NALD), infantile Refsum disease (IRD), and
DE   classical rhizomelic chondrodysplasia punctata type 1 (RCDP1). ZWS,
DE   NALD and IRD are distinct from RCDP1 and constitute a clinical
DE   continuum of overlapping phenotypes known as Zellweger spectrum. The
DE   PBD group is genetically heterogeneous with at least 12 distinct
DE   genetic groups as concluded from complementation studies.
SY   PBD; Peroxisome-biogenesis disorder.
HI   Disease: Peroxisome biogenesis disorder.
CA   Disease.
//
ID   Peters anomaly.
AC   KW-1059
DE   Protein which, if defective, causes Peters anomaly, an ocular disorder
DE   characterized by congenital central corneal leukoma, absence of the
DE   posterior corneal stroma and Descemet membrane, and a variable degree
DE   of iris and lenticular attachments to the central aspect of the
DE   posterior cornea.
HI   Disease: Peters anomaly.
CA   Disease.
//
ID   PHA biosynthesis.
AC   KW-0577
DE   Protein involved in the synthesis of poly(3-hydroxyalkanoates) (PHA).
DE   In Pseudomonas oleovorans large amounts of this polyester are
DE   synthesized when cells are grown under nitrogen-limiting conditions.
DE   When nitrogen is further supplied in the medium, the accumulated PHA
DE   is degraded.
SY   PHA anabolism; PHA biosynthetic process; PHA formation; PHA synthesis;
SY   Poly(3-hydroxyalkanoate) anabolism;
SY   Poly(3-hydroxyalkanoate) biosynthesis;
SY   Poly(3-hydroxyalkanoate) biosynthetic process;
SY   Poly(3-hydroxyalkanoate) formation;
SY   Poly(3-hydroxyalkanoate) synthesis.
GO   GO:0042621; poly(3-hydroxyalkanoate) biosynthetic process
HI   Biological process: PHA biosynthesis.
CA   Biological process.
//
ID   Phagocytosis.
AC   KW-0581
DE   Protein that is involved in phagocytosis or that renders the organism
DE   resistant to phagocytosis, the process by which a cell is engulfed and
DE   broken down by another for purposes of defense or sustenance.
GO   GO:0006909; phagocytosis
HI   Biological process: Phagocytosis.
CA   Biological process.
//
ID   Pharmaceutical.
AC   KW-0582
DE   Protein which is used or may be used as a pharmaceutical drug, e.g. to
DE   treat specific diseases.
HI   Technical term: Pharmaceutical.
CA   Technical term.
//
ID   PHB biosynthesis.
AC   KW-0583
DE   Protein involved in the synthesis of poly-hydroxybutyrate (PHB). It
DE   accumulates in a variety of bacteria as an energy source. This
DE   polyester is thermoplastic with biodegradable properties.
SY   PHB anabolism; PHB biosynthetic process; PHB formation; PHB synthesis;
SY   Poly-(3-hydroxybutyrate) anabolism;
SY   Poly-(3-hydroxybutyrate) biosynthesis;
SY   Poly-(3-hydroxybutyrate) biosynthetic process;
SY   Poly-(3-hydroxybutyrate) formation;
SY   Poly-(3-hydroxybutyrate) synthesis;
SY   Poly-beta-hydroxybutyrate anabolism;
SY   Poly-beta-hydroxybutyrate biosynthesis;
SY   Poly-beta-hydroxybutyrate biosynthetic process;
SY   Poly-beta-hydroxybutyrate formation;
SY   Poly-beta-hydroxybutyrate synthesis; Poly-hydroxybutyrate anabolism;
SY   Poly-hydroxybutyrate biosynthesis;
SY   Poly-hydroxybutyrate biosynthetic process;
SY   Poly-hydroxybutyrate formation; Poly-hydroxybutyrate synthesis.
GO   GO:0042619; poly-hydroxybutyrate biosynthetic process
HI   Biological process: PHB biosynthesis.
CA   Biological process.
//
ID   Phenylalanine biosynthesis.
AC   KW-0584
DE   Protein involved in the biosynthesis of the aromatic amino acid
DE   phenylalanine.
SY   Phenylalanine anabolism; Phenylalanine biosynthetic process;
SY   Phenylalanine formation; Phenylalanine synthesis.
GO   GO:0009094; L-phenylalanine biosynthetic process
HI   Biological process: Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Phenylalanine biosynthesis.
CA   Biological process.
//
ID   Phenylalanine catabolism.
AC   KW-0585
DE   Protein involved in the degradation of the aromatic amino acid
DE   phenylalanine.
SY   Phenylalanine breakdown; Phenylalanine catabolic process;
SY   Phenylalanine degradation.
GO   GO:0006559; L-phenylalanine catabolic process
HI   Biological process: Phenylalanine catabolism.
CA   Biological process.
//
ID   Phenylketonuria.
AC   KW-0586
DE   Protein which, if defective, causes phenylketonuria, an autosomal
DE   recessive disorder in which the body is unable to break down the amino
DE   acid phenylalanine. The resulting buildup of phenylalanine in the body
DE   causes intellectual disability, mental disturbances, eczema and skin
DE   pigmentation.
HI   Disease: Phenylketonuria.
CA   Disease.
//
ID   Phenylpropanoid metabolism.
AC   KW-0587
DE   Protein involved in the biochemical reactions with phenylpropanoids.
SY   Phenylpropanoid metabolic process.
GO   GO:0009698; phenylpropanoid metabolic process
HI   Biological process: Phenylpropanoid metabolism.
CA   Biological process.
//
ID   Pheromone.
AC   KW-0588
DE   Proteins which acts as a pheromone. Pheromones are odours of
DE   conspecifics which elicit an adaptive behavioral response, e.g. insect
DE   sex pheromones. Generally, they are comprised of mixtures of compounds
DE   and behavioral responsiveness to them is largely instinctual,
DE   sexually-dimorphic, and attributable to a specialized component(s) of
DE   the olfactory system.
GO   GO:0005186; pheromone activity
HI   Molecular function: Pheromone.
CA   Molecular function.
//
ID   Pheromone response.
AC   KW-0589
DE   Protein involved in the pheromone response.
SY   Pheromone response pathway; Response to pheromone.
GO   GO:0019236; response to pheromone
HI   Biological process: Pheromone response.
CA   Biological process.
//
ID   Pheromone-binding.
AC   KW-0590
DE   Protein which binds pheromones, the odours of conspecifics which
DE   elicit an adaptive behavioral response, e.g. insect sex pheromones.
GO   GO:0005550; pheromone binding
HI   Ligand: Pheromone-binding.
CA   Ligand.
//
ID   Phosphate transport.
AC   KW-0592
DE   Protein involved in the transport of phosphate.
GO   GO:0006817; phosphate ion transport
HI   Biological process: Transport; Phosphate transport.
CA   Biological process.
//
ID   Phospholipase A2 inhibitor.
AC   KW-0593
DE   Protein which inhibits phospholipase A2 (EC 3.1.1.4) (PA2), an enzyme
DE   which releases fatty acids from the second carbon group of glycerol.
DE   Phospholipase A2 inhibitors are widely distributed in venoms and
DE   digestive secretions.
GO   GO:0019834; phospholipase A2 inhibitor activity
HI   Molecular function: Phospholipase A2 inhibitor.
CA   Molecular function.
//
ID   Phospholipid biosynthesis.
AC   KW-0594
DE   Protein involved in the synthesis of phospholipids, the major lipid
DE   component of most cellular membranes. Phospholipids are usually
DE   composed of two fatty acid chains esterified to two of the carbons of
DE   glycerol phosphate, the phosphate being esterified to a hydroxyl group
DE   of another hydrophilic compound, such as choline, ethanolamine or
DE   serine.
SY   Phospholipid anabolism; Phospholipid biosynthetic process;
SY   Phospholipid formation; Phospholipid synthesis.
GO   GO:0008654; phospholipid biosynthetic process
HI   Biological process: Lipid metabolism; Lipid biosynthesis; Phospholipid biosynthesis.
HI   Biological process: Lipid metabolism; Phospholipid metabolism; Phospholipid biosynthesis.
CA   Biological process.
//
ID   Phospholipid degradation.
AC   KW-0595
DE   Protein involved in the breakdown of phospholipids, the major lipid
DE   component of most cellular membranes. Phospholipids are usually
DE   composed of two fatty acid chains esterified to two of the carbons of
DE   glycerol phosphate, the phosphate being esterified to a hydroxyl group
DE   of another hydrophilic compound, such as choline, ethanolamine or
DE   serine.
SY   Phospholipid breakdown; Phospholipid catabolic process;
SY   Phospholipid catabolism.
GO   GO:0009395; phospholipid catabolic process
HI   Biological process: Lipid metabolism; Lipid degradation; Phospholipid degradation.
HI   Biological process: Lipid metabolism; Phospholipid metabolism; Phospholipid degradation.
CA   Biological process.
//
ID   Phospholipid metabolism.
AC   KW-1208
DE   Protein involved in the metabolism of phospholipids, the major lipid
DE   component of most cellular membranes. Phospholipids are usually
DE   composed of two fatty acid chains esterified to two of the carbons of
DE   glycerol phosphate, the phosphate being esterified to a hydroxyl group
DE   of another hydrophilic compound, such as choline, ethanolamine or
DE   serine.
SY   Phospholipid metabolic process.
HI   Biological process: Lipid metabolism; Phospholipid metabolism.
CA   Biological process.
//
ID   Phosphonate transport.
AC   KW-0918
DE   Protein involved in the transport of phosphonates. Phosphonates are a
DE   class of organophosphorus compounds characterized by a chemically
DE   stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread
DE   among naturally occurring compounds in all kingdoms of wildlife, but
DE   only prokaryotic microorganisms are able to cleave this bond. Certain
DE   bacteria such as Escherichia coli can use alkylphosphonates as a
DE   phosphorus source.
GO   GO:0015716; organic phosphonate transport
HI   Biological process: Transport; Phosphonate transport.
CA   Biological process.
//
ID   Phosphopantetheine.
AC   KW-0596
DE   Protein which contains at least one phosphopantetheine as the
DE   prosthetic group. In acyl carrier proteins (ACP) for example, it
DE   serves as a 'swinging arm' for the attachment of activated fatty acid
DE   and amino-acid groups.
SY   Pantetheine 4'phosphate.
HI   PTM: Phosphopantetheine.
CA   PTM.
//
ID   Phosphoprotein.
AC   KW-0597
DE   Protein which is posttranslationally modified by the attachment of
DE   either a single phosphate group, or of a complex molecule, such as 5'-
DE   phospho-DNA, through a phosphate group. Target amino acid is usually
DE   serine, threonine or tyrosine residues (mostly in eukaryotes),
DE   aspartic acid or histidine residues (mostly in prokaryotes).
SY   Phosphorylation.
HI   PTM: Phosphoprotein.
CA   PTM.
//
ID   Phosphotransferase system.
AC   KW-0598
DE   Protein involved in the phosphotransferase system, the major
DE   carbohydrate transport system in bacteria. This phosphotransferase
DE   system catalyzes the transfer of the phosphoryl group from
DE   phosphoenolpyruvate to incoming sugar substrates concomitant with
DE   their translocation across the cell membrane.
SY   Phosphoenolpyruvate-dependent sugar phosphotransferase system; PTS;
SY   Sugar phosphotransferase system.
GO   GO:0009401; phosphoenolpyruvate-dependent sugar phosphotransferase system
HI   Biological process: Phosphotransferase system.
CA   Biological process.
//
ID   Photoprotein.
AC   KW-0599
DE   Luminescent proteins, which are involved in the phenomenon of light
DE   emission in certain living organisms. E.g., green fluorescent protein
DE   which is unique among fluorescent proteins in that its chromophore is
DE   not a separately synthesized prostethic group but is composed of
DE   modified amino acid residues within its polypeptide chain.
GO   GO:0008218; bioluminescence
HI   Biological process: Luminescence; Photoprotein.
HI   Molecular function: Photoprotein.
CA   Molecular function.
//
ID   Photoreceptor protein.
AC   KW-0600
DE   Protein involved in the convertion of light directly into a signal.
DE   These proteins are classified in a limited number of families based on
DE   the chemical structure of the light-absorbing chromophores involved,
DE   and also on protein sequence similarities to discriminate the many
DE   photoreceptor proteins that bind a flavin derivative. Accordingly, the
DE   most important families are the rhodopsins, the phytochromes, the
DE   xanthopsins, the cryptochromes, the phototropins and the BLUF
DE   proteins.
SY   Light-sensing protein; Photosensor protein.
GO   GO:0009881; photoreceptor activity
HI   Ligand: Chromophore; Photoreceptor protein.
HI   Molecular function: Receptor; Photoreceptor protein.
HI   Biological process: Sensory transduction; Photoreceptor protein.
CA   Molecular function.
//
ID   Photorespiration.
AC   KW-0601
DE   Protein involved in a light-dependent process to convert 2-phospho-
DE   glycolate (2-PG) into 3-phospho-D-glycerate (3-PG), where oxygen is
DE   consumed and carbon dioxide released. It takes place in plants and
DE   cyanobacteria during the light period, since in the presence of O(2)
DE   their type of Rubisco can catalyze the oxidative fragmentation of
DE   ribulose 1,5-biphosphate to 3-PG and 2-PG. 2-PG inhibits the Calvin
DE   cycle enzyme triose-phosphate isomerase, and so must be eliminated
DE   quickly. In plants 2-PG is recycled to 3-PG via reactions in
DE   peroxisomes, mitochondria as well as chloroplasts. For every 2
DE   molecules of 2-PG, one molecule of 3-PG is formed and one molecule of
DE   CO(2) is lost. In cyanobacteria it seems there are two mechanisms to
DE   deal with 2-PG; a path similar to that described for plants and the
DE   bacterial-like glycerate pathway.
GO   GO:0009853; photorespiration
HI   Biological process: Photorespiration.
CA   Biological process.
//
ID   Photosynthesis.
AC   KW-0602
DE   Protein involved in photosynthesis, the process in which light energy
DE   is absorbed by photosynthetic pigments (e.g. chlorophyll) and
DE   converted to chemical energy (usually ATP and NADPH, =light reaction).
DE   This energy is subsequently used as an energy source for the reduction
DE   of carbon dioxide to carbohydrate (=Calvin cycle). The general
DE   reaction is: CO(2) + 2H(2)A = (CH(2)O) + 2A + H(2)O, where 2H(2)A is
DE   any reduced compound that can serve as an electron donor. In plants,
DE   algae and cyanobacteria H(2)O serves as a reductant, generating O(2).
DE   Non-oxygenic organisms use other electron donors, for example H(2)S in
DE   purple sulfur bacteria, generating sulfur.
GO   GO:0015979; photosynthesis
HI   Biological process: Photosynthesis.
CA   Biological process.
//
ID   Photosystem I.
AC   KW-0603
DE   Protein involved in photosystem I (PSI), a complex that uses light
DE   energy to mediate electron flow in the chloroplast thylakoid membrane
DE   of plants and in cyanobacteria. In linear electron flow, PSII is
DE   coupled to PSI and produces a pH gradient, ATP and NADPH. In cyclic
DE   electron flow, PSI generates a pH gradient and ATP. PSI is excited
DE   best by light at about 700 nm, and is thus sometimes called P700. PSI
DE   is an iron-sulfur type reaction center (RC), sharing a common ancestor
DE   with the RCs of Heliobacteriaceae, green sulfur and green non-sulfur
DE   bacteria.
SY   P700; PSI.
GO   GO:0009522; photosystem I
HI   Biological process: Photosynthesis; Photosystem I.
HI   Cellular component: Photosystem I.
CA   Cellular component.
//
ID   Photosystem II.
AC   KW-0604
DE   Protein involved in photosystem II (PSII), a complex that uses light
DE   energy to mediate electron flow in the chloroplast thylakoid membrane
DE   of plants and in cyanobacteria. PSII splits water, releasing hydrogen
DE   ions and molecular oxygen. PSII cannot use photons of a wavelength
DE   greater than 680 nm, and is thus sometimes called P680. PSII is a
DE   quinone type rection center (RC), sharing a common ancestor with the
DE   RCs of purple bacteria.
SY   P680; PSII.
GO   GO:0009523; photosystem II
HI   Biological process: Photosynthesis; Photosystem II.
HI   Cellular component: Photosystem II.
CA   Cellular component.
//
ID   Phycobilisome.
AC   KW-0605
DE   Protein found in phycobilisome, an accessory light energy harvesting
DE   structure on the outer face of the thylakoid membranes in
DE   cyanobacteria and red algae. Phycobilisomes are mainly composed of
DE   phycobiliproteins (such as allophycocyanin, phycocyanin and
DE   phycoerythrin) together with linker polypeptides.
GO   GO:0030089; phycobilisome
HI   Cellular component: Antenna complex; Phycobilisome.
CA   Cellular component.
//
ID   Phytochrome signaling pathway.
AC   KW-0607
DE   Protein involved in the relay of information from the activated
DE   phytochrome molecule to target genes. Different phytochromes use both
DE   separate and common early signaling pathways. These pathways converge
DE   downstream in a process of signal integration that regulates
DE   photomorphogenesis and the circadian clock. This provides the means by
DE   which information from specific wavelengths of light may be amplified
DE   and coordinated.
GO   GO:0009585; red, far-red light phototransduction
GO   GO:0010017; red or far-red light signaling pathway
HI   Biological process: Phytochrome signaling pathway.
CA   Biological process.
//
ID   Pigment.
AC   KW-0608
DE   Protein which binds or transport pigments, any coloring matter in
DE   animals, plants or microorganisms.
GO   GO:0031409; pigment binding
HI   Ligand: Pigment.
CA   Ligand.
//
ID   Plant defense.
AC   KW-0611
DE   Protein involved in plant defense, either as part of preexisting,
DE   developmentally regulated defense barriers (such as thionins,
DE   defensins or hydroxyproline-rich glycoproteins fortifying the cell
DE   wall) or as components of the defense responses induced upon pathogen
DE   infection during hypersensitive cell death (HR), local acquired
DE   resistance (LAR) or systemic acquired resistance (SAR). This includes
DE   proteins involved in various pathways, such as the gene-for-gene
DE   resistance, the salicylic acid (SA)-dependant resistance, the
DE   jasmonate (JA) and/or ethylene (ET)-dependant resistance and the
DE   induced systemic resistance (ISR), as well as the final products of
DE   those pathways such as the pathogenesis-related proteins.
GO   GO:0006952; defense response
HI   Biological process: Plant defense.
CA   Biological process.
//
ID   Plasmid.
AC   KW-0614
DE   Protein encoded on a plasmid, a self-replicating circular DNA that is
DE   found in a variety of bacterial, archaeal, fungal, algal and plant
DE   species, and can be transferred from one organism to another. Plasmids
DE   often carry antibiotic-resistant genes and are widely used in
DE   molecular biology as vectors of genes and in cloning.
HI   Technical term: Plasmid.
CA   Technical term.
//
ID   Plasmid copy control.
AC   KW-0615
DE   Protein involved in the plasmid copy control, the ability of a plasmid
DE   to control its own copy number in a cell. Copy number is a function of
DE   the rate at which DNA synthesis is initiated.
GO   GO:0006276; plasmid maintenance
HI   Biological process: Plasmid copy control.
CA   Biological process.
//
ID   Plasmid partition.
AC   KW-0616
DE   Protein involved in plasmid partition, the process whereby newly
DE   replicated plasmids are distributed properly to daughter cells during
DE   cell division.
GO   GO:0030541; plasmid partitioning
HI   Biological process: Plasmid partition.
CA   Biological process.
//
ID   Plasminogen activation.
AC   KW-0617
DE   Protein involved in the plasminogen activation which occurs when an
DE   heterogeneous group of proteolytic enzymes convert plasminogen to
DE   plasmin.
HI   Biological process: Plasminogen activation.
CA   Biological process.
//
ID   Plastid.
AC   KW-0934
DE   Protein encoded by or localized in a plastid, a semi-autonomous, self-
DE   reproducing organelle. Plastids are remnants of a photosynthetic
DE   organism that was engulfed by the host, although not all are now
DE   photosynthetic. Plastid genomes encode genes for rRNAs, tRNAs and
DE   between about 28 and 150 proteins. Plastids can be categorized in 4
DE   main groups: chloroplasts, cyanelles, apicoplasts and non-
DE   photosynthetic. The latter are found is some land plants (Epifagus
DE   virginiana), chlorophyte algae (Prototheca wickerhamii) and euglenoids
DE   (Astasis longa), which do not encode the genes necessary for
DE   photosynthesis and so are not photosynthetic but still contain a
DE   plastid. Non-photosynthetic plastids probably do not contain
DE   thylakoids.
GO   GO:0009536; plastid
HI   Cellular component: Plastid.
CA   Cellular component.
//
ID   Plastid inner membrane.
AC   KW-1001
DE   Protein found in or associated with the inner membrane of a plastid,
DE   which separates the plastid stroma from the intermembrane space.
SY   Inner plastidic membrane; Inner plastid membrane;
SY   Plastidic inner membrane.
GO   GO:0009528; plastid inner membrane
HI   Cellular component: Membrane; Plastid inner membrane.
HI   Cellular component: Plastid; Plastid inner membrane.
CA   Cellular component.
//
ID   Plastid outer membrane.
AC   KW-1002
DE   Protein found in or associated with the outer membrane of a plastid,
DE   which is the membrane facing the cytoplasm.
SY   Outer plastidic membrane; Outer plastid membrane;
SY   Plastidic outer membrane.
GO   GO:0009527; plastid outer membrane
HI   Cellular component: Membrane; Plastid outer membrane.
HI   Cellular component: Plastid; Plastid outer membrane.
CA   Cellular component.
//
ID   Plastoquinone.
AC   KW-0618
DE   Protein which interacts with plastoquinone, a substituted quinone
DE   called plastoquinone because it appeared concentrated in the
DE   chloroplasts of higher plants. Plastoquinone transfers electrons from
DE   the photosystem II reaction center to the cytochrome bf complex and
DE   carries protons across the photosynthetic membrane.
HI   Ligand: Plastoquinone.
CA   Ligand.
//
ID   Platelet aggregation activating toxin.
AC   KW-1202
DE   Toxin which induces agonist-induced platelet aggregation, the self-
DE   adhesion of platelets via adhesion molecules. Numerous snake venom
DE   families have the capacity to induce platelet aggregation.
HI   Molecular function: Toxin; Hemostasis impairing toxin; Platelet aggregation activating toxin.
CA   Molecular function.
//
ID   Platelet aggregation inhibiting toxin.
AC   KW-1201
DE   Toxin which inhibits agonist-induced platelet aggregation, the self-
DE   adhesion of platelets via adhesion molecules. Numerous snake venom
DE   families have the capacity to inhibit platelet aggregation.
HI   Molecular function: Toxin; Hemostasis impairing toxin; Platelet aggregation inhibiting toxin.
CA   Molecular function.
//
ID   Polyamine biosynthesis.
AC   KW-0620
DE   Protein involved in polyamine biosynthesis. The polyamines, e.g.
DE   putrescine, cadaverine, agmatine, spermidine and spermine, are wide-
DE   spread in all organisms, and have been shown to play a role in the
DE   regulation of growth and differentiation of virtually all types of
DE   cells.
GO   GO:0006596; polyamine biosynthetic process
HI   Biological process: Polyamine biosynthesis.
CA   Biological process.
//
ID   Polysaccharide degradation.
AC   KW-0624
DE   Protein involved in polysaccharide degradation, the breakdown of
DE   polysaccharides.
GO   GO:0000272; polysaccharide catabolic process
HI   Biological process: Carbohydrate metabolism; Polysaccharide degradation.
CA   Biological process.
//
ID   Polysaccharide transport.
AC   KW-0625
DE   Protein involved in the transport of polysaccharides.
GO   GO:0015774; polysaccharide transport
HI   Biological process: Transport; Sugar transport; Polysaccharide transport.
CA   Biological process.
//
ID   Pontocerebellar hypoplasia.
AC   KW-1021
DE   Protein which, if defective, causes pontocerebellar hypoplasia, a
DE   heterogeneous group of congenital disorders characterized by
DE   hypoplasia and atrophy of the cerebellar cortex, dentate nuclei,
DE   pontine nuclei and inferior olives. Additional defects of other brain
DE   and spinal cord structures can be present, resulting in clinical
DE   manifestations that vary among cases.
SY   PCH; Pontocerebellar atrophy.
HI   Disease: Pontocerebellar hypoplasia.
CA   Disease.
//
ID   Pore-mediated penetration of viral genome into host cell.
AC   KW-1172
DE   Virion-associated pore-forming protein that induces the formation of a
DE   transmembrane pore or channel in the host membrane(s) to allow the
DE   viral genome to enter the host cytoplasm. This mechanism is used by
DE   non-enveloped viruses such as human rhinovirus 2 or poliovirus. Many
DE   tailed bacteriophages carry specialized proteins which open a pore or
DE   a channel in the host membrane(s) to allow penetration of the virion
DE   tail into host envelope and genome delivery into host cytoplasm.
SY   Membrane puncture-mediated penetration of viral genome into host cell.
GO   GO:0044694; pore-mediated entry of viral genome into host cell
HI   Biological process: Virus entry into host cell; Viral penetration into host cytoplasm; Pore-mediated penetration of viral genome into host cell.
CA   Biological process.
//
ID   Porin.
AC   KW-0626
DE   Membrane protein which in a multimeric form constitutes a water-filled
DE   transmembrane channel (a pore). This pore allows the passage of ions
DE   and numerous other, non-specific molecules through the membrane. Found
DE   in the mitochondrial and plastid outer membrane of eukaryotes, in many
DE   Gram-negative bacteria, at least some Corynebacterineae, archaea and
DE   in sea anemones.
