HCLSIG BioRDF Subgroup/Data/SwissProt Keywords

<?xml version="1.0" encoding='UTF-8'?> <rdf:RDF xmlns="urn:lsid:uniprot.org:ontology:" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:rdfs="http://www.w3.org/2000/01/rdf-schema#" xmlns:owl="http://www.w3.org/2002/07/owl#"> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:2"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>3D-structure</name> <rdfs:comment>Protein, or part of a protein, whose three-dimensional structure has been resolved experimentally (for example by X-ray crystallography or NMR spectroscopy) and whose coordinates are available in the PDB database. Can also be used for theoretical models.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:5"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Acetoin biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of acetoin (3-hydroxy-2-butanone). Acetoin is a component of the butanediol cycle (butanediol fermentation) in microorganisms.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:45151"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:6"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Acetoin catabolism</name> <name>Acetoin degradation</name> <rdfs:comment>Protein involved in the degradation of acetoin (3-hydroxy-2-butanone). Acetoin is a component of the butanediol cycle (butanediol fermentation) in microorganisms.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:45150"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:7"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Acetylation</name> <rdfs:comment>Protein which is posttranslationally modified by the attachment of at least one acetyl group; generally at the N-terminus.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:8"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Acetylcholine receptor inhibitor</name> <rdfs:comment>Protein that inhibits both nicotinic (nAChR) and muscarinic (mAChR) acetylcholine receptors. The nAChR is a postsynaptic membrane protein that, after binding acetylcholine, responds by an extensive change in conformation, which leads to opening of an ion-conducting channel across the plasma membrane. The mAChR is a membrane protein that acts through G proteins and mediates various cellular responses, including inhibition of adenylate cyclase, breakdown of phosphoinositides and modulation of potassium channels through the action of G proteins.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:30550"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:9"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Actin-binding</name> <rdfs:comment>Protein which binds to actin, and thereby can modulate the properties and/or functions of the actin filament.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:3779"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:117"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Actin capping</name> <rdfs:comment>Protein that binds to the free end of the actin filament and thereby blocks further addition of subunits.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:10"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Activator</name> <rdfs:comment>Protein that positively regulates either the transcription of one or more genes, or the translation of mRNA.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:11"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Acute phase</name> <rdfs:comment>Protein involved in acute phase, a response of the vertebrate body to insults, infections, immunological reactions or inflammatory processes; characterised by redness (rubor), heat (calor), swelling (tumor), pain (dolor) and sometimes loss of function.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6953"/> <rdfs:seeAlso rdf:resource="http://www.copewithcytokines.de/cope.cgi?228"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:13"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>ADP-ribosylation</name> <rdfs:comment>Protein which is posttranslationally modified by the attachment of at least one ADP-ribosyl group.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:14"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>AIDS</name> <name>Acquired immunodeficiency syndrome</name> <rdfs:comment>Protein encoded by either the human, simian or other immunodeficiency viruses which are the cause of acquired immunodeficiency syndrome. In human, the disease is caused by an infection with the human immunodeficiency viruses (HIV-1 and HIV-2) and is characterized by a severe defect of cell-mediated immunity which is often accompanied by cancers such as Kaposi's sarcoma as well as secondary infections such as tuberculosis.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:15"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Albinism</name> <rdfs:comment>Protein which, if defective, causes albinism, a genetically determined or environmentally induced absence of pigmentation in animals normally pigmented. This can lead for example to lack of pigmentation in hair, skin and eyes.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:16"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Alginate biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of alginate. Alginate is an exopolysaccharide in the cell walls of brown algae and in the capsular material of certain strains of Pseudomonas and Azotobacter, in which it provides a protective barrier against host immune defenses and antibiotics.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:42121"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:17"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Alkaloid metabolism</name> <rdfs:comment>Protein involved in a biochemical reaction with alkaloids, a group of nitrogenous organic molecules usually found in plants. Various alkaloids have toxic or medical properties, such as caffeine, morphine and nicotine.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9820"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:19"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Alkylphosphonate uptake</name> <rdfs:comment>Protein involved in alkylphosphonate uptake. Certain bacteria such as Escherichia coli can use alkylphosphonates as a phosphorus source.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:15716"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:20"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Allergen</name> <rdfs:comment>Protein that stimulates the production of, and reacts with, antibodies (IgE) thus creating an allergic reaction (immediate-type hypersensitivity). Examples are pollen allergens from plants, venom allergens from insects, dust-mite allergens, and animal hair allergens.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:16068"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:21"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Allosteric enzyme</name> <rdfs:comment>Enzyme whose activity is modified by the noncovalent binding of an allosteric effector at a site other than the active site. This binding mediates conformational changes, altering its catalytic or binding properties.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:3824"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:22"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Alpha-amylase inhibitor</name> <rdfs:comment>Protein that inhibits alpha-amylase, an enzyme that catalyzes the endohydrolysis of 1,4-alpha-glucosidic linkages in oligosaccharides and polysaccharides.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:15066"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:23"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Alport syndrome</name> <rdfs:comment>Protein which, if defective, causes Alport syndrome, an hereditary disorder characterized by a progressive glomerulonephritis leading to end-stage renal disease, often associated with sensorineural hearing loss and ocular abnormalities.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:24"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Alternative initiation</name> <rdfs:comment>Protein for which at least two isoforms exist due to the usage of alternative initiation codons in the same mRNA (the resulting isoforms differ in their N-terminus).