keywlist.txt
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UniProt Knowledgebase:
Swiss-Prot Protein Knowledgebase
TrEMBL Protein Database
Swiss Institute of Bioinformatics (SIB); 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: 2012_01 of 25-Jan-2012
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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 Fe2S2; [2Fe-2S] cluster; [Fe2S2] cluster; Fe2/S2 (inorganic) cluster;
SY Di-mu-sulfido-diiron; 2 iron, 2 sulfur cluster binding.
GO GO:0051537; 2 iron, 2 sulfur cluster binding
HI Ligand: Iron; 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; 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; 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 mediated 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 inhibitor.
AC KW-0008
DE Protein that inhibits both nicotinic (nAChR) and muscarinic (mAChR)
DE acetylcholine receptors. The nAChR is a postsynaptic membrane protein
DE that, after binding acetylcholine, responds by an extensive change in
DE conformation, which leads to opening of an ion-conducting channel
DE across the plasma membrane. The mAChR is a membrane protein that acts
DE through G proteins and mediates various cellular responses, including
DE inhibition of adenylate cyclase, breakdown of phosphoinositides and
DE modulation of potassium channels through the action of G proteins.
SY AChR inhibitor.
GO GO:0030550; acetylcholine receptor inhibitor activity
HI Molecular function: Toxin; Neurotoxin; Postsynaptic neurotoxin; Acetylcholine receptor inhibitor.
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 Ligand: Actin-binding.
CA Ligand.
//
ID Actin-dependent active transport of viral material.
AC KW-1178
DE Viral protein that interacts with actin and/or host cell motor
DE proteins and allows active transport along actin filaments of viral
DE material across the host cell cytoplasm. This transport probably
DE involves motor proteins like myosins or
DE polymerization/depolymerization reactions as a driving force. It is
DE apparently much more rapid than microtubule-dependent transport.
DE Viruses such as poliovirus utilize this type of intracellular
DE transport.
HI Biological process: Initiation of viral infection; Cytoplasmic active transport of viral material; Actin-dependent active transport of viral material.
CA Biological process.
//
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 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.
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.
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.
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; transferase activity, transferring acyl groups
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.
HI Biological process: Immunity; Adaptive immunity.
WW http://www.nature.com/nri/journal/v10/n1/full/nri2686.html
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-rybosylated.
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; 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 Technical term: Allosteric enzyme.
CA Technical term.
//
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 synthesis; Amino-acid anabolism; Amino-acid formation.
GO GO:0008652; cellular 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 Aminoacyl-tRNA synthase; Aminoacyl-tRNA ligase; Amino acid translase.
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:0015696; ammonium 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 Functional amyloid; Amyloid-forming; Amyloid fibril-forming;
SY Amyloid-like fibril-forming; Amyloid filament-forming;
SY Amyloid-like filament-forming; Amyloid fibre-forming;
SY Amyloid-like fibre-forming.
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:0015301; anion:anion 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 synthesis; Antibiotic anabolism; Antibiotic formation.
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.
GO GO:0050826; response to freezing
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; Exchange transporter; Exchanger.
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.
GO GO:0009615; 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 programmed cell death. Apoptosis is an active
DE process requiring metabolic activity by the dying cell; often
DE characterised by cleavage of the DNA into fragments that give a so-
DE called "laddering pattern" on gels. It serves as a balance to mitosis
DE in regulating the size of animal tissues.
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 Archaeal protein present in or involved in the biogenesis or function
DE of a flagellum, a long hair-like cell surface appendage made of
DE polymerized flagellin with an attached hook. This rotating structure
DE with switches propels the cell through a liquid medium. The archaeal
DE flagellum is distinct from its bacterial equivalent in terms of
DE architecture, composition and mechanism of assembly. Thinner (10-15
DE nm) compared to the bacterial flagellum (18-24 nm), it is usually
DE composed of several types of flagellins and is glycosylated. The
DE archeal flagellum is considered as a type IV pilus-like structure.
SY Archaeal flagella; Archaeal flagellar apparatus.
GO GO:0009288; bacterial-type flagellum
HI Cellular component: Archaeal flagellum.
CA Cellular component.
//
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 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 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 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 ATP biosynthesis; ATP anabolism; ATP formation;
SY ATP biosynthetic process; Adenosine 5'-triphosphate biosynthesis;
SY Adenosine 5'-triphosphate anabolism;
SY Adenosine 5'-triphosphate formation;
SY Adenosine 5'-triphosphate biosynthetic process;
SY Adenosine triphosphate biosynthesis; Adenosine triphosphate anabolism;
SY Adenosine triphosphate biosynthetic process;
SY Adenosine triphosphate 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 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 Disease: Autoimmune uveitis.
HI Biological process: Sensory transduction; Vision; 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 mediated 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:0043064; 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 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:0019835; cytolysis
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:0019835; cytolysis
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:0030414; peptidase inhibitor activity
GO GO:0010466; negative regulation of peptidase 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 mental retardation. Secondary
DE features include diabetes mellitus, hypertension and congenital heart
DE 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; 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 Vitamin B7; Vitamin B8; Vitamin H; Coenzyme R; Biopeiderm.
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
DE damaged surface, and the intrinsic pathway, induced by a trauma,
DE converge in a final common pathway to form cross-linked fibrin clots.
GO GO:0007596; blood coagulation
HI Biological process: Blood coagulation.
CA Biological process.
//
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 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 family 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 family 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 synthesis; 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 Brominated; Bromated.
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; Cyclic dinucleotide di-GMP; Cyclic diguanylate;
SY Bis-(3'-5')-cyclic dimeric guanosine monophosphate; c-(Gpgp); cGpGp;
SY Guanosine 3',5'-cyclic monophosphate; 3'-5'-cyclic diguanylic acid;
SY Bis-(3'-5') cyclic diguanylic acid; Cyclic diguanylic acid;
SY Cyclic-bis(3',5')diguanylic acid.
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 Cd; Cadmium ion.
HI Ligand: Cadmium.
WW http://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 http://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 Molecular function: Ionic channel; Calcium channel.
HI Biological process: Transport; Ion transport; Calcium transport; Calcium channel.
HI Ligand: Calcium; Calcium channel.
CA Molecular function.
//
ID Calcium channel inhibitor.
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:0019855; calcium channel inhibitor activity
HI Molecular function: Toxin; Ionic channel inhibitor; Calcium channel inhibitor.
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 Ca transport; Calcium ion transport.
GO GO:0006816; calcium ion transport
HI Biological process: Transport; Ion transport; Calcium transport.
HI Ligand: Calcium; Calcium transport.
CA Biological process.
//
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 Ligand: Calmodulin-binding.
CA Ligand.
//
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'-phosphate;
SY Adenosine-3',5'-cyclic-monophosphate; Cyclic adenylic acid;
SY 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; 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;
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; 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; Adenosine 3',5'-phosphate-binding;
SY Adenosine-3',5'-cyclic-monophosphate-binding;
SY Cyclic adenylic acid-binding; Cyclic AMP-binding.
GO GO:0030552; cAMP binding
HI Ligand: Nucleotide-binding; cAMP-binding.
HI Ligand: cAMP; 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.
HI Biological process: Cap snatching.
CA Biological process.
//
ID Capsid assembly.
AC KW-0118
DE Viral protein that helps in the assembly of the capsid proteins, but
DE is not integrated in the virion.
SY Coat assembly; Viral capsid assembly.
GO GO:0019069; viral capsid assembly
HI Biological process: Capsid assembly.
CA Biological process.
//
ID Capsid maturation.
AC KW-0917
DE Viral protein involved in the maturation of the procapsid into the
DE mature capsid. Maturation usually involves proteolysis events and
DE changes in the folding of the capsid proteins.
SY Viral procapsid maturation.
GO GO:0046797; viral procapsid maturation
HI Biological process: Capsid maturation.
CA Biological process.
//
ID Capsid protein.
AC KW-0167
DE Structural protein of the virion that protects the nucleic acids of
DE the virus.
SY Coat protein.
GO GO:0019028; viral capsid
HI Molecular function: Capsid protein.
HI Cellular component: Virion; Capsid protein.
CA Molecular function.
//
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 metabolism;
SY Sugar metabolic process.
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 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.
HI Biological process: Initiation of viral infection; 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 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 bacterial cell inner membrane,
DE a selectively permeable membrane which separates the cytoplasm from
DE the periplasm in Gram-negative bacterial cells.
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:0030054; cell junction
HI Cellular component: Cell junction.
WW http://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 cell membrane, a selectively
DE permeable membrane which separates the cytoplasm from its
DE surroundings. In most archaea, bacteria, fungi, plants, and algae the
DE cell membrane is enclosed by at least the cell wall. Also used when it
DE is not known if the protein is found in or associated with the inner
DE or outer cell membrane.
SY Plasma membrane; Plasmalemma; Cytoplasmic 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 bacterial cell outer membrane,
DE a selectively permeable membrane which separates the bacterial
DE periplasm from the Gram-negative bacterial cell surroundings. In most
DE bacteria, the cell membrane is enclosed by at least the cell wall.
SY Outer membrane.