GO   GO:0015288; porin activity
GO   GO:0046930; pore complex
HI   Biological process: Transport; Ion transport; Porin.
HI   Domain: Transmembrane; Porin.
HI   Molecular function: Porin.
CA   Molecular function.
//
ID   Porphyrin biosynthesis.
AC   KW-0627
DE   Protein involved in the synthesis of porphyrins which are compounds
DE   that contain the porphin structure, e.g. four pyrrole rings connected
DE   by methine bridges in a cyclic configuration to which a variety of
DE   side chains are attached. Porphyrins often chelate metal ions (Fe, Mg,
DE   Co, Zn, Cu, Ni). Examples are, heme proteins (which contain iron
DE   porphyrins) like myoglobin, hemoglobin, cytochromes, or related
DE   macrocycles including chlorophylls (which have a central magnesium
DE   ion) and pheophytins (which are metal free) and vitamin B-12 (which
DE   has cobalt).
GO   GO:0006779; porphyrin-containing compound biosynthetic process
HI   Biological process: Porphyrin biosynthesis.
CA   Biological process.
//
ID   Postsynaptic cell membrane.
AC   KW-0628
DE   Protein characteristic of the postsynaptic membrane. In a chemical
DE   synapse, the postsynaptic membrane is the membrane that receives a
DE   signal (binds neurotransmitter) from the presynaptic cell and responds
DE   via depolarisation or hyperpolarisation. The postsynaptic membrane is
DE   separated from the presynaptic membrane by the synaptic cleft.
SY   Postsynaptic membrane.
GO   GO:0045211; postsynaptic membrane
HI   Cellular component: Membrane; Postsynaptic cell membrane.
HI   Cellular component: Synapse; Postsynaptic cell membrane.
CA   Cellular component.
//
ID   Postsynaptic neurotoxin.
AC   KW-0629
DE   Protein which acts as a neurotoxin at the postsynaptic membrane. They
DE   bind to acetylcholine receptors and so inhibit their activity.
GO   GO:0035792; host cell postsynaptic membrane
HI   Molecular function: Toxin; Neurotoxin; Postsynaptic neurotoxin.
CA   Molecular function.
//
ID   Potassium.
AC   KW-0630
DE   Protein which binds at least one potassium, or protein whose function
DE   is potassium-dependent. Potassium is an alkali metal, chemical symbol
DE   K.
HI   Ligand: Potassium.
WW   https://www.webelements.com/potassium/
CA   Ligand.
//
ID   Potassium channel.
AC   KW-0631
DE   Protein which is part of a transmembrane protein complex that forms a
DE   hydrophilic channel across the lipid bilayer through which potassium
DE   ions can diffuse down their electrochemical gradient. The channels are
DE   gated and only open in response to a specific stimulus, such as a
DE   change in membrane potential (voltage-gated). They are important for
DE   the regulation of the resting membrane potential and for the control
DE   of the shape and frequency of action potentials.
GO   GO:0005267; potassium channel activity
GO   GO:0071805; potassium ion transmembrane transport
HI   Molecular function: Ion channel; Potassium channel.
HI   Ligand: Potassium; Potassium channel.
HI   Biological process: Transport; Ion transport; Potassium transport; Potassium channel.
CA   Molecular function.
//
ID   Potassium channel impairing toxin.
AC   KW-0632
DE   Protein which interferes with the function of potassium channels which
DE   are membrane proteins forming a channel in a biological membrane
DE   selectively permeable to potassium ions. They are found in various
DE   venoms from snakes, scorpions and spiders.
GO   GO:0015459; potassium channel regulator activity
HI   Molecular function: Toxin; Ion channel impairing toxin; Potassium channel impairing toxin.
CA   Molecular function.
//
ID   Potassium transport.
AC   KW-0633
DE   Protein involved in the transport of potassium ions.
GO   GO:0006813; potassium ion transport
HI   Biological process: Transport; Ion transport; Potassium transport.
HI   Ligand: Potassium; Potassium transport.
CA   Biological process.
//
ID   PQQ.
AC   KW-0634
DE   Protein which non-covalently binds at least one pyrroloquinoline
DE   quinone (PQQ) cofactor.
SY   Methoxatin; Pyrroloquinoline quinone.
HI   Ligand: PQQ.
CA   Ligand.
//
ID   PQQ biosynthesis.
AC   KW-0884
DE   Protein involved in the biosynthesis of the cofactor pyrroloquinoline
DE   quinone (PQQ).
SY   Pyrroloquinoline quinone biosynthesis.
GO   GO:0018189; pyrroloquinoline quinone biosynthetic process
HI   Biological process: PQQ biosynthesis.
CA   Biological process.
//
ID   Pregnancy.
AC   KW-0635
DE   Protein which plays a role in pregnancy, the condition of having a
DE   developing embryo or fetus in the body, after union of an ovum and
DE   spermatozoon.
GO   GO:0007565; female pregnancy
HI   Biological process: Pregnancy.
CA   Biological process.
//
ID   Premature ovarian failure.
AC   KW-1066
DE   Protein which, if defective, causes premature ovarian failure, a
DE   condition characterized by the arrest of normal ovarian function
DE   before the age of 40 years, due to a primary ovarian defect. It is
DE   characterized by absent menarche (primary amenorrhea) or premature
DE   depletion of ovarian follicles (secondary amenorrhea).
SY   Primary ovarian insufficiency.
HI   Disease: Premature ovarian failure.
CA   Disease.
//
ID   Prenylation.
AC   KW-0636
DE   Protein which is posttranslationally modified by the attachment of at
DE   least one prenyl group (e.g. farnesyl, geranylgeranyl) usually on
DE   cysteine residues which are at or near the C-terminal extremity.
HI   PTM: Lipoprotein; Prenylation.
CA   PTM.
//
ID   Prenyltransferase.
AC   KW-0637
DE   Enzyme that catalyzes the transfer of an isoprenoid (farnesyl or
DE   geranylgeranyl) usually on cysteine residues, which are three residues
DE   away from the C-terminal extremity.
GO   GO:0004659; prenyltransferase activity
HI   Molecular function: Transferase; Prenyltransferase.
CA   Molecular function.
//
ID   Presynaptic neurotoxin.
AC   KW-0638
DE   Protein which acts as a neurotoxin at the presynaptic membrane and
DE   usually blocks neuromuscular transmission.
GO   GO:0044231; host cell presynaptic membrane
HI   Molecular function: Toxin; Neurotoxin; Presynaptic neurotoxin.
CA   Molecular function.
//
ID   Primary ciliary dyskinesia.
AC   KW-0990
DE   Protein which, if defective, causes primary ciliary dyskinesia, a rare
DE   and genetically heterogeneous disorder characterized by sino-pulmonary
DE   disease, laterality defects and male infertility. Primary ciliary
DE   dyskinesia is due to dysfunction of motile cilia and flagella in
DE   various organ systems.
SY   CILD; ICS; Immotile cilia syndrome; PCD.
HI   Disease: Ciliopathy; Primary ciliary dyskinesia.
CA   Disease.
//
ID   Primary hypomagnesemia.
AC   KW-0982
DE   Protein which, if defective, causes primary hypomagnesemia. Primary
DE   hypomagnesemia defines a heterogeneous group of disorders
DE   characterized by low magnesium serum content due to primary renal or
DE   intestinal magnesium wasting. Primary hypomagnesemia disorders
DE   generally share symptoms of magnesium depletion, such as tetany and
DE   generalized convulsions. They often include associated disturbances in
DE   calcium excretion.
HI   Disease: Primary hypomagnesemia.
CA   Disease.
//
ID   Primary microcephaly.
AC   KW-0905
DE   Protein which, if defective, causes primary microcephaly. This is a
DE   neurodevelopmental condition characterized by a head circumference
DE   more than 3 standard deviations below the age, sex and ethnically
DE   matched mean, and absence of other syndromic features or significant
DE   neurological deficits. Brain weight is markedly reduced and the
DE   cerebral cortex is disproportionately small. Primary microcephaly is
DE   also known as true microcephaly or microcephaly vera.
HI   Disease: Primary microcephaly.
CA   Disease.
//
ID   Primary mitochondrial disease.
AC   KW-1274
DE   Protein which, if defective, causes any one of a clinically
DE   heterogeneous group of disorders arising from dysfunction of the
DE   mitochondrial respiratory chain. The phenotypic spectrum ranges from
DE   isolated diseases affecting single organs to severe multisystem
DE   disorders. Common clinical features include ptosis, external
DE   ophthalmoplegia, proximal myopathy and exercise intolerance,
DE   cardiomyopathy, sensorineural deafness, optic atrophy, pigmentary
DE   retinopathy, encephalopathy, seizures, stroke-like episodes, ataxia,
DE   and spasticity. Mitochondrial disorders can be caused by mutations of
DE   mitochondrial DNA or nuclear DNA that either affect oxidative
DE   phosphorylation proteins directly, or affect respiratory chain
DE   function by impacting the production of the complex machinery needed
DE   to run this process.
SY   Mitochondrial disorder; Mitochondrial encephalomyopathy;
SY   Mitochondrial myopathy; Oxidative phosphorylation disorder; PMD;
SY   Respiratory chain disorder.
HI   Disease: Primary mitochondrial disease.
CA   Disease.
//
ID   Primosome.
AC   KW-0639
DE   Component of the complex involved in the synthesis of RNA primer
DE   sequences used in DNA replication. Main components are primases and
DE   replicative DNA helicases that move as a unit along the replication
DE   fork.
GO   GO:0006269; DNA replication, synthesis of RNA primer
GO   GO:1990077; primosome complex
HI   Cellular component: Primosome.
CA   Cellular component.
//
ID   Prion.
AC   KW-0640
DE   Protein which is able to form a prion, a self-propagating protein
DE   conformation (infectious protein). Formation of prions involves
DE   conversion of the native proteins into an infectious, amyloid form.
DE   This class of proteins includes the members of the prion family which
DE   can form proteinaceous infectious particles responsible for
DE   transmissible spongiform encephalopathies (TSE) in many animals, such
DE   as Kuru and Creutzfeldt-Jakob syndrome in humans, scrapies in sheep
DE   and BSE in cattle. These prion diseases represent special cases of
DE   neurodegenerative amyloidoses, because they result from the
DE   transmissibility and infectivity of the amyloid.
HI   Cellular component: Amyloid; Prion.
HI   Molecular function: Prion.
CA   Molecular function.
//
ID   Progressive external ophthalmoplegia.
AC   KW-0935
DE   Protein which, if defective, causes progressive external
DE   ophthalmoplegia with mitochondrial DNA deletions. Progressive external
DE   ophthalmoplegia (PEO) is characterized by ptosis and weakness of the
DE   extraocular muscles. Typical symptoms are ophthalmoparesis and
DE   exercise intolerance. Some people also may develop cardiomyopathy,
DE   cataracts, ataxia, peripheral neuropathy, hypogonadism or major
DE   depression. The diagnosis depends on the demonstration, by Southern
DE   blotting, of multiple deletions of mtDNA in muscle biopsy specimens.
DE   Both autosomal dominant and autosomal recessive inheritance can occur.
DE   The autosomal recessive form, which is often associated with
DE   multisystemic disorders, is clinically more heterogenous than the
DE   autosomal dominant form and can be more severe.
HI   Disease: Primary mitochondrial disease; Progressive external ophthalmoplegia.
CA   Disease.
//
ID   Proline biosynthesis.
AC   KW-0641
DE   Protein involved in the biosynthesis of the cyclic amino acid proline.
DE   The structure of proline differs from the structure of other amino
DE   acids in that its side chain is bonded to the nitrogen of the amino
DE   group as well as to the carbon atom. This makes the amino group a
DE   secondary amine, and because of this, proline is also described as an
DE   imino acid. The presence of proline residues strongly influences the
DE   secondary structure of proteins.
GO   GO:0006561; proline biosynthetic process
HI   Biological process: Amino-acid biosynthesis; Proline biosynthesis.
CA   Biological process.
//
ID   Proline metabolism.
AC   KW-0642
DE   Protein involved in a biochemical reaction with the cyclic amino acid
DE   proline. The structure of proline differs from the structure of other
DE   amino acids in that its side chain is bonded to the nitrogen of the
DE   amino group as well as to the carbon atom. This makes the amino group
DE   a secondary amine, and because of this, proline is also described as
DE   an imino acid. The presence of proline residues strongly influences
DE   the secondary structure of proteins.
GO   GO:0006560; proline metabolic process
HI   Biological process: Proline metabolism.
CA   Biological process.
//
ID   Prostaglandin biosynthesis.
AC   KW-0643
DE   Protein involved in the biosynthesis of prostaglandins. Prostaglandins
DE   are fatty acids composed of 20 carbons with a substituted cyclopentane
DE   ring. There are four major classes of prostaglandin, which differ in
DE   the position of the double bonds and/or the oxygen substituents on the
DE   ring: PGA, PGB, PGE, and PGF. They are found in many mammalian
DE   tissues.
GO   GO:0001516; prostaglandin biosynthetic process
HI   Biological process: Lipid metabolism; Fatty acid metabolism; Fatty acid biosynthesis; Prostaglandin biosynthesis.
HI   Biological process: Lipid metabolism; Lipid biosynthesis; Fatty acid biosynthesis; Prostaglandin biosynthesis.
HI   Biological process: Lipid metabolism; Fatty acid metabolism; Prostaglandin metabolism; Prostaglandin biosynthesis.
CA   Biological process.
//
ID   Prostaglandin metabolism.
AC   KW-0644
DE   Protein involved in a biochemical reaction with prostaglandins.
DE   Prostaglandins are fatty acids composed of 20 carbons with a
DE   substituted cyclopentane ring. There are four major classes of
DE   prostaglandin, which differ in the position of the double bonds and/or
DE   the oxygen substituents on the ring: PGA, PGB, PGE, and PGF. They are
DE   found in many mammalian tissues.
GO   GO:0006693; prostaglandin metabolic process
HI   Biological process: Lipid metabolism; Fatty acid metabolism; Prostaglandin metabolism.
CA   Biological process.
//
ID   Protease.
AC   KW-0645
DE   Enzyme which hydrolyzes peptide bonds.
SY   Peptidase; Peptide hydrolase; Proteinase.
GO   GO:0006508; proteolysis
GO   GO:0008233; peptidase activity
HI   Molecular function: Hydrolase; Protease.
CA   Molecular function.
//
ID   Protease inhibitor.
AC   KW-0646
DE   Protein which inhibits or antagonizes the biosynthesis of proteases or
DE   their activity.
GO   GO:0010466; negative regulation of peptidase activity
GO   GO:0030414; peptidase inhibitor activity
HI   Molecular function: Protease inhibitor.
CA   Molecular function.
//
ID   Proteasome.
AC   KW-0647
DE   Protein which is part of the proteasome, a large protein complex in
DE   the cytosol that is responsible for degrading proteins which have been
DE   marked for destruction by ubiquitination or by some other means.
SY   Macropain; Prosome.
GO   GO:0000502; proteasome complex
HI   Cellular component: Proteasome.
CA   Cellular component.
//
ID   Protein biosynthesis.
AC   KW-0648
DE   Protein involved in the biosynthesis of proteins from mRNA molecules.
DE   This process, called translation, is carried out by ribosomes, where
DE   activated amino acids are added to the nascent polypeptide chain.
GO   GO:0006412; translation
HI   Biological process: Protein biosynthesis.
CA   Biological process.
//
ID   Protein kinase inhibitor.
AC   KW-0649
DE   Protein which inhibits the activity of a protein kinase.
GO   GO:0004860; protein kinase inhibitor activity
HI   Molecular function: Protein kinase inhibitor.
CA   Molecular function.
//
ID   Protein phosphatase.
AC   KW-0904
DE   Enzyme that catalyzes the hydrolysis of phosphate monoesters bonds of
DE   phosphoserines, phosphothreonines, phosphotyrosines or phosphoaspartic
DE   acids. While many protein phosphatases inhibit the activities of
DE   phosphorylation cascades, some activate them.
SY   Phosphoprotein phosphatase.
GO   GO:0004721; phosphoprotein phosphatase activity
HI   Molecular function: Hydrolase; Protein phosphatase.
WW   http://www.phosphorylation.biochem.vt.edu/
CA   Molecular function.
//
ID   Protein phosphatase inhibitor.
AC   KW-0650
DE   Protein which inhibits the activity of a protein phosphatase.
GO   GO:0004864; protein phosphatase inhibitor activity
HI   Molecular function: Protein phosphatase inhibitor.
CA   Molecular function.
//
ID   Protein splicing.
AC   KW-0651
DE   Protein which undergoes protein self-splicing, a posttranslational
DE   modification involving the excision of an intervening protein sequence
DE   (intein) from a protein precursor and the concomitant ligation of the
DE   flanking protein fragments (exteins) to form a mature extein protein
DE   and the free intein.
HI   PTM: Autocatalytic cleavage; Protein splicing.
CA   PTM.
//
ID   Protein synthesis inhibitor.
AC   KW-0652
DE   Protein which blocks the synthesis of proteins (translation) through
DE   various mechanisms, including hydrolysis of cellular tRNA, and
DE   inactivation of the 60S subunits of eukaryotic ribosome.
GO   GO:0017148; negative regulation of translation
HI   Molecular function: Protein synthesis inhibitor.
CA   Molecular function.
//
ID   Protein transport.
AC   KW-0653
DE   Protein involved in the intracellular transport of proteins from one
DE   location to another. All proteins (except the ones synthesized in
DE   mitochondria and plastids) are synthesized on ribosomes in the
DE   cytosol. Most proteins remain in the cytosol. Proteins with a signal
DE   sequence either become plasma membrane components or are exported from
DE   the cell of origin.
GO   GO:0015031; protein transport
HI   Biological process: Transport; Protein transport.
CA   Biological process.
//
ID   Proteoglycan.
AC   KW-0654
DE   Protein containing one or more covalently linked and usually sulfated
DE   glycosaminoglycans, (e.g., chondroitin sulfate, dermatan sulfate,
DE   heparan sulfate, heparin, keratan sulfate). Glycosaminoglycans are
DE   polysaccharides made of repeating disaccharides (usually 40-100
DE   times), which consist of uronic acid (or galactose) and hexosamines.
DE   Aggrecan, for example, is the major component in articular cartilage.
HI   PTM: Glycoprotein; Proteoglycan.
CA   PTM.
//
ID   Proteomics identification.
AC   KW-1267
DE   Protein whose amino acid sequence has been partially or completely
DE   confirmed using publicly available mass spectrometry based data. The
DE   mapping from the mass spectrometry data to UniProtKB sequences may be
DE   subject to quality metrics from both UniProt and the data providers.
HI   Technical term: Proteomics identification.
CA   Technical term.
//
ID   Prothrombin activator.
AC   KW-0655
DE   Protein which activates prothrombin, the inactive precursor of
DE   thrombin. For example, staphylocoagulase, an extracellular protein
DE   produced by Staphylococcus aureus, forms a complex with prothrombin
DE   which can clot fibrinogen without any proteolytic cleavage of
DE   prothrombin.
GO   GO:0010952; positive regulation of peptidase activity
GO   GO:0016504; peptidase activator activity
HI   Molecular function: Prothrombin activator.
CA   Molecular function.
//
ID   Proto-oncogene.
AC   KW-0656
DE   Protein whose normal cellular gene can be converted into a cancer-
DE   promoting oncogene by activating mutations, chromosomal translocation
DE   or DNA amplification. Once activated a proto-oncogene can promote cell
DE   transformation in culture or tumorigenesis in animals. Examples
DE   include the regulatory GTPase HRAS, which is commonly activated by
DE   dominant gain of function point mutations, and the transcription
DE   factor MYC, which can be activated by both chromosomal amplification
DE   and chromosomal translocation.
HI   Disease: Proto-oncogene.
CA   Disease.
//
ID   Proton-gated sodium channel impairing toxin.
AC   KW-1275
DE   Protein which interferes with the function of proton-gated sodium
DE   channels (ASICs) which are membrane proteins forming a channel in a
DE   biological membrane selectively permeable to sodium ions, and open in
DE   response to an increase of extracellular protons. These toxins are
DE   found in various venoms from snakes, spiders, sea anemones, and cone
DE   snails.
HI   Molecular function: Toxin; Ion channel impairing toxin; Proton-gated sodium channel impairing toxin.
CA   Molecular function.
//
ID   Pseudohermaphroditism.
AC   KW-0657
DE   Protein which, if defective, causes pseudohermaphroditism, a condition
DE   in humans in which the individual has gonads of one sex but shows
DE   ambiguous morphologic criteria of sex.
HI   Disease: Pseudohermaphroditism.
CA   Disease.
//
IC   PTM.
AC   KW-9991
DE   Keywords assigned to proteins because their sequences can differ from
DE   the mere translation of their corresponding genes, due to some post-
DE   translational modification.
//
ID   Purine biosynthesis.
AC   KW-0658
DE   Protein involved in the biosynthesis of purine, a nitrogenous
DE   heterocyclic base, e.g. adenine, guanine, hypoxanthine and xanthine.
DE   De novo synthesis involves a complex, energy-expensive pathway that
DE   yields inosine 5'-monophosphate (IMP), a purine ribonucleotide. AMP
DE   and GMP are then formed from IMP in separate pathways. Adenine and
DE   guanine are found in both DNA and RNA. Hypoxanthine and xanthine are
DE   important intermediates in the synthesis and degradation of the purine
DE   nucleotides.
GO   GO:0006164; purine nucleotide biosynthetic process
HI   Biological process: Purine biosynthesis.
CA   Biological process.
//
ID   Purine metabolism.
AC   KW-0659
DE   Protein involved in a biochemical reaction with purines. Purines are
DE   nitrogenous heterocyclic bases, e.g. adenine, guanine, hypoxanthine
DE   and xanthine. The degradation of purines leads to uric acid, which is
DE   excreted in primates, birds and some other animals. In many other
DE   vertebrates uric acid is degraded further to the excretory product
DE   allantoin.
GO   GO:0006144; purine nucleobase metabolic process
HI   Biological process: Purine metabolism.
CA   Biological process.
//
ID   Purine salvage.
AC   KW-0660
DE   Protein involved in the biosynthesis of purine nucleotides from free
DE   purines salvaged from their catabolism. This process is less expensive
DE   energetically and exerts feedback control on the de novo synthesis.
GO   GO:0006166; purine ribonucleoside salvage
HI   Biological process: Purine salvage.
CA   Biological process.
//
ID   Putrescine biosynthesis.
AC   KW-0661
DE   Protein involved in the biosynthesis of putrescine, a foul-smelling
DE   polyamine. This metabolic precursor of the polyamines spermine and
DE   spermidine is often produced during breakdown of some of the amino
DE   acids by bacteria.
SY   1,4-butanediamine biosynthesis; 1,4-diaminobutane biosynthesis.
GO   GO:0009446; putrescine biosynthetic process
HI   Biological process: Putrescine biosynthesis.
CA   Biological process.
//
ID   Pyridine nucleotide biosynthesis.
AC   KW-0662
DE   Protein involved in the biosynthesis of the pyridine nucleotides NAD
DE   and NADP. NAD may be synthesized de novo from aspartate and
DE   dihydroxyacetone phosphate or from tryptophan. NAD may also be
DE   synthesized from nicotinamide or nicotinic acid. NADP is formed via
DE   the phosphorylation of NAD by NAD+ kinase.
GO   GO:0019363; pyridine nucleotide biosynthetic process
HI   Biological process: Pyridine nucleotide biosynthesis.
CA   Biological process.
//
ID   Pyridoxal phosphate.
AC   KW-0663
DE   Protein which uses at least one pyridoxal phosphate as cofactor or
DE   protein required for its synthesis. This coenzyme, derived from
DE   vitamin B6, is important in amino acid metabolism, e.g., in reactions
DE   involving transamination, decarboxylation, racemization, elimination
DE   or replacement.
HI   Ligand: Pyridoxal phosphate.
CA   Ligand.
//
ID   Pyridoxine biosynthesis.
AC   KW-0664
DE   Protein involved in the biosynthesis of pyridoxine, a precursor to the
DE   coenzyme pyridoxal phosphate.
SY   Pyridoxol biosynthesis; Vitamin B6 biosynthesis.
GO   GO:0008615; pyridoxine biosynthetic process
HI   Biological process: Pyridoxine biosynthesis.
CA   Biological process.
//
ID   Pyrimidine biosynthesis.
AC   KW-0665
DE   Protein involved in the biosynthesis of pyrimidine, a nitrogenous
DE   heterocyclic base, e.g. uracil, thymine, cytosine and orotic acid.
DE   Pyrimidines are synthesized from carbamoyl phosphate and aspartate.
DE   Ribose-5-phosphate is then attached to yield pyrimidine
DE   ribonucleotides. Cytosine is found in both DNA and RNA. Uracil is
DE   found only in RNA. Thymine is normally found in DNA. Sometimes tRNA
DE   contains some thymine as well as uracil.
GO   GO:0006221; pyrimidine nucleotide biosynthetic process
HI   Biological process: Pyrimidine biosynthesis.
CA   Biological process.
//
ID   Pyrogen.
AC   KW-0666
DE   Protein producing fever. The major endogenous pyrogen in mammals is
DE   probably interleukin-1, which is produced by activated macrophages and
DE   acts on the hypothalamic thermoregulatory centre.
GO   GO:0001660; fever generation
HI   Biological process: Inflammatory response; Pyrogen.
HI   Molecular function: Pyrogen.
CA   Molecular function.
//
ID   Pyropoikilocytosis.