</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:877"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Alternative promoter usage</name> <rdfs:comment>Protein for which at least two isoforms exist due to the alternative usage of promoters.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:25"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Alternative splicing</name> <rdfs:comment>Protein for which at least two isoforms exist due to distinct pre-mRNA splicing events.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:26"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Alzheimer's disease</name> <rdfs:comment>Protein which, if defective, causes Alzheimer's disease. This neurological disorder is often observed in elderly people and involves atrophy of neurones in the cerebral cortex leading to progressive dementia.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:27"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Amidation</name> <rdfs:comment>Peptide which is posttranslationally modified by C-terminal amidation. The amino acid to be modified is followed by a glycine, which provides the amide group. In a first reaction step the glycine is oxidized to form alpha-hydroxy-glycine. Then the modified glycine is converted into the C-terminally amidated peptide and a glyoxylate. C-terminal amidation is essential to the biological activity of many neuropeptides and hormones.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:28"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Amino-acid biosynthesis</name> <name>Amino acid biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of naturally-occuring amino acids. In addition to their use for protein biosynthesis, they are the precursors of many molecules such as purines, pyrimidines, histamines, adrenaline and melanin.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:8652"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:878"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Amphibian defense peptide</name> <rdfs:comment>Protein specifically found in the skin of animals belonging to the vertebrate class amphibia, that includes frogs, toads, newts, salamanders and worm-like apoda. The skins of anuran amphibians, in addition to mucous glands, contain highly specialized poison glands, which, in reaction to stress or attack, exude a complex noxious species-specific cocktail of biologically active molecules. These secretions often contain a plethora of peptides such as neuropeptides and hormones. The frog dermatous glands also synthesize and store an extraordinarily rich variety of wide-spectrum antimicrobial peptides that are released onto the outer layer of the skin to provide an effective and fast-acting defense against harmful microorganisms.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6952"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:34"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Amyloid</name> <rdfs:comment>Protein which, if defective, causes amyloidosis, or constituent of amyloid deposits. Amyloid is a starch-like, complex proteinaceous fibrillar material deposited in heart, liver and other organs in various forms of amyloidosis. Amyloid deposits in the brain are characteristic of Alzheimer's disease, trisomy 21 and, to a limited extent, in normal aging.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:35"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Amyloplast</name> <rdfs:comment>Protein found in the amyloplast, a colorless plant plastid that forms and stores starch. Amyloplasts are found in many tissues, particularly in storage tissues.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9501"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:36"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Amyotrophic lateral sclerosis</name> <name>ALS</name> <rdfs:comment>Protein which, if defective, causes amyotrophic lateral sclerosis (ALS), a degenerative disorder of motor neurons in the cortex, brain stem and spinal cord. ALS is characterized by muscular weakness and atrophy.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:37"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Angiogenesis</name> <name>Vascularization</name> <rdfs:comment>Protein involved in angiogenesis, the sprouting or splitting of capillaries from pre-existing vasculature. Angiogenesis plays an important role for example during embryonic development, normal growth of tissues and maintenance of the normal vasculature, wound healing, tumor growth and metastasis.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:1525"/> <rdfs:seeAlso rdf:resource="http://www.copewithcytokines.de/cope.cgi?517"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:38"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Anhidrotic ectodermal dysplasia</name> <name>EDA</name> <name>Hypohidrotic ectodermal dysplasia</name> <name>HED</name> <rdfs:comment>Protein which, if defective, causes anhidrotic ectodermal dysplasia (EDA), a genetically heterogeneous disorder also known as hypohidrotic ectodermal dysplasia (HED). It is characterized by sparse hair (atrichosis or hypotrichosis), abnormal or missing teeth and the inability to sweat due to the absence of sweat glands.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:40"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>ANK repeat</name> <name>ANK motif</name> <name>Ankyrin repeat</name> <rdfs:comment>Protein containing at least one ANK repeat, a conserved domain of approximately 33 amino acids, that was originally identified in ankyrin. It has been described as an L-shaped structure consisting of a beta-hairpin and two alpha-helices. Many ankyrin repeat regions are known to function as protein-protein interaction domains.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:41"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Annexin</name> <rdfs:comment>Protein containing at least one annexin repeat, a conserved domain of 61 residues, which is present in proteins of the annexin family in either four or eight copies. The annexin calcium binding sites are found within the repeated domains.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:42"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Antenna complex</name> <name>Light-harvesting antenna</name> <name>Light-harvesting complex</name> <rdfs:comment>Component of an antenna complex or protein regulating the expression of such components. Antenna complexes are light-harvesting systems (LHC) which are protein-pigment complexes in or on photosynthetic membranes. LHCs receive radiant energy and transfer it to the reaction centers; an array of LHCs is often referred to as an "antenna". LHCs typically include one or more associated pigments (phycobilins, chlorophylls, bacteriochlorophylls and carotenoids).</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:30076"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:43"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Anti-oncogene</name> <name>Antitumor</name> <name>Tumor suppressor</name> <rdfs:comment>Protein that negatively regulates the cell cycle. If it is inactivated or defective the cell can proceed to rapid division. These proteins may suppress the development of tumors.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:45786"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:44"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Antibiotic</name> <name>Bactericide</name> <rdfs:comment>Protein with antibacterial activity.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6805"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:45"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Antibiotic biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of antibiotics. Antibiotics are organic compounds produced by living organims that can selectively inhibit the growth of, or kill bacteria.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:17000"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:46"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Antibiotic resistance</name> <rdfs:comment>Protein that confers, on bacteria, the ability to withstand antibiotics. The resistance is often due either to mutations that prevent antibiotic binding to the protein or to amplification of the gene encoding the protein.