GO GO:0009279; cell outer membrane
HI Cellular component: Membrane; Cell 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 is surrounded by the outer
DE membrane in gram-negative bacteria, and envelopes the inner or plasma
DE membrane in gram-negative, gram-positive and acid-fast bacteria. Cell
DE walls of bacteria contain peptidoglycan whereas those of archaea do
DE not. Some archaea may contain pseudopeptidoglycan, which is composed
DE of N-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:0007047; cellular 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 Cellular component: CF(0).
HI Biological process: Transport; Ion transport; Hydrogen ion transport; 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 Cellular component: CF(1).
HI Biological process: ATP synthesis; 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'-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;
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.
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: Nucleotide-binding; cGMP-binding.
HI Ligand: cGMP; 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 ion; Chloride anion; Cl-.
HI Ligand: Chloride.
WW http://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 lemma
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 ion channel; Chloride anion channel; Cl- channel.
GO GO:0005254; chloride channel activity
GO GO:0006821; chloride transport
GO GO:0034707; chloride channel complex
HI Molecular function: Ionic channel; Chloride channel.
HI Biological process: Transport; Ion transport; Chloride channel.
HI Ligand: Chloride; Chloride channel.
CA Molecular function.
//
ID Chloride channel inhibitor.
AC KW-0870
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.
SY Chloride ion channel inhibitor; Chloride anion channel inhibitor;
SY Cl- channel inhibitor.
GO GO:0019869; chloride channel inhibitor activity
HI Molecular function: Toxin; Ionic channel inhibitor; Chloride channel inhibitor.
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 Cellular component: Chlorosome.
HI Biological process: Photosynthesis; 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 synthesis; Steroid biosynthesis; 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; 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:0016568; chromatin modification
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.
GO GO:0018298; protein-chromophore linkage
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 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 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 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 central
DE pair of microtubules. The axonemal microtubules of all cilia nucleate
DE and extend from a basal body, a centriolar structure most often
DE 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 http://www.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.
HI Biological process: Initiation of viral infection; 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.
HI Biological process: Initiation of viral infection; Viral penetration into host cytoplasm; Virus endocytosis by host; Clathrin-mediated endocytosis of virus by host.
CA Biological process.
//
ID Cleavage of host translation factors by virus.
AC KW-1075
DE Viral protein responsible for the cleavage of host translation
DE initiation factor(s). Viruses have evolved ways of interacting with
DE the host translational machinery to shutoff host gene expression
DE without affecting viral translation.
HI Biological process: Host-virus interaction; Cleavage of host translation factors by virus.
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; 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 ion; Co ion; Cobalt cation; Co cation.
HI Ligand: Cobalt.
WW http://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 Co cation transport; Co ion transport; Co transport;
SY Cobalt cation transport; Cobalt ion transport.
GO GO:0006824; cobalt ion transport
HI Biological process: Transport; Ion transport; Cobalt transport.
HI Ligand: Cobalt; 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 Coenzyme A anabolism; Coenzyme A biosynthetic process;
SY Coenzyme A formation; Coenzyme A synthesis; CoA biosynthesis;
SY CoA anabolism; CoA biosynthetic process; CoA formation; CoA synthesis;
SY CoASH biosynthesis; CoASH anabolism; CoASH biosynthetic process;
SY CoASH formation; CoASH 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 Coenzyme M anabolism; Coenzyme M biosynthetic process;
SY Coenzyme M formation; Coenzyme M synthesis; CoM biosynthesis;
SY CoM anabolism; CoM biosynthetic process; CoM formation; CoM synthesis;
SY 2-mercaptoethanesulfonic acid biosynthesis;
SY 2-mercaptoethanesulfonic acid anabolism;
SY 2-mercaptoethanesulfonic acid biosynthetic process;
SY 2-mercaptoethanesulfonic acid formation;
SY 2-mercaptoethanesulfonic acid 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
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; Properdin system;
SY Complement activation alternative pathway.
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 Complete proteome.
AC KW-0181
DE A complete proteome is the set of protein sequences that can be
DE derived by translation of all protein coding genes of a completely
DE sequenced genome, including alternative products such as splice
DE variants for those species in which these may occur. Complete
DE proteomes may include protein sequences from both the reviewed
DE (UniProtKB /Swiss-Prot) and unreviewed (UniProtKB/TrEMBL) sections of
DE the UniProt Knowledgebase. Note that some proportion of the predicted
DE protein sequences of a given complete proteome may require further
DE review or correction. The precise proportion depends on the relative
DE distributions of protein sequences between the two sections of
DE UniProtKB, and the quality of the underlying genome sequence and gene
DE predictions. See FAQs 'What are Complete Proteome Sets?' and 'How to
DE retrieve a complete set of protein sequences?'
HI Technical term: Complete proteome.
WW http://www.uniprot.org/faq/15
WW http://www.uniprot.org/faq/38
CA Technical term.
//
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 mental retardation
DE 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. Mental retardation with
DE or without structural brain changes are defects, with or without
DE mental retardation, are additional features of 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 Conidium formation; Conidium biosynthesis; Conidia biosynthesis;
SY Conidia 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.
GO GO:0000746; conjugation
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 ion; Copper cation; Cu; Cu ion; Cu cation.
HI Ligand: Copper.
WW http://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 Cu transport; Copper ion transport; Copper cation transport.
GO GO:0006825; copper ion transport
HI Biological process: Transport; Ion transport; Copper transport.
HI Ligand: Copper; 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 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 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 and the presence
DE of carboxysomes are cyanobacteria-like. Historically, the term
DE cyanelle is derived from a classification as endosymbiotic
DE cyanobacteria, and thus is not fully correct.
SY Muroplast; Cyanoplast.
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 Cyclosporin.
AC KW-0197
DE Protein binding cyclosporin or protein whose function is inhibited by
DE cyclosporin, e.g. cyclophilins. Cyclosporins are peptides obtained
DE from certain hyphomycetes which have potent immuno-suppressant
DE activity on humoral and cellular systems. Cyclosporin is used in
DE transplant surgery to suppress the immune response.
SY Cyclosporin A.
GO GO:0042277; peptide binding
HI Ligand: Cyclosporin.
CA Ligand.
//
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; cytoadherence to microvasculature, mediated by symbiont protein
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 mediated 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:0019835; cytolysis
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 active transport of viral material.
AC KW-1176
DE Viral protein that interacts with the cytoskeleton and/or host cell
DE motor proteins, and allows the active transport of viral components
DE exceeding 20 nm through the host cytosol along cytoskeletal filaments.
DE Components can be transported across the cytoplasm during both virus
DE entry and egress. Viruses such as adenoviruses, adeno-associated
DE virus, vaccinia virus, poliovirus, canine parvovirus, African swine
DE fever virus, rabies virus, human herpes virus 1, foamy virus are
DE thought to use active intracellular transport of viral components.
HI Biological process: Initiation of viral infection; Cytoplasmic active transport of viral material.
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 structure that fills the
DE cytoplasm of eukaryotic cells. The cytoskeleton is both a muscle and a
DE skeleton, and is responsible for cell movement, cytokinesis, and the
DE organization of the organelles within the cell. The major components
DE of cytoskeleton are the microfilaments (of actin), microtubules (of
DE tubulin) and intermediate filament systems in cells.
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 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 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;
SY Deoxyribonucleotide biosynthetic process;
SY Deoxyribonucleotide formation; Deoxyribonucleotide biosynthesis.
GO GO:0009263; deoxyribonucleotide biosynthetic process
HI Biological process: Deoxyribonucleotide synthesis.
CA Biological process.
//
ID Dephosphorylation of host translation factors by virus.
AC KW-1076
DE Viral protein responsible for the dephosphorylation of host
DE translation initiation factor(s). Viruses have evolved strategies to
DE rapidly inhibit protein synthesis from host mRNA and, at the same
DE time, promote protein synthesis from its own mRNA.
HI Biological process: Host-virus interaction; Dephosphorylation of host translation factors by virus.
CA Biological process.
//
ID Dermonecrosis.
AC KW-1061
DE Protein involved in the necrosis of the skin.
HI Biological process: Dermonecrosis.
CA Biological process.
//
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 toxin
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 organismal 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 syndrome; Aase-Smith syndrome II; Blackfan-Diamond disease;
SY Blackfan-Diamond syndrome; BDS;
SY Congenital erythroid hypoplastic anemia;
SY Congenital hypoplastic anemia of Blackfan and Diamond;
SY Chronic congenital aregenerative anemia; 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:0016702; oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen
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 mutation.
AC KW-0225
DE Protein for which at least one variant, responsible for a disease, is
DE described in the feature table of its Swiss-Prot entry.
HI Disease: Disease mutation.
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; response to DNA damage stimulus
HI Biological process: DNA damage.
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; recombinase activity
GO GO:0003677; DNA binding
GO GO:0006310; DNA recombination
HI Molecular function: DNA invertase.
HI Biological process: DNA recombination; DNA invertase.
HI Ligand: DNA-binding; DNA invertase.
CA Molecular function.
//
ID DNA packaging.
AC KW-0231
DE Protein involved in the packaging of replicated viral DNA into the
DE viral capsid and of mature bacteriophage DNA into proheads.