AC   KW-0668
DE   Protein which, if defective, causes hereditary pyropoikilocytosis
DE   (HPP), a recessively inherited hemolytic anemia characterized by
DE   microspherocytosis, poikilocytosis (deformation of the erythrocytes),
DE   and an unusual thermal sensitivity of red cells. Frequently associated
DE   with abnormalities in alpha-spectrin, one of the principal structural
DE   proteins of the erythrocyte membrane skeleton.
SY   HPP.
HI   Disease: Hereditary hemolytic anemia; Pyropoikilocytosis.
CA   Disease.
//
ID   Pyrrolidone carboxylic acid.
AC   KW-0873
DE   Protein which is posttranslationally modified by the cyclization of a
DE   N-terminal glutamine.
SY   Pyro-Glu; Pyroglutamic acid.
HI   PTM: Pyrrolidone carboxylic acid.
CA   PTM.
//
ID   Pyrrolysine.
AC   KW-0669
DE   Protein which contains a pyrrolysine, a naturally occurring amino acid
DE   so far only found in some archaeal proteins. Pyrrolysine is a lysine
DE   in an amide linkage to (4R,5R)-4-substituted-pyrroline-5-carboxylate.
HI   Coding sequence diversity: Pyrrolysine.
CA   Coding sequence diversity.
//
ID   Pyruvate.
AC   KW-0670
DE   Protein which uses at least one pyruvate as cofactor (pyruvoyl) or
DE   substrate, or protein required for pyruvate synthesis or degradation.
DE   Pyruvate is an intermediate compound in the metabolism of
DE   carbohydrates, proteins and fats.
HI   Ligand: Pyruvate.
CA   Ligand.
//
ID   Queuosine biosynthesis.
AC   KW-0671
DE   Protein involved in the synthesis of queuosine (nucleoside Q), a
DE   modified guanosine derivative found only in tRNAs for aspartic acid,
DE   asparagine, histidine and tyrosine. It can pair with either C or U.
SY   Nucleoside Q biosynthesis.
GO   GO:0008616; queuosine biosynthetic process
HI   Biological process: Queuosine biosynthesis.
CA   Biological process.
//
ID   Quinate metabolism.
AC   KW-0672
DE   Protein involved in the biochemical reactions of quinate. Quinate is
DE   the ionized form of quinic acid which is found in plants, e.g. in
DE   cinchona bark.
GO   GO:0019630; quinate metabolic process
HI   Biological process: Quinate metabolism.
CA   Biological process.
//
ID   Quinone.
AC   KW-0874
DE   Protein which interacts with quinones. Quinones are aromatic
DE   dicarbonyl compounds, where the two carbonyl groups are usually in the
DE   para position. Most naturally occuring quinones contain a long
DE   isoprenoid side chain, and are divided in two major structural groups,
DE   the naphtoquinones and benzoquinones; the number of isoprene units
DE   depends on the organism. These highly hydrophobic molecules are mainly
DE   involved in electron transport, as electron carriers in redox
DE   reactions. For example, ubiquinone (coenzyme Q) and menaquinone
DE   (vitamin K2) are essential components of the respiratory electron
DE   transport chain. Plastoquinone, found in chloroplasts and in
DE   cyanobacteria, functions as one of the carrier molecules of the
DE   electron transport chain in photosynthesis. Phylloquinone (vitamin K1)
DE   is the major form of vitamin K found in plants. Chlorobiumquinone,
DE   demethylmenaquinone, alpha-tocopherolquinone, rhodoquinone,
DE   epoxyubiquinone and caldariellaquinone are other quinones found in
DE   several species.
GO   GO:0048038; quinone binding
HI   PTM: Quinone.
CA   PTM.
//
ID   Quorum sensing.
AC   KW-0673
DE   Protein involved in quorum sensing (QS). QS is a phenomenon whereby
DE   the accumulation of signaling molecules enables a single cell to sense
DE   the number of bacteria (cell density). The bacterial reponse to QS
DE   includes adaptation to availability of nutrients, defence against
DE   other microorganisms which may compete for the same nutrients and the
DE   avoidance of toxic compounds potentially dangerous for the bacteria.
GO   GO:0009372; quorum sensing
HI   Biological process: Quorum sensing.
CA   Biological process.
//
ID   Reaction center.
AC   KW-0674
DE   Protein which is a component of the reaction center, a system
DE   consisting of proteins and cofactors which facilitate light energy and
DE   electron transfer in plants. The system also acts as a light-driven
DE   electron pump across the photosynthetic membrane of photosynthetic
DE   bacteria.
HI   Biological process: Photosynthesis; Reaction center.
HI   Cellular component: Reaction center.
CA   Cellular component.
//
ID   Receptor.
AC   KW-0675
DE   Protein which binds to, or responds to, a ligand with high
DE   specificity.
HI   Molecular function: Receptor.
CA   Molecular function.
//
ID   Redox-active center.
AC   KW-0676
DE   Protein which possesses at least one active center which mediates its
DE   participation in redox reactions, usually via reversible oxidation of
DE   a cysteine residue leading to a cysteine-sulfenic acid that can either
DE   be stabilized, or react with an unmodified cysteine residue and form a
DE   stable but reversible disulfide bond.
HI   Domain: Redox-active center.
CA   Domain.
//
ID   Reference proteome.
AC   KW-1185
DE   Protein which is part of a reference proteome. Reference proteomes are
DE   a subset of proteomes that have been selected either manually or
DE   algorithmically according to a number of criteria to provide a broad
DE   coverage of the tree of life and a representative cross-section of the
DE   taxonomic diversity found within UniProtKB, as well as the proteomes
DE   of well-studied model organisms and other species of interest for
DE   biomedical research.
HI   Technical term: Reference proteome.
CA   Technical term.
//
ID   Repeat.
AC   KW-0677
DE   Protein which contains a stretch of amino acids present in multiple
DE   copies.
HI   Domain: Repeat.
CA   Domain.
//
ID   Repressor.
AC   KW-0678
DE   Protein which interferes with transcription, usually by binding to
DE   specific sites on DNA. Also used for proteins which repress
DE   translation.
HI   Molecular function: Repressor.
CA   Molecular function.
//
ID   Respiratory chain.
AC   KW-0679
DE   Protein involved in respiratory chain. In aerobic respiration
DE   electrons are transferred from metabolites to molecular oxygen through
DE   a series of redox reactions mediated by an electron transport chain.
DE   The resulting free energy is used for the formation of ATP and NAD. In
DE   anaerobic respiration analogous reactions take place with an inorganic
DE   compound other than oxygen as ultimate electron acceptor.
SY   Electron transport chain; Respiration chain.
GO   GO:0070469; respirasome
HI   Biological process: Transport; Electron transport; Respiratory chain.
CA   Biological process.
//
ID   Restriction system.
AC   KW-0680
DE   Protein involved in the restriction system present in many bacteria
DE   and archaea. This defense mechanism is composed principally of a
DE   restriction endonuclease and a methylase. The restriction endonuclease
DE   cuts the invading DNA of viruses (or phages) at a specific recognition
DE   site. The bacterial DNA is protected by the methylase which adds a
DE   methyl group to a specific nucleotide, immediately following
DE   replication, in the same target site as the restriction enzyme.
SY   Restriction-modification system.
GO   GO:0009307; DNA restriction-modification system
HI   Biological process: Restriction system.
CA   Biological process.
//
ID   Restriction-modification system evasion by virus.
AC   KW-1258
DE   Viral anti-restriction protein that counteracts the host restriction-
DE   modification (R-M) system. R-M system is a prokaryotic host defense
DE   system that recognizes incoming unmodified viral DNA and rapidly
DE   degrades it. Methylation and phosphorothioation (S-modification) are
DE   two known modifications used by the host to to label its genomic DNA
DE   as 'self'. Many prokaryotic viruses have evolved antirestriction
DE   strategies such as expressing their own methylase, stimulating the
DE   host methylase so that it confers protection to the virus genome or
DE   shutting down host restriction endonuclease.
GO   GO:0099018; evasion by virus of host restriction-modification system
HI   Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; Restriction-modification system evasion by virus.
CA   Biological process.
//
ID   Retinal protein.
AC   KW-0681
DE   Protein found in the retina or, in the case of bacteriorhodopsin, in
DE   the purple membrane of halobacteria, and which acts as a photoreceptor
DE   and which binds a retinal chromophore.
GO   GO:0007602; phototransduction
HI   Ligand: Chromophore; Retinal protein.
HI   Molecular function: Receptor; Photoreceptor protein; Retinal protein.
CA   Molecular function.
//
ID   Retinitis pigmentosa.
AC   KW-0682
DE   Protein which, if defective, causes retinitis pigmentosa, a hereditary
DE   progressive degeneration of the neuroepithelium of the retina,.
HI   Disease: Retinitis pigmentosa.
CA   Disease.
//
ID   Retinol-binding.
AC   KW-0683
DE   Protein which binds retinol, one of the active form of Vitamin A, a
DE   fat-soluble vitamin derived from carotenes. It is a precursor of
DE   retinal, the light-absorbing group of visual pigments. Vitamin A is
DE   also required for growth.
SY   Vitamin A-binding.
GO   GO:0019841; retinol binding
HI   Ligand: Retinol-binding.
CA   Ligand.
//
ID   Rhamnose metabolism.
AC   KW-0684
DE   Protein involved in the biochemical reactions of rhamnose. Rhamnose is
DE   a methylpentose sugar structurally derived from mannose. The L-isomer
DE   occurs naturally as a component of many plant glycosides and in
DE   lipopolysaccharides of some bacteria with 2 membranes (Gram-negative
DE   bacteria).
SY   6-deoxy-L-mannose metabolism.
GO   GO:0019299; rhamnose metabolic process
HI   Biological process: Rhamnose metabolism.
CA   Biological process.
//
ID   Rhizomelic chondrodysplasia punctata.
AC   KW-0685
DE   Protein which, if defective, causes rhizomelic chondrodysplasia
DE   punctata (RCDP). This lethal autosomal recessive disease is
DE   characterized by proximal limb shortening, severely disturbed
DE   endochondrial bone formation, and intellectual disability. RCDP type 1
DE   (RCDP1) is the classical and most common form. It is a peroxisome
DE   biogenesis disorder caused by mutations in the PEX7 gene, which
DE   encodes the PTS2-receptor peroxin-7. RCDP type 2 (RCDP2) and RCDP type
DE   3 (RCDP3) result from single peroxisomal enzyme deficiencies:
DE   dihydroxyacetone phosphate synthase is deficient in RCDP2 and
DE   dihydroxyacetone phosphate acyltransferase in RCDP3. Both enzymes are
DE   involved in the biosynthesis of plasmalogens.
SY   RCDP.
HI   Disease: Rhizomelic chondrodysplasia punctata.
CA   Disease.
//
ID   Riboflavin biosynthesis.
AC   KW-0686
DE   Protein involved in the synthesis of riboflavin (Vitamin B2), which
DE   consists of ribose attached to a flavin moiety. It is synthesized by
DE   all green plants and most microorganisms and occurs free in milk, the
DE   retina, whey and urine. It is found in most cells as a component of
DE   the coenzymes flavin adenine dinucleotide (FAD) and flavin
DE   mononucleotide (FMN).
SY   Vitamin B2 biosynthesis.
GO   GO:0009231; riboflavin biosynthetic process
HI   Biological process: Riboflavin biosynthesis.
CA   Biological process.
//
ID   Ribonucleoprotein.
AC   KW-0687
DE   Proteins conjugated with ribonucleic acid (RNA). Ribonucleoprotein are
DE   involved in a wide range of cellular processes. Besides ribosomes, in
DE   eukaryotic cells both initial RNA transcripts in the nucleus (hnRNA)
DE   and cytoplasmic mRNAs exist as complexes with specific sets of
DE   proteins. Processing (splicing) of the former is carried out by small
DE   nuclear RNPs (snRNPs). Other examples are the signal recognition
DE   particle responsible for targetting proteins to endoplasmic reticulum
DE   and a complex involved in termination of transcription.
GO   GO:1990904; ribonucleoprotein complex
HI   Molecular function: Ribonucleoprotein.
CA   Molecular function.
//
ID   Ribosomal frameshifting.
AC   KW-0688
DE   Protein produced by programmed ribosomal frameshifting, a
DE   translational recoding mechanism which causes the ribosome to alter
DE   its reading of the genetic code to produce either an alternative
DE   product not directly encoded by the mRNA or two or more different
DE   isoforms.
HI   Coding sequence diversity: Ribosomal frameshifting.
CA   Coding sequence diversity.
//
ID   Ribosomal protein.
AC   KW-0689
DE   Protein of the ribosome, large ribonucleoprotein particles where the
DE   translation of messenger RNA (mRNA) into protein occurs. They are both
DE   free in the cytoplasm and attached to membranes of eukaryotic and
DE   prokaryotic cells. Ribosomes are also present in all plastids and
DE   mitochondria, where they translate organelle-encoded mRNA.
GO   GO:0005840; ribosome
HI   Molecular function: Ribonucleoprotein; Ribosomal protein.
CA   Molecular function.
//
ID   Ribosomal skipping.
AC   KW-1197
DE   Protein produced by ribosomal 'skipping', in which a specific sequence
DE   in the nascent peptide chain prevents the ribosome from creating the
DE   peptide bond with the next proline. Nevertheless, translation
DE   continues and gives rise to a second chain. This mechanism results in
DE   apparent co-translational cleavage of the polyprotein. This process is
DE   induced by a '2A-like', or CHYSEL (cis-acting hydrolase element)
DE   sequence.
HI   Coding sequence diversity: Ribosomal skipping.
CA   Coding sequence diversity.
//
ID   Ribosome biogenesis.
AC   KW-0690
DE   Protein involved in the synthesis of ribosomes.
GO   GO:0042254; ribosome biogenesis
HI   Biological process: Ribosome biogenesis.
CA   Biological process.
//
ID   RNA editing.
AC   KW-0691
DE   Protein which is derived from an RNA which has been modified by RNA
DE   editing, a process that changes the nucleotide sequence of an RNA from
DE   that of the DNA template encoding it. RNA editing can be due to
DE   nucleotide conversion, insertion and/or deletion.
HI   Coding sequence diversity: RNA editing.
CA   Coding sequence diversity.
//
ID   RNA repair.
AC   KW-0692
DE   Protein involved in the repair of RNA, the various biochemical
DE   processes by which damaged RNA can be restored.
GO   GO:0042245; RNA repair
HI   Biological process: RNA repair.
CA   Biological process.
//
ID   RNA suppression of termination.
AC   KW-1159
DE   Protein which is derived from an mRNA by suppression of termination, a
DE   process in which a tRNA misreads a termination codon thereby producing
DE   a longer protein. RNA secondary structure after the stop codon plays a
DE   role in this process. The efficiency of suppression of termination is
DE   about 10% for most viruses. Termination suppression is involved in
DE   polyprotein synthesis of gamma and epsilon retroviruses, as well as
DE   all togaviridae.
HI   Coding sequence diversity: RNA suppression of termination.
CA   Coding sequence diversity.
//
ID   RNA termination-reinitiation.
AC   KW-1158
DE   Protein which is derived from an mRNA by termination-reinitiation, a
DE   process in which ribosomes translate the upstream ORF but following
DE   termination, a proportion of 40S subunits remain tethered to the mRNA
DE   and reinitiates at the start codon of the downstream ORF to another
DE   open reading frame. Termination-reinitiation operates in animals and
DE   yeast translational systems.
HI   Coding sequence diversity: RNA termination-reinitiation.
CA   Coding sequence diversity.
//
ID   RNA translational shunting.
AC   KW-1156
DE   Protein which is derived from an mRNA by translational shunting, a
DE   process in which ribosomes are loaded onto mRNA at the 5'-cap
DE   structure, start scanning for a short distance before bypassing the
DE   large internal leader region and initiating at a downstream start
DE   site. Shunting operates in plants, animals, and yeast translational
DE   systems, both in vivo and in vitro.
HI   Coding sequence diversity: RNA translational shunting.
CA   Coding sequence diversity.
//
ID   RNA-binding.
AC   KW-0694
DE   Protein which binds to RNA.
GO   GO:0003723; RNA binding
HI   Molecular function: RNA-binding.
CA   Molecular function.
//
ID   RNA-directed DNA polymerase.
AC   KW-0695
DE   Enzyme (EC 2.7.7.49) which synthesizes (-)DNA on a (+)RNA template.
DE   They are encoded by the pol gene of retroviruses and by certain
DE   retrovirus-like elements.
SY   Reverse transcriptase.
GO   GO:0003964; RNA-directed DNA polymerase activity
HI   Molecular function: Transferase; Nucleotidyltransferase; RNA-directed DNA polymerase.
CA   Molecular function.
//
ID   RNA-directed RNA polymerase.
AC   KW-0696
DE   Enzyme (EC 2.7.7.48) which synthesizes (+)RNA on a (-)RNA template.
DE   They are encoded by many viruses.
GO   GO:0003968; RNA-dependent RNA polymerase activity
HI   Molecular function: Transferase; Nucleotidyltransferase; RNA-directed RNA polymerase.
CA   Molecular function.
//
ID   RNA-mediated gene silencing.
AC   KW-0943
DE   Protein involved in RNA-mediated gene silencing. This term describes a
DE   number of related processes which use 21- to 25-nucleotide RNAs to
DE   repress the expression of specific target genes. These processes
DE   include the post-transcriptional regulation of mRNA by either RNA
DE   interference (RNAi) or endogenously encoded microRNAs (miRNAs) and the
DE   transcriptional regulation of mRNA by RNAi-mediated chromatin
DE   silencing. RNAi is generally triggered by the presence of dsRNA
DE   produced by bidirectional transcription or by the transcription of an
DE   inverted repeat or hairpin sequence. dsRNA is processed into small
DE   interfering RNAs (siRNAs) of around 21 nucleotide which are then
DE   incorporated into the RNA-induced silencing complex (RISC), which
DE   cleaves mRNAs with sequences fully complementary to the siRNA. miRNAs
DE   differ from siRNAs principally in their biogenesis. miRNA genes encode
DE   precursors with complex hairpin structures which are processed by
DE   endonucleolytic cleavage to form mature miRNAs. Like siRNAs, miRNAs
DE   function in RISC-like complexes. Animal miRNAs generally inhibit
DE   translation of target mRNAs following imperfect base pairing to the
DE   3'-untranslated region (3'-UTR), while most plant miRNAs show nearly
DE   precise complementarity to coding regions of target mRNAs and trigger
DE   mRNA degradation similar to siRNAs. Finally, in RNAi-mediated
DE   chromatin silencing, siRNAs derived from repeat element transcripts
DE   are incorporated into the nuclear RNAi-induced initiator of
DE   transcriptional silencing complex (RITS), where they guide chromatin
DE   modifications such as histone methylation which lead to
DE   transcriptional silencing.
SY   Cosuppression; Post-transcriptional gene silencing; PTGS; Quelling;
SY   RNAi; RNA interference; TGS; Transcriptional gene silencing.
GO   GO:0031047; regulatory ncRNA-mediated gene silencing
HI   Biological process: RNA-mediated gene silencing.
CA   Biological process.
//
ID   Rotamase.
AC   KW-0697
DE   Enzyme (EC 5.2.1.8) which accelerates the folding of proteins by
DE   catalyzing the cis-trans isomerization of proline imidic peptide bonds
DE   in oligopeptides.
GO   GO:0003755; peptidyl-prolyl cis-trans isomerase activity
HI   Molecular function: Isomerase; Rotamase.
CA   Molecular function.
//
ID   rRNA processing.
AC   KW-0698
DE   Protein involved in the processing of the primary rRNA transcript to
DE   yield a functional rRNA. This includes the cleavage and other
DE   modifications.
SY   Ribosomal RNA processing.
GO   GO:0006364; rRNA processing
HI   Biological process: rRNA processing.
CA   Biological process.
//
ID   rRNA-binding.
AC   KW-0699
DE   Protein which binds to ribosomal RNA.
GO   GO:0019843; rRNA binding
HI   Molecular function: RNA-binding; rRNA-binding.
CA   Molecular function.
//
ID   Ryanodine-sensitive calcium-release channel impairing toxin.
AC   KW-1219
DE   Protein which interferes with the function of ryanodine receptors
DE   (Ryr) which are a class of intracellular calcium channels in various
DE   forms of excitable animal tissue like muscles and neurons. These
DE   toxins are mostly found in scorpion and snake venom.
SY   Ryanodine receptor inhibitor; Ryr inhibitor.
HI   Molecular function: Toxin; Ion channel impairing toxin; Calcium channel impairing toxin; Ryanodine-sensitive calcium-release channel impairing toxin.
CA   Molecular function.
//
ID   S-adenosyl-L-methionine.
AC   KW-0949
DE   Protein which binds at least one S-adenosyl-L-methionine (SAM), or
DE   protein whose function is SAM-dependent. S-adenosyl-L-methionine, a
DE   conjugate of the nucleotide adenosine and the amino acid methionine,
DE   is a substrate/cofactor in numerous enzyme-catalyzed reactions.
DE   Enzymatic reactions that involve interactions of proteins with S-
DE   adenosyl-L-methionine include transfer of methyl, thiomethyl,
DE   aminoalkyl and adenosyl groups. It not only provides methyl groups to
DE   be transferred in numerous biological reactions, but also acts as a
DE   precursor in the biosynthesis of polyamines and metal ion chelating
DE   compounds. It is also a source of catalytic 5'-deoxyadenosyl radicals
DE   produced as reaction intermediates by a superfamily of radical
DE   enzymes. It is also involved in decarboxylation reactions.
SY   AdoMet; AdoMet radical; radical S- adenosylmethionine;
SY   S-adenosylmethionine; S-adenosyl methionine; S-adenosyl-methionine;
SY   SAM; SAM radical.
HI   Ligand: S-adenosyl-L-methionine.
CA   Ligand.
//
ID   S-layer.
AC   KW-0701
DE   Protein of the paracrystalline mono-layered assembly which coats the
DE   surface of bacteria and archaea.
GO   GO:0030115; S-layer
HI   Cellular component: Secreted; Cell wall; S-layer.
CA   Cellular component.
//
ID   S-nitrosylation.
AC   KW-0702
DE   Protein which is posttranslationally modified by the attachment of a
DE   nitric oxide group on the sulfur atom of one or more cysteine
DE   residues.
HI   PTM: S-nitrosylation.
CA   PTM.
//
ID   Sarcoplasmic reticulum.
AC   KW-0703
DE   Protein found in a special form of agranular reticulum located in the
DE   sarcoplasm of striated muscle. The agranular reticulum comprises and
DE   comprising a system of smooth-surfaced tubules which form a plexus
DE   around each myofibril.
GO   GO:0016529; sarcoplasmic reticulum
HI   Cellular component: Sarcoplasmic reticulum.
CA   Cellular component.
//
ID   Schiff base.
AC   KW-0704
DE   Enzyme which forms a covalent enzyme-substrate complex, a Schiff's
DE   base or ketimine between the amino group of a lysine residue of the
DE   enzyme and the carbonyl group of the substrate.
HI   Ligand: Schiff base.
CA   Ligand.
//
ID   Schizophrenia.
AC   KW-1211
DE   Protein which, if defective, is associated with schizophrenia, a
DE   multifactorial psychotic disorder characterized by disturbances in the
DE   form and content of thought (e.g. delusions, hallucinations), in mood
DE   (e.g. inappropriate affect), in sense of self and relationship to the
DE   external world (e.g. loss of ego boundaries, withdrawal), and in
DE   behavior (e.g bizarre or apparently purposeless behavior).
SY   SCZD.
HI   Disease: Schizophrenia.
CA   Disease.
//
ID   SCID.
AC   KW-0705
DE   Protein which, if defective, causes severe combined (or congenital)
DE   immunodeficiency disease. An heterogeneous group of inherited
DE   disorders characterized by gross functional impairment of the immune
DE   system.
SY   Severe combined immunodeficiency disease;
SY   Severe congenital immunodeficiency disease.
HI   Disease: SCID.
CA   Disease.
//
ID   Secreted.
AC   KW-0964
DE   Protein secreted into the cell surroundings.
GO   GO:0005576; extracellular region
HI   Cellular component: Secreted.
CA   Cellular component.
//
ID   Seed storage protein.
AC   KW-0708
DE   Protein required for the development or growth of seeds.
GO   GO:0045735; nutrient reservoir activity
HI   Molecular function: Storage protein; Seed storage protein.
CA   Molecular function.
//
ID   Segmentation polarity protein.
AC   KW-0709
DE   Protein involved in the division of the embryo into segments and which
DE   is responsible for determining the internal polarity of the segments.
DE   Segment polarity gene mutations are lethal and change the pattern and,
DE   often the polarity, of every segment.
SY   Segment polarity protein.
GO   GO:0007367; segment polarity determination
HI   Molecular function: Developmental protein; Segmentation polarity protein.
CA   Molecular function.
//
ID   Selenium.
AC   KW-0711
DE   Protein which binds at least one selenium, or protein whose function
DE   is selenium-dependent. Selenium is a nonmetallic trace element,
DE   chemical symbol Se.
HI   Ligand: Selenium.
WW   https://www.webelements.com/selenium/
CA   Ligand.
//
ID   Selenocysteine.
AC   KW-0712
DE   Protein which contains a selenocysteine, a naturally occurring amino
DE   acid in both eukaryotic and prokaryotic organisms.
SY   3-selenyl-L-alanine.
HI   Coding sequence diversity: Selenocysteine.
CA   Coding sequence diversity.
//
ID   Self-incompatibility.
AC   KW-0713
DE   Protein involved in the self-incompatibility system, which is to say
DE   the inability of pollen grains to fertilize flowers of the same plant
DE   or a close relative. This mechanism ensures out-breeding in certain
DE   plant species.
GO   GO:0060320; rejection of self pollen
HI   Biological process: Self-incompatibility.