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:46677"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:47"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Antifreeze protein</name> <rdfs:comment>Protein that lowers the freezing point of blood or other biological fluids by inhibiting the formation of water ice crystals.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:50825"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:42309"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:50826"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:48"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Antigen</name> <name>Immunogen</name> <rdfs:comment>Protein recognized by the immune system, which elicits an immune reaction.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:49"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Antioxidant</name> <rdfs:comment>Protein capable of counteracting the damaging effects of oxidation, e.g. by trapping free radicals generated during the metabolic burst and possibly inhibiting ageing. Scavengers of highly reactive and harmful oxygen species.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:16209"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:51"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Antiviral</name> <rdfs:comment>Protein with activity against viruses, such as preventing viral replication by inhibiting viral DNA polymerase, binding to specific cell-surface receptors by inhibiting viral penetration or uncoating, inhibiting viral protein synthesis, blocking late stages of virus assembly, etc.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6952"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:52"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Apoplast</name> <rdfs:comment>Protein which is found in the part of the plant which is external to the living protoplast, ie the cell wall, the intercellular space and the lumina of dead cells such as xylem vessels and tracheids.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:48046"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:53"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Apoptosis</name> <name>Programmed cell death</name> <name>Active cell death</name> <rdfs:comment>Protein involved in programmed cell death. Apoptosis is an active process requiring metabolic activity by the dying cell; often characterised by cleavage of the DNA into fragments that give a so-called "laddering pattern" on gels. It serves as a balance to mitosis in regulating the size of animal tissues.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6915"/> <rdfs:seeAlso rdf:resource="http://www.copewithcytokines.de/cope.cgi?638"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:55"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Arginine biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of the basic amino acid arginine (Arg).</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:28"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6526"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:56"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Arginine metabolism</name> <rdfs:comment>Protein involved in biochemical reactions with the basic amino acid arginine (Arg).</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6525"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:57"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Aromatic amino acid biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of an amino acid with an aromatic side-chain: phenylalanine (Phe), tyrosine (Tyr) and tryptophan (Trp).</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:28"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9073"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:58"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Aromatic hydrocarbons catabolism</name> <rdfs:comment>Protein involved in the breakdown of aromatic hydrocarbons. Aromatic hydrocarbons are compounds which only contain carbon and hydrogen, examples include the common pollutants benzene and naphthalene.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19439"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:59"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Arsenical resistance</name> <name>Arsenic resistance</name> <rdfs:comment>Protein that confers, on bacteria and other microorganisms, the ability to withstand aromatic compounds of arsenic.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:46685"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:60"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Ascorbate biosynthesis</name> <name>Vitamin C biosynthesis</name> <name>Ascorbic acid biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of ascorbate, the ionized form of ascorbic acid (vitamin C). Ascorbic acid is derived from glucose via the uronic acid pathway. This water-soluble vitamin is essential for the synthesis of bone, cartilage and dentine. It is required in the diet of primates and some other species that cannot synthesize L-ascorbic acid because of their deficiency in L-gulono-gamma-lactone oxidase, a key enzyme for the biosynthesis of this vitamin.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19853"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:61"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Asparagine biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of the polar amino acid asparagine (Asn).</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:28"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6529"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:65"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Atherosclerosis</name> <name>Arteriosclerosis</name> <rdfs:comment>Protein which, if defective, causes atherosclerosis, which is characterized by deposits of plaques (atheromas) in the blood vessels, thus narrowing the vessel lumen and restricting blood flow. Atheromas consist of lipids (cholesterol), carbohydrates, blood products, fibrous tissue and calcium deposits.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:66"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>ATP synthesis</name> <rdfs:comment>Protein involved in the synthesis of adenosine 5'-triphosphate (ATP). ATP is a ribonucleotide adenosine (a purine base adenine linked to the sugar D-ribofuranose) which carries 3 phosphate groups esterified to the sugar moiety. It is the cell's source for energy and phosphate.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6754"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:67"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>ATP-binding</name> <rdfs:comment>Protein which binds adenosine 5'-triphosphate (ATP), a ribonucleotide adenosine (a purine base adenine linked to the sugar D-ribofuranose) that carries three phosphate groups esterified to the sugar moiety. It is the cell's source for energy and phosphate.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5524"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:68"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Autocatalytic cleavage</name> <rdfs:comment>Protein catalyzing its own cleavage.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:69"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Autoimmune encephalomyelitis</name> <name>Autoimmune encephalitis</name> <rdfs:comment>Protein which, if defective, causes autoimmune encephalomyelitis. This form of autoimmune inflammation of the brain and spinal cord causes demyelination.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:70"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Autoimmune uveitis</name> <rdfs:comment>Protein which, if defective, causes autoimmune inflammation of the uvea, which is the vascular middle coat of the eye, comprising the iris, ciliary body and choroid.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:71"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Autoinducer synthesis</name> <rdfs:comment>Protein involved in the synthesis of an autoinducer, a molecule which triggers the regulators of biosynthetic genes.