GO GO:0006323; DNA packaging
HI Biological process: DNA packaging.
CA Biological process.
//
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:0006260; DNA replication
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 Ligand: DNA-binding.
CA Ligand.
//
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:0003899; DNA-directed RNA polymerase activity
GO GO:0006351; transcription, DNA-dependent
HI Cellular component: DNA-directed RNA polymerase.
HI Biological process: Transcription; 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 mental retardation, short stature and
DE poor muscle tone. Common (1 in 700 live births); incidence increases
DE with maternal age. The cause is usually non-disjunction at meiosis but
DE occasionally a translocation of fused chromosomes 21 and 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:0003774; motor activity
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 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.
GO GO:0022900; electron transport chain
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 Molecular function: Elongation factor.
HI Biological process: Protein biosynthesis; 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 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 biosynthesis; Enterochelin anabolism;
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.
GO GO:0009405; pathogenesis
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 to Golgi transport; ER/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 Red blood cell maturation; RBC 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 mediated signaling pathway
HI Biological process: Ethylene signaling pathway.
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 Molecular function: Excision nuclease.
HI Biological process: DNA damage; DNA repair; 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 Exopolysaccharide biosynthesis; Exopolysaccharide anabolism;
SY Exopolysaccharide biosynthetic process; Exopolysaccharide formation;
SY EPS biosynthesis; EPS synthesis; EPS anabolism;
SY EPS biosynthetic process; EPS 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:0005578; proteinaceous 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) such as many oxidation-reduction enzymes. FAD is an
DE electron carrier molecule that functions as a hydrogen acceptor. The
DE generic term "flavin" derives from the Latin word flavius ("yellow")
DE because of the brilliant yellow color they exhibit as solids and in
DE neutral aqueous solutions.
SY Flavin adenine dinucleotide.
HI Ligand: 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 synthesis; Fatty acid anabolism;
SY Fatty acid biosynthetic process; Fatty acid formation.
GO GO:0006633; fatty acid biosynthetic process
HI Biological process: Lipid synthesis; 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 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: Blood coagulation; Fibrinolysis.
CA Biological process.
//
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; Pilus; Pili.
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; Pilus biogenesis; Pili biogenesis.
HI Biological process: Fimbrium biogenesis.
CA Biological process.
//
ID Flagellum.
AC KW-0282
DE Protein present in or involved in the biogenesis or function of the
DE flagellum, a long whip-like or feathery structure which propels the
DE cell through a liquid medium. This motile cilium is produced by the
DE unicellular eukaryotes, and by the motile male gametes of many
DE eukaryotic organisms. The flagella commonly have a characteristic
DE axial '9+2' microtubular array (axoneme) and bends are generated along
DE the length of the flagellum by restricted sliding of the nine outer
DE doublets.
SY Flagella; Motile cilium; Motile cilia; Undulipodium; Undulipodia.
GO GO:0019861; flagellum
HI Cellular component: Cell projection; Cilium; Flagellum.
CA Cellular component.
//
ID Flagellar rotation.
AC KW-0283
DE Protein involved in the movement of the flagella.
SY Flagellar motility; Flagellum rotation; Flagellum motility;
SY Flagella rotation; Flagella motility.
GO GO:0001539; ciliary or flagellar motility
HI Biological process: Flagellar rotation.
CA Biological process.
//
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 synthesis; Flavonoid anabolism;
SY Flavonoid biosynthetic process; Flavonoid formation.
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. Flavoproteins are involved, for example, in the
DE oxidative degradation of pyruvate, fatty acids and amino acids, and in
DE 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), such as many oxidation-reduction enzymes. FMN is an
DE electron carrier molecule that functions as a hydrogen acceptor. The
DE generic term "flavin" derives from the Latin word flavius ("yellow")
DE because of the brilliant yellow color they exhibit as solids and in
DE neutral aqueous solutions.
SY Flavin adenine mononucleotide; Flavin mononucleotide;
SY Riboflavin 5'-phosphate.
HI Ligand: 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 Folate synthesis; Folate anabolism; Folate biosynthetic process;
SY Folate formation; Folacin biosynthesis; Folacin synthesis;
SY Folacin anabolism; Folacin biosynthetic process; Folacin formation;
SY Folic acid biosynthesis; Folic acid synthesis; Folic acid anabolism;
SY Folic acid biosynthetic process; Folic acid formation;
SY Pteroylglutamic acid biosynthesis; Pteroylglutamic acid synthesis;
SY Pteroylglutamic acid anabolism;
SY Pteroylglutamic acid biosynthetic process;
SY Pteroylglutamic acid formation.
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 Pteroylglutamic acid-binding; Folacin-binding; Folic 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; 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 other 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 plasma membrane during viral penetration into host cell. Virus fusion
DE 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 plasma membrane.
SY Viral entry into host cell via plasma membrane fusion.
HI Biological process: Initiation of viral infection; 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.
HI Biological process: Initiation of viral infection; 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 the
DE host membrane during viral penetration or egress in 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 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).
SY Viral entry into host cell via membrane fusion.
HI Biological process: Initiation of viral infection; Viral penetration into host cytoplasm; Fusion of virus membrane with host membrane.
CA Biological process.
//
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 GPCR; 7TM receptor.
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 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.
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.
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 Galactitol metabolic process; Dulcitol metabolism;
SY Dulcitol 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 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 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 Gas vesicle.
AC KW-0304
DE Protein component of, or involved in the formation of, gas vesicles,
DE which are a rigid, hollow structure found in five phyla of the
DE Bacteria and two groups of the Archaea, but mostly restricted to
DE planktonic microorganisms, in which they provide buoyancy. By
DE regulating their relative gas vesicle content, aquatic microbes are
DE able to perform vertical migrations. The gas vesicle is impermeable to
DE liquid water, but is highly permeable to gases and is normally filled
DE with air. Two proteins have been shown to be present in the gas
DE vesicle: GVPa, which makes the ribs that form the structure, and GVPc,
DE which binds to the outside of the ribs and stiffens the structure
DE against collapse.
GO GO:0031411; gas vesicle
HI Cellular component: Vacuole; 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
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 Biological process: Gastrulation.
HI Molecular function: Developmental protein; 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 synthesis; Glutamate anabolism;
SY Glutamate biosynthetic process; Glutamate formation;
SY Glutamic acid biosynthesis; Glutamic acid synthesis;
SY Glutamic acid anabolism; Glutamic acid biosynthetic process;
SY Glutamic acid formation.
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 Glutaric aciduria; GA.
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 synthesis; Glutathione anabolism;
SY Glutathione biosynthetic process; Glutathione formation.
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 synthesis; Glycogen anabolism; Glycogen biosynthetic process;
SY Glycogen formation.
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; Photorespiration pathway;
SY Photosynthetic carbon oxydation cycle;
SY Oxidative photosynthetic carbon pathway.
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; glycolysis
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:0016798; hydrolase activity, acting on glycosyl bonds
GO GO:0008152; metabolic process
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; transferase activity, transferring glycosyl groups
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 synthesis; GMP anabolism; GMP biosynthetic process; GMP formation;
SY Guanosine 5'-monophosphate synthesis;
SY Guanosine 5'-monophosphate anabolism;
SY Guanosine 5'-monophosphate biosynthetic process;
SY Guanosine 5'-monophosphate formation; Guanylic acid synthesis;
SY Guanylic acid anabolism; Guanylic acid biosynthetic process;
SY Guanylic acid formation.
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 stack; Golgi complex.
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:0031225; anchored to membrane
HI PTM: Lipoprotein; GPI-anchor.
HI PTM: Glycoprotein; 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 GPI-anchor synthesis; GPI-anchor anabolism;
SY GPI-anchor biosynthetic process; GPI-anchor formation;
SY Glycosylphosphatidylinositol anchor biosynthesis;
SY Glycosylphosphatidylinositol anchor synthesis;
SY Glycosylphosphatidylinositol anchor anabolism;
SY Glycosylphosphatidylinositol anchor biosynthetic process;
SY Glycosylphosphatidylinositol anchor formation.
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 Cellular quiescence; Cell cycle arrest.
GO GO:0007050; cell cycle arrest
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 Ligand: Growth factor binding.
CA Ligand.
//
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.
GO GO:0040008; regulation of 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.
HI Molecular function: Capsid protein; Helical capsid protein.
HI Cellular component: Virion; Helical capsid protein.
CA Molecular function.
//
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 Molecular function: Hydrolase; Helicase.
HI Ligand: Nucleotide-binding; ATP-binding; 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 Heme synthesis; Heme anabolism; Heme biosynthetic process;
SY Heme formation; Haeme biosynthesis; Haeme synthesis; Haeme anabolism;
SY Haeme biosynthetic process; Haeme formation.
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 Hemolymph coagulation; Haemolymph clotting.
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:0044179; hemolysis in other 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 Disease: Hemophilia.
HI Biological process: Blood coagulation; Hemophilia.
CA Disease.
//
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: Blood coagulation; Hemostasis.
CA Biological process.
//
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 Ligand: Heparin-binding.
CA Ligand.