CA   Biological process.
//
ID   Senior-Loken syndrome.
AC   KW-0980
DE   Protein which, if defective, causes Senior-Loken syndrome, a
DE   genetically and clinically heterogeneous disease characterized by
DE   nephronophthisis and retinal abnormalities manifesting as congenital
DE   retinal blindness or retinitis pigmentosa. Senior-Loken syndrome can
DE   be associated with manifestations such as cerebellar ataxia and
DE   skeletal abnormalities including cone epiphyses.
SY   Juvenile nephronophthisis with Leber amaurosis; Loken-Senior syndrome;
SY   Renal dysplasia and retinal aplasia; Renal-retinal syndrome;
SY   Senior-Loeken syndrome.
HI   Disease: Ciliopathy; Senior-Loken syndrome.
CA   Disease.
//
ID   Sensory transduction.
AC   KW-0716
DE   Protein involved in sensory transduction, the process by which a cell
DE   converts an extracellular signal, such as light, taste, sound, touch
DE   or smell, into electric signals.
GO   GO:0050896; response to stimulus
HI   Biological process: Sensory transduction.
CA   Biological process.
//
ID   Septation.
AC   KW-0717
DE   Protein involved in septation, the formation of a separating wall
DE   (septum) between daughter cells during cell division.
GO   GO:0000917; division septum assembly
HI   Biological process: Cell cycle; Cell division; Septation.
CA   Biological process.
//
ID   Serine biosynthesis.
AC   KW-0718
DE   Protein involved in the synthesis of the amino acid serine, a
DE   constituent of proteins and precursor of several metabolites,
DE   including cysteine, glycine and choline. Serine is mostly formed from
DE   3-phosphoglycerate in a 3-step reaction pathway.
GO   GO:0006564; L-serine biosynthetic process
HI   Biological process: Amino-acid biosynthesis; Serine biosynthesis.
CA   Biological process.
//
ID   Serine esterase.
AC   KW-0719
DE   Enzyme which catalyzes the hydrolysis of esters and is characterized
DE   by a catalytically active serine residue in its active site.
GO   GO:0052689; carboxylic ester hydrolase activity
HI   Molecular function: Hydrolase; Serine esterase.
CA   Molecular function.
//
ID   Serine protease.
AC   KW-0720
DE   Proteolytic enzyme with a serine residue (Ser) in its active site. The
DE   reactivity of the serine residue is ensured by the vicinity of a
DE   histidine and an aspartate residue (catalytic triad), all three
DE   residues are required for the charge relay system to take place.
SY   Serine endopeptidase; Serine peptidase; Serine proteinase.
GO   GO:0008236; serine-type peptidase activity
HI   Molecular function: Hydrolase; Protease; Serine protease.
CA   Molecular function.
//
ID   Serine protease homolog.
AC   KW-0721
DE   Protein which is related to serine proteases but seems to have no
DE   proteolytic activity.
HI   Molecular function: Serine protease homolog.
CA   Molecular function.
//
ID   Serine protease inhibitor.
AC   KW-0722
DE   Protein which inhibits serine proteases, a group of proteolytic
DE   enzymes which are characterized by a catalytically active serine
DE   residue in their active site.
SY   Serine endopeptidase inhibitor; Serine peptidase inhibitor;
SY   Serine proteinase inhibitor.
GO   GO:0004867; serine-type endopeptidase inhibitor activity
HI   Molecular function: Protease inhibitor; Serine protease inhibitor.
CA   Molecular function.
//
ID   Serine/threonine-protein kinase.
AC   KW-0723
DE   Protein which catalyzes the phosphorylation of serine or threonine
DE   residues on target proteins by using ATP as phosphate donor. Such
DE   phosphorylation may cause changes in the function of the target
DE   protein. Protein kinases share a conserved catalytic core common to
DE   both serine/ threonine and tyrosine protein kinases.
GO   GO:0004674; protein serine/threonine kinase activity
HI   Molecular function: Transferase; Kinase; Serine/threonine-protein kinase.
CA   Molecular function.
//
ID   Serotonin biosynthesis.
AC   KW-0724
DE   Protein involved in the synthesis of the biochemical messenger and
DE   regulator serotonin which is formed by the hydroxylation and
DE   subsequent decarboxylation of L-tryptophan. In humans, serotonin
DE   mediates several important physiological functions, including
DE   neurotransmission, gastrointestinal motility, hemostasis and
DE   cardiovascular integrity.
SY   5-HT; 5-hydroxytryptamine.
GO   GO:0042427; serotonin biosynthetic process
HI   Biological process: Serotonin biosynthesis.
CA   Biological process.
//
ID   Sexual differentiation.
AC   KW-0726
DE   Protein involved in both the determination of cells to become sexual
DE   tissue in embryonic development and in the process by which male and
DE   female tissue becomes structurally and functionally specialized during
DE   embryonic development.
GO   GO:0007548; sex differentiation
HI   Biological process: Differentiation; Sexual differentiation.
CA   Biological process.
//
ID   SH2 domain.
AC   KW-0727
DE   Protein with at least one Src homology 2 (SH2) domain. The SH2 domain,
DE   which was first identified in the oncoproteins Src and Fps, is about
DE   100 amino-acid residues long. It functions as a regulatory module of
DE   intracellular signaling cascades by interacting with high affinity to
DE   phosphotyrosine-containing target peptides in a sequence-specific and
DE   strictly phosphorylation-dependent manner.
HI   Domain: SH2 domain.
CA   Domain.
//
ID   SH3 domain.
AC   KW-0728
DE   Protein with at least one Src homology 3 (SH3) domain It is a small
DE   protein domain of about 50 amino-acid residues first identified as a
DE   conserved sequence in the non-catalytic part of several cytoplasmic
DE   protein tyrosine kinases (e.g. Src). Since then, it has been found in
DE   a great variety of other intracellular or membrane-associated
DE   proteins. The SH3 module might mediate the assembly of specific
DE   protein complexes by binding to proline-rich peptides.
HI   Domain: SH3 domain.
CA   Domain.
//
ID   SH3-binding.
AC   KW-0729
DE   Protein with at least one SH3-binding site and which mediates the
DE   binding to the Src homology 3 (SH3) region, a module present in a
DE   large group of proteins, including cytoskeletal elements and signaling
DE   proteins.
GO   GO:0017124; SH3 domain binding
HI   Domain: SH3-binding.
CA   Domain.
//
ID   Short QT syndrome.
AC   KW-0940
DE   Protein which, if defective, causes short QT syndrome, a heart
DE   disorder characterized by the presence of a short QT interval on ECG,
DE   associated with syncope, palpitations, cardiac arrest and sudden
DE   death.
SY   SQTS.
HI   Disease: Short QT syndrome.
CA   Disease.
//
ID   Sialic acid.
AC   KW-0730
DE   Protein with at least one sialic acid. The term "sialic acid" refers
DE   to the group of sugars including neuraminic acid and its derivatives,
DE   not to a specific sugar. They are widely distributed in bacteria and
DE   animal tissue as components of polysaccharides, glycoproteins and
DE   glycolipids. They are typically the terminal residues on cell surface
DE   oligosaccharides.
HI   PTM: Glycoprotein; Sialic acid.
HI   Ligand: Sialic acid.
CA   Ligand.
//
ID   Sigma factor.
AC   KW-0731
DE   Initiation factors that bind to bacterial DNA-dependent RNA
DE   polymerases and promote attachment to specific initiation sites on
DE   DNA. Following attachment, the sigma factor is released.
GO   GO:0006355; regulation of DNA-templated transcription
GO   GO:0016987; sigma factor activity
HI   Biological process: Transcription; Transcription regulation; Sigma factor.
HI   Molecular function: Sigma factor.
CA   Molecular function.
//
ID   Signal.
AC   KW-0732
DE   Protein which has a signal sequence, a peptide usually present at the
DE   N-terminus of proteins and which is destined to be either secreted or
DE   part of membrane components. The signal sequence (usually 20-30 amino
DE   acids long) interacts with the signal recognition particle and directs
DE   the ribosome to the endoplasmic reticulum where co-translational
DE   insertion takes place. Signal peptides are highly hydrophobic but have
DE   some positively charged amino acids. Normally, the signal sequence is
DE   removed from the growing peptide chain by specific peptidases (signal
DE   peptidases) located on the cisternal face of the endoplasmic
DE   reticulum.
SY   Signal peptide; Signal sequence.
HI   Domain: Signal.
CA   Domain.
//
ID   Signal recognition particle.
AC   KW-0733
DE   Protein of the signal recognition particle (SRP) which is a cytosolic
DE   ribonucleoprotein complex that induces elongation arrest of nascent
DE   presecretory and membrane proteins until the ribosome becomes
DE   associated with the rough endoplasmic reticulum or the prokaryotic
DE   cytoplasmic membrane.
GO   GO:0005786; signal recognition particle, endoplasmic reticulum targeting
HI   Molecular function: Ribonucleoprotein; Signal recognition particle.
HI   Cellular component: Signal recognition particle.
CA   Cellular component.
//
ID   Signal transduction inhibitor.
AC   KW-0734
DE   Protein which inhibits signal transduction, the process by which
DE   extracellular signals induce intracellular responses. Usually a
DE   hormone or neurotransmitter binds to a cell surface receptor which is
DE   coupled to a second messenger system, such as that involving cAMP, or
DE   to an ion channel. The final downstream consequence of signal
DE   transduction is a change in the cell's function, such as a
DE   modification in glucose uptake or in cell division. Such a change may
DE   be the result of an activation or an inhibition event.
GO   GO:0009968; negative regulation of signal transduction
HI   Molecular function: Signal transduction inhibitor.
CA   Molecular function.
//
ID   Signal-anchor.
AC   KW-0735
DE   Single-pass transmembrane protein (type II, III, and IV) possessing a
DE   membrane-spanning domain which targets the protein to the ER membrane.
DE   Typical features of signal-anchors are the presence of positively
DE   charged residues on the amino terminal side followed by an apolar
DE   segment of approx. 20 residues. The amino-acid composition is not very
DE   different from typical signal sequences.
HI   Domain: Transmembrane; Signal-anchor.
CA   Domain.
//
ID   Signalosome.
AC   KW-0736
DE   Protein of the signalosome complex, a multifunctional protein complex
DE   essential for development and possibly involved in the regulation of
DE   protein degradation.
SY   COP9 complex; COP9 signalosome; COP9 signalosome complex; CSN.
GO   GO:0008180; COP9 signalosome
HI   Cellular component: Signalosome.
CA   Cellular component.
//
ID   Silk protein.
AC   KW-0737
DE   Protein found in silk, a strong, soft, lustrous fiber made of fibroin,
DE   a structural protein consisting almost entirely of stacked
DE   antiparallel beta pleated sheets. It is produced by certain spiders
DE   and by the larvae of certain bombycine moths.
HI   Molecular function: Silk protein.
CA   Molecular function.
//
ID   Sodium.
AC   KW-0915
DE   Protein which binds at least one sodium, or protein whose function is
DE   sodium-dependent. Sodium is an alkali metal, chemical symbol Na.
HI   Ligand: Sodium.
WW   https://www.webelements.com/sodium/
CA   Ligand.
//
ID   Sodium channel.
AC   KW-0894
DE   Protein which is part of a cation channel permeable for sodium found
DE   in the plasma membrane and in intracellular membranes. Sodium channels
DE   have been classified according to their gating mechanisms, which may
DE   depend on changes in the transmembrane electric field (voltage-gated
DE   sodium channels) or not (non-voltage-gated sodium channels, e.g.
DE   degenerins which are permeable also to lithium and potassium).
DE   Voltage-gated sodium channels, by opening in response to membrane
DE   depolarization, allow sodium entry and thus the propagation of
DE   depolarization along the plasma membrane of nerve, muscle and other
DE   electrically excitable cells. They play a role in different processes
DE   such as sensation, emotions, thought and movement. Another class of
DE   sodium channel is the degenerin/epithelial sodium channel (ENaC)
DE   superfamily, which is a group of proteins involved in diverse
DE   biological processes, including sodium homeostasis, salt taste,
DE   nociception, pain transduction, touch sensation and
DE   mechanotransduction.
GO   GO:0005272; sodium channel activity
HI   Molecular function: Ion channel; Sodium channel.
HI   Biological process: Transport; Ion transport; Sodium transport; Sodium channel.
HI   Ligand: Sodium; Sodium channel.
CA   Molecular function.
//
ID   Sodium transport.
AC   KW-0739
DE   Protein involved in the movement of sodium ions across energy-
DE   transducing cell membranes. Primary active sodium transport is coupled
DE   to an energy-yielding chemical reaction such as ATP hydrolysis.
DE   Secondary active transport utilizes the voltage and ion gradients
DE   produced by the primary transport to drive the cotransport of other
DE   ions or molecules. These may be transported in the same (symport) or
DE   opposite (antiport) direction.
GO   GO:0006814; sodium ion transport
HI   Biological process: Transport; Ion transport; Sodium transport.
HI   Ligand: Sodium; Sodium transport.
CA   Biological process.
//
ID   Sodium/potassium transport.
AC   KW-0740
DE   Protein involved in the active transport system which simultaneously
DE   moves two potassium ions into the cell and three sodium ions out of
DE   the cell.
GO   GO:0006813; potassium ion transport
GO   GO:0006814; sodium ion transport
HI   Ligand: Potassium; Sodium/potassium transport.
HI   Biological process: Transport; Ion transport; Potassium transport; Sodium/potassium transport.
HI   Biological process: Transport; Ion transport; Sodium transport; Sodium/potassium transport.
HI   Ligand: Sodium; Sodium/potassium transport.
CA   Biological process.
//
ID   SOS mutagenesis.
AC   KW-0741
DE   Protein involved in the DNA repair system also known as error-prone
DE   repair in which apurinic DNA molecules are repaired by the
DE   incorporation of a base that may be the wrong base but that permits
DE   replication.
HI   Biological process: DNA damage; SOS response; SOS mutagenesis.
CA   Biological process.
//
ID   SOS response.
AC   KW-0742
DE   Protein involved in an SOS response, which implies the coordinated
DE   activation of diverse unlinked genes (ca. 20 in E.coli) involved in
DE   DNA repair, error-prone DNA replication, etc., in response to severe
DE   DNA damage. The SOS system is tightly regulated and its expression
DE   only occurs when absolutely required.
SY   SOS repair system; SOS response system; SOS system.
GO   GO:0009432; SOS response
HI   Biological process: DNA damage; SOS response.
CA   Biological process.
//
ID   Spermatogenesis.
AC   KW-0744
DE   Protein involved in sperm cell development. A process whereby
DE   primordial germ cells form mature spermatozoa, which includes
DE   spermatocytogenesis (successive mitotic and meiotic divisions) and
DE   spermiogenesis (a metamorphic change).
GO   GO:0007283; spermatogenesis
HI   Biological process: Differentiation; Spermatogenesis.
WW   https://en.wikipedia.org/wiki/Spermatogenesis
CA   Biological process.
//
ID   Spermidine biosynthesis.
AC   KW-0745
DE   Protein involved in the synthesis of spermidine, a widely distributed
DE   polyamine which acts as a growth factor for some microorganisms and
DE   stabilizes the membrane structure of bacteria, as well as the
DE   structure of ribosomes, some viruses and the DNA of many organisms.
SY   N-(3-aminopropyl)-1,4-butanediamine.
GO   GO:0008295; spermidine biosynthetic process
HI   Biological process: Spermidine biosynthesis.
CA   Biological process.
//
ID   Sphingolipid metabolism.
AC   KW-0746
DE   Protein involved in the biochemical reactions of sphingolipids. These
DE   are structurally complex saponifiable lipids which contain a fatty
DE   acid covalently linked to the amino alcohol sphingosine (or a related
DE   base), as backbone structure, to which is attached a polar head group.
DE   They are synthesized in the Golgi complex and are important membrane
DE   components in both plant and animal cells. They are present in
DE   especially large amounts in brain and nerve tissue.
GO   GO:0006665; sphingolipid metabolic process
HI   Biological process: Lipid metabolism; Sphingolipid metabolism.
CA   Biological process.
//
ID   Spinocerebellar ataxia.
AC   KW-0950
DE   Protein which, if defective, causes autosomal dominant spinocerebellar
DE   ataxia, a clinically and genetically heterogeneous group of autosomal
DE   dominant cerebellar ataxias (ADCA). Patients show progressive
DE   incoordination of gait and often poor coordination of hands, speech
DE   and eye movements. Spinocerebellar ataxia is caused by degeneration of
DE   the cerebellum with variable involvement of the brainstem and spinal
DE   cord. Three clinical types are distinguished, according to the extent
DE   of extra-cerebellar signs: cerebellar ataxia with additional features
DE   like optic atrophy, ophthalmoplegia, bulbar and extrapyramidal signs,
DE   peripheral neuropathy and dementia, is known as ADCA type I;
DE   cerebellar ataxia with retinal degeneration and pigmentary macular
DE   dystrophy is defined as ADCA type II; pure cerebellar ataxia without
DE   additional signs is classified as ADCA type III.
SY   ADCA; Autosomal dominant cerebellar ataxia;
SY   Autosomal dominant spinocerebellar ataxia;
SY   Olivopontocerebellar atrophy; OPCA; SCA; Spinocerebellar atrophy.
HI   Disease: Neurodegeneration; Spinocerebellar ataxia.
CA   Disease.
//
ID   Spliceosome.
AC   KW-0747
DE   Protein of the spliceosome, a very large complex of small nuclear
DE   RNA/protein particles (snRNPs) which assemble with pre-mRNA to achieve
DE   RNA splicing.
GO   GO:0005681; spliceosomal complex
HI   Biological process: mRNA processing; mRNA splicing; Spliceosome.
HI   Cellular component: Spliceosome.
CA   Cellular component.
//
ID   Sporozoite.
AC   KW-0748
DE   Protein expressed in the sporozoite stage which is the infectious
DE   stage of the malaria parasite. Malaria is transmitted by mosquitos to
DE   the vertebrate host. This term also refers to the motile infectious
DE   stage of other sporozoans (parasitic protozoans).
HI   Developmental stage: Sporozoite.
CA   Developmental stage.
//
ID   Sporulation.
AC   KW-0749
DE   Protein involved in the production of spores, i.e. sporulation.
GO   GO:0030435; sporulation resulting in formation of a cellular spore
HI   Biological process: Sporulation.
CA   Biological process.
//
ID   Starch biosynthesis.
AC   KW-0750
DE   Protein involved in the synthesis of starch, the carbohydrate storage
DE   of plants. Starch consists of amylose (a linear alpha(1-4)-glucan) and
DE   amylopectin (an alpha(1-4)-glucan with alpha(1-6)-branch points).
DE   Starch (glucans and amylopectins) is synthesised via the ADP-glucose
DE   pathway by three key enzymes: ADP-glucose pyrophosphorylase, starch
DE   synthases and starch branching enzymes. The randomly branched glucan
DE   molecules are then specifically debranched via a debranching enzyme in
DE   order to produce amylopectins. Amylopectins are branched in highly
DE   ordered clusters and are crystalline in nature, but also contain
DE   covalently bound phosphate.
GO   GO:0019252; starch biosynthetic process
HI   Biological process: Starch biosynthesis.
CA   Biological process.
//
ID   Stargardt disease.
AC   KW-0751
DE   Protein which, if defective, causes Stargardt disease (SD). SD is a
DE   hereditary degeneration of the macula lutea occurring between the ages
DE   of six and twenty, marked by rapid loss of visual accuity and by
DE   abnormal appearance and pigmentation of the macular aerea.
SY   SD.
HI   Disease: Stargardt disease.
CA   Disease.
//
ID   Steroid biosynthesis.
AC   KW-0752
DE   In vivo synthesis of steroids (steroidogenesis), a large group of
DE   complex polycyclic lipids that consist of a 17-carbon ring system.
DE   Examples are bile acids, sterols, various hormones and saponins.
GO   GO:0006694; steroid biosynthetic process
HI   Biological process: Lipid metabolism; Lipid biosynthesis; Steroid biosynthesis.
CA   Biological process.
//
ID   Steroid metabolism.
AC   KW-0753
DE   Protein involved in the biochemical reactions of steroids. Steroids
DE   are a large group of complex tetracyclic lipids that consist of a 17-
DE   carbon-ring system. Examples are bile acids, sterols, various hormones
DE   and saponins.
GO   GO:0008202; steroid metabolic process
HI   Biological process: Lipid metabolism; Steroid metabolism.
CA   Biological process.
//
ID   Steroid-binding.
AC   KW-0754
DE   Protein which binds steroids.
GO   GO:0005496; steroid binding
HI   Ligand: Lipid-binding; Steroid-binding.
CA   Ligand.
//
ID   Steroidogenesis.
AC   KW-0755
DE   Biosynthesis of steroid hormones which takes place in the mitochondria
DE   of the adrenal cortex. Oxidation of two adjacent carbon atoms in the
DE   side chain of cholesterol, followed by the cleavage between them,
DE   produces pregnenolone, a precursor of all other steroid hormones. The
DE   hydroxylation and oxygenation reactions are catalyzed by cytochrome
DE   P450 and mixed-functions oxidases that use NADPH and O2.
GO   GO:0006694; steroid biosynthetic process
HI   Biological process: Steroidogenesis.
CA   Biological process.
//
ID   Sterol biosynthesis.
AC   KW-0756
DE   Protein involved in the synthesis of sterols, any steroid alcohol
DE   which are components of cell membranes in plants, animals and fungi.
GO   GO:0016126; sterol biosynthetic process
HI   Biological process: Lipid metabolism; Lipid biosynthesis; Steroid biosynthesis; Sterol biosynthesis.
HI   Biological process: Lipid metabolism; Steroid metabolism; Sterol metabolism; Sterol biosynthesis.
CA   Biological process.
//
ID   Sterol metabolism.
AC   KW-1207
DE   Protein involved in the metabolism of sterols, any steroid alcohol.
DE   Sterols are components of cell membranes in plants, animals and fungi.
HI   Biological process: Lipid metabolism; Steroid metabolism; Sterol metabolism.
CA   Biological process.
//
ID   Stickler syndrome.
AC   KW-0757
DE   Protein which, if defective, causes Stickler syndrome (STL), also
DE   known as hereditary progressive arthro-ophthalmopathy. It is a
DE   genetically and phenotypically heterogeneous disorder with ocular,
DE   oro-facial, auditory and skeletal manifestations. Clinical features
DE   include high myopia, vitreo-retinal degeneration, retinal detachment,
DE   cleft palate, midfacial hypoplasia, osteoarthritis, and sensorineural
DE   hearing loss. Inheritance is autosomal dominant.
SY   STL.
HI   Disease: Stickler syndrome.
CA   Disease.
//
ID   Storage protein.
AC   KW-0758
DE   Protein which is a source of nutrients for the development or growth
DE   of an organism.
GO   GO:0045735; nutrient reservoir activity
HI   Molecular function: Storage protein.
CA   Molecular function.
//
ID   Streptomycin biosynthesis.
AC   KW-0759
DE   Protein involved in the synthesis of streptomycin, an antibiotic
DE   substance produced by the soil actinomycete Streptomyces griseus. The
DE   three parts of the molecule (streptidine-6-P, dTDP-dihydrostreptose
DE   and N-methyl-glucosamine) are synthesized by separate biochemical
DE   pathways and the subunits brought together at the end. The final
DE   intermediate in the pathway, streptomycin P, becomes biologically
DE   active upon removal of the phosphate. The synthesis of the key
DE   streptomycin biosynthesis enzymes is mainly regulated by differing
DE   levels of factor A. Streptomycin binds to the small subunit of
DE   ribosomes of prokaryotic cells and causes inhibition and misreading.
GO   GO:0019872; streptomycin biosynthetic process
HI   Biological process: Antibiotic biosynthesis; Streptomycin biosynthesis.
CA   Biological process.
//
ID   Stress response.
AC   KW-0346
DE   Protein involved in the response to stress, a change in state or
DE   activity of a cell or an organism (in terms of movement, secretion,
DE   enzyme production, gene expression, etc.) as a result of some
DE   stressful conditions. The stress is usually, but not necessarily,
DE   exogenous (e.g. temperature, humidity, ionizing radiation,
DE   hypertonicity, amino acid deprivation).
HI   Biological process: Stress response.
CA   Biological process.
//
ID   Sugar transport.
AC   KW-0762
DE   Protein involved in the transfer of sugars across a biological
DE   membrane by a carrier protein.
GO   GO:0008643; carbohydrate transport
HI   Biological process: Transport; Sugar transport.
CA   Biological process.
//
ID   Sulfate respiration.
AC   KW-0763
DE   Protein involved in sulfate respiration, which is the use of sulfate
DE   (or other oxidized compounds of sulfur) as the terminal electron
DE   acceptor in the anaerobic respiratory metabolism of sulfate- or
DE   sulfur-reducing bacteria.
SY   Dissimilatory sulfate reduction.
GO   GO:0009061; anaerobic respiration
HI   Biological process: Sulfate respiration.
CA   Biological process.
//
ID   Sulfate transport.
AC   KW-0764
DE   Protein involved in the translocation of sulfate, or sulfate-
DE   containing compounds, such as thiosulfate, across a biological
DE   membrane.
GO   GO:0008272; sulfate transport
HI   Biological process: Transport; Sulfate transport.
CA   Biological process.
//
ID   Sulfation.
AC   KW-0765
DE   Protein which is posttranslationally modified by the attachment of at
DE   least one sulfate group to a tyrosine residue. Serine and threonine
DE   may also serve as sulfate group acceptors.
SY   Sulfatation.
HI   PTM: Sulfation.
CA   PTM.
//
ID   Superantigen.