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:72"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Autophagy</name> <rdfs:comment>Protein participating in autophagy, a process of intracellular bulk degradation in which cytoplasmic components including organelles are directed to the lysosome/vacuole by a membrane-mediated process.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6914"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:73"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Auxin biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of auxins. Auxins are plant hormones which play a role in many aspects of plant growth and development.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9851"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:75"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>B-cell activation</name> <rdfs:comment>Protein involved in the activation and proliferation of B-cells. B-cells are activated by the binding of antigen to receptors on its cell surface which causes the cell to divide and proliferate. Some stimulated B-cells become plasma cells, which secrete antibodies. Others become long-lived memory B-cells which can be stimulated at a later time to differentiate into plasma cells.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:42113"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:875"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Bacterial capsule</name> <rdfs:comment>Protein which is part of a bacterial capsule or which is involved in its formation and maintenance. The bacterial capsule is a layer of material, usually polysaccharide, attached to the cell wall possibly via covalent attachments to either phospholipid or lipid-A molecules. It has several functions: promote bacterial adhesion to surfaces or interaction with other organisms; act as a permeability barrier, as a defense mechanism against phagocytosis and/or as a nutrient reserve. Among pathogens, capsule formation often correlates with pathogenicity.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:78"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Bacteriocin</name> <rdfs:comment>Peptidic antibiotic, often plasmid encoded, produced by specific strains of bacteria that is lethal against other strains of the same or related species. E.g. bacteriocin, colicin, lantibiotic.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:44"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5102"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19835"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:871"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Bacteriocin biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of a bacteriocin.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:45"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:30152"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:79"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Bacteriocin immunity</name> <rdfs:comment>Protein that confers to a bacteria immunity against a specific bacteriocin that it synthesizes.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:30153"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:81"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Bacteriolytic enzyme</name> <rdfs:comment>Enzyme, e.g. lysozyme or endopeptidase, essential for lysis of bacterial cell walls.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:3824"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19835"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:42742"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:82"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Bait region</name> <rdfs:comment>Protein having a peptide stretch which contains specific cleavage sites for different proteinases, and which enables inhibition of all four classes of proteinases.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:17114"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:83"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Bardet-Biedl syndrome</name> <name>BBS</name> <rdfs:comment>Protein which, if defective, causes Bardet-Biedl syndrome (BBS), a genetically heterogeneous, autosomal recessive disorder. It is characterized by pigmentary retinopathy, obesity, polydactyly, hypogenitalism, renal malformation and mental retardation. Secondary features include diabetes mellitus, hypertension and congenital heart disease.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:85"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Behavior</name> <rdfs:comment>Protein which affects the behavior, the action or reaction, of an organism to a stimulus or situation.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7610"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:86"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Bence-Jones protein</name> <rdfs:comment>Protein which is a dimer of immunoglobulin light chains synthesized in large amounts by patients who have myeloma or bone marrow tumor. Bence-Jones protein is sufficiently small to be excreted by the kidney into urine.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:87"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Bernard Soulier syndrome</name> <name>BSS</name> <rdfs:comment>Protein which, if defective, causes Bernard Soulier syndrome (BSS), a familial coagulation disorder characterized by a prolonged bleeding time, unusually large platelets, and impaired prothrombin consumption. BSS is caused by a genetic deficiency in platelet membrane glycoprotein Ib alpha chain and platelet glycoprotein IX, where platelets aggregate normally but do not stick to collagen of the sub-endothelial membrane.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:90"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Biological rhythms</name> <rdfs:comment>Protein involved in the generation of rhythmic pattern of behaviors or activities, e.g. circadian rhythm which is a metabolic or behavioural rhythm within a cycle of 24 hours.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7622"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:91"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Biomineralization</name> <rdfs:comment>Protein involved in the process by which mineral crystals are deposited in an organized fashion in the matrix (either cellular or extracellular) of living organisms. Such process give rise to inorganic-based structures such as bone, tooth, ivory, shells, cuticles, corals or bacterial magnetosomes.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:1503"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:92"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Biotin</name> <name>Vitamin B8</name> <name>Vitamin H</name> <rdfs:comment>Protein which contains at least one biotin as prosthetic group or cofactor (e.g. some carboxylases and decarboxylases, and biotin carboxyl carrier protein) or which binds biotin, like avidin. Biotin is a water-soluble vitamin (member of the B complex vitamins) essential for fatty acid biosynthesis, catabolism, and it acts as a growth factor for many cells.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9374"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:93"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Biotin biosynthesis</name> <name>Vitamin B8 biosynthesis</name> <name>Vitamin H biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of biotin, a prosthetic group for some carboxylase and decarboxylase enzymes. This water-soluble vitamin is essential for fatty acid biosynthesis, catabolism, and it acts as a growth factor for many cells.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9102"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:94"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Blood coagulation</name> <rdfs:comment>Protein involved in blood clotting, a complex enzymatic cascade, in which the activated form of one factor catalyzes the activation of the next factor. Both, the extrinsic clotting pathway, induced by a damaged surface, and the intrinsic pathway, induced by a trauma, converge in a final common pathway to form cross-linked fibrin clots.