//
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 differentiation
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 synthesis; Histidine anabolism;
SY Histidine biosynthetic process; Histidine formation.
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 bacterial host cell inner
DE membrane, the selectively permeable membrane which separates the host
DE cytoplasm from the host periplasm in Gram-negative host bacterial
DE cells. a selectively permeable membrane which separates the cytoplasm
DE from the periplasm in Gram-negative bacterial cells.
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 membrane.
AC KW-1032
DE Protein found in or associated with the host cell membrane, the
DE selectively permeable membrane which separates the host cytoplasm from
DE its surroundings.
SY Host plasma membrane; Host plasmalemma; Host cytoplasmic 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 bacterial host cell outer
DE membrane, the selectively permeable membrane which separates the
DE bacterial host periplasm from the Gram-negative host bacterial cell
DE surroundings. In most bacteria, the cell membrane is enclosed by at
DE least the cell wall.
SY Host outer membrane.
GO GO:0020002; host cell plasma membrane
HI Cellular component: Membrane; Host membrane; Host cell 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.
SY Viral 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.
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 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 Golgi; Host Golgi complex; Host complexus golgiensis;
SY Host apparatus golgiensis.
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 lipid particle; Host lipid body; Host lipid bodies;
SY Host oil body; Host oil bodies; Host oleosome; Host spherosome;
SY Host monolayer-surrounded lipid storage body; Host adiposome.
GO GO:0044186; host cell lipid particle
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:0044189; host cell microsome
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 mitochondrial inner membrane; Host inner mitochondrial 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 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 cell junction; 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 Protein involved in direct interaction between the host cell
DE macromolecular machinery and viral proteins.
GO GO:0044419; interspecies interaction between organisms
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:0015992; proton 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 Biological process: Hydrogen peroxide.
HI Molecular function: Oxidoreductase; Peroxidase; 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; modulation by symbiont 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;
SY Isolated hypogonadotropic hypogonadism; IHH.
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 synthesis; Hypusine anabolism; Hypusine biosynthetic process;
SY Hypusine formation.
GO GO:0008612; peptidyl-lysine modification to 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 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 Ligand: IgA-binding protein.
CA Ligand.
//
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 Ligand: IgE-binding protein.
CA Ligand.
//
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 Ligand: IgG-binding protein.
CA Ligand.
//
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.
HI Biological process: Immunity.
CA Biological process.
//
ID Immunoglobulin C region.
AC KW-0392
DE Protein encoded by a constant region gene (C gene / C segment). The
DE constant region is the region of the immunoglobulin (Ig) that is
DE invariable in its amino acid sequence within any class of
DE immunoglobulin. Each immunoglobulin is a tetramer of two identical
DE light chains and two identical heavy chains linked by disulfide bonds.
DE The light chain has one variable region (VL) and one constant region
DE (CL) domain, whereas the heavy chain has one variable region (VH) and
DE three or four constant region domains (CH1 to CH4). Variable and
DE constant regions are encoded by separated genes, called V genes and C
DE genes respectively, which join during cell differentiation.
GO GO:0003823; antigen binding
HI Domain: Immunoglobulin domain; Immunoglobulin C region.
CA Domain.
//
ID Immunoglobulin domain.
AC KW-0393
DE Protein which contains at least one immunoglobulin domain, a
DE characteristic beta-sheet fold of the immunoglobulin domain which has
DE been found in many other proteins of diverse biological function.
SY Immunoglobulin fold.
HI Domain: Immunoglobulin domain.
CA Domain.
//
ID Immunoglobulin V region.
AC KW-0394
DE Protein encoded by a variable region gene (V gene / V segment). The
DE variable region is the region of the immunoglobulin (Ig) which varies
DE greatly in amino acid sequence among different immunoglobulins of the
DE same class. Each immunoglobulin molecules is a tetramer of two
DE identical light chains and two identical heavy chains linked by
DE disulfide bonds. The light chain has one variable region (VL) and one
DE constant region (CL) domain, whereas the heavy chain has one variable
DE region (VH) and three or four constant region domains (CH1 to CH4).
DE The V regions confer the antigenic specificity, and are associated
DE with the antigen-binding site. Variable and constant regions are
DE encoded by separated genes, called V genes and C genes respectively,
DE which join during cell differentiation.
GO GO:0003823; antigen binding
HI Domain: Immunoglobulin domain; Immunoglobulin V region.
CA Domain.
//
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 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. A lot of viruses
DE escape the adaptive immune response by different mechanisms including
DE interference with the presentation of antigenic peptides at the
DE surface of infected cells.
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.
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.
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.
HI Biological process: Host-virus interaction; Inhibition of host autophagy 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).
HI Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; Inhibition of host interferon signaling pathway by virus; Inhibition of host tetherin 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.
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.
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.
HI Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host complement factors 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.
HI Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; Inhibition of host IFN-mediated response initiation by virus; Inhibition of host RIG-I 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.
HI Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; Inhibition of host IFN-mediated response initiation by virus; Inhibition of host MDA5 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.
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.
HI Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; Inhibition of host interferon signaling pathway by virus; Inhibition of host interferon receptors 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.
HI Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; Inhibition of host IFN-mediated response initiation 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.
HI Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; Inhibition of host IFN-mediated response initiation 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.
HI Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; 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.
HI Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; 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.
HI Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; 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.
HI Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; Inhibition of host IFN-mediated response initiation by virus; Inhibition of host MAVS 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.
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 host translation. This global inhibition
DE of cellular protein synthesis serves to ensure maximal viral gene
DE expression and to evade host immune response.
HI Biological process: Host-virus interaction; 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.
HI Biological process: Host-virus interaction; Inhibition of host NF-kappa-B 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. Many viruses target the host
DE translational machinery either to evade cellular defense mechanisms or
DE to subvert the host translational machinery. One common target is the
DE translation initiation factor PABPC1. For example, picornavirus viral
DE proteases are able to cleave PABPC1, while rotavirus displace PABPC1 from
DE EIF4G1.
HI Biological process: Host-virus interaction; Inhibition of host poly(A)-binding protein 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.
HI Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; Inhibition of host interferon signaling pathway by virus; Inhibition of host PKR 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 host cell 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.
HI Biological process: Host-virus interaction; Inhibition of host pre-mRNA processing 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 host cell 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.
HI Biological process: Host-virus interaction; 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.
HI Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; 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.
HI Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; 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 by
DE inhibiting the TAP complex. Transporter associated with antigen (TAP),
DE 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.
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.
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-IKBKE-DDX3 complex by virus.
AC KW-1109
DE Viral protein involved in the evasion of host innate defenses by
DE inhibiting the TBK1-IKBKE-DDX3 complex. Upon infection, the virus is
DE recognized and the signal is transmitted to TBK1 and IKBKE that in
DE turn phosphorylate and activate IRF3 and IRF7. Once phosphorylated,
DE IRF3 and IRF7 homodimerize and translocate into the nucleus to drive
DE transcription of interferons. Several viruses including Ebolavirus and
DE Bornavirus interact directly with and inhibit TBK1 to prevent IRFs
DE activation. Other viruses such as vaccinia virus inhibit host DDX3 to
DE block the signaling pathway.
HI Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; Inhibition of host IFN-mediated response initiation by virus; Inhibition of host TBK1-IKBKE-DDX3 complex 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.
HI Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; Inhibition of host IFN-mediated response initiation by virus; Inhibition of host TRAFs by virus.
CA Biological process.
//
ID Inhibition of 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 host
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.
HI Biological process: Host-virus interaction; Inhibition of host transcription initiation 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.
HI Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; Inhibition of host interferon signaling pathway by virus; Inhibition of host TYK2 by virus.
CA Biological process.
//
ID Inhibition of host IFN-mediated response initiation by virus.
AC KW-1113
DE Viral protein involved in the evasion of host innate defense by
DE inhibiting the pathway leading to the triggering of interferon-
DE mediated response. This pathway usually starts with the recognition of
DE viral RNA or DNA by host proteins including DDX58 or IFIH1. Then, the
DE signal is transmitted through MAVS and TRAFs leading to the activation
DE and nuclear localization of transcription factors IRF3 and IRF7 to
DE induce IFNalpha/beta transcription and protein production. Many
DE viruses interact with components of this pathway to inhibit production
DE of interferons and establishment of the antiviral state.
HI Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; Inhibition of host IFN-mediated response initiation 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.
HI Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; Inhibition of host interferon signaling pathway 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 by
DE 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.
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 by
DE 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.
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 proteasome antigen processing by virus.
AC KW-1117
DE Viral protein involved in the evasion of host adaptive immune response by
DE inhibiting MHC class I peptide antigen generation by the proteasome.
DE The processing of foreign proteins leads to the presentation of viral
DE peptides by MHC class I molecules to cytotoxic T lymphocytes and
DE triggers immune response. Several viral proteins have evolved
DE mechanisms to avoid synthesis of antigenic peptide by the proteasome.
DE Epstein-Barr virus EBNA-1 for example contains an internal repeat
DE exclusively composed of glycines and alanines that inhibits its
DE proteasomal degradation.
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 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 Molecular function: Initiation factor.
HI Biological process: Protein biosynthesis; Initiation factor.