AC   KW-0766
DE   Bacterial or virus secreted protein that induces a strong T-lymphocyte
DE   activity. When a normal antigen stimulates 0,001% of the body's T-
DE   cells, superantigens can stimulate up to 20% of body's T-cells. They
DE   simultaneously interact with the Vb domain of the T-cell receptor
DE   (TCR) and with the class II major histocompatibility complex (MHC)
DE   molecules on the surface of an antigen-presenting cell. This compels
DE   the MHC to interact with the TCR, thereby inducing T-cells activation.
DE   Most superantigens are bacterial toxins, but some are produced by
DE   viruses. Staphylococcal enterotoxins are the best known superantigens.
SY   SAG.
HI   Molecular function: Superantigen.
CA   Molecular function.
//
ID   Superinfection exclusion.
AC   KW-1260
DE   Viral protein that is expressed by a prokaryotic virus, integrated or
DE   not, to help protect the host cell from superinfection, a process by
DE   which a cell that has previously been infected by one virus
DE   subsequently gets coinfected with a different strain of the virus, or
DE   another virus. Superinfection exclusion can be achieved for example by
DE   expressing viral enzymes that alter a portion of a surface receptor
DE   thereby blocking entry of incoming viruses with this receptor
DE   specificity. Exclusion protein can also target and block the ejection
DE   and/or DNA delivery by new incoming phages.
GO   GO:0098669; superinfection exclusion
HI   Biological process: Host-virus interaction; Superinfection exclusion.
CA   Biological process.
//
ID   Suppressor of RNA silencing.
AC   KW-0941
DE   Protein which suppresses host RNA-mediated gene silencing. The most
DE   common form of RNA-mediated gene silencing is RNA interference (RNAi),
DE   a sequence-specific RNA-degradation mechanism that operates as a
DE   natural antiviral system in plants and invertebrates cells. RNAi is
DE   mediated by small interfering RNAs (siRNA) of about 21- to 25-nt that
DE   target homologous RNAs for destruction. RNA silencing by endogenous
DE   micro-RNAs (miRNAs) may also play a role in the antiviral defences of
DE   mammals. miRNAs differ from siRNAs in that they generally base pair
DE   imperfectly with target RNAs and inhibit their translation by an
DE   unknown mechanism.
SY   Suppressor of RNAi; Suppressor of RNA interference.
HI   Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; Suppressor of RNA silencing.
CA   Biological process.
//
ID   Surface film.
AC   KW-0767
DE   Protein found in the film of pulmonary surfactants which cover the
DE   alveolar surface of the mammalian lung. These surfactants are composed
DE   of 90% phospholipids and 10% proteins.
GO   GO:0005576; extracellular region
HI   Biological process: Gaseous exchange; Surface film.
HI   Cellular component: Secreted; Surface film.
CA   Cellular component.
//
ID   Sushi.
AC   KW-0768
DE   Protein which contains at least one sushi domain, a motif of
DE   approximately 60 amino acids characterized by a framework of four
DE   conserved half-cystine residues (1-3 and 2-4 disulfide-bonded) and
DE   several other highly conserved residues including proline, tryptophan,
DE   tyrosine/phenylalanine and cysteine. This type of structure, also
DE   designated SCR (Short Consensus Repeat), is predominantly present in
DE   proteins associated with the complement system.
HI   Domain: Sushi.
CA   Domain.
//
ID   Symport.
AC   KW-0769
DE   Protein involved in the transport of solutes across a biological
DE   membrane in one direction, which depends on the transport of another
DE   solute in the same direction. One molecule can move up an
DE   electrochemical gradient because the movement of the other molecule is
DE   more favorable. Example: the sodium/glucose co-transport.
GO   GO:0015293; symporter activity
HI   Biological process: Transport; Symport.
CA   Biological process.
//
ID   Synapse.
AC   KW-0770
DE   Protein found in the synapses. Synapses are the communicating cell-
DE   cell junctions that allow signals to pass from a nerve cell to a
DE   target cell. In a chemical synapse, the signal is carried by a
DE   neurotransmitter which diffuses across a narrow synaptic cleft and
DE   activates a receptor on the postsynaptic membrane of the target cell.
DE   The target may be a dendrite, cell body, neuronal axon, a specialized
DE   region of a muscle or a secretory cell. In an electrical synapse, a
DE   direct connection is made between the cytoplasms of two cells via gap
DE   junctions.
GO   GO:0045202; synapse
HI   Cellular component: Synapse.
CA   Cellular component.
//
ID   Synaptosome.
AC   KW-0771
DE   Protein found in synaptosomes, the pinched-off nerve endings and their
DE   contents of vesicles and cytoplasm together with the attached
DE   subsynaptic area of the membrane of the postsynaptic cell. They are
DE   largely artificial structures produced by fractionation after
DE   selective centrifugation of nervous tissue homogenates.
GO   GO:0043005; neuron projection
HI   Cellular component: Synapse; Synaptosome.
CA   Cellular component.
//
ID   Syncytium formation induced by viral infection.
AC   KW-1180
DE   Viral protein that mediates fusion of an infected cell with
DE   neighboring cells leading to the formation of multi-nucleate enlarged
DE   cells called syncytia. Usually these syncytia are the result of
DE   expression of a viral fusion protein at the host cell membrane during
DE   viral replication. Viruses such as herpesviruses are known to induce
DE   the formation of syncytia.
SY   Induction by virus of host cell-cell fusion;
SY   Polykaryons formation in virally infected cells.
GO   GO:0060141; positive regulation of syncytium formation by virus
HI   Biological process: Syncytium formation induced by viral infection.
CA   Biological process.
//
ID   Systemic lupus erythematosus.
AC   KW-0772
DE   Protein involved in the systemic lupus erythematosus (SLE), a chronic
DE   autoimmune disease where the immune system is over-active and produces
DE   too many abnormal antibodies that react with the patient's own
DE   tissues. The exact cause of lupus is not known, but heredity,
DE   environment and hormonal changes may be involved. The immune complex
DE   deposition in many tissues leads to the manifestations of the disease.
DE   Immune complexes can be deposited in glomeruli, skin, lungs, synovium,
DE   mesothelium, and other places. Many SLE patients develop renal
DE   complications.
SY   SLE.
HI   Disease: Systemic lupus erythematosus.
CA   Disease.
//
ID   T cell receptor.
AC   KW-1279
DE   The T cell receptor (TCR) is the antigen receptor expressed on CD4-
DE   positive and CD8-positive T lymphocytes that recognizes complexes of
DE   peptides bound to self-MHC molecules on the surface of antigen
DE   presenting cells. Structurally, TCR is composed of a heterodimer of
DE   two disulfide-linked transmembrane polypeptide chains designated alpha
DE   and beta, each containing one terminal immunoglobulin (Ig)-like
DE   variable domain, one Ig-like constant domain, a hydrophobic
DE   transmembrane region and a short cytoplasmic region. A less common
DE   type of TCR, composed of gamma and delta chains, is found on a small
DE   subset of T cells and recognizes different forms of antigens. Each T
DE   cell expresses a unique TCR that is generated by randomly assorting
DE   genes. This ensures that T cells can respond (at the population level)
DE   to almost any infection.
GO   GO:0042101; T cell receptor complex
HI   Biological process: Immunity; Adaptive immunity; T cell receptor.
HI   Cellular component: T cell receptor.
CA   Cellular component.
//
ID   T=1 icosahedral capsid protein.
AC   KW-1140
DE   Viral protein that forms an icosahedral capsid with a T=1 symmetry to
DE   protect the viral genome. The T=1 capsid is composed of 60 subunits,
DE   each subunit occupying a quasi-equivalent position. The capsid
DE   diameter ranges from 18 to 35 nm.
GO   GO:0039615; T=1 icosahedral viral capsid
HI   Cellular component: Virion; Capsid protein; T=1 icosahedral capsid protein.
HI   Cellular component: Virion; T=1 icosahedral capsid protein.
CA   Cellular component.
//
ID   T=13 icosahedral capsid protein.
AC   KW-1146
DE   Viral protein that forms an icosahedral capsid with a T=13 symmetry to
DE   protect the viral genome. The T=13 capsid is composed of 780 subunits,
DE   each subunit occupying a quasi-equivalent position. Its diameter
DE   ranges from 70 to 80 nm.
GO   GO:0039621; T=13 icosahedral viral capsid
HI   Cellular component: Virion; Capsid protein; T=13 icosahedral capsid protein.
HI   Cellular component: Virion; T=13 icosahedral capsid protein.
CA   Cellular component.
//
ID   T=147 icosahedral capsid protein.
AC   KW-1149
DE   Viral protein that forms an icosahedral capsid with a T=147 symmetry
DE   to protect the viral genome. The T=147 capsid is composed of 8820
DE   subunits. Its diameter is about 185 nm.
GO   GO:0039627; T=147 icosahedral capsid
HI   Cellular component: Virion; Capsid protein; T=147 icosahedral capsid protein.
HI   Cellular component: Virion; T=147 icosahedral capsid protein.
CA   Cellular component.
//
ID   T=16 icosahedral capsid protein.
AC   KW-1147
DE   Viral protein that forms an icosahedral capsid with a T=16 symmetry to
DE   protect the viral genome. The T=16 capsid is composed of 960 subunits,
DE   each subunit occupying a quasi-equivalent position. Its diameter is
DE   about 100 nm.
GO   GO:0039622; T=16 icosahedral viral capsid
HI   Cellular component: Virion; Capsid protein; T=16 icosahedral capsid protein.
HI   Cellular component: Virion; T=16 icosahedral capsid protein.
CA   Cellular component.
//
ID   T=169 icosahedral capsid protein.
AC   KW-1150
DE   Viral protein that forms an icosahedral capsid with a T=169 symmetry
DE   to protect the viral genome. The T=169 capsid is composed of 10140
DE   subunits. Its diameter is about 165-190 nm.
GO   GO:0039628; T=169 icosahedral viral capsid
HI   Cellular component: Virion; Capsid protein; T=169 icosahedral capsid protein.
HI   Cellular component: Virion; T=169 icosahedral capsid protein.
CA   Cellular component.
//
ID   T=2 icosahedral capsid protein.
AC   KW-1141
DE   Viral protein that forms an icosahedral capsid with a T=2* symmetry to
DE   protect the viral genome. The T=2* capsid is composed of 120 subunits.
DE   The T=2* symmetry does not exist under the rules described by Caspar
DE   and Klug, strictly speaking the capsid has a T=1 symmetry composed of
DE   60 dimeric subunits. The capsid diameter is about 40 nm.
GO   GO:0039616; T=2 icosahedral viral capsid
HI   Cellular component: Virion; Capsid protein; T=2 icosahedral capsid protein.
HI   Cellular component: Virion; T=2 icosahedral capsid protein.
CA   Cellular component.
//
ID   T=219 icosahedral capsid protein.
AC   KW-1151
DE   Viral protein that forms an icosahedral capsid with a T=219 symmetry
DE   to protect the viral genome. The T=219 capsid is composed of 13140
DE   subunits. Its diameter is about 130-160 nm.
GO   GO:0039629; T=219 icosahedral capsid
HI   Cellular component: Virion; Capsid protein; T=219 icosahedral capsid protein.
HI   Cellular component: Virion; T=219 icosahedral capsid protein.
CA   Cellular component.
//
ID   T=25 icosahedral capsid protein.
AC   KW-1148
DE   Viral protein that forms an icosahedral capsid with a T=25 symmetry to
DE   protect the viral genome. The T=25 capsid is composed of 1500
DE   subunits, each subunit occupying a quasi-equivalent position. Its
DE   diameter is about 90 nm.
GO   GO:0039623; T=25 icosahedral viral capsid
HI   Cellular component: Virion; Capsid protein; T=25 icosahedral capsid protein.
HI   Cellular component: Virion; T=25 icosahedral capsid protein.
CA   Cellular component.
//
ID   T=3 icosahedral capsid protein.
AC   KW-1142
DE   Viral protein that forms an icosahedral capsid with a T=3 symmetry to
DE   protect the viral genome. The T=3 capsid is composed of 180 subunits,
DE   each subunit occupying a quasi-equivalent position. The capsid
DE   diameter ranges from 26 to 40 nm.
GO   GO:0039617; T=3 icosahedral viral capsid
HI   Cellular component: Virion; Capsid protein; T=3 icosahedral capsid protein.
HI   Cellular component: Virion; T=3 icosahedral capsid protein.
CA   Cellular component.
//
ID   T=4 icosahedral capsid protein.
AC   KW-1144
DE   Viral protein that forms an icosahedral capsid with a T=4 symmetry to
DE   protect the viral genome. The T=4 capsid is composed of 240 subunits,
DE   each subunit occupying a quasi-equivalent position. The capsid
DE   diameter ranges from 30 to 40 nm.
GO   GO:0039619; T=4 icosahedral viral capsid
HI   Cellular component: Virion; Capsid protein; T=4 icosahedral capsid protein.
HI   Cellular component: Virion; T=4 icosahedral capsid protein.
CA   Cellular component.
//
ID   T=7 icosahedral capsid protein.
AC   KW-1145
DE   Viral protein that forms an icosahedral capsid with a T=7 symmetry to
DE   protect the viral genome. The T=7 capsid is composed of 420 subunits,
DE   each subunit occupying a quasi-equivalent position. Papillomavirus and
DE   Polyomavirus T=7 capsids are composed of pentameric capsomeres for a
DE   total of 360 capsid proteins. Its diameter ranges from 45 to 60 nm.
GO   GO:0039620; T=7 icosahedral viral capsid
HI   Cellular component: Virion; Capsid protein; T=7 icosahedral capsid protein.
HI   Cellular component: Virion; T=7 icosahedral capsid protein.
CA   Cellular component.
//
ID   T=pseudo3 icosahedral capsid protein.
AC   KW-1143
DE   Viral protein that forms an icosahedral capsid with a pseudo T=3
DE   symmetry to protect the viral genome. The pseudo T=pseudo3 capsid is
DE   composed of 180 subunits. Each subunit does not occupy a quasi-
DE   equivalent position, therefore the structure is called pseudo. The
DE   capsid diameter ranges from 26 to 40 nm.
GO   GO:0039618; T=pseudo3 icosahedral viral capsid
HI   Cellular component: Virion; Capsid protein; T=pseudo3 icosahedral capsid protein.
HI   Cellular component: Virion; T=pseudo3 icosahedral capsid protein.
CA   Cellular component.
//
ID   Tachyzoite.
AC   KW-1137
DE   Protein expressed in the infectious tachyzoite stage, a rapidly
DE   growing, lytic and disease-causing stage in the life stage of
DE   coccidians (e.g. Toxoplasmy). Tachyzoites, which can infect most
DE   nucleated cells, replicate inside a parasitophorous vacuole, egress,
DE   and then infect neighboring cells. Aggregates of numerous tachyzoites
DE   are called clones, terminal colonies, or groups.
SY   Endodyozoite; Endozoite.
HI   Developmental stage: Tachyzoite.
CA   Developmental stage.
//
ID   Target cell cytoplasm.
AC   KW-1266
DE   Protein found in a target cell cytoplasm, the contents of a target
DE   cell within the plasma membrane and which, in eukaryotic cells,
DE   surrounds the host nucleus. This term is used to describe a toxin
DE   located in the cytoplasm of a target cell.
SY   Target cytoplasm.
HI   Cellular component: Target cell cytoplasm.
CA   Cellular component.
//
ID   Target cell membrane.
AC   KW-1052
DE   Protein found in or associated with a target cell membrane, the
DE   selectively permeable membrane which separates the target cell
DE   cytoplasm from its surroundings. This term is used to describe a toxin
DE   located to the cell membrane of a target cell.
SY   Target cytoplasmic membrane; Target plasmalemma;
SY   Target plasma membrane.
HI   Cellular component: Membrane; Target membrane; Target cell membrane.
CA   Cellular component.
//
ID   Target membrane.
AC   KW-1053
DE   Protein which is membrane-bound or membrane-associated with the target
DE   membrane, a lipid bilayer which surrounds target cell enclosed spaces
DE   and compartments. This selectively permeable structure is essential
DE   for effective separation of a target cell or targeet cell organelle
DE   from its surroundings. This term is used to describe a toxin located
DE   to a membrane of a target cell.
GO   GO:0044218; other organism cell membrane
HI   Cellular component: Membrane; Target membrane.
CA   Cellular component.
//
ID   Taste.
AC   KW-0919
DE   Protein involved in taste signal transduction. Human perceives five
DE   basic taste qualities: bitter, salty, sour, sweet, and umami, the
DE   taste of glutamate. Taste perception begins when a taste-eliciting
DE   molecule, or tastant, interacts with specialized receptors in the
DE   membrane of taste receptor cells. Taste responses to bitter, sweet,
DE   and umami compounds are initiated by G-protein-coupled receptors and
DE   transduced via G-protein signaling cascades. Salty and sour tastes are
DE   transduced by ion channels.
SY   Gustation.
GO   GO:0050909; sensory perception of taste
HI   Biological process: Sensory transduction; Taste.
CA   Biological process.
//
ID   Taste-modifying protein.
AC   KW-0776
DE   Protein that function as a natural sweetener or flavor enhancer. TMPs
DE   are found in the fruit or seed of several plants and show no primary
DE   sequence similarity. TMPs interact with taste receptors in a potent
DE   and specific manner. TMPs are natural and have been used by some
DE   cultures for centuries. West Africans have long used TMPs to improve
DE   flavor and suppress bitterness of food and drink.
SY   Sweet-taste protein; TMP.
HI   Molecular function: Taste-modifying protein.
CA   Molecular function.
//
ID   Taxol biosynthesis.
AC   KW-0876
DE   Protein involved in the synthesis of taxol, a complex diterpenoid
DE   isolated from the bark of yew (Taxus) species. Taxol is a potent
DE   antimitotic agent with activity against a number of leukamias and
DE   solid tumors. It has become a chemotherapeutic drug under the generic
DE   name of paclitaxel.
SY   Paclitaxel biosynthesis.
GO   GO:0042617; paclitaxel biosynthetic process
HI   Biological process: Taxol biosynthesis.
CA   Biological process.
//
IC   Technical term.
AC   KW-9990
DE   Keywords assigned to proteins according to 'technical' reasons.
//
ID   Teichoic acid biosynthesis.
AC   KW-0777
DE   Protein involved in the synthesis of teichoic acid, a polymer of
DE   mainly glycerol phosphate or ribitol phosphate substituted extensively
DE   with amino acids and/or sugars. Teichoic acid occurs in the cell wall
DE   of Gram-positive bacteria.
SY   C polysaccharide biosynthesis.
GO   GO:0019350; teichoic acid biosynthetic process
HI   Biological process: Teichoic acid biosynthesis.
CA   Biological process.
//
ID   Tellurium resistance.
AC   KW-0778
DE   Protein that confers resistance to tellurium.
GO   GO:0046690; response to tellurium ion
HI   Biological process: Tellurium resistance.
CA   Biological process.
//
ID   Telomere.
AC   KW-0779
DE   Protein involved in telomere replication, length regulation,
DE   structure, etc. The telomere is a nucleoprotein structure comprising
DE   the terminal section of a eukaryotic chromosome. It has a specialized
DE   structure which is replicated by a special process, thereby
DE   counteracting the tendency of a chromosome to be shortened during each
DE   round of replication.
GO   GO:0000781; chromosome, telomeric region
HI   Cellular component: Chromosome; Telomere.
CA   Cellular component.
//
ID   Terminal addition.
AC   KW-0780
DE   Protein involved in the random addition of deoxynucleoside 5'-
DE   triphosphate to the 3'end of a DNA initiator.
GO   GO:0003912; DNA nucleotidylexotransferase activity
GO   GO:0006304; DNA modification
HI   Molecular function: Transferase; Nucleotidyltransferase; Terminal addition.
HI   Biological process: Terminal addition.
CA   Biological process.
//
ID   Tetrahydrobiopterin biosynthesis.
AC   KW-0783
DE   Protein involved in the synthesis of tetrahydrobiopterin, the reduced
DE   form of dihydrobiopterin, a reduced pteridine derivative related to
DE   folic acid. It is a coenzyme for the enzyme phenylalanine-4-
DE   hydroxylase which is involved in phenylalanine degradation.
GO   GO:0006729; tetrahydrobiopterin biosynthetic process
HI   Biological process: Tetrahydrobiopterin biosynthesis.
CA   Biological process.
//
ID   Thiamine biosynthesis.
AC   KW-0784
DE   Protein involved in the synthesis of thiamine, a water-soluble vitamin
DE   member of the vitamin B complex. It occurs in cells largely as its
DE   active coenzyme form thiamine pyrophosphate, formerly called
DE   cocarboxylase. Thiamine is necessary in the diet of most vertebrates
DE   and some microorganisms. Its deficiency causes beriberi in man and
DE   polyneuritis in birds. Thiamine pyrophosphate serves as coenzyme in
DE   aldehyde-group transfers.
SY   Aneurin biosynthesis; Thiamin biosynthesis; Vitamin B1 biosynthesis.
GO   GO:0009228; thiamine biosynthetic process
HI   Biological process: Thiamine biosynthesis.
CA   Biological process.
//
ID   Thiamine catabolism.
AC   KW-0785
DE   Protein involved in the degradation of thiamine, a water-soluble
DE   vitamin which is a member of the vitamin B complex. It occurs in cells
DE   largely as its active coenzyme form thiamine pyrophosphate, formerly
DE   called cocarboxylase. Thiamine is necessary in the diet of most
DE   vertebrates and some microorganisms. Its deficiency causes beriberi in
DE   man and polyneuritis in birds. Thiamine pyrophosphate serves as a
DE   coenzyme in aldehyde-group transfers.
SY   Aneurin catabolism; Thiamin catabolism; Vitamin B1 catabolism.
GO   GO:0009230; thiamine catabolic process
HI   Biological process: Thiamine catabolism.
CA   Biological process.
//
ID   Thiamine pyrophosphate.
AC   KW-0786
DE   Protein which contains at least one thiamine pyrophosphate, the active
DE   form of vitamin B1 (thiamine). It is a required coenzyme for the
DE   pyruvate decarboxylase, pyruvate dehydrogenase and ketoglutarate
DE   dehydrogenase reactions.
SY   TDP; Thiamin diphosphate; Thiamin pyrophosphate; TPP.
HI   Ligand: Thiamine pyrophosphate.
CA   Ligand.
//
ID   Thick filament.
AC   KW-0787
DE   Protein found in, or associated with, the thick filaments which are
DE   formed by bipolar myosin-II filaments (12-14 nm in diameter, 1.6 mm
DE   long) found striated muscle. Myosin filaments elsewhere are often
DE   referred to as 'thick filaments', although their length may be
DE   considerably less. The myosin heads project from the thick filament in
DE   a regular fashion.
GO   GO:0032982; myosin filament
HI   Molecular function: Muscle protein; Thick filament.
HI   Cellular component: Thick filament.
CA   Cellular component.
//
ID   Thioester bond.
AC   KW-0882
DE   Protein which is posttranslationally modified by the formation of a
DE   thioester crosslink between two amino acids in the polypeptidic
DE   chain(s), usually formed between a cysteine side chain and the
DE   carboxamide group of an asparagine or glutamine side chain.
SY   Thiolester bond.
HI   PTM: Thioester bond.
CA   PTM.
//
ID   Thioether bond.
AC   KW-0883
DE   Protein which is posttranslationally modified by the formation of a
DE   thioether crosslink between two amino acids in the polypeptidic
DE   chain(s), usually formed between a cysteine side chain and the side
DE   chain of a serine or a threonine.
HI   PTM: Thioether bond.
CA   PTM.
//
ID   Thiol protease.
AC   KW-0788
DE   Proteolytic enzyme with a cysteine residue (Cys) in its active site.
DE   There are many families of thiol proteases. The most well known one is
DE   the papain family (C1 in MEROPS classification) which is known to
DE   exist in most eukaryotes.
SY   Sulfhydryl protease; Thiol peptidase; Thiol proteinase.
GO   GO:0008234; cysteine-type peptidase activity
HI   Molecular function: Hydrolase; Protease; Thiol protease.
CA   Molecular function.
//
ID   Thiol protease inhibitor.
AC   KW-0789
DE   Protein which inhibits the activity of a thiol protease, a class of
DE   proteases that contains an active site cysteine residue (Cys), e.g.
DE   papain, cathepsins, etc.
SY   Thiol peptidase inhibitor; Thiol proteinase inhibitor.
GO   GO:0004869; cysteine-type endopeptidase inhibitor activity
HI   Molecular function: Protease inhibitor; Thiol protease inhibitor.
CA   Molecular function.
//
ID   Threonine biosynthesis.
AC   KW-0791
DE   Protein involved in the synthesis of the essential amino acid
DE   threonine.
GO   GO:0009088; threonine biosynthetic process
HI   Biological process: Amino-acid biosynthesis; Threonine biosynthesis.
CA   Biological process.
//
ID   Threonine protease.
AC   KW-0888
DE   Proteolytic enzyme with a threonine residue (Thr) in its active site.
DE   The prototype members of this class of enzymes are the proteasome
DE   catalytic subunits.
GO   GO:0004298; threonine-type endopeptidase activity
HI   Molecular function: Hydrolase; Protease; Threonine protease.
CA   Molecular function.
//
ID   Thrombophilia.
AC   KW-0792
DE   Protein which, if defective, causes thrombophilia, a disorder of
DE   hemostasis in which the individuals are prone to serious spontaneous
DE   thrombosis.
SY   Recurrent venous thrombosis.
HI   Biological process: Hemostasis; Blood coagulation; Thrombophilia.
HI   Disease: Thrombophilia.
CA   Disease.
//
ID   Thylakoid.