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7596"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:95"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Blood group antigen</name> <name>Agglutinogen</name> <rdfs:comment>Protein belonging to the set of cell surface antigens found chiefly, but not solely, on blood cells. More than fifteen different blood group systems are recognised in humans. In most cases the antigenic determinant resides in the carbohydrate chains of membrane glycoproteins or glycolipids.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:48"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:96"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Bombesin family</name> <rdfs:comment>Protein belonging to the bombesin/neuromedin b/ranatensin family. Bombesin is a tetradecapeptide neurohormone with paracrine/autocrine effects first isolated from skin of fire-bellied toad (Bombina bombina); the mammalian equivalent is gastrin-releasing peptide (GRP).</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:100"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Branched-chain amino acid biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of the essential aliphatic branched-chain amino acids leucine (Leu), isoleucine (Ile) and valine (Val).</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:28"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9082"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:101"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Branched-chain amino acid catabolism</name> <rdfs:comment>Protein involved in the degradation of the branched-chain amino acids leucine (Leu), isoleucine (Ile) and valine (Val).</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9083"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:102"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Bromination</name> <rdfs:comment>Protein which is posttranslationally modified by the attachment of at least one bromine.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:103"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Bromodomain</name> <rdfs:comment>Protein containing at least one bromodomain. The bromodomain is a conserved region, approximately 70 amino acids, characteristic for a class of regulatory proteins. It mediates interactions with proteins that are necessary for transcriptional activation.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:104"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Cadmium</name> <rdfs:comment>Protein which binds at least one cadmium atom, or protein whose function is cadmium-dependent. Cadmium is a heavy metal, chemical symbol Cd.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:105"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Cadmium resistance</name> <rdfs:comment>Protein that confers, on bacteria and other microorganisms, the ability to withstand the transition metal cadmium (Cd).</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:46686"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:106"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Calcium</name> <rdfs:comment>Protein whose function is calcium-dependent. Calcium is essential for a variety of bodily functions, such as neurotransmission, muscle contraction and proper heart function. The metal calcium has the chemical symbol Ca.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:110"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Calcium-binding</name> <rdfs:comment>Protein which binds at least one calcium ion. Calcium is essential for a variety of bodily functions, such as neurotransmission, muscle contraction and proper heart function.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5509"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:111"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Calcium/phospholipid-binding</name> <rdfs:comment>Protein which contains at least one binding site for calcium and phospholipid. For example, proteins with annexin repeats, of which a pair may form one binding site for calcium and phospholipid, or some proteins with C2 domains.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:110"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5544"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:112"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Calmodulin-binding</name> <rdfs:comment>Protein which binds at least one calmodulin, an ubiquitous small calcium-binding protein. Its binding to proteins may cause a conformational change which either activates or inactivates their function.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5516"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:114"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>cAMP</name> <name>Cyclic AMP</name> <rdfs:comment>Protein whose function is cAMP-dependent or which catalyzes its hydrolysis. cAMP is the abbreviation for cyclic AMP, adenosine 3',5'-cyclic monophosphate, the first second messenger hormone signaling system to be characterised. It is generated from ATP by the action of adenyl cyclase that is coupled to hormone receptors by G proteins. cAMP activates a specific protein kinase and is inactivated by phosphodiesterase action giving 5'AMP.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:115"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>cAMP biosynthesis</name> <name>Cyclic AMP biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of cAMP. cAMP is the abbreviation for cyclic AMP, adenosine 3',5'-cyclic monophosphate.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6171"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:118"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Capsid assembly</name> <name>Coat assembly</name> <rdfs:comment>Protein involved in the assembly of the external protein coat of a virus. The capsid is formed by self-assembly of one or more protein subunits into a regular structure. Its role is to protect the nucleic acids of the virus. The capsid may itself be surrounded by a membranous envelope.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19069"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:119"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Carbohydrate metabolism</name> <rdfs:comment>Protein participating in biochemical reactions in which carbohydrates are involved. Carbohydrate is a general term for sugars and related compounds with the general formula Cn(H2O)n. The smallest are monosaccharides (e.g. glucose); polysaccharides (e.g. starch, cellulose, glycogen) can be large and vary in length.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5975"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:120"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Carbon dioxide fixation</name> <rdfs:comment>Protein involved in the process of carbon dioxide fixation, e.g. incorporation of carbon dioxide into carbohydrates by photosynthetic organisms or formation of oxaloacetate from pyruvate.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:15977"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:122"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Cardiomyopathy</name> <rdfs:comment>Protein which, if defective, causes cardiomyopathy, a chronic disorder which affects the heart muscle causing a reduced pumping function. It is a major cause of morbidity and mortality.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:124"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Carnitine biosynthesis</name> <rdfs:comment>Protein involved in the biosynthesis of carnitine (L-3-hydroxy-4, N,N,N-trimethylaminobutyrate), an essential metabolite with a number of indispensable roles in intermediary metabolism.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:45329"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:125"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Carotenoid biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of carotenoids, a group of orange, yellow, red, purple or brown pigments in plants, bacteria and some fungi. Carotenoids, which comprise the carotenes and the xanthophylls, are long polyisoprenoid molecules having conjugated double bonds enabling light absorbtion.