CA Molecular function.
//
ID Initiation of viral infection.
AC KW-1160
DE Viral protein involved in the virion's initiation of infection into a
DE host cell, including internalization and penetration into the host
DE cell cytoplasm, intracellular transport of viral components and genome
DE release to the replication site of the virus.
HI Biological process: Initiation of viral infection.
CA Biological process.
//
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 http://www.nature.com/nri/journal/v10/n1/full/nri2686.html
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.
HI Molecular function: Capsid protein; Inner capsid protein.
CA Molecular function.
//
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 synthesis; Inositol anabolism; Inositol biosynthetic process;
SY Inositol formation.
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 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:0030683; evasion by virus of host immune response
HI Biological process: 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.
HI Molecular function: Capsid protein; Intermediate capsid protein.
CA Molecular function.
//
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 Biological process: Intron homing.
HI Molecular function: Hydrolase; Nuclease; Endonuclease; 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 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; ion transport
HI Biological process: Transport; Ion transport.
CA Biological process.
//
ID Ionic 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:0005216; ion channel activity
HI Molecular function: Ionic channel.
HI Biological process: Transport; Ion transport; Ionic channel.
CA Molecular function.
//
ID Ionic channel inhibitor.
AC KW-0872
DE Protein which interferes with the function of ionic channels, which
DE are hydrophilic channels across the lipid bilayer through which
DE specific inorganic ions can diffuse down their electrochemical
DE gradients.
GO GO:0008200; ion channel inhibitor activity
HI Molecular function: Toxin; Ionic channel inhibitor.
CA Molecular function.
//
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: Ionic channel inhibitor; 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 Iron ion; Iron cation; Fe; Fe ion; Fe cation.
HI Ligand: Iron.
WW http://www.webelements.com/iron/
CA Ligand.
//
ID Iron storage.
AC KW-0409
DE Protein involved in the storage of iron.
GO GO:0006879; cellular iron ion homeostasis
HI Biological process: Iron storage.
HI Ligand: Iron; Iron storage.
CA Biological process.
//
ID Iron transport.
AC KW-0410
DE Protein involved in the transport of iron.
SY Iron ion transport; Iron cation transport; Fe transport.
GO GO:0055072; iron ion homeostasis
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: Metal-binding; Iron-sulfur.
HI Ligand: Iron; 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 synthesis; Isoleucine anabolism;
SY Isoleucine biosynthetic process; Isoleucine formation.
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 synthesis; Isoprene anabolism; Isoprene biosynthetic process;
SY Isoprene formation.
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 Joubert-Boltshauser syndrome; JBTS; 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;
SY Hypogonadotropic hypogonadism and anosmia; HHA; 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 attachement 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 Inhibitor Cystine Knot; ICK.
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 synthesis; Lactose anabolism; Lactose biosynthetic process;
SY Lactose formation.
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; receptor binding
GO GO:0019835; cytolysis
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 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 ion; Lead cation; Pb; Pb ion; Pb cation.
HI Ligand: Lead.
WW http://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 maternally inherited disease resulting from a deficit of ATP and
DE leading to acute bilateral blindness, predominantly in young men. It
DE is characterized by degeneration of the optic nerve and papillomacular
DE bundle.
HI 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:0005529; sugar 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: 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 synthesis; Leucine anabolism; Leucine biosynthetic process;
SY Leucine formation.
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 synthesis; Leukotriene anabolism;
SY Leukotriene biosynthetic process; Leukotriene formation.
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 Ligand-gated channel; LGIC.
HI Molecular function: Ionic channel; Ligand-gated ion channel.
HI Biological process: Transport; Ion transport; 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 synthesis; Lignin anabolism; Lignin biosynthetic process;
SY Lignin formation.
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 Domain: LIM domain.
HI Ligand: Metal-binding; LIM domain.
HI Ligand: Zinc; 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 synthesis; Lipid A anabolism; Lipid A biosynthetic process;
SY Lipid A formation.
GO GO:0009245; lipid A biosynthetic process
HI Biological process: Lipid synthesis; Lipid A 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 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 Lipid particle; Lipid body; Lipid bodies; Oil body; Oil bodies;
SY Oleosome; Spherosome; Monolayer-surrounded lipid storage body;
SY Adiposome.
GO GO:0005811; lipid particle
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 synthesis.
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 biosynthesis; Lipid anabolism; Lipid biosynthetic process;
SY Lipid formation.
GO GO:0008610; lipid biosynthetic process
HI Biological process: Lipid synthesis.
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 synthesis; Lipopolysaccharide anabolism;
SY Lipopolysaccharide biosynthetic process; Lipopolysaccharide formation.
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 Lithium ion; Lithium cation; Li; Li ion; Li cation.
HI Ligand: Lithium.
WW http://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 tyrosylquinone; Lysine topaquinone.
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 synthesis; Lysine anabolism; Lysine biosynthetic process;
SY Lysine formation.
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 ion; Magnesium cation; Mg; Mg ion; Mg cation.
HI Ligand: Magnesium.
WW http://www.webelements.com/magnesium/
CA Ligand.
//
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 ion; Manganese cation; Mn; Mn ion; Mn cation.
HI Ligand: Manganese.
WW http://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:0007126; meiosis
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 synthesis; Melanin anabolism; Melanin biosynthetic process;
SY Melanin formation.
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 heterogenious disorder, characterized by episodic
DE vomiting, seizures, and recurrent cerebral insults resembling strokes
DE and causing hemiparesis, hemianopsia, or cortical blindness.
HI 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 synthesis; Melatonin anabolism;
SY Melatonin biosynthetic process; Melatonin formation.
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 Cellular component: Membrane attack complex.
HI Biological process: Immunity; Innate immunity; Complement pathway; Membrane attack complex.
HI Biological process: Cytolysis; 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 synthesis; Menaquinone anabolism;
SY Menaquinone biosynthetic process; Menaquinone formation;
SY Vitamin K2 biosynthesis; Vitamin K2 synthesis; Vitamin K2 anabolism;
SY Vitamin K2 biosynthetic process; Vitamin K2 formation.
GO GO:0009234; menaquinone biosynthetic process
HI Biological process: Menaquinone biosynthesis.
CA Biological process.
//
ID Mental retardation.
AC KW-0991
DE Protein which, if defective, causes mental retardation, a disorder
DE characterized by subnormal intellectual functioning and manifested
DE during the developmental period. Mental retardation is associated with
DE impaired adaptive behavior.
SY Mental deficiency; Mental subnormality.
HI Disease: Mental retardation.
CA Disease.
//
ID Mercuric resistance.
AC KW-0475
DE Protein that confers bacteria or other microorganisms the ability to
DE withstand mercury salts.
SY Mercuric ion resistance; Mercuric cation 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 Mercury ion; Mercury cation; Hg; Hg ion; Hg cation.
HI Ligand: Mercury.
WW http://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.
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 synthesis; Methionine anabolism;
SY Methionine biosynthetic process; Methionine formation.
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 Protein of the major histocompatibility complex (MHC) class I which is
DE involved in the induction of strong immune reaction. MHC I is involved
DE in immune responses against virus-infected cells and rejection of
DE transplanted tissue.
GO GO:0002474; antigen processing and presentation of peptide antigen via MHC class I
GO GO:0042612; MHC class I protein complex
HI Cellular component: MHC I.
HI Biological process: Immunity; MHC I.
CA Cellular component.
//
ID MHC II.
AC KW-0491
DE Protein of the major histocompatibility complex (MHC) class II which
DE is involved in the induction of strong immune reaction. MHC II is
DE involved in the control the expression of surface structures on
DE lymphocytes and macrophages.
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 Cellular component: MHC II.
HI Biological process: Immunity; 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.
HI Cellular component: Endoplasmic reticulum; Microsome.
CA Cellular component.
//
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 Microtubule-dependent active transport of viral material.
AC KW-1177
DE Viral protein that interacts with microtubules and/or host cell motor
DE proteins and allows active transport along microtubules of viral
DE material across the host cell cytoplasm. Components can be transported
DE across the cytoplasm during both virus entry and egress. This
DE transport, which probably involves motor proteins like dynein and
DE kinesin or polymerization/depolymerization reactions as a driving
DE force, is mostly used by viruses that replicate their genomes near or
DE in the nucleus. The trafficking direction is usually toward the
DE nuclear membrane during entry and toward the periphery during egress
DE after replication. Neurotropic viruses for example, often enter
DE neurons at the terminal axon and their viral genome must be moved to
DE cell bodies by axonal transport (retrograde transport). Viruses such
DE as adenovirus, Adeno-associated virus, rabies virus, canine
DE parvovirus, vaccinia, foamy virus, human papillomavirus 16 and herpes
DE virus utilize this type of intracellular transport.
HI Biological process: Initiation of viral infection; Cytoplasmic active transport of viral material; Microtubule-dependent active transport of viral material.
HI Biological process: Host-virus interaction; Microtubule-dependent active transport of viral material.
CA Biological process.
//
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 Mitochondrial inner membrane; Inner mitochondrial 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.
GO GO:0007067; mitosis
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 Molecular function: Mobility protein.