AC   KW-0793
DE   Protein located in or on the thylakoid, a membranous cisterna of the
DE   chloroplast. Thylakoids stack up to form the grana or stay as single
DE   cisternae and interconnect the grana. The thylakoid contains the
DE   photosynthetic pigments, reaction centers and electron-transport
DE   chain. Thylakoid, where photosynthesis occurs, are also found in
DE   cyanelles and in photosynthetic bacteria where they are the extensive
DE   invaginations of the plasma membrane.
GO   GO:0009579; thylakoid
HI   Cellular component: Thylakoid.
CA   Cellular component.
//
ID   Thyroid hormone.
AC   KW-0795
DE   Protein precursor of thyroid hormones which are secreted by the thymus
DE   gland and participate in the development of the lymphoid system as
DE   well as the maturation of the cellular immune response. Also used for
DE   proteins which bind thyroid hormones or thyroid hormone receptor
DE   antagonists.
HI   Molecular function: Hormone; Thyroid hormone.
CA   Molecular function.
//
ID   Thyroid hormones biosynthesis.
AC   KW-0893
DE   Protein involved in the synthesis of thyroid hormones.
GO   GO:0042446; hormone biosynthetic process
HI   Biological process: Thyroid hormones biosynthesis.
CA   Biological process.
//
ID   Tight junction.
AC   KW-0796
DE   Protein which is a component of the tight junction or are associated
DE   with it. These specialized regions of the plasma membrane prevent the
DE   diffusion of dissolved molecules between adjacent epithelial cells,
DE   seal off body cavities such as intestine or stomach lumen and prevent
DE   the diffusion of membrane proteins and glycolipids between the apical
DE   and basolateral regions of the plasma membrane.
GO   GO:0005923; bicellular tight junction
HI   Cellular component: Cell junction; Tight junction.
CA   Cellular component.
//
ID   Tissue remodeling.
AC   KW-0797
DE   Protein involved in tissue remodeling. As an example the matrix-
DE   degrading plasminogen activators (PAs) and matrix metalloproteinases
DE   (MMPs) are general proteolytic enzyme systems which mediate tissue
DE   remodeling and tissue destruction in a variety of physiological and
DE   pathological conditions, including ovulation, angiogenesis,
DE   implantation, tumor invasion and inflammatory diseases such as
DE   rheumatoid arthritis (RA).
GO   GO:0048771; tissue remodeling
HI   Biological process: Tissue remodeling.
CA   Biological process.
//
ID   TonB box.
AC   KW-0798
DE   Protein with a TonB box. In Escherichia coli the TonB protein
DE   interacts with outer membrane receptor proteins that carry out high-
DE   affinity binding and energy-dependent uptake of specific substrates
DE   into the periplasmic space. These substrates are either poorly
DE   permeable through the porin channels or are encountered at very low
DE   concentrations. In the absence of TonB these receptors bind their
DE   substrates but do not carry out active transport. TonB also interacts
DE   with some colicins and is involved in the energy dependent,
DE   irreversible steps of bacteriophages phi-80 and T1 infection.
HI   Domain: TonB box.
CA   Domain.
//
ID   Topoisomerase.
AC   KW-0799
DE   Enzymes capable of altering the degree of supercoiling of double-
DE   stranded DNA molecules. Various topoisomerases can increase or relax
DE   supercoiling, convert single-stranded rings to intertwined double-
DE   stranded rings, tie and untie knots in single stranded and duplex
DE   rings or catenate and decatenate duplex rings. Any enzyme that cleaves
DE   only one strand of a DNA duplex and then reseals it is classified as a
DE   type I topoisomerase (Topo I). Type II topoisomerases (Topo II) change
DE   DNA topology by breaking and rejoining double-stranded DNA.
GO   GO:0003916; DNA topoisomerase activity
HI   Molecular function: Isomerase; Topoisomerase.
CA   Molecular function.
//
ID   Toxin.
AC   KW-0800
DE   Naturally-produced poisonous protein that damages or kills other
DE   cells, or the producing cells themselves in some cases in bacteria.
DE   Toxins are produced by venomous and poisonous animals, some plants,
DE   some fungi and some pathogenic bacteria. Animal toxins (mostly from
DE   snakes, scorpions, spiders, sea anemones and cone snails) are
DE   generally secreted in the venom of the animal.
GO   GO:0090729; toxin activity
HI   Molecular function: Toxin.
CA   Molecular function.
//
ID   Toxin-antitoxin system.
AC   KW-1277
DE   Bacterial, archaeal or viral protein belonging to a toxin-antitoxin
DE   (TA) system. Toxin protein expression is poisonous to the cell and is
DE   counteracted by its co-expressed, short-lived "antidote" antitoxin.
DE   Antitoxins can be protein (type II, IV, V, VI) or RNA (type I, III)
DE   and act directly or indirectly on the toxin protein or transcript.
DE   Genes for the 2 components are closely linked; in many type II TA
DE   systems the toxin-antitoxin complex regulates transcription of its
DE   operon. Toxins belong to recognizable protein families, antitoxins
DE   usually do not. Orphan toxin genes are occasionally found in complete
DE   genomes.
SY   Toxin-antitoxin module.
HI   Biological process: Toxin-antitoxin system.
CA   Biological process.
//
ID   TPQ.
AC   KW-0801
DE   Protein which is posttranslationally modified on a tyrosine residue to
DE   form TPQ. This modification of a strictly conserved active-site
DE   tyrosine residue proceeds via the hydroxylation of tyrosine to Topa
DE   (Trihydroxyphenylalanine) and then to TPQ (Topaquinone). It is a self-
DE   processing pathway requiring only the protein, copper and molecular
DE   oxygen. TPQ is the redox cofactor of most copper-containing amine
DE   oxidases.
SY   Topaquinone.
HI   PTM: TPQ.
CA   PTM.
//
ID   TPR repeat.
AC   KW-0802
DE   Protein with at least one TPR repeat. The TPR repeat of typically 34
DE   amino acids was first described in the yeast cell division control
DE   protein 23 (CDC23) and later found to occur in a large number of
DE   proteins. A function for this repeat seems to be protein-protein
DE   interaction.
SY   Tetratricopeptide repeat.
HI   Domain: TPR repeat.
CA   Domain.
//
ID   Transcription.
AC   KW-0804
DE   Protein involved in the transfer of genetic information from DNA to
DE   messenger RNA (mRNA) by DNA-directed RNA polymerase. In the case of
DE   some RNA viruses, protein involved in the transfer of genetic
DE   information from RNA to messenger RNA (mRNA) by RNA-directed RNA
DE   polymerase.
HI   Biological process: Transcription.
CA   Biological process.
//
ID   Transcription antitermination.
AC   KW-0889
DE   Protein involved in transcription antitermination, the process whereby
DE   RNA polymerase is allowed to read through specific RNA secondary
DE   structures that normally terminate transcription.
GO   GO:0031564; transcription antitermination
HI   Biological process: Transcription; Transcription regulation; Transcription antitermination.
CA   Biological process.
//
ID   Transcription regulation.
AC   KW-0805
DE   Protein involved in the regulation of the transcription process.
HI   Biological process: Transcription; Transcription regulation.
CA   Biological process.
//
ID   Transcription termination.
AC   KW-0806
DE   Protein involved in transcription termination.
GO   GO:0006353; DNA-templated transcription termination
HI   Biological process: Transcription; Transcription regulation; Transcription termination.
CA   Biological process.
//
ID   Transducer.
AC   KW-0807
DE   Protein which converts an input signal into an output signal of a
DE   different form.
GO   GO:0007165; signal transduction
HI   Molecular function: Transducer.
CA   Molecular function.
//
ID   Transferase.
AC   KW-0808
DE   Enzyme that transfers a chemical group, e.g. a methyl group or a
DE   glycosyl group from one compound (donor) to another compound
DE   (acceptor).
GO   GO:0016740; transferase activity
HI   Molecular function: Transferase.
CA   Molecular function.
//
ID   Transit peptide.
AC   KW-0809
DE   Proteins which have an N-terminal presequence which directs them to an
DE   organelle (chloroplast, mitochondria, microbody, cyanelle). The
DE   transit peptide is required for their transport across the relevant
DE   membranes from their site of synthesis in the cytoplasm.
HI   Domain: Transit peptide.
CA   Domain.
//
ID   Translation regulation.
AC   KW-0810
DE   Protein involved in the regulation of peptide formation on ribosomes,
DE   directed by messenger RNA (mRNA).
GO   GO:0006417; regulation of translation
HI   Biological process: Translation regulation.
CA   Biological process.
//
ID   Translational shunt.
AC   KW-1155
DE   Protein which is involved in the translational shunt, an unusual
DE   translation process in which ribosomes are loaded onto mRNA at the 5'-
DE   cap structure, start scanning for a short distance before bypassing
DE   the large internal leader region and initiating at a downstream start
DE   site. Shunting operates in plants, animals, and yeast translational
DE   systems, both in vivo and in vitro.
SY   Ribosomal shunt; Ribosome shunt; Shunting.
HI   Molecular function: Translational shunt.
CA   Molecular function.
//
ID   Translocase.
AC   KW-1278
DE   Protein that uses enzyme activity to effect transmembrane transport,
DE   as exemplified by transmembrane transport coupled to ATP hydrolysis
DE   and oxidoreductases involved in transmembrane proton or electron
DE   transport. Not to be confused with ligand-gated ion channels or other
DE   transmembrane transporters without enzyme activity.
HI   Molecular function: Translocase.
CA   Molecular function.
//
ID   Translocation.
AC   KW-0811
DE   Protein involved in the transport of proteins across a membrane. As an
DE   example translocation into the nucleus occurs via nuclear pores which
DE   allow rapid diffusion of small molecules. Larger molecules (maximum 9
DE   nm) take longer. Translocation into the mitochondria or chloroplast
DE   occurs at sites of adhesion between the outer and inner membranes and
DE   is driven by ATP hydrolysis as well as the electrochemical gradient of
DE   the inner membrane.
GO   GO:0015031; protein transport
HI   Biological process: Transport; Protein transport; Translocation.
CA   Biological process.
//
ID   Transmembrane.
AC   KW-0812
DE   Protein with at least one transmembrane domain, a membrane-spanning
DE   helical or beta-stranded domain embedded in a membrane.
HI   Cellular component: Membrane; Transmembrane.
HI   Domain: Transmembrane.
CA   Domain.
//
ID   Transmembrane beta strand.
AC   KW-1134
DE   Protein with at least one transmembrane beta stranded domain, a
DE   membrane-spanning stretch, typically 5-10 amino acids long, whose
DE   peptide backbones are almost fully extended with the sidechains of two
DE   neighboring residues projected in the opposite direction from the
DE   backbone. Two or more hydrogen bonded (parallel or anti-parallel) beta
DE   strands form a beta sheet. A beta barrel is formed by a closed beta
DE   sheet around a central pore. Beta barrels consist usually of an even
DE   number of beta strands (between 8 and 24), they are found only in
DE   bacterial outer membranes, mitochondria and plastids.
HI   Cellular component: Membrane; Transmembrane beta strand.
HI   Domain: Transmembrane; Transmembrane beta strand.
CA   Domain.
//
ID   Transmembrane helix.
AC   KW-1133
DE   Protein with at least one transmembrane helical domain, a membrane-
DE   spanning domain with an hydrogen-bonded helical configuration,
DE   including alpha-, 3-10-, and pi-helices. The transmembrane alpha-helix
DE   is very common, while the 3-10-helix is found at the ends of alpha-
DE   helices and the pi-helix, is more rare.
SY   Alpha-helical transmembrane; Pauling-Corey-Branson alpha helix.
HI   Cellular component: Membrane; Transmembrane helix.
HI   Domain: Transmembrane; Transmembrane helix.
CA   Domain.
//
ID   Transport.
AC   KW-0813
DE   Protein involved in the transport of a molecule (metabolite, protein,
DE   etc), a ion or an electron across cell membranes, inside the cell or
DE   in a tissue fluid.
HI   Biological process: Transport.
CA   Biological process.
//
ID   Transposable element.
AC   KW-0814
DE   Protein encoded by a transposable element, or transposon, a mobile DNA
DE   segment that can replicate and insert a copy at another site within
DE   the genome. Simple transposons only contains genes needed for
DE   insertion. More complex types also carry genes with functions
DE   unrelated to insertion, e.g. genes for resistance to antibiotics or
DE   heavy metals.
SY   Transposon.
HI   Technical term: Transposable element.
CA   Technical term.
//
ID   Transposition.
AC   KW-0815
DE   Protein involved in the movement of a specific DNA sequence
DE   - generally known as a transposable element or transposon - to another
DE   location within the genome by replication of the sequence and
DE   insertion of the copy at its target site, at random or at some
DE   specific site. Proteins necessary for the transposition, such as the
DE   enzyme transposase, are usually encoded by the transposable element
DE   itself.
GO   GO:0032196; transposition
HI   Biological process: Transposition.
CA   Biological process.
//
ID   Tricarboxylic acid cycle.
AC   KW-0816
DE   Protein involved in the tricarboxylic acid cycle, a series of
DE   metabolic reactions in aerobic cellular respiration, which occurs in
DE   the mitochondria of animals and plants and in which acetyl-CoA, formed
DE   from pyruvate produced during glycolysis, is completely oxidized to
DE   CO2 via the interconversion of various carboxylic acids. It results in
DE   the reduction of NAD and FAD to NADH and FADH2, whose reducing power
DE   is then used indirectly in the synthesis of ATP by oxidative
DE   phosphorylation. The TCA cycle also provides intermediates for many
DE   other biosynthetic processes.
SY   Citric acid cycle; Krebs cycle; TCA cycle.
GO   GO:0006099; tricarboxylic acid cycle
HI   Biological process: Tricarboxylic acid cycle.
CA   Biological process.
//
ID   Trimethoprim resistance.
AC   KW-0817
DE   Protein that confers, on bacteria or other microorganisms, the ability
DE   to withstand the antibacterial agent trimethroprim that inhibits
DE   dihydrofolate reductase (DHFR), an enzyme required for de novo glycine
DE   and purine synthesis.
GO   GO:0046677; response to antibiotic
HI   Biological process: Antibiotic resistance; Trimethoprim resistance.
CA   Biological process.
//
ID   Triplet repeat expansion.
AC   KW-0818
DE   Protein encoded by a gene which has a triplet repeat expansion, i.e.
DE   the increase of triplet (trinucleotide) repeats within the gene
DE   sequence. The length of such repeats is frequently polymorphic, and
DE   there is often a correlation between repeat length and disease
DE   severity.
HI   Coding sequence diversity: Triplet repeat expansion.
CA   Coding sequence diversity.
//
ID   tRNA processing.
AC   KW-0819
DE   Protein involved in the processing of the primary tRNA transcript to
DE   yield a functional tRNA. Transcription of tRNA genes results in a
DE   large precursor molecule which may even contain sequences for several
DE   tRNA molecules. This primary transcript is subsequently processed by
DE   cleavage and by modification of the appropriate bases.
SY   Transfer RNA processing; tRNA biosynthesis.
GO   GO:0008033; tRNA processing
HI   Biological process: tRNA processing.
CA   Biological process.
//
ID   tRNA-binding.
AC   KW-0820
DE   Protein which binds transfer RNA, for example some ribosomal proteins
DE   or some aminoacyl-tRNA synthetases.
SY   Transfer RNA binding.
GO   GO:0000049; tRNA binding
HI   Molecular function: RNA-binding; tRNA-binding.
CA   Molecular function.
//
ID   Trophozoite.
AC   KW-1138
DE   Protein expressed in the trophozoite stage, a motile replicating and
DE   disease-causing stage of in the life cycle of some sporozoan
DE   parasites.
HI   Developmental stage: Trophozoite.
CA   Developmental stage.
//
ID   Trypanosomiasis.
AC   KW-0821
DE   Protein involved in trypanosomiasis, a human or animal disease caused
DE   by Trypanosoma, a genus of parasitic flagellate protozoa. Such
DE   diseases include African sleeping sickness, Nagana and American
DE   Chagas' disease.
HI   Disease: Trypanosomiasis.
CA   Disease.
//
ID   Tryptophan biosynthesis.
AC   KW-0822
DE   Protein involved in the synthesis of the aromatic amino acid
DE   tryptophan (Trp) in bacteria, fungi and plants from chorismate. Trp is
DE   needed to synthesize proteins and as a precursor to niacin, serotonin
DE   and melatonin.
GO   GO:0000162; tryptophan biosynthetic process
HI   Biological process: Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Tryptophan biosynthesis.
CA   Biological process.
//
ID   Tryptophan catabolism.
AC   KW-0823
DE   Protein involved in the degradation of the aromatic amino acid
DE   tryptophan (Trp).
GO   GO:0006569; tryptophan catabolic process
HI   Biological process: Tryptophan catabolism.
CA   Biological process.
//
ID   TTQ.
AC   KW-0824
DE   Protein which contains at least one tryptophan tryptophylquinone (TTQ)
DE   cross-link modification. TTQ, the cofactor of methylamine
DE   dehydrogenase (MADH), is formed by oxidation of the indole ring of a
DE   tryptophan to form tryptophylquinone followed by covalent cross-
DE   linking with another tryptophan residue. MADH converts primary amines
DE   to their corresponding aldehydes plus ammonia. During the catalytic
DE   cycle, TTQ mediates electron transfer from the substrate to a copper
DE   protein, amicyanin. These electrons are transferred to the respiratory
DE   chain via a C-type cytochrome.
SY   Tryptophan tryptophylquinone.
HI   PTM: TTQ.
CA   PTM.
//
ID   Tumor antigen.
AC   KW-0825
DE   Protein on the surfaces of tumor cells detected by cell-mediated
DE   immunity. Different categories of tumor antigens which induce
DE   cytotoxic T lymphocyte (CTL) responses in vitro and in vivo, have been
DE   identified. These are, namely, "cancer testis" (CT) antigens expressed
DE   in different tumours and normal testis, melanocyte differentiation
DE   antigens, point mutations of normal genes, self antigens that are
DE   overexpressed in malignant tissues and viral antigens.
SY   Cancer antigen.
HI   Molecular function: Tumor antigen.
CA   Molecular function.
//
ID   Tumor suppressor.
AC   KW-0043
DE   Protein that suppresses tumorigenesis. Tumor suppressors generally
DE   function as negative regulators of cell cycle progression or cell
DE   proliferation. They may act to enforce cell cycle arrest in response
DE   to specific signals, such as DNA damage, thereby allowing DNA repair
DE   to occur prior to DNA replication. Tumor suppressors that act in this
DE   way include TP53 and its downstream effector CDKN1A/p21. They may also
DE   act to induce programmed cell death (apoptosis) in response to
DE   specific developmental signals or under circumstances where DNA repair
DE   cannot be completed. Tumor suppressors that act in this way include
DE   PTEN and BAX.
SY   Anti-oncogene; Antitumor.
HI   Disease: Tumor suppressor.
CA   Disease.
//
ID   Tungsten.
AC   KW-0826
DE   Protein which binds at least one tungsten atom, or protein whose
DE   function is tungsten-dependent. Tungsten is a metallic element,
DE   chemical symbol W.
HI   Ligand: Tungsten.
WW   https://www.webelements.com/tungsten/
CA   Ligand.
//
ID   Two-component regulatory system.
AC   KW-0902
DE   Protein involved in a system responding to environmental changes
DE   characterized usually by a sensor kinase in the cell membrane that
DE   phosphorylates itself in response to a signal and a response regulator
DE   to which the phosphoryl group is transferred. The responder is
DE   typically a DNA-binding protein that regulates transcription. Several
DE   of these systems are quite complex, involving many proteins in a
DE   signaling cascade or contributing to several responses simultaneously.
DE   They are involved in a variety processes such as chemotaxis,
DE   osmoregulation, magnesium transport, pH tolerance, sporulation, or
DE   response of virulent species to host cell's environments.
SY   Phosphorelay system; Phospho-relay system;
SY   Two-component sensory transduction system;
SY   Two-component signal transduction system; Two-component system.
GO   GO:0000160; phosphorelay signal transduction system
HI   Biological process: Two-component regulatory system.
CA   Biological process.
//
ID   Tyrosine biosynthesis.
AC   KW-0827
DE   Protein involved in the synthesis of the aromatic amino acid tyrosine.
DE   In microorganisms and plants, tyrosine is synthesized from chorismate
DE   via a simple pathway using prephenate as an intermediate. In rat, this
DE   nonessential amino acid is produced by hydroxylating the essential
DE   amino acid phenylalanine.
GO   GO:0006571; tyrosine biosynthetic process
HI   Biological process: Amino-acid biosynthesis; Aromatic amino acid biosynthesis; Tyrosine biosynthesis.
CA   Biological process.
//
ID   Tyrosine catabolism.
AC   KW-0828
DE   Protein involved in the degradation of the aromatic amino acid
DE   tyrosine. In mammals, tyrosine degradation is catalyzed by a series of
DE   5 enzymatic reactions which yield acetoacetate (ketogenic) and the
DE   Krebs cycle intermediate fumarate (glucogenic).
GO   GO:0006572; tyrosine catabolic process
HI   Biological process: Tyrosine catabolism.
CA   Biological process.
//
ID   Tyrosine-protein kinase.
AC   KW-0829
DE   Enzyme which catalyzes the transfer of the terminal phosphate of ATP
DE   to a specific tyrosine residue on its target protein. Many of these
DE   kinases play significant roles in development and cell division.
DE   Tyrosine-protein kinases can be divided into two subfamilies: receptor
DE   tyrosine kinases, which have an intracellular tyrosine kinase domain,
DE   a transmembrane domain and an extracellular ligand-binding domain; and
DE   non-receptor (cytoplasmic) tyrosine kinases, which are soluble,
DE   cytoplasmic kinases.
GO   GO:0004713; protein tyrosine kinase activity
HI   Molecular function: Transferase; Kinase; Tyrosine-protein kinase.
CA   Molecular function.
//
ID   Ubiquinone.
AC   KW-0830
DE   Protein which interacts with ubiquinone. This fat soluble benzoquinone
DE   has a long isoprenoid side chain, which varies in length depending on
DE   the species. For example, S.cerevisiae has CoQ-6, E.coli has CoQ-8,
DE   rat and R.capsulatus have CoQ-9 and S.pombe, G.suboxydans and humans
DE   have CoQ-10. Ubiquinone is a carrier of hydrogen atoms (protons plus
DE   electrons) and functions as an ubiquitous coenzyme in redox reactions,
DE   where it is first reduced to the enzyme-bound intermediate radical
DE   semiquinone and in a second reduction to ubiquinol (Dihydroquinone;
DE   CoQH2). Ubiquinone is not tightly bound or covalently linked to a
DE   protein complex but is very mobile.
SY   Coenzyme Q; CoQ.
HI   Ligand: Ubiquinone.
CA   Ligand.
//
ID   Ubiquinone biosynthesis.
AC   KW-0831
DE   Protein involved in the synthesis of ubiquinone which involves the
DE   conversion of chorismate into 4-hydroxy-benzoate, to which is added
DE   six to ten isoprene units to form polyprenyl phenol. The addition of a
DE   further oxygen atom at C3, followed by the transfer of three methyl
DE   groups from S-adenosine methionine gives rise to ubiquinol, which is
DE   further reduced to ubiquinone (6-polyprenyl-2,3-dimethoxy-5-methyl-
DE   1,4-benzoquinone).
SY   Coenzyme Q biosynthesis; CoQ biosynthesis.
GO   GO:0006744; ubiquinone biosynthetic process
HI   Biological process: Ubiquinone biosynthesis.
CA   Biological process.
//
ID   Ubl conjugation.
AC   KW-0832
DE   Protein which is posttranslationally modified by the attachment of at
DE   least one ubiquitin-like modifier protein, such as ubiquitin, SUMO,
DE   APG12, URM1 or RUB1. Ubiquitin, for example, is linked through a
DE   isopeptide bond between its C-terminus and the epsilon group of a
DE   lysine residue present on either another ubiquitin-like modifier
DE   protein or a target protein.
SY   Sumoylation; Ubiquitination; Ubiquitin conjugation;
SY   Ubiquitin-like modifier conjugation; Ubiquitinylation.
HI   PTM: Ubl conjugation.
CA   PTM.
//
ID   Ubl conjugation pathway.
AC   KW-0833
DE   Protein involved in ubiquitin-like modifier processing, activation,
DE   conjugation or deconjugation such as Ubl-activating enzymes (E1s),
DE   Ubl-conjugating enzymes (E2s), Ubl-protein ligases (E3s), some thiol
DE   proteases (Ubiquitin carboxyl-terminal hydrolases (UCH), Ubiquitin-
DE   specific processing proteases (UBP) and ubiquitin-like proteases) and
DE   the ubiquitin-like modifier proteins. Besides signaling proteolysis,
DE   ubiquitination for example can be a signal for trafficking, kinase
DE   activation and other nonproteolytic fates.
SY   Ubiquitin conjugation pathway;
SY   Ubiquitin-like modifier conjugation pathway.
HI   Biological process: Ubl conjugation pathway.
CA   Biological process.
//
ID   Unfolded protein response.
AC   KW-0834
DE   Protein involved in the unfolded protein response. An accumulation of
DE   unfolded proteins in the ER lumen triggers a stress response,
DE   resulting in the transcriptional induction in the nucleus of a set of
DE   genes, whose products are involved in protein folding, assembly and
DE   modification as well as in phospholipid biosynthesis. The unfolded
DE   protein response (UPR) is the intracellular pathway that mediates
DE   signaling from the endoplasmic reticulum (ER) to the nucleus. UPR is
DE   also tightly linked to ER-associated protein degradation (ERAD). UPR
DE   is a ubiquitous mechanism observed in all eukaryotes from humans to
DE   yeast.