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:16117"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:898"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Cataract</name> <rdfs:comment>Protein which, if defective, causes cataract, a partial or complete ocular opacity that affects the crystalline lens or its capsule, leading to impaired vision or blindness. The many types of cataract are classified by their morphology (size, shape, location) or etiology (cause and time of occurrence). Cataracts may occur as an isolated anomaly, as part of generalized ocular developmental defects, or as a component of a multisystem disorder.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:127"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Catecholamine biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of catecholamines, which are amine derivatives of catechol (2-hydroxyphenol). They are synthesized from the amino acid tyrosine (Tyr) in sympathetic-nerve terminals and in the adrenal gland. Catecholamines act as hormones or neuro-transmitters, e.g. adrenaline, noradrenaline and dopamine.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:42423"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:128"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Catecholamine metabolism</name> <rdfs:comment>Protein participating the biochemical reactions in which catecholamines are involved. Catecholamines are amine derivatives of catechol (2-hydroxyphenol). They are synthesized from the amino acid tyrosine (Tyr) in sympathetic-nerve terminals and in the adrenal gland. Catecholamines act as hormones or neuro-transmitters, e.g. adrenaline, noradrenaline and dopamine.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6584"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:129"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>CBS domain</name> <rdfs:comment>Protein containing at least one CBS domain, a conserved domain found in a wide range of proteins, which is named after cystathionine beta-synthase (CBS), an enzyme that contains 2 copies of this domain.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:130"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Cell adhesion</name> <rdfs:comment>Protein involved in the adherence of cells to other cells or to a matrix. Cell adhesion is mediated by cell surface proteins.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5515"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7155"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:131"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Cell cycle</name> <rdfs:comment>Protein involved in the complex series of events by which the cell duplicates its contents and divides into two. The cell cycle can be divided in four phases termed G1 (first gap period), S (synthesis, phase during which the DNA is replicated), G2 (second gap period) and M (mitosis).</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7049"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:132"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Cell division</name> <rdfs:comment>Protein involved in the separation of one cell into two daughter cells. In eukaryotic cells, cell division includes the nuclear division (mitosis) and the subsequent cytoplasmic division (cytokinesis).</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:131"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:133"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Cell shape</name> <rdfs:comment>Protein involved in the formation and maintenance of the cell shape, the physical dimensions of a cell. In most plants, algae, bacteria and fungi the cell wall is responsible for the shape of the cells.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:902"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:134"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Cell wall</name> <rdfs:comment>Protein which is part of the cell wall or which is involved in the formation and maintenance of it. The cell wall is an extracellular layer outside the plasma membrane which protects the cell against mechanical damage, osmotic strength and which determines the cell shape. It is prominent in most plants, algae, bacteria and fungi.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5618"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:135"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Cellulose biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of cellulose, a linear polymer of (1-4)-beta-linked D-glucose subunits. It is the most abundant cell-wall and structural polysaccharide in plants and it is also found in some lower invertebrates. Cellulose is the major component of wood and thus of paper. Cotton is the purest natural form of cellulose. As a raw material, it forms the basis for many derivatives used in chromatography, ion exchange materials, explosives manufacturing and pharmaceutical preparations.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:30244"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:137"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Centromere</name> <rdfs:comment>Protein which binds centromeres or which is required for the assembly and movement of centromeres. Centromeres are the regions of replicated eukaryotic chromosomes where the two chromatids are joined together.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:775"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:138"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>CF(0)</name> <rdfs:comment>Protein component of the F-type ATP synthase complex CF(0) or protein involved in its assembly. F-type ATPases consist of the two complex components CF(0), the membrane proton channel, and CF(1), the catalytic core.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:139"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>CF(1)</name> <rdfs:comment>Protein component of the F-type ATP synthase complex CF(1) or protein involved in its assembly. F-type ATPases consist of the two complex components CF(0), the membrane proton channel, and CF(1), the catalytic core.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:140"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>cGMP</name> <name>Cyclic GMP</name> <rdfs:comment>Protein whose function is cGMP-dependent or which catalyzes its hydrolysis. cGMP is the abbreviation for cyclic GMP, guanosine 3',5'-cyclic monophosphate. It acts as a second messenger.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:141"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>cGMP biosynthesis</name> <name>Cyclic GMP biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of cGMP. cGMP is the abbreviation for cyclic GMP, guanosine 3',5'-cyclic monophosphate.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6182"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:143"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Chaperone</name> <rdfs:comment>Protein which is transiently involved in the noncovalent folding, assembly and/or disassembly of other polypeptides or RNA molecules, including any transport and oligomerisation processes they may undergo, and the refolding and reassembly of protein and RNA molecules denatured by stress. Though involved in these processes, chaperones are not an integral part of these functioning molecules.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:51082"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6457"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:144"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Charcot-Marie-Tooth disease</name> <rdfs:comment>Protein which, if defective, causes Charcot-Marie-Tooth disease (CMT), a heterogeneous group of hereditary motor and sensory neuropathies (HMSN) characterized by distal muscular atrophy and weakness, hollow feet, absent or diminished deep-tendon reflexes and impaired sensation. CMT is classified into two major classes. CMT type 1 includes demyelinating neuropathies that are characterized by nerve conductance velocities (NCVs) less than 38m/s and segmental demyelination and remyelination; CMT type 2 includes axonal neuropathies that are characterized by normal or mildly reduced NCVs and chronic axonal degeneration and regeneration.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:147"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Chitin-binding</name> <rdfs:comment>Protein which binds chitin, a linear polysaccharide consisting of (1->4)-beta-linked D-glucosamine residues, most of which are N-acetylated. The 30-43 amino acids long chitin-binding domain contains several conserved glycine and cysteines residues. The conserved cysteines form disulfide bonds. Chitin-binding domains have been found in plant, fungal and bacterial proteins.