HI Biological process: Conjugation; Mobility protein.
CA Molecular function.
//
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.
HI Biological process: Host-virus interaction; Viral immunoevasion; Modulation of host dendritic cell activity by virus.
CA Biological process.
//
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.
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.
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.
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.
HI Biological process: Host-virus interaction; Modulation of host chromatin 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.
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.
HI Biological process: Host-virus interaction; Viral immunoevasion; Modulation of host immunity by viral IgG Fc receptor-like protein.
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.
HI Biological process: Host-virus interaction; Viral immunoevasion; Evasion of host immunity by viral interleukin-like protein.
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.
HI Biological process: Host-virus interaction; Viral immunoevasion; Inhibition of host innate immune response by virus; 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.
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 viral
DE proteins usually target several host proteins for proteasomal
DE degradation.
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.
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.
HI Biological process: Host-virus interaction; Modulation of host ubiquitin pathway by virus.
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.
HI Biological process: Host-virus interaction; Viral immunoevasion; Modulation of host NK-cell activity 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 Molybdenum ion; Molybdenum cation; Mo; Mo ion; Mo cation.
HI Ligand: Molybdenum.
WW http://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 Molybdenum cofactor synthesis; Molybdenum cofactor anabolism;
SY Molybdenum cofactor biosynthetic process;
SY Molybdenum cofactor formation; Moco biosynthesis; Moco synthesis;
SY Moco anabolism; Moco biosynthetic process; Moco formation;
SY Molybdopterin biosynthesis; Molybdopterin synthesis;
SY Molybdopterin anabolism; Molybdopterin biosynthetic process;
SY Molybdopterin formation.
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:0016015; morphogen activity
GO GO:0009653; anatomical structure morphogenesis
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; 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 Technical term: Multifunctional enzyme.
CA Technical term.
//
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 formation; Muscle development.
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 n-tetradecanoate; Myristylated.
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 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 NM; NEM; 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: Ciliopathy; Nephronophthisis.
CA Disease.
//
ID Neurodegeneration.
AC KW-0523
DE Protein which, if defective, causes neurodegeneration.
GO GO:0008219; cell death
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 formation; Nervous system development.
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; 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 synthesis; Neurotransmitter anabolism;
SY Neurotransmitter biosynthetic process; Neurotransmitter formation.
GO GO:0042136; neurotransmitter biosynthetic process
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.
GO GO:0042135; neurotransmitter catabolic process
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 Nickel ion; Nickel cation; Ni; Ni ion; Ni cation.
HI Ligand: Nickel.
WW http://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 ion transport; Nickel cation transport; Ni transport.
GO GO:0015675; nickel ion transport
HI Biological process: 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 NPD; Niemann's disease.
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 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 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 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 Cellular component: Nucleus; Nuclear pore complex.
HI Biological process: Transport; Protein transport; Translocation; Nuclear pore complex.
HI Biological process: Transport; mRNA transport; 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 plasmid 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 Ligand: 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 synthesis; Nucleotide anabolism;
SY Nucleotide biosynthetic process; Nucleotide formation.
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 chromatophora, a
DE photosynthetic thecate amoeba. It probably derives from a different
DE endosymbiotic event than that which led to all other plastids; the
DE question is open as to whether or not this is a true plastid. It
DE encodes and houses the machinery necessary for photosynthesis and
DE CO(2) fixation; it also has the genetic capacity to synthesize some
DE amino acids, some fatty acids and a few cofactors. It contains
DE thylakoid membranes, and a residual peptidoglycan wall between the 2
DE envelope membranes. There 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 Ossification; Bone formation.
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 disease; Lobstein's 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.
HI Molecular function: Capsid protein; Outer capsid protein.
CA Molecular function.
//
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
GO GO:0055114; oxidation-reduction process
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 transporter 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 synthesis; Oxylipin anabolism; Oxylipin biosynthetic process;
SY Oxylipin formation.
GO GO:0031408; oxylipin biosynthetic process
HI Biological process: Lipid synthesis; 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 organismal 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 synthesis; Pantothenate anabolism;
SY Pantothenate biosynthetic process; Pantothenate formation.
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 Parkinson's disease; PD; Paralysis agitans.
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 Molecular function: Pathogenesis-related protein.
HI Biological process: Plant defense; 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 the production of NADPH. Then 6-phosphogluconate is converted to
DE ribulose-5-phosphate and CO2 and a second molecule of NADH. This
DE pathway is an 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-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 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 Peptidoglycan biosynthesis; Peptidoglycan anabolism;
SY Peptidoglycan biosynthetic process; Peptidoglycan formation;
SY Murein biosynthesis; Murein synthesis; Murein anabolism;
SY Murein biosynthetic process; Murein formation;
SY Pseudomurein biosynthesis; Pseudomurein synthesis;
SY Pseudomurein anabolism; Pseudomurein biosynthetic process;
SY Pseudomurein formation.
GO GO:0009252; peptidoglycan biosynthetic process
HI Biological process: Peptidoglycan synthesis.
HI Biological process: Cell shape; Peptidoglycan synthesis.
CA Biological process.
//
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 formation; Peroxisome assembly.
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 Peroxisome-biogenesis disorder; PBD.
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 synthesis; PHA anabolism; PHA biosynthetic process; PHA formation;
SY Poly(3-hydroxyalkanoate) biosynthesis;
SY Poly(3-hydroxyalkanoate) synthesis;
SY Poly(3-hydroxyalkanoate) anabolism;
SY Poly(3-hydroxyalkanoate) biosynthetic process;
SY Poly(3-hydroxyalkanoate) formation.
GO GO:0042621; poly(3-hydroxyalkanoate) biosynthetic process
HI Biological process: PHA biosynthesis.
CA Biological process.
//
ID Phage lysis protein.
AC KW-0578
DE Phage protein involved in the lysis of the bacterial cell wall
DE allowing the release of mature, newly formed phages.
GO GO:0016998; cell wall macromolecule catabolic process
GO GO:0019835; cytolysis
HI Molecular function: Phage lysis protein.
CA Molecular function.
//
ID Phage maturation.
AC KW-0579
DE Protein involved in phage maturation, the formation of complete phage
DE viruses ready for release.
GO GO:0019067; viral assembly, maturation, egress, and release
HI Biological process: Phage maturation.
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 synthesis; PHB anabolism; PHB biosynthetic process; PHB formation;
SY Poly-hydroxybutyrate biosynthesis; Poly-hydroxybutyrate synthesis;
SY Poly-hydroxybutyrate anabolism;
SY Poly-hydroxybutyrate biosynthetic process;
SY Poly-hydroxybutyrate formation;
SY Poly-beta-hydroxybutyrate biosynthesis;
SY Poly-beta-hydroxybutyrate synthesis;
SY Poly-beta-hydroxybutyrate anabolism;
SY Poly-beta-hydroxybutyrate biosynthetic process;
SY Poly-beta-hydroxybutyrate formation;
SY Poly-(3-hydroxybutyrate) biosynthesis;
SY Poly-(3-hydroxybutyrate) synthesis;
SY Poly-(3-hydroxybutyrate) anabolism;
SY Poly-(3-hydroxybutyrate) biosynthetic process;
SY Poly-(3-hydroxybutyrate) formation.
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 synthesis; Phenylalanine anabolism;
SY Phenylalanine biosynthetic process; Phenylalanine formation.
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 mental retardation, 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 synthesis; Phospholipid anabolism;
SY Phospholipid biosynthetic process; Phospholipid formation.
GO GO:0008654; phospholipid biosynthetic process
HI Biological process: 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: Phospholipid degradation.
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; 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 Ligand: Phosphopantetheine.
CA Ligand.
//
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 Molecular function: Photoprotein.
HI Biological process: Luminescence; 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 Molecular function: Receptor; Photoreceptor protein.
HI Ligand: Chromophore; 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 PSI; P700.
GO GO:0009522; photosystem I
HI Cellular component: Photosystem I.
HI Biological process: Photosynthesis; 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 flows 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 PSII; P680.
GO GO:0009523; photosystem II
HI Cellular component: Photosystem II.
HI Biological process: Photosynthesis; 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: 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 Pilus-mediated viral adsorption onto host cell.
AC KW-1175
DE Viral protein involved in interaction with bacterial conjugative F-
DE pili, which are retractile filaments that protrude from gram-negative
DE bacteria and normally mediate horizontal gene transfer. Binding to the
DE pilus is followed by retraction of the pilus, which brings the
DE bacteriophage in contact with the host cell membrane. Examples of
DE bacteriophages which utilize the host-cell pilus as an attachment
DE structure are bacteriophages M13, f1, fd, R17, Qbeta, Pf1, Pf3, phiKMV
DE or phi6.
HI Biological process: Initiation of viral infection; Viral attachment to host cell; Pilus-mediated viral adsorption onto host cell.
CA Biological process.
//
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 later is 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. They probably do not contain 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 Plastidic inner membrane; Inner plastid membrane;
SY Inner plastidic 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 Plastidic outer membrane; Outer plastid membrane;
SY Outer plastidic 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 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 Polymorphism.