SY   ER stress pathway; ER stress response; UPR.
GO   GO:0006986; response to unfolded protein
HI   Biological process: Unfolded protein response.
CA   Biological process.
//
ID   Urea cycle.
AC   KW-0835
DE   Protein involved in the urea cycle. This is a metabolic pathway in
DE   which ammonia, produced during amino acid degradation, is converted to
DE   urea in the liver, through a series of reactions that are distributed
DE   between the mitochondrial matrix and the cytosol.
SY   Krebs-Henseleit cycle.
GO   GO:0000050; urea cycle
HI   Biological process: Urea cycle.
CA   Biological process.
//
ID   Usher syndrome.
AC   KW-0836
DE   Protein which, if defective, causes Usher syndrome, an autosomal
DE   recessive disorder characterized by sensorineural hearing loss and
DE   retinitis pigmentosa leading to visual impairment. There are three
DE   clinical subtypes: Usher syndrome type 1 (USH1), characterized by
DE   congenital profound deafness, constant vestibular dysfunction, and
DE   prepubertal onset of retinitis pigmentosa; Usher syndrome type 2
DE   (USH2), associated with moderate to severe hearing loss, normal
DE   vestibular function, and onset of retinitis pigmentosa during the
DE   second decade of life; and Usher syndrome type 3 (USH3), characterized
DE   by progressive hearing loss, variable vestibular function, and adult
DE   onset retinitis pigmentosa.
SY   Sensorineural deafness with retinitis pigmentosa; Usher's syndrome.
HI   Disease: Deafness; Usher syndrome.
CA   Disease.
//
ID   Vacuole.
AC   KW-0926
DE   Protein related to the vacuole of a cell. The precise form and
DE   function of vacuoles may vary between phyla. Plant vacuoles are among
DE   the best characterized. They are generally large fluid-filled
DE   compartments in the cytoplasm, bounded by a membrane called the
DE   tonoplast; individual vacuoles can fuse to form larger species.
DE   Examples include the lytic vacuole, the storage vacuole and the
DE   lutoid. One important function of plant vacuoles is the maintenance of
DE   hydrostatic pressure. Other eukaryotes employ vacuoles for a variety
DE   of purposes, including storage (as in the yeast lysosome/vacuole),
DE   secretion and phagocytosis. In Protozoa, contractile vacuoles can be
DE   used to discharge water from the cytoplasm to the external
DE   environment.
GO   GO:0005773; vacuole
HI   Cellular component: Vacuole.
CA   Cellular component.
//
ID   Vanadium.
AC   KW-0837
DE   Protein whose function is vanadium-dependent. Vanadium is a transition
DE   metal, chemical symbol V.
HI   Ligand: Vanadium.
WW   https://www.webelements.com/vanadium/
CA   Ligand.
//
ID   Vasoactive.
AC   KW-0838
DE   Protein which is vasoactive, i.e. has a constricting or dilating
DE   effect on the caliber of blood vessels.
GO   GO:0097746; blood vessel diameter maintenance
HI   Molecular function: Vasoactive.
CA   Molecular function.
//
ID   Vasoconstrictor.
AC   KW-0839
DE   Protein which constricts the caliber of blood vessels.
GO   GO:0042310; vasoconstriction
HI   Molecular function: Vasoactive; Vasoconstrictor.
CA   Molecular function.
//
ID   Vasodilator.
AC   KW-0840
DE   Protein which dilates the caliber of blood vessels.
GO   GO:0042311; vasodilation
HI   Molecular function: Vasoactive; Vasodilator.
CA   Molecular function.
//
ID   Viral attachment to host adhesion receptor.
AC   KW-1233
DE   Virion surface protein implicated in the initial binding to a specific
DE   host adhesion molecule. Adhesion receptors can be for example
DE   proteoglycans, sialic acids or a protein receptor. This initial
DE   attachment is not sufficient for triggering virus entry into host
DE   cell. In prokaryotic viruses, the primary attachment is called
DE   reversible adsorption.
GO   GO:0098671; adhesion receptor-mediated virion attachment to host cell
HI   Cellular component: Virion; Viral attachment to host adhesion receptor.
HI   Biological process: Host-virus interaction; Viral attachment to host cell; Viral attachment to host adhesion receptor.
HI   Biological process: Virus entry into host cell; Viral attachment to host cell; Viral attachment to host adhesion receptor.
CA   Biological process.
//
ID   Viral attachment to host cell.
AC   KW-1161
DE   Viral surface protein implicated in the binding to specific host
DE   surface molecule(s). This binding can lead to virion entry into the
DE   host cell, it can trigger signaling pathways, or it can allow the
DE   virion to be carried by the host cell to a specific organ.
SY   Virion attachment to host cell surface.
GO   GO:0019062; virion attachment to host cell
HI   Biological process: Host-virus interaction; Viral attachment to host cell.
HI   Cellular component: Virion; Viral attachment to host cell.
HI   Biological process: Virus entry into host cell; Viral attachment to host cell.
CA   Biological process.
//
ID   Viral attachment to host cell flagellum.
AC   KW-1240
DE   Virion protein involved in the primary attachment to host flagellar
DE   receptor. This attachment allows the prokaryotic virus to move along
DE   the host flagellum to find its entry receptor for viral genome
DE   penetration. Some prokaryotic viruses such as bacteriophages Chi or
DE   PV22 specifically interact with their host's flagellum, move toward
DE   the base of the flagellum to come in contact with the host cytoplasmic
DE   membrane and deliver the viral genome into the host cytoplasm.
GO   GO:0098931; virion attachment to host cell flagellum
HI   Cellular component: Virion; Viral attachment to host cell flagellum.
HI   Biological process: Host-virus interaction; Viral attachment to host cell; Viral attachment to host cell flagellum.
HI   Biological process: Virus entry into host cell; Viral attachment to host cell; Viral attachment to host cell flagellum.
CA   Biological process.
//
ID   Viral attachment to host cell pilus.
AC   KW-1175
DE   Virion protein involved in the interaction with bacterial pili, which
DE   are retractile filaments that protrude from bacteria with 2 membranes
DE   (Gram-negative bacteria). Binding to the pilus is followed by
DE   retraction of the pilus, which translocates the bound virion to the
DE   bacterial surface and allows subsequent viral genome penetration into
DE   host cytoplasm. Bacteriophages M13, f1, fd, R17, Qbeta, Pf1, Pf3,
DE   phiKMV or phi6 for example utilize the host cell pilus as an
DE   attachment structure.
GO   GO:0039666; virion attachment to host cell pilus
HI   Cellular component: Virion; Viral attachment to host cell pilus.
HI   Biological process: Host-virus interaction; Viral attachment to host cell; Viral attachment to host cell pilus.
HI   Biological process: Virus entry into host cell; Viral attachment to host cell; Viral attachment to host cell pilus.
CA   Biological process.
//
ID   Viral attachment to host entry receptor.
AC   KW-1234
DE   Virion surface protein implicated in the binding to a secondary
DE   specific host surface molecule(s), which triggers the internalization
DE   of viral genome and possibly other viral components into the host
DE   cell. In prokaryotic viruses, the attachment to a host entry receptor
DE   is called irreversible adsorption.
GO   GO:0098670; entry receptor-mediated virion attachment to host cell
HI   Cellular component: Virion; Viral attachment to host entry receptor.
HI   Biological process: Host-virus interaction; Viral attachment to host cell; Viral attachment to host entry receptor.
HI   Biological process: Virus entry into host cell; Viral attachment to host cell; Viral attachment to host entry receptor.
CA   Biological process.
//
ID   Viral baseplate protein.
AC   KW-1226
DE   Viral protein part of the virion base plate of tailed prokaryotic
DE   viruses such as Caudovirales. The baseplate is a multiprotein
DE   component at the end of the tail and to which fibers of tailed phages
DE   may be attached. Sometimes referred to as the tail tip or tip
DE   structure in Siphoviridae.
GO   GO:0098025; virus tail, baseplate
HI   Cellular component: Virion; Viral tail protein; Viral baseplate protein.
CA   Cellular component.
//
ID   Viral budding.
AC   KW-1198
DE   Viral protein involved in the budding of a viral particle through a
DE   cellular membrane into the extracellular space or into a cellular
DE   compartment.
GO   GO:0046755; viral budding
HI   Biological process: Viral release from host cell; Viral budding.
CA   Biological process.
//
ID   Viral budding via the host ESCRT complexes.
AC   KW-1187
DE   Viral protein which recruits the cellular ESCRT (Endosomal Sorting
DE   Complex Required for Transport) to mediate host-assisted viral
DE   budding. Specific motifs in enveloped viruses' proteins called late
DE   assembly domains (L-domains) are responsible for recruiting the ESCRT
DE   machinery directly or via ESCRT-associated proteins like PDCD6IP.
GO   GO:0039702; viral budding via host ESCRT complex
HI   Biological process: Host-virus interaction; Viral budding via the host ESCRT complexes.
HI   Biological process: Viral release from host cell; Viral budding; Viral budding via the host ESCRT complexes.
CA   Biological process.
//
ID   Viral capsid assembly.
AC   KW-0118
DE   Viral protein involved in the assembly of the capsid. In most cases
DE   virion assembly is spontaneous, but viruses like adenoviruses,
DE   herpesviruses, microviruses and tailed bacteriophages need the help of
DE   scaffolding proteins to assemble their capsid. Maturation steps that
DE   remove the scaffolding proteins and induce structural changes in the
DE   assembled capsid are also often part of the assembly process.
SY   Viral procapsid assembly.
GO   GO:0019069; viral capsid assembly
HI   Biological process: Viral release from host cell; Viral capsid assembly.
CA   Biological process.
//
ID   Viral capsid maturation.
AC   KW-1273
DE   Viral protein involved in the refolding and structural rearrangements
DE   of the procapsid shell that give rise to the more stable mature capsid
DE   structure. These maturation events occur during the intracellular
DE   capsid assembly process. In many cases, procapsid maturation is
DE   initiated by the activation of a viral protease. Most bacterial
DE   viruses as well as Herpesviruses assemble as a procapsid that mature
DE   through a massive conformational change of the surface shell.
SY   Viral procapsid maturation.
GO   GO:0046797; viral procapsid maturation
HI   Biological process: Viral release from host cell; Viral capsid assembly; Viral capsid maturation.
CA   Biological process.
//
ID   Viral contractile tail ejection system.
AC   KW-1242
DE   Viral protein that constitutes the contractile ejection system carried
DE   by some tailed prokaryotic viruses such as the Myoviridae. This
DE   structure is able to penetrate the host cell envelope, to deliver the
DE   viral genome, and possibly some specific proteins, into the cell
DE   cytoplasm. A contractile ejection system is composed at least of the
DE   contractile sheath, the internal noncontractile tube, the baseplate
DE   and the terminator complex. Sheath contraction drives the rigid
DE   internal tube through the host cell envelope. Proteins of the ejection
DE   apparatus can play an active or a structural role in ejection.
SY   Viral genome injection via long contractile tail.
GO   GO:0099000; viral genome ejection through host cell envelope, contractile tail mechanism
HI   Cellular component: Virion; Viral contractile tail ejection system.
HI   Biological process: Virus entry into host cell; Viral penetration into host cytoplasm; Viral genome ejection through host cell envelope; Viral contractile tail ejection system.
HI   Molecular function: Viral contractile tail ejection system.
CA   Molecular function.
//
ID   Viral DNA replication.
AC   KW-1194
DE   Viral protein involved in the synthesis of multiple copies of the
DE   viral DNA genome. The replicated genomes provide support for further
DE   viral transcription or are assembled into progeny virions.
GO   GO:0039693; viral DNA genome replication
HI   Biological process: DNA replication; Viral DNA replication.
HI   Biological process: Viral DNA replication.
CA   Biological process.
//
ID   Viral envelope protein.
AC   KW-0261
DE   Protein of the viral envelope, a lipoprotein membrane which forms the
DE   outermost layer of the virion in certain viruses.
GO   GO:0019031; viral envelope
HI   Cellular component: Virion; Viral envelope protein.
CA   Cellular component.
//
ID   Viral exotoxin.
AC   KW-1255
DE   Virally encoded toxin that acts as a host virulence factor against
DE   another organism. Viral exotoxins are mostly expressed from integrated
DE   viral genomes. Bacterium host, bacterial populations, and the encoding
DE   virus/provirus probably benefit from the expression of such exotoxins.
DE   Although prokaryotic viruses can kill their host if they switch to the
DE   lytic cycle, provirus encoding exotoxins (e.g. shiga toxin, diphtheria
DE   toxin) are often retained for the sake of bacterial utility.
HI   Molecular function: Toxin; Viral exotoxin.
HI   Biological process: Virulence; Modulation of host virulence by virus; Viral exotoxin.
CA   Molecular function.
//
ID   Viral extrusion.
AC   KW-1249
DE   Viral protein involved in the extrusion of viral particles from the
DE   host prokaryotic cell. Extrusion is a concerted mechanism of assembly
DE   and secretion used by filamentous phages to release mature viral
DE   particles without inducing host cell lysis.
GO   GO:0099045; viral extrusion
HI   Biological process: Viral release from host cell; Viral extrusion.
CA   Biological process.
//
ID   Viral genome circularization.
AC   KW-1253
DE   Viral protein that is involved in or facilitates the conversion of a
DE   linear double stranded DNA viral genome into a circular form, either
DE   by homologous recombination between redundant ends or by association
DE   of complementary single stranded ends (sticky ends). Circular genomes
DE   can support rolling circle replication and, for many viruses, genome
DE   circularization is also necessary for latency.
GO   GO:0099009; viral genome circularization
HI   Biological process: Virus entry into host cell; Viral genome circularization.
CA   Biological process.
//
ID   Viral genome ejection through host cell envelope.
AC   KW-1171
DE   Viral protein that constitutes the ejection system carried by some
DE   prokaryotic viruses. These structures are able to penetrate the host
DE   cell envelope in order to deliver the viral genome, and possibly also
DE   some specific proteins, into the cell cytoplasm.
SY   Viral genome ejection through host membranes.
GO   GO:0039678; viral genome ejection through host cell envelope
HI   Biological process: Virus entry into host cell; Viral penetration into host cytoplasm; Viral genome ejection through host cell envelope.
CA   Biological process.
//
ID   Viral genome excision.
AC   KW-1250
DE   Viral protein involved in latent provirus DNA excision from the host
DE   genome following induction. Bacteriophage lambda for example expresses
DE   an excisionase that manages excision of the viral genome from the host
DE   genome.
GO   GO:0032359; provirus excision
HI   Biological process: Viral genome excision.
CA   Biological process.
//
ID   Viral genome integration.
AC   KW-1179
DE   Viral protein involved in the integration of a virus genome into the
DE   host DNA. Integrated viral DNA is referred to as a provirus in the
DE   case of retroviruses or prophage in the case of prokaryotic viruses.
DE   The integrated viral genome does not necessarily make new DNA copies
DE   of itself while integrated into a host genome. Instead, it can remain
DE   latent and be passively replicated along with the host genome and
DE   passed on to the original cell's offspring; all descendants of the
DE   infected cell will also bear it in their genomes. The host's
DE   environmental conditions changes can however reactivate the virus
DE   leading to viral transcription and production of new infectious
DE   viruses (productive infection). Integration is a crucial step in
DE   replication of retroviruses, as well as some phages. Integration is
DE   not part of the viral replication cycle of phycodnaviruses, adeno-
DE   associated virus type 2, and human herpesvirus 6A genome, but can
DE   occasionally occur.
GO   GO:0044826; viral genome integration into host DNA
GO   GO:0075713; establishment of integrated proviral latency
HI   Biological process: DNA integration; Viral genome integration.
HI   Biological process: Virus entry into host cell; Viral genome integration.
CA   Biological process.
//
ID   Viral genome packaging.
AC   KW-0231
DE   Protein involved in actively packaging the replicated viral genome
DE   into a protective shell or envelope. Such packaging proteins are
DE   present for example in adenoviruses, herpesviruses and tailed
DE   bacteriophages. In bacteriophages, the packaging proteins complex is
DE   involved in recognizing and selecting a neo-synthesized viral genome
DE   in order to translocate it into a pre-assembled empty procapsid. DNA
DE   cleavage is sometimes coupled to genome packaging as well as
DE   maturation steps that induce structural changes in the assembled
DE   capsid.
GO   GO:0019072; viral genome packaging
HI   Biological process: Viral release from host cell; Viral genome packaging.
CA   Biological process.
//
ID   Viral immunoevasion.
AC   KW-0899
DE   Viral protein involved in evading host innate and adaptive immune
DE   responses, allowing optimized viral replication, propagation, or
DE   persistence in the host. The protein allows viruses to avoid/escape
DE   immune detection or neutralize/inactivate the host immune defenses to
DE   ensure virus survival within its host. The innate immune system is a
DE   non-specific defense system found in all cellular organisms. In
DE   metazoans and plants, it includes the intracellular pattern
DE   recognition receptors (PRRs) that detect pathogen-associated molecular
DE   patterns (PAMPs). In plants and invertebrates, it includes the RNA
DE   interference (RNAi) system. Plants also have effector-triggered
DE   immunity (ETI). In metazoans, it includes the cell-dependent
DE   mechanisms (e.g. phagocytes) or secreted factors. Bacteria and archaea
DE   have an innate immune system relying on various systems (e.g. the
DE   restriction-modification system, Pycsar). The adaptive (or acquired)
DE   immune system is a specific defense. In vertebrates, it is mediated by
DE   T and B lymphocytes expressing specific receptors. Bacteria and
DE   archaea have adaptive immunity, the CRISPR-Cas system.
SY   Immunoevasin; Viral host defense evasion; Viral immune evasion.
GO   GO:0019049; mitigation of host antiviral defense response
HI   Biological process: Host-virus interaction; Viral immunoevasion.
CA   Biological process.
//
ID   Viral ion channel.
AC   KW-1182
DE   Small transmembrane protein that homo-oligomerizes to form a viral ion
DE   channel usually expressed in the viral envelope and host cell
DE   membranes. These channels affect membrane permeability to ions and
DE   play an important role in facilitating virus entry, assembly and
DE   release, as well as modulating the ion homeostasis of host cells.
DE   Viral ion channels are not necessarily required for the production of
DE   infectious virions, although their expression usually significantly
DE   increases growth. During influenza A virus entry for example, the M2
DE   proton channel allows protons from the acidic endosome to enter the
DE   enveloped virion, initiating pH-dependent uncoating of the genome. In
DE   certain influenza A subtypes, M2 also equilibrates the intraluminal pH
DE   of the trans-Golgi network with the cytoplasm, preventing premature
DE   conformational changes in the viral fusion protein during budding.
SY   Viroporin.
GO   GO:0005216; monoatomic ion channel activity
GO   GO:0033644; host cell membrane
GO   GO:0039707; pore formation by virus in membrane of host cell
GO   GO:0051259; protein complex oligomerization
HI   Biological process: Transport; Ion transport; Viral ion channel.
HI   Molecular function: Ion channel; Viral ion channel.
CA   Molecular function.
//
ID   Viral latency.
AC   KW-1251
DE   Viral protein expressed primarily to establish, maintain or terminate
DE   latency, the part of the viral life cycle during which a virus lies
DE   dormant (latent) within a cell. This part of the virus life cycle is
DE   called the lysogenic part in prokaryotic viruses. During latency, the
DE   viral genome can either exist as a provirus integrated in the host
DE   genome (proviral latency) or as a linear or circular plasmid in the
DE   host cell (episomal latency). The virus does not replicate, but is
DE   passively duplicated when the host divides. In eukaryotes for example,
DE   HHV-1 and HHV-3 establish episomal latency in neurons. HIV is
DE   integrated as a provirus in the genome of resting CD4-positive T
DE   cells, allowing the virus to persist for years. Following changes in
DE   the environmental conditions of the host, reactivation of the virus
DE   can occur leading to viral transcription and production of new
DE   infectious viruses.
SY   Viral lysogeny.
GO   GO:0019042; viral latency
HI   Biological process: Viral latency.
CA   Biological process.
//
ID   Viral latency initiation and maintenance.
AC   KW-1276
DE   Viral protein expressed primarily to establish and maintain latency,
DE   the part of the viral life cycle during which a virus lies dormant
DE   (latent) within a cell. This part of the virus life cycle is called
DE   the lysogenic part in prokaryotic viruses. During latency, the viral
DE   genome can either exist as a provirus integrated in the host genome
DE   (proviral latency) or as a linear or circular plasmid in the host cell
DE   (episomal latency). The virus does not replicate, but is passively
DE   duplicated when the host divides.
HI   Biological process: Viral latency; Viral latency initiation and maintenance.
CA   Biological process.
//
ID   Viral long flexible tail ejection system.
AC   KW-1243
DE   Viral protein that constitutes the noncontractile ejection system
DE   carried by some long-tailed prokaryotic viruses such as the
DE   Siphoviridae. This ejection system is composed at least of a
DE   noncontractile tube and a tail tip which is able to penetrate the host
DE   cell envelope to deliver the viral genome, and possibly some specific
DE   proteins, into the cell cytoplasm. Proteins of the ejection apparatus
DE   can play an active or a structural role in ejection.
SY   Viral genome injection via long noncontractile tail.
GO   GO:0099001; viral genome ejection through host cell envelope, long flexible tail mechanism
HI   Cellular component: Virion; Viral long flexible tail ejection system.
HI   Biological process: Virus entry into host cell; Viral penetration into host cytoplasm; Viral genome ejection through host cell envelope; Viral long flexible tail ejection system.
HI   Molecular function: Viral long flexible tail ejection system.
CA   Molecular function.
//
ID   Viral matrix protein.
AC   KW-0468
DE   Protein that organises and maintains virion structure. It usually
DE   interacts directly with cellular membranes and is involved in the
DE   budding process. In some enveloped RNA viruses, it acts as a bridge
DE   between virion membrane and nucleocapsid.
GO   GO:0039660; structural constituent of virion
HI   Cellular component: Virion; Viral matrix protein.
CA   Cellular component.
//
ID   Viral movement protein.
AC   KW-0916
DE   Plant viral protein that enables the viral nucleic acid to move
DE   between adjacent plant cells via the plasmodesmata.
GO   GO:0046740; transport of virus in host, cell to cell
HI   Biological process: Transport; Viral movement protein.
HI   Molecular function: Viral movement protein.
CA   Molecular function.
//
ID   Viral nucleoprotein.
AC   KW-0543
DE   Viral protein conjugated with nucleic acid (DNA or RNA).
SY   Viral nucleocapsid protein.
GO   GO:0019013; viral nucleocapsid
HI   Cellular component: Virion; Viral nucleoprotein.
HI   Molecular function: Viral nucleoprotein.
CA   Molecular function.
//
ID   Viral occlusion body.
AC   KW-0842
DE   Protein component of the viral occlusion body, a crystalline protein
DE   matrix which surrounds the nucleocapsids of some insect viruses
DE   (baculoviridae, entomopoxvirinae, cypovirus). Viral occlusion bodies
DE   are produced either in the nucleus (baculoviridae) or in the cytoplasm
DE   (poxvirinae and cypovirus) of the infected cells and confer resistance
DE   to adverse environmental conditions on viruses. They are made from
DE   polyhedrin (nucleopolyhedrovirus, cypovirus), granulin (granulovirus),
DE   spheroidin and spherulin (entomopox-virinae) and are dissolved by the
DE   alkaline pH of the insect gut, thus resulting in the release of
DE   infectious virus particles.
GO   GO:0039679; viral occlusion body
HI   Cellular component: Viral occlusion body.
CA   Cellular component.
//
ID   Viral penetration into host cytoplasm.
AC   KW-1162
DE   Viral protein involved in the entry of the entire virion, some of its
DE   contents or at least its genetic material into the host cell
DE   cytoplasm. Entry is achieved through pore formation, membrane fusion,
DE   pilus retraction, ejection, permeabilization and/or endocytosis
DE   mechanisms. Penetration reactions occur mainly in five locations: the
DE   cell membrane, early and late endosomes, caveosomes, and the ER. In
DE   prokaryotes, membrane fusion, pore formation through a puncturing
DE   device, ejection, pilus retraction or permeabilization occur at the
DE   plasma membrane, as well as at the outer membrane in prokaryotes with
DE   2 membranes.
SY   Translocation of virus into host cell;
SY   Virion penetration into host cell.
GO   GO:0046718; viral entry into host cell
HI   Biological process: Virus entry into host cell; Viral penetration into host cytoplasm.
CA   Biological process.
//
ID   Viral penetration into host cytoplasm via pilus retraction.
AC   KW-1241
DE   Viral protein involved in the entry of the virion into the host
DE   cytoplasm via the host pili, which are retractile filaments that
DE   protrude from bacteria with 2 membranes (Gram-negative bacteria).
DE   Entry of bound prokaryotic viruses such as filamentous viruses is
DE   achieved through the retraction of host pilus and translocation of the
DE   virion through the basis of the pilus to reach the host cytoplasm.
DE   Examples of bacteriophages which utilize the host cell pilus to
DE   penetrate into host cytoplasm are bacteriophages M13, f1, fd, R17.
GO   GO:0039667; viral entry into host cell via pilus retraction
HI   Cellular component: Virion; Viral penetration into host cytoplasm via pilus retraction.
HI   Biological process: Virus entry into host cell; Viral penetration into host cytoplasm; Viral penetration into host cytoplasm via pilus retraction.
CA   Biological process.
//
ID   Viral penetration into host nucleus.
AC   KW-1163
DE   Viral protein necessary for the penetration of the viral genome into
DE   the host cell nucleus either via active nuclear transport through
DE   nuclear pore complexes (NPCs) or DNA injection through the nuclear
DE   membrane. Nuclear membrane permeabilization might also be possible.