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:8061"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:868"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Chloride</name> <rdfs:comment>Protein which binds at least one chloride, or protein whose function is chloride-dependent. Chloride is a negatively-charged ion, which is abbreviated Cl(-).</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:149"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Chlorophyll biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of chlorophylls. These photosynthetic pigments are magnesium-porphyrin complexes with a long hydrophobic terpenoid side chain (the alcohol phytol). Angiosperms have only a light-dependent pathway for chlorophyll biosynthesis, other oxygenic organisms seem to have both the light-dependent and the light-independent pathways.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:15995"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:881"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Chlorophyll catabolism</name> <rdfs:comment>Protein involved in the degradation of chlorophylls. These photosynthetic pigments are magnesium-porphyrin complexes with a long hydrophobic terpenoid side chain (the alcohol phytol).</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:150"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Chloroplast</name> <rdfs:comment>Protein encoded by or localized in the chloroplast, a photosynthetic organelle of eukaryotic cells, in which light-harvesting and ATP synthesis occurs.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9507"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:151"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Chlorosome</name> <rdfs:comment>Photosynthetic light-harvesting complexes found in green bacteria. Chlorosomes are sac-like organelles appressed to the cytoplasmic membrane of the cell membrane.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:891"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Chondrogenesis</name> <rdfs:comment>Protein involved in chondrogenesis, the mechanism of cartilage formation. Chondrogenesis proceeds through determination of cells and their aggregation into prechondrogenic condensations, differentiation into chondrocytes, and later maturation. The formation of the long bones requires a cartilage template.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:154"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Chorion</name> <rdfs:comment>Protein present in the chorion or involved in its assembly. The chorion, secreted by the follicle cells, is either a protective membrane which surrounds the eggs of insects and fishes, or the extraembryonic membrane derived from the trophoblast and which surrounds the embryo of amniote vertebrates.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5213"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:155"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Chromate resistance</name> <rdfs:comment>Protein that enables bacteria and other microorganisms to withstand chromate, a salt of chromic acid (H2CrO4).</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:46687"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:156"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Chromatin regulator</name> <rdfs:comment>Protein controlling the opening or closing of chromatin.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:16568"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:157"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Chromophore</name> <rdfs:comment>Protein which interacts with one or more chromophores. A chromophore absorbs and transmits light energy. Originally it was used for visibly colored molecules, but it applies also to UV- and IR-absorbing molecules.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:18298"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:158"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Chromosomal protein</name> <rdfs:comment>Protein which is associated with chromosomal DNA, including histones, protamines and high mobility group proteins.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5694"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:159"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Chromosome partition</name> <name>Chromosome segregation</name> <rdfs:comment>Protein involved in chromosome partition, the process by which newly replicated plasmids and chromosomes are actively segregated prior to cell division. E.g., par and soj which contribute to efficient chromosome partitioning by serving functions analogous to centromeres (i.e. pairing or positioning of sister chromosomes).</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7059"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:160"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Chromosomal translocation</name> <rdfs:comment>Protein which can be altered by chromosomal translocation, a chromosomal aberration often involved in cancer or another disease. Chromosomal translocation is most commonly a two break event that results in an exchange of telomeres between non-homologous chromosomes.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:161"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Chronic granulomatous disease</name> <name>CGD</name> <rdfs:comment>Protein which, if defective, causes chronic granulomatous disease (CGD), a disease characterized by the failure of activated phagocytes to generate superoxide.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:162"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Chylomicron</name> <rdfs:comment>Protein component of the chylomicrons or involved in their catabolism. Chylomicrons are the largest lipoprotein complexes with the lowest protein-to-lipid ratio. They are present in the blood or lymph and transport exogenous (dietary) cholesterol, triacylglycerols and other lipids from the intestine to the liver or to the adipose tissue.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:163"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Citrate utilization</name> <rdfs:comment>Protein which allows the utilization of the 6-carbon tricarboxylic acid citrate as a sole source of carbon and energy.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5371"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:164"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Citrullination</name> <rdfs:comment>Protein which is posttranslationally modified by the deimination of one or more arginine residues.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:165"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Cleavage on pair of basic residues</name> <rdfs:comment>Protein which is posttranslationally modified by the cleavage on at least one pair of basic residues, in order to release one or more mature active peptides (such as hormones).</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:166"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Cnidocyst</name> <name>Nematocyst</name> <rdfs:comment>Protein localized in the cnidocyst, an organelle found in cnidoblast (nematoblast) cells. When matured, these stinging organelles store toxins and can deliver them when the cnidocil (a short extension of the cnidocyst) is stimulated by a prey or another stimulus. These proteins are principally found in anemones and jellyfishes.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:42151"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:167"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Coat protein</name> <name>Capsid protein</name> <rdfs:comment>Protein which is present in the viral coat. These proteins protect the nucleic acids of the virus.