AC KW-0621
DE Protein for which there is at least one variant within the same
DE species, that is not directly responsible for a disease. We make use
DE of this keyword only in the context of multicellular organisms.
HI Coding sequence diversity: Polymorphism.
CA Coding sequence diversity.
//
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 Viral pore-forming protein, associated with the viral capsid, that
DE induces the formation of a transmembrane pore in the host membrane to
DE allow the viral genome to enter the cytoplasm. This mechanism is used
DE by non-enveloped viruses such as human rhinovirus 2, poliovirus, and
DE some bacteriophages.
SY Membrane puncture-mediated penetration of viral genome into host cell.
HI Biological process: Initiation of viral infection; 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 dimeric, trimeric or tetrameric form,
DE constitutes a water-filled transmembrane channel ("pore"). This pore
DE allows the passage of ions and numerous other, non-specific molecules
DE through the membrane. Found in the mitochondrial outer membrane of
DE eukaryotes, in many Gram-negative bacteria and in sea anemones.
GO GO:0015288; porin activity
GO GO:0046930; pore complex
HI Molecular function: Porin.
HI Biological process: Transport; Ion transport; Porin.
HI Domain: Transmembrane; 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: Cell junction; Synapse; Postsynaptic cell membrane.
HI Cellular component: Membrane; 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; other organism 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 http://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: Ionic channel; Potassium channel.
HI Biological process: Transport; Ion transport; Potassium transport; Potassium channel.
HI Ligand: Potassium; Potassium channel.
CA Molecular function.
//
ID Potassium channel inhibitor.
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:0019870; potassium channel inhibitor activity
HI Molecular function: Toxin; Ionic channel inhibitor; Potassium channel inhibitor.
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 Pyrroloquinoline quinone; Methoxatin.
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:0072556; other organism 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; PCD; Immotile cilia syndrome; ICS.
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-related mean, and
DE absence of other syndromic features or significant neurological
DE deficits. Brain weight is markedly reduced and the cerebral cortex is
DE disproportionately small. Primary microcephaly is also known as true
DE microcephaly or microcephaly vera.
HI Disease: Primary microcephaly.
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:0005658; alpha DNA polymerase:primase 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 Molecular function: Prion.
HI Cellular component: Amyloid; 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: 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 synthesis; Fatty acid biosynthesis; 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:0008233; peptidase activity
GO GO:0006508; proteolysis
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:0030414; peptidase inhibitor activity
GO GO:0010466; negative regulation of peptidase 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 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:0016504; peptidase activator activity
GO GO:0010952; positive regulation of peptidase 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 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.
HI Biological process: Initiation of viral infection; Viral genome integration.
HI Biological process: DNA integration; Viral genome integration.
CA Biological process.
//
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 base 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-diaminobutane biosynthesis; 1,4-butanediamine 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 Molecular function: Pyrogen.
HI Biological process: Inflammatory response; 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 Pyroglutamic acid; Pyro-Glu.
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 Cellular component: Reaction center.
HI Biological process: Photosynthesis; Reaction center.
CA Cellular component.
//
ID Receptor.
AC KW-0675
DE Protein which binds to, or responds to, a ligand with high
DE specificity.
GO GO:0004872; receptor activity
HI Molecular function: Receptor.
CA Molecular function.
//
ID Reference proteome.
AC KW-1185
DE A reference proteome is a set of protein sequences derived from a
DE complete proteome which constitutes a defined standard for a
DE particular user community. Reference proteomes are manually defined
DE according to a number of criteria. They cover the proteomes of well-
DE studied model organisms and other proteomes of interest for biomedical
DE and biotechnological research. Reference proteomes have been selected
DE to provide broad coverage of the tree of life, and constitute a
DE representative cross-section of the taxonomic diversity to be found
DE within UniProtKB.
HI Technical term: Complete proteome; Reference proteome.
CA Technical term.
//
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 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 Respiration chain; Electron transport chain.
GO GO:0070469; respiratory chain
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 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 Molecular function: Receptor; Photoreceptor protein; Retinal protein.
HI Ligand: Chromophore; 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 gram-negative 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 mental retardation. 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:0030529; 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 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-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 RNA interference; RNAi; Transcriptional gene silencing; TGS.
GO GO:0031047; gene silencing by RNA
HI Biological process: RNA-mediated gene silencing.
CA Biological process.
//
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 replication.
AC KW-0693
DE Protein involved in the replication of RNAs, thus resulting in the
DE duplication of RNA by making a new copy of an existing molecule.
GO GO:0032774; RNA biosynthetic process
HI Biological process: RNA replication.
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 Ligand: RNA-binding.
CA Ligand.
//
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-directed RNA polymerase activity
HI Molecular function: Transferase; Nucleotidyltransferase; RNA-directed RNA polymerase.
CA Molecular function.
//
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
GO GO:0006457; protein folding
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 Ligand: RNA-binding; rRNA-binding.
CA Ligand.
//
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 S-adenosyl methionine; S-adenosyl-methionine; S-adenosylmethionine;
SY SAM; AdoMet; AdoMet radical; SAM radical;
SY radical S- adenosylmethionine.
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 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 http://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; barrier 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:0004091; carboxylesterase 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-hydroxytryptamine; 5-HT.
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 Ligand: Sialic acid.
HI PTM: Glycoprotein; 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:0016987; sigma factor activity
GO GO:0006355; regulation of transcription, DNA-dependent
HI Molecular function: Sigma factor.
HI Biological process: Transcription; Transcription regulation; 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 sequence; Signal peptide.
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. It consists of a 7S
DE RNA and at least six polypeptide subunits. One of the SRP proteins
DE (srp54) binds GTP and in association with 7S RNA and srp19 has GTPase
DE activity.
GO GO:0005786; signal recognition particle, endoplasmic reticulum targeting
HI Cellular component: Signal recognition particle.
HI Molecular function: Ribonucleoprotein; 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 signalosome; CSN; COP9 complex; COP9 signalosome complex.
GO GO:0008180; 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 http://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: Ionic channel; Sodium channel.
HI Biological process: Transport; Ion transport; Sodium transport; Sodium channel.
HI Ligand: Sodium; Sodium channel.
CA Molecular function.
//
ID Sodium channel inhibitor.
AC KW-0738
DE Protein which interferes with the function of sodium channels which
DE are membrane proteins forming a channel in a biological membrane
DE selectively permeable to sodium ions. They are found in various venoms
DE from snakes, scorpions and spiders.
GO GO:0019871; sodium channel inhibitor activity
HI Molecular function: Toxin; Ionic channel inhibitor; Sodium channel inhibitor.
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 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.
HI Ligand: Potassium; 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; DNA repair; 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 response system; SOS system; SOS repair system.
GO GO:0009432; SOS response
HI Biological process: DNA damage; DNA repair; 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 http://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 Autosomal dominant spinocerebellar ataxia; SCA;
SY Autosomal dominant cerebellar ataxia; ADCA;
SY Olivopontocerebellar atrophy; OPCA; 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 Cellular component: Spliceosome.
HI Biological process: mRNA processing; mRNA splicing; 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 synthesis; 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 synthesis; Steroid biosynthesis; Sterol biosynthesis.
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).
GO GO:0006950; response to stress
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 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 RNA interference; Suppressor of RNAi.
HI Molecular function: Suppressor of RNA silencing.
CA Molecular function.
//
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 Cellular component: Secreted; Surface film.
HI Biological process: Gaseous exchange; 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: Cell junction; 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:0019717; synaptosome
HI Cellular component: Cell junction; 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; Polykaryons formation in virally infected cells.
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=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.
HI Molecular function: Capsid protein; T=1 icosahedral capsid protein.
HI Cellular component: Virion; T=1 icosahedral capsid protein.
CA Molecular function.
//
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.
HI Molecular function: Capsid protein; T=13 icosahedral capsid protein.
HI Cellular component: Virion; T=13 icosahedral capsid protein.
CA Molecular function.
//
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.
HI Molecular function: Capsid protein; T=147 icosahedral capsid protein.
HI Cellular component: Virion; T=147 icosahedral capsid protein.
CA Molecular function.
//
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.
HI Molecular function: Capsid protein; T=16 icosahedral capsid protein.
HI Cellular component: Virion; T=16 icosahedral capsid protein.
CA Molecular function.
//
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.
HI Molecular function: Capsid protein; T=169 icosahedral capsid protein.
HI Cellular component: Virion; T=169 icosahedral capsid protein.
CA Molecular function.
//
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.
HI Molecular function: Capsid protein; T=2 icosahedral capsid protein.
HI Cellular component: Virion; T=2 icosahedral capsid protein.
CA Molecular function.
//
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.
HI Molecular function: Capsid protein; T=219 icosahedral capsid protein.
HI Cellular component: Virion; T=219 icosahedral capsid protein.
CA Molecular function.
//
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.
HI Molecular function: Capsid protein; T=25 icosahedral capsid protein.
HI Cellular component: Virion; T=25 icosahedral capsid protein.
CA Molecular function.
//
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.
HI Molecular function: Capsid protein; T=3 icosahedral capsid protein.
HI Cellular component: Virion; T=3 icosahedral capsid protein.