DE   Viruses can also enter the nucleus during mitosis when the nuclear
DE   membrane temporarily disintegrates (e.g. most retroviruses). All these
DE   strategies to cross the nuclear envelope barrier are associated with
DE   various levels of capsid disassembly, since virus can pass intact
DE   (e.g. papovaviruses) or, in the case of injection, only the viral
DE   genome enters the nucleus (e.g. herpesviruses).
SY   Entry of virus into host nucleus; Virion entry into host nucleus;
SY   Virion penetration into host nucleus.
GO   GO:0075732; viral penetration into host nucleus
HI   Biological process: Virus entry into host cell; Viral penetration into host nucleus.
CA   Biological process.
//
ID   Viral penetration via lysis of host organellar membrane.
AC   KW-1174
DE   Viral membrane-lytic protein, usually associated with the viral capsid
DE   or released through partial programmed disassembly of the capsid, that
DE   induces major rupture of the bilayer integrity of host endosomal,
DE   lysosomal, or caveosomal membrane to allow viral escape and
DE   penetration into the cytoplasm. These viral lytic proteins may need to
DE   be activated, mostly through endosomal acidic pH or receptor binding
DE   to display membrane lytic activity. Viruses such as human adenoviruses
DE   group C and D lyse the host endosomal membrane to penetrate into the
DE   host cytoplasm.
GO   GO:0039664; lysis of host organelle involved in viral entry into host cell
HI   Biological process: Virus entry into host cell; Viral penetration into host cytoplasm; Viral penetration via lysis of host organellar membrane.
CA   Biological process.
//
ID   Viral penetration via permeabilization of host membrane.
AC   KW-1173
DE   Viral membrane-penetration protein, usually associated with the viral
DE   capsid or released through partial programmed disassembly of the
DE   capsid, that locally permeabilizes the bilayer of a host membrane to
DE   allow virion penetration into the cytoplasm. Viral membrane-
DE   penetration proteins often need to be activated, mostly through
DE   endosomal acidic pH or receptor binding to display their membrane
DE   penetrating activity. Non-enveloped viruses such as parvovirus, human
DE   reovirus, BDV, BTV, rotavirus, papillomavirus, Flock house virus
DE   permeabilize the host endosomal membrane to penetrate the host
DE   cytoplasm.
SY   Viral penetration via host membrane disruption by virus;
SY   Viral penetration via perforation of host membrane by virus.
GO   GO:0039665; permeabilization of host organelle membrane involved in viral entry into host cell
GO   GO:0099008; viral entry via permeabilization of inner membrane
HI   Biological process: Virus entry into host cell; Viral penetration into host cytoplasm; Viral penetration via permeabilization of host membrane.
CA   Biological process.
//
ID   Viral primary envelope fusion with host outer nuclear membrane.
AC   KW-1181
DE   Viral protein implicated in fusion of the herpesviruses' primary
DE   envelope with the host outer nuclear membrane during egress. During
DE   egress, herpesviruses acquire a transitory, primary envelope as they
DE   bud at the inner nuclear membrane and gain access to the perinuclear
DE   space. This membrane is lost by fusing with the outer nuclear membrane
DE   during nuclear exit.
GO   GO:0039700; fusion of viral membrane with host outer nuclear membrane
HI   Biological process: Viral release from host cell; Viral primary envelope fusion with host outer nuclear membrane.
CA   Biological process.
//
ID   Viral reactivation from latency.
AC   KW-1272
DE   Viral protein involved in virus reactivation from latency to
DE   replication, thereby putting an end to the latency phase in the viral
DE   life cycle. Changes in the environmental conditions of the host often
DE   reactivate the virus leading to viral transcription and production of
DE   new infectious viruses (productive infection).
SY   Release from viral latency.
GO   GO:0019046; release from viral latency
HI   Biological process: Viral latency; Viral reactivation from latency.
HI   Biological process: Viral reactivation from latency.
CA   Biological process.
//
ID   Viral receptor tropism switching.
AC   KW-1264
DE   A switch in the host range specificity occurs in some bacterial
DE   viruses through massive sequence variation of their host-binding
DE   receptor. Sequence variation can be induced by site-specific inversion
DE   of a DNA segment in their genome or by a diversity-generating
DE   retroelement. Inversion is catalyzed by a specific recombinase called
DE   invertase and consists of a reciprocal recombination event within two
DE   inverted repeats present in the viral genome that leads to the
DE   alternate expression of two different sets of genes involved in tail
DE   fiber biosynthesis. Mu-like viruses and P1-like viruses, for example,
DE   encode a recombinase responsible for the switch in the targeted host.
DE   Diversity-generating retroelements (DGR) like in BPP-1 virus also
DE   allow tropism switching by creating a mutant copy of an invariant DNA
DE   template repeat by transcription and reverse transcription and
DE   introducing this mutated sequence in the receptor-binding protein
DE   sequence.
GO   GO:0098678; viral tropism switching
HI   Biological process: Virus entry into host cell; Viral receptor tropism switching.
CA   Biological process.
//
ID   Viral release from host cell.
AC   KW-1188
DE   Viral protein involved in the release of virions from an infected cell
DE   to allow cell-to-cell spread of virus. Once assembled at the
DE   replication site, viral particles can be released by budding,
DE   exocytosis, extrusion or host cell lysis. Some viruses also mediate
DE   direct transport of their viral genome to adjacent cells thanks to
DE   movement proteins.
GO   GO:0019076; viral release from host cell
HI   Biological process: Viral release from host cell.
CA   Biological process.
//
ID   Viral RNA replication.
AC   KW-0693
DE   Viral protein involved in the SYnthesis of multiple copies of the
DE   viral RNA genome. The replicated genomes provide support for further
DE   viral transcription or are assembled into progeny virions.
GO   GO:0039694; viral RNA genome replication
HI   Biological process: Viral RNA replication.
CA   Biological process.
//
ID   Viral short tail ejection system.
AC   KW-1244
DE   Virion protein that constitutes the noncontractile ejection system
DE   carried by some short-tailed prokaryotic viruses such as some
DE   Podoviridae. This ejection system is composed at least of the tail
DE   tube and ejection proteins. Upon receptor binding, proteins located
DE   inside the capsid (head) rearrange to extend the tail tube, creating a
DE   channel spanning the periplasmic space. This hydrophilic channel
DE   directs the viral genome, and possibly some specific proteins, into
DE   the cytoplasm and protects it from periplasmic nucleases. Once the
DE   viral genome is in the host cytoplasm, the channel collapses and
DE   seals. Bacteriophage T7 for example expresses ejection proteins that
DE   partition into the host outer and cytoplasmic membranes and allow
DE   transport of viral DNA across the host envelope. Proteins of the
DE   ejection apparatus can play an active or a structural role in
DE   ejection.
SY   Viral genome injection via short noncontractile tail.
GO   GO:0099002; viral genome ejection through host cell envelope, short tail mechanism
HI   Cellular component: Virion; Viral short tail ejection system.
HI   Biological process: Virus entry into host cell; Viral penetration into host cytoplasm; Viral genome ejection through host cell envelope; Viral short tail ejection system.
HI   Molecular function: Viral short tail ejection system.
CA   Molecular function.
//
ID   Viral tail assembly.
AC   KW-1245
DE   Viral protein involved in tail assembly. Some tailed bacteriophages
DE   need chaperones that help with the assembly of their tail.
GO   GO:0098003; viral tail assembly
HI   Biological process: Viral release from host cell; Viral tail assembly.
CA   Biological process.
//
ID   Viral tail fiber assembly.
AC   KW-1246
DE   Viral protein involved in tail fibers or spike assembly. Some tailed
DE   bacteriophages need chaperones that help with the assembly of their
DE   fibers or spikes. T4 for example encodes a general tail fiber
DE   chaperone that is needed for the correct assembly of the short and
DE   long tail fiber proteins.
GO   GO:0098004; virus tail fiber assembly
HI   Biological process: Viral release from host cell; Viral tail assembly; Viral tail fiber assembly.
CA   Biological process.
//
ID   Viral tail fiber protein.
AC   KW-1230
DE   Viral fibrous protein part of the virion fiber, which is a thin long
DE   rod like structure, unique or multiple, appended to the tail of
DE   prokaryotic viruses and used for attachment to the host cell. Shorter
DE   appendages are called tail spikes (e.g. Podoviridae) or whiskers.
GO   GO:0098024; virus tail, fiber
HI   Cellular component: Virion; Viral tail protein; Viral tail fiber protein.
CA   Cellular component.
//
ID   Viral tail protein.
AC   KW-1227
DE   Viral protein part of the virion tail of prokaryotic viruses such as
DE   Caudovirales. The tail is usually composed of a tube, a tail sheath
DE   when contractile, a base plate or tip and tail long or short fibers.
GO   GO:0098015; virus tail
HI   Cellular component: Virion; Viral tail protein.
CA   Cellular component.
//
ID   Viral tail sheath protein.
AC   KW-1229
DE   Viral protein part of the virion tail sheath of prokaryotic viruses.
DE   The tail sheath is an external contractile envelope wrapping the tail
DE   tube in some viruses (e.g. Myoviridae).
GO   GO:0098027; virus tail, sheath
HI   Cellular component: Virion; Viral tail protein; Viral tail sheath protein.
HI   Molecular function: Viral contractile tail ejection system; Viral tail sheath protein.
CA   Cellular component.
//
ID   Viral tail tube protein.
AC   KW-1228
DE   Viral protein part of the virion tail tube of prokaryotic viruses such
DE   as Caudovirales. The tail tube is the channel for DNA ejection into
DE   the host cytoplasm and can be wrapped in an external contractile
DE   envelope in some viruses (e.g. Myoviridae). Also called tail shaft in
DE   some Siphoviridae.
GO   GO:0098026; virus tail, tube
HI   Biological process: Virus entry into host cell; Viral penetration into host cytoplasm; Viral genome ejection through host cell envelope; Viral tail tube protein.
HI   Cellular component: Virion; Viral tail protein; Viral tail tube protein.
CA   Cellular component.
//
ID   Viral transcription.
AC   KW-1195
DE   Viral Protein involved in the synthesis of messenger RNAs. The process
DE   can occur in the host cell nucleus or cytoplasm, and the genomic
DE   template can be viral DNA or RNA, single- or double-stranded.
GO   GO:0019083; viral transcription
HI   Biological process: Viral transcription.
CA   Biological process.
//
ID   Virion.
AC   KW-0946
DE   Viral protein detected in the virion.
GO   GO:0044423; virion component
HI   Cellular component: Virion.
CA   Cellular component.
//
ID   Virion maturation.
AC   KW-0917
DE   Viral protein involved in the maturation of the immature virion into
DE   the mature virion, once the virion has been released from the host
DE   cell. Maturation usually involves proteolysis events and changes in
DE   the folding of the virion proteins.
SY   Viral procapsid maturation.
GO   GO:0019075; virus maturation
HI   Biological process: Viral release from host cell; Virion maturation.
CA   Biological process.
//
ID   Virion tegument.
AC   KW-0920
DE   Viral structural protein of the tegument, a protein structure that
DE   resides between the capsid and envelope of herpesviruses and which
DE   appears amorphous in electron micrographs.
GO   GO:0019033; viral tegument
HI   Cellular component: Virion; Virion tegument.
CA   Cellular component.
//
ID   Virulence.
AC   KW-0843
DE   Protein involved in virulence, the degree of pathogenicity within a
DE   group or species of microorganisms or viruses, as indicated by case
DE   fatality rates and/or the ability of the organism to invade the
DE   tissues of the host. In some cases, the virulence factor can be borne
DE   by another organism in symbiosis with the one whose virulence is
DE   increased. Some prokaryotic viruses/proviruses for example bear
DE   exotoxins that increase the virulence of their host. A well-known
DE   bacterial exotoxin encoded by a provirus is the diphtheria toxin.
HI   Biological process: Virulence.
CA   Biological process.
//
ID   Virus endocytosis by host.
AC   KW-1164
DE   Viral protein involved in virus internalization by the host cell via
DE   endocytosis. Endocytosis can occur via: clathrin-mediated endocytosis,
DE   caveolin-mediated endocytosis or clathrin- and caveolae-independent
DE   endocytosis.
GO   GO:0075509; endocytosis involved in viral entry into host cell
HI   Biological process: Virus entry into host cell; Viral penetration into host cytoplasm; Virus endocytosis by host.
CA   Biological process.
//
ID   Virus entry into host cell.
AC   KW-1160
DE   Viral protein involved in the virion entry into a host cell. Entry is
DE   a multistep process that mostly requires binding to the target cell,
DE   penetration into the host cell cytoplasm, intracellular transport of
DE   viral components and genome release to the replication site of the
DE   virus.
GO   GO:0046718; viral entry into host cell
HI   Biological process: Virus entry into host cell.
CA   Biological process.
//
ID   Vision.
AC   KW-0844
DE   Protein involved in vision, the special sense by which objects in the
DE   external environment are perceived by the light they give off or
DE   reflect, which stimulates the photoreceptors in the retina.
GO   GO:0007601; visual perception
HI   Biological process: Sensory transduction; Vision.
CA   Biological process.
//
ID   Vitamin A.
AC   KW-0845
DE   Protein which interacts with any form of the fat-soluble vitamin A.
DE   There are three active forms of vitamin A: retinol, retinal
DE   (retinaldehyde) and retinoic acid, which are all derived from the
DE   plant beta-carotene (provitamin A). Vitamin A is essential to night
DE   vision and is also required for epithelium differentiation, bone
DE   development, reproduction and the immune response. Symptoms associated
DE   with a deficiency of vitamin A are night blindness, changes in the
DE   eyes, poor bone development, weak tooth enamel and dry skin.
SY   Retinol.
GO   GO:0016918; retinal binding
HI   Ligand: Vitamin A.
CA   Ligand.
//
ID   Vitamin C.
AC   KW-0847
DE   Protein which contains at least one vitamin C as cofactor. This water-
DE   soluble vitamin is a reducing agent in a number of reactions. As
DE   cofactor, it is required for the hydroxylation of proline residues in
DE   collagen, and in many other metabolic reactions such as in the
DE   catabolism of tyrosine and the synthesis of bile acids. Deficiency in
DE   vitamin C leads to the disease scurvy.
SY   Ascorbic acid.
GO   GO:0031418; L-ascorbic acid binding
HI   Ligand: Vitamin C.
CA   Ligand.
//
ID   Vitamin D.
AC   KW-0848
DE   Protein which interacts with any form of the fat-soluble vitamin D or
DE   protein whose transcription is regulated by the biologically active
DE   form of vitamin D, i.e. 1,25-dihydroxy vitamin D3 (1,25
DE   dihydroxycholecalciferol) also termed calcitriol. Active calcitriol is
DE   derived from ergosterol (produced in plants) and 7-dehydrocholesterol
DE   (produced in the skin). Ergocalciferol (vitamin D2) and
DE   cholecalciferol (vitamin D3) are formed by UV irradiation of
DE   ergosterol and 7-dehydrocholesterol, respectively, and processed by
DE   the same enzymatic pathway in the body to D2-calcitriol and D3-
DE   calcitriol. Deficiency in vitamin D leads to the disease rickets, in
DE   children, and osteomalacia, in adults.
GO   GO:0005499; vitamin D binding
HI   Ligand: Vitamin D.
CA   Ligand.
//
ID   VLDL.
AC   KW-0850
DE   Protein present in particles of Very Low-Density Lipoproteins or
DE   protein which interacts with them. VLDL are composed of 50%
DE   triacylglycerols, 12% cholesteryl esters, 7% free cholesterol, 18%
DE   phospholipids, and 10% proteins including apoB-100, apoC-I, apoC-II,
DE   apoC-III and apoE. Excess fatty acids or carbohydrate in the diet can
DE   be converted into triacylglycerols in the liver and packaged into
DE   VLDL. These lipoproteins are transported by the blood to muscle and
DE   adipose tissue, where activation of lipoprotein lipase by apoC-II
DE   causes the release of free fatty acids from the triacylglycerols of
DE   the VLDL.
GO   GO:0034361; very-low-density lipoprotein particle
HI   Cellular component: VLDL.
CA   Cellular component.
//
ID   Voltage-gated calcium channel impairing toxin.
AC   KW-1218
DE   Protein which interferes with the function of voltage-gated calcium
DE   channels (Cav) which are membrane proteins forming a channel in a
DE   biological membrane selectively permeable to calcium ions and open in
DE   response to a change in membrane potential. They are mostly found
DE   spider and cone snail venoms.
SY   Cav channel inhibitor.
HI   Molecular function: Toxin; Ion channel impairing toxin; Calcium channel impairing toxin; Voltage-gated calcium channel impairing toxin.
CA   Molecular function.
//
ID   Voltage-gated channel.
AC   KW-0851
DE   Protein which is a component of a voltage-gated channel. Voltage-gated
DE   ion channels are responsible for the electrical activity in a variety
DE   of cell types. They probably exist in all life forms.
SY   Voltage-gated cation channel; Voltage-gated ion channel.
GO   GO:0034220; monoatomic ion transmembrane transport
GO   GO:0034702; monoatomic ion channel complex
HI   Biological process: Transport; Ion transport; Voltage-gated channel.
HI   Molecular function: Ion channel; Voltage-gated channel.
CA   Molecular function.
//
ID   Voltage-gated chloride channel impairing toxin.
AC   KW-0870
DE   Protein which interferes with the function of voltage-gated chloride
DE   channels (ClC) which are membrane proteins forming a channel in a
DE   biological membrane selectively permeable to chloride ions, and open
DE   in response to a change in membrane potential. They are found in
DE   venoms from scorpions.
GO   GO:0017081; chloride channel regulator activity
HI   Molecular function: Toxin; Ion channel impairing toxin; Chloride channel impairing toxin; Voltage-gated chloride channel impairing toxin.
CA   Molecular function.
//
ID   Voltage-gated potassium channel impairing toxin.
AC   KW-1220
DE   Protein which interferes with the function of voltage-gated potassium
DE   channels (Kv) which are membrane proteins forming a channel in a
DE   biological membrane selectively permeable to potassium ions and open
DE   in response to a change in membrane potential. They are mostly found
DE   in scorpion and spider venoms.
HI   Molecular function: Toxin; Ion channel impairing toxin; Potassium channel impairing toxin; Voltage-gated potassium channel impairing toxin.
CA   Molecular function.
//
ID   Voltage-gated sodium channel impairing toxin.
AC   KW-0738
DE   Protein which interferes with the function of voltage-gated sodium
DE   channels (Nav) which are membrane proteins forming a channel in a
DE   biological membrane selectively permeable to sodium ions, and open in
DE   response to a change in membrane potential. They are found in various
DE   venoms from snakes, scorpions and spiders.
GO   GO:0017080; sodium channel regulator activity
HI   Molecular function: Toxin; Ion channel impairing toxin; Voltage-gated sodium channel impairing toxin.
CA   Molecular function.
//
ID   von Willebrand disease.
AC   KW-0852
DE   Protein which, if defective, causes von Willebrand disease, a
DE   hemorrhagic disorder in which the von Willebrand factor is either
DE   quantitatively or qualitatively abnormal. Usually inherited as an
DE   autosomal dominant trait though rare kindreds are autosomal recessive.
DE   Symptoms vary depending on severity and disease type but may include
DE   prolonged bleeding time, deficiency of factor VIII and impaired
DE   platelet adhesion.
HI   Biological process: Hemostasis; Blood coagulation; von Willebrand disease.
HI   Disease: von Willebrand disease.
CA   Disease.
//
ID   Waardenburg syndrome.
AC   KW-0897
DE   Protein which, if defective, causes Waardenburg syndrome, an autosomal
DE   dominant disorder, characterized by sensorineural deafness associated
DE   with pigmentary changes of the irides, hair and skin; each of these
DE   features may be uni- or bilateral. On the basis of the presence or
DE   absence of dystopia canthorum (lateral displacement of the inner
DE   corner of the eye), Waardenburg syndrome type 1 (WS1) and type 2 (WS2)
DE   are distinguished. Additionally, the association of WS1 with limb
DE   anomalies defines Waardenburg syndrome type 3 (WS3), while the
DE   association of Waardenburg features with Hirschsprung disease defines
DE   Waardenburg syndrome type 4 (WS4).
SY   WS.
HI   Disease: Deafness; Waardenburg syndrome.
CA   Disease.
//
ID   WD repeat.
AC   KW-0853
DE   Protein which contains at least one WD repeat, a conserved domain of
DE   about 40 amino acids in length. Most copies contain a central
DE   conserved Trp-Asp motif.
SY   Trp-Asp repeat; WD-40 repeat.
HI   Domain: WD repeat.
CA   Domain.
//
ID   Whooping cough.
AC   KW-0855
DE   Protein involved in the induction of whooping cough, a respiratory
DE   infection caused by the very small Gram-negative aerobic coccobacillus
DE   Bordetella pertussis. It is characterized by paroxysmal coughing often
DE   ending in a characteristic inspiratory gasp (whoop). The bacterium is
DE   a pathogen for humans and possibly for higher primates.
HI   Disease: Whooping cough.
CA   Disease.
//
ID   Williams-Beuren syndrome.
AC   KW-0856
DE   Protein which, if defective, causes Williams-Beuren syndrome (WBS), a
DE   contiguous gene deletion syndrome involving genes from chromosome band
DE   7q11.23. It is a rare developmental autosomal dominant disorder
DE   characterized by cardiovascular abnormalities, elfin face, mental and
DE   statural deficiency, characteristic dental malformation, and infantile
DE   hypercalcemia.
SY   WBS.
HI   Disease: Williams-Beuren syndrome.
CA   Disease.
//
ID   Wnt signaling pathway.
AC   KW-0879
DE   Protein involved in the Wnt signaling pathway. Wnts are a large family
DE   of cysteine-rich secreted glycoproteins that control development in
DE   organisms ranging from nematodes to mammals. Wnt genes are defined by
DE   sequence homology to the original members of the family, Wnt1 in the
DE   mouse and wingless (wg) in Drosophila. Wnt signaling is a very complex
DE   pathway which includes numerous ligands, receptors and transcriptional
DE   effectors. There is a well-characterized canonical pathway as well as
DE   diverse, less-characterized noncanonical pathways. Several components
DE   of Wnt signaling are implicated in the genesis of human cancer.
SY   Wnt signaling cascade; Wnt signalling pathway;
SY   Wnt signal transduction pathway.
GO   GO:0016055; Wnt signaling pathway
HI   Biological process: Wnt signaling pathway.
CA   Biological process.
//
ID   Xeroderma pigmentosum.
AC   KW-0857
DE   Protein which, if defective, causes xeroderma pigmentosum, an
DE   autosomal recessive disease characterized by extreme photosensitivity
DE   to ultraviolet light and the development of multiple skin cancers.
HI   Disease: Xeroderma pigmentosum.
CA   Disease.
//
ID   Xylan degradation.
AC   KW-0858
DE   Protein involved in the hydrolysis of xylan to xylose and other
DE   sugars. Xylan is a major component of hemicellulose, which is the
DE   second most common plant material in nature. The structures of xylans
DE   are complex, and several enzymes are involved in their breakdown.
DE   Xylan degrading enzymes are produced by a variety of microorganisms.
SY   Xylan hydrolysis.
GO   GO:0045493; xylan catabolic process
HI   Biological process: Carbohydrate metabolism; Polysaccharide degradation; Xylan degradation.
CA   Biological process.
//
ID   Xylose metabolism.
AC   KW-0859
DE   Protein involved in the biochemical reactions with the 5-carbon sugars
DE   xylose or xylulose. Xylose is the second most abundant sugar found in
DE   hardwood and agricultural residues.
GO   GO:0042732; D-xylose metabolic process
HI   Biological process: Carbohydrate metabolism; Xylose metabolism.
CA   Biological process.
//
ID   Zellweger syndrome.
AC   KW-0861
DE   Protein which, if defective, causes Zellweger syndrome, a fatal
DE   peroxisome biogenesis disorder associated with severe abnormalities in
DE   the brain, liver and kidney and death soon after birth. This disease
DE   is characterized by the presence of empty peroxisomes in the cells due
DE   to impaired transport of peroxisomal proteins into the peroxisomes.
SY   Cerebrohepatorenal syndrome; Cerebro-hepato-renal syndrome;
SY   CHR syndrome; ZWS.
HI   Disease: Peroxisome biogenesis disorder; Zellweger syndrome.
CA   Disease.
//
ID   Zinc.
AC   KW-0862
DE   Protein which binds at least one zinc atom, or protein whose function
DE   is zinc-dependent. Zinc is a metallic trace element, chemical symbol
DE   Zn.
HI   Ligand: Zinc.
WW   https://www.webelements.com/zinc/
CA   Ligand.
//
ID   Zinc transport.
AC   KW-0864
DE   Protein involved in the transport of zinc.
GO   GO:0006829; zinc ion transport
HI   Biological process: Transport; Ion transport; Zinc transport.
HI   Ligand: Zinc; Zinc transport.
CA   Biological process.
//
ID   Zinc-finger.
AC   KW-0863
DE   Protein which contains at least one zinc finger. A small, functional,
DE   independently folded domain that requires coordination of one or more
DE   zinc ions to stabilize its structure. Zinc fingers vary widely in
DE   structure, as well as in function, which ranges from DNA or RNA
DE   binding to protein-protein interactions and membrane association.
HI   Ligand: Metal-binding; Zinc-finger.
HI   Ligand: Zinc; Zinc-finger.
HI   Domain: Zinc-finger.
CA   Domain.
//
ID   Zymogen.
AC   KW-0865
DE   The enzymatically inactive precursor of mostly proteolytic enzymes.
SY   Proenzyme.
HI   PTM: Zymogen.
CA   PTM.
//
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