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5198"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19028"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:168"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Coated pits</name> <rdfs:comment>Protein which is a component of coated pits. Coated pits are regions of the plasma membrane specialized in receptor-mediated endocytosis. Their cytoplasmic surface is coated with a bristlelike structure made of clathrin and other proteins. During the first steps of endocytosis, coated pits are internalized to form coated vesicles which transport proteins from organelle to organelle.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5905"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:169"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Cobalamin biosynthesis</name> <name>Vitamin B12 biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of cobalamin. Cobalamin, which is synthesized by microorganisms, has equatorial sites occupied by a modified porphyrin ring system, with two of the four pyrrol rings fused directly (without an intervening methine bridge). The modified porphyrin system binds a cobalt(III) ion in the center, and this is called a corrin ring system. One axial site is occupied usually by an intramolecularly-bound dimethylbenzimidazole nucleotide and the other axial site is occupied by a number of different ligands such as water (aquacobalamin), cyanide (cyanocobalamine=vitamin B12), glutathione (glutathionylcobalamine), 5'deoxyadenosine (adenosylcobalamine=coenzyme B12) or a methyl group (methylcobalamin). Vitamin B12, for instance, is a prosthetic group of certain mammalian enzymes, where it is essential for the normal maturation and development of erythrocytes. A deficiency in the diet or more frequently the failure to absorb the vitamin B12 give rise to pernicious anemia.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9236"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:170"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Cobalt</name> <rdfs:comment>Protein which binds at least one cobalt atom, or protein whose function is cobalt-dependent. Cobalt is a metallic element, chemical symbol Co.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:172"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Cockayne's syndrome</name> <name>CS</name> <rdfs:comment>Protein which, if defective, causes Cockayne's syndrome (CS), an autosomal recessive disease characterized by UV-sensitive skin (without pigmentation abnormalities), neurological dysfunction due to demyelination of neurons and calcification of basal ganglia (psychomotor retardation, deafness, optic atrophy, retinal pigmentation and hyperreflexes) and dysmorphic dwarfism (immature sexual development and microcephaly).</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:173"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Coenzyme A biosynthesis</name> <name>CoA biosynthesis</name> <name>CoASH biosynthesis</name> <rdfs:comment>Protein involved in the biosynthetic pathway leading from pantothenate to coenzyme A (CoA). CoA has two halves in phosphodiester linkage: a 3',5'-ADP residue, and 4-phosphopantetheine. The phosphopantetheine moiety is itself composed of three structural entities: a branched chain dihydroxy acid in amide linkage to a beta-alanyl residue, which is in turn linked to a cysteamide containing the reactive thiol. Coenzyme A functions as a carrier of acetyl and acyl groups and is essential for numerous biosynthetic, energy-yielding, and degradative metabolic pathways. Acetyl-CoA is the common cellular currency for acetyl transfers.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:15937"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:174"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Coenzyme M biosynthesis</name> <name>CoM biosynthesis</name> <name>2-mercaptoethanesulfonic acid biosynthesis</name> <rdfs:comment>Protein involved in the biosynthesis of coenzyme M. Coenzyme M (2-mercaptoethanesulfonic acid) is the smallest known organic cofactor. CoM serves as a methyl group carrier in key reactions within the pathway of methane formation from C1 precursors. In the alkene metabolism pathway, it is involved in aliphatic epoxyde carboxylation.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19295"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:175"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Coiled coil</name> <name>Heptad repeat pattern</name> <rdfs:comment>Protein which contains at least one coiled coil domain, a type of secondary structure composed of two or more alpha helices which entwine to form a cable structure. In proteins, the helical cables serve a mechanical role in forming stiff bundles of fibres.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:176"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Collagen</name> <rdfs:comment>Protein which contains one or more collagen-like domain. Collagen is a fibrous protein found in vertebrates, the major element of skin, bone, tendon, cartilage, blood vessels and teeth. It forms insoluble fibres of high tensile strength and which contains the unusual amino acids hyroxyproline and hydroxylysine. It is rich in glycine but lacks cysteine and tryptophan, and has an unusually regular amino-acid domain.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:177"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Collagen degradation</name> <rdfs:comment>Protein involved in the degradation of collagen, a family of fibrous proteins found in skin, bones, teeth, cartilage and other tissues of vertebrates.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:30574"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:178"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Competence</name> <rdfs:comment>Protein involved in competence, the state in which a cell or organism is able to take up DNA and become genetically transformed.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:179"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Complement alternate pathway</name> <name>Alternate complement pathway</name> <name>Properdin system</name> <rdfs:comment>Protein involved in the complement alternate pathway which activates the proteins of the complement system. This pathway can be activated by IgA immune complexes, but also by bacterial endotoxins, polysaccharides and cell walls, without participation of an antigen-antibody reaction.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6957"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:180"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Complement pathway</name> <name>Classical complement pathway</name> <rdfs:comment>Pathway which activates the proteins of the complement system, a group of blood proteins of the globulin class involved in the lysis of foreign cells after they have been coated with antibody, and which also promote the removal of antibody-coated foreign particles by phagocytic cells. The pathway proceeds by a cascade reaction of successive binding and proteolytic cleavage of complement components. This pathway can be activated by either IgG or IgM binding to an antigen.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6958"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:181"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Complete proteome</name> <rdfs:comment>Protein which is thought to be expressed by an organism whose genome has been completely sequenced. This keyword is so far only used for microbial (bacterial and archaeal) proteins. A complete set of proteins from a microbial genome can therefore be obtained using this keyword across Swiss-Prot and TrEMBL.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:182"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Cone-rod dystrophy</name> <rdfs:comment>Protein which, if defective, causes cone-rod dystrophy, a disease where dystrophy of cone-rod cells is characterized by the initial degeneration of cone photoreceptor cells, thus causing early loss of visual acuity and color vision, followed by the degeneration of rod photoreceptor cells and leading to progressive night blindness and peripheral visual field loss.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7601"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:900"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Congenital disorder of glycosylation</name> <rdfs:comment>Protein which, if defective, causes a congenital disorder of glycosilation. In the endoplasmic reticulum (