CA Molecular function.
//
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.
HI Molecular function: Capsid protein; T=4 icosahedral capsid protein.
HI Cellular component: Virion; T=4 icosahedral capsid protein.
CA Molecular function.
//
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.
HI Molecular function: Capsid protein; T=7 icosahedral capsid protein.
HI Cellular component: Virion; T=7 icosahedral capsid protein.
CA Molecular function.
//
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.
HI Molecular function: Capsid protein; T=pseudo3 icosahedral capsid protein.
HI Cellular component: Virion; T=pseudo3 icosahedral capsid protein.
CA Molecular function.
//
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 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 plasma membrane; Target plasmalemma;
SY Target cytoplasmic membrane.
GO GO:0044218; other organism cell 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:0044279; other organism 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 TMP; Sweet-taste protein.
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 Biological process: Terminal addition.
HI Molecular function: Transferase; Nucleotidyltransferase; 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 Thiamin biosynthesis; Vitamin B1 biosynthesis; Aneurin 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 Thiamin catabolism; Vitamin B1 catabolism; Aneurin 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 Thiamin pyrophosphate; TPP; Thiamin diphosphate; TDP.
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 Cellular component: Thick filament.
HI Molecular function: Muscle protein; 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 Thiol peptidase; Thiol proteinase; Sulfhydryl protease.
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 Disease: Thrombophilia.
HI Biological process: Blood coagulation; 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; 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.
HI Molecular function: Toxin.
CA Molecular function.
//
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.
GO GO:0006351; transcription, DNA-dependent
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.
GO GO:0006355; regulation of transcription, DNA-dependent
HI Biological process: Transcription; Transcription regulation.
CA Biological process.
//
ID Transcription termination.
AC KW-0806
DE Protein involved in transcription termination.
GO GO:0006353; transcription termination, DNA-dependent
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:0004871; signal transducer activity
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 Ribosome shunt; Ribosomal shunt; Shunting.
HI Molecular function: Translational shunt.
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:0006810; 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.
GO GO:0016021; integral to membrane
HI Domain: Transmembrane.
HI Cellular component: Membrane; Transmembrane.
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 Domain: Transmembrane; Transmembrane helix.
HI Cellular component: Membrane; Transmembrane helix.
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 Domain: Transmembrane; Transmembrane beta strand.
HI Cellular component: Membrane; Transmembrane beta strand.
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.
GO GO:0006810; transport
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 TCA cycle; Citric acid cycle; Krebs 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 Ligand: RNA-binding; tRNA-binding.
CA Ligand.
//
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 Antitumor; Anti-oncogene.
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 http://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 Two-component system; Phosphorelay system; Phospho-relay system;
SY Two-component sensory transduction system;
SY Two-component signal transduction system.
GO GO:0000160; two-component signal transduction system (phosphorelay)
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 thioester 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 Ubiquitin conjugation; Ubiquitination; Ubiquitinylation; Sumoylation;
SY Ubiquitin-like modifier conjugation.
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 UPR; ER stress response; ER stress pathway.
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 Usher's syndrome; Sensorineural deafness with retinitis pigmentosa.
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. Aquatic microorganisms may employ gas vacuoles (composed
DE of clusters of inert gas vesicles) to provide buoyancy.
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 http://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:0050880; regulation of blood vessel size
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 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.
HI Biological process: Initiation of viral infection; Viral attachment to host cell.
HI Biological process: Host-virus interaction; Viral attachment to host cell.
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.
HI Cellular component: Virion; Viral envelope protein.
CA Cellular component.
//
ID Viral genome injection through bacterial membranes.
AC KW-1171
DE This process is mediated by the viral capsid which remains outside the
DE cell, and involves local degradation of cell wall by viral lysozymes.
DE Viruses belonging to the caudovirales (bacteriophages) have been shown
DE to inject their genome through the host membranes.
SY Viral genome ejection through host membranes.
HI Biological process: Initiation of viral infection; Viral penetration into host cytoplasm; Viral genome injection through bacterial membranes.
CA Biological process.
//
ID Viral immunoevasion.
AC KW-0899
DE Viral protein involved in host immune evasion thereby optimizing viral
DE growth and dissemination. Viral immune evasion strategies are typical
DE of viruses which persist in their host throughout life. For example:
DE Herpesviridae, Adenoviridae, Poxviridae and Retroviridae have
DE developed subversions of the MHC class I antigen-presentation pathway.
DE In order to reduce the effectiveness of cytotoxic T-lymphocytes
DE immunity, they express proteins that either down-modulate MHC class I
DE expression (degradation or mislocalization) or interfere with the
DE antigen binding/presentation process (down-regulation of the
DE expression of the transporter associated with antigen processing TAP).
DE Some proteins of these virus families also down-regulate other
DE molecules involved in immune recognition.
SY Viral host defense evasion; Viral immune evasion; Immunoevasin.
GO GO:0030683; evasion by virus of host immune response
HI Biological process: Host-virus interaction; Viral immunoevasion.
CA Biological process.
//
ID Viral ionic channel.
AC KW-1182
DE Small transmembrane protein that homo-oligomerizes to form a viral
DE ionic 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 ionic homeostasis of host cells.
DE Viral ionic channels are not necessarily required for the production
DE of 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.
HI Molecular function: Ionic channel; Viral ionic channel.
HI Biological process: Transport; Ion transport; Viral ionic channel.
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.
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; spread of virus in host, cell to cell
HI Molecular function: Viral movement protein.
HI Biological process: Transport; 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:0003676; nucleic acid binding
HI Ligand: Viral nucleoprotein.
HI Cellular component: Virion; Viral nucleoprotein.
CA Ligand.
//
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.
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 or its
DE genetic material into the host cell cytoplasm. Entry is achieved
DE through pore formation, membrane fusion and/or endocytosis mechanisms.
DE Penetration reactions occur mainly in five locations: the cell
DE membrane, early and late endosomes, caveosomes, and the ER.
SY Translocation of virus into host cell; Virion penetration into host cell.
HI Biological process: Initiation of viral infection; Viral penetration into host cytoplasm.
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; Virion penetration into host nucleus.
HI Biological process: Initiation of viral infection; 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.
HI Biological process: Initiation of viral infection; Viral penetration into host cytoplasm; Viral penetration via lysis of host organellar membrane.
CA Biological process.
//
ID Viral penetration via permeabilization of host organellar 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 organellar
DE membrane to allow viral escape and penetration into the cytoplasm.
DE Viral membrane-penetration proteins often need to be activated, mostly
DE through endosomal acidic pH or receptor binding to display their
DE membrane penetrating activity. Non-enveloped viruses such as
DE parvovirus, human reovirus, BDV, BTV, rotavirus, papillomavirus, Flock
DE house virus permeabilize the host endosomal membrane to penetrate the
DE host cytoplasm.
SY Viral penetration via host endosomal membrane disruption by virus; Viral penetration via perforation of host organellar membrane by virus.
HI Biological process: Initiation of viral infection; Viral penetration into host cytoplasm; Viral penetration via permeabilization of host organellar 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.
HI Biological process: Viral primary envelope fusion with host outer nuclear membrane.
CA Biological process.
//
ID Virion.
AC KW-0946
DE Viral protein detected in the virion.
GO GO:0019012; virion
HI Cellular component: Virion.
CA Cellular component.
//
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.
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.
GO GO:0009405; pathogenesis
HI Biological process: Virulence.
CA Biological process.
//
ID Virus-mediated host mRNA decay by hyperadenylation.
AC KW-1132
DE Viral protein involved in the degradation of host mRNA by
DE hyperadenylation. Viruses have evolved ways of interacting with the
DE cellular RNA decay machinery to favor their survival and maximize the
DE expression of their own mRNAs. Proper 3' end formation and
DE polyadenylation are required for mRNA export to the cytoplasm.
DE Therefore, hyperadenylation by viruses triggers host mRNA nuclear
DE retention and subsequent degradation by quality control pathways.
HI Biological process: Host-virus interaction; Virus-mediated host mRNA decay by hyperadenylation.
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.
HI Biological process: Initiation of viral infection; Viral penetration into host cytoplasm; Virus endocytosis by host.
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 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 ion channel; Voltage-gated cation channel.
GO GO:0005244; voltage-gated ion channel activity
GO GO:0034765; regulation of ion transmembrane transport
HI Molecular function: Ionic channel; Voltage-gated channel.
HI Biological process: Transport; Ion transport; Voltage-gated channel.
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 Disease: von Willebrand disease.
HI Biological process: Blood coagulation; 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 WD-40 repeat; Trp-Asp 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 signalling pathway; Wnt signal transduction pathway;
SY Wnt signaling cascade.
GO GO:0016055; Wnt receptor 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: 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 http://www.webelements.com/zinc/
CA Ligand.
//
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 Domain: Zinc-finger.
HI Ligand: Zinc; Zinc-finger.
HI Ligand: Metal-binding; Zinc-finger.
CA Domain.
//
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 Zymogen.
AC KW-0865
DE The enzymatically inactive precursor of mostly proteolytic enzymes.
SY Proenzyme.
HI PTM: Zymogen.
CA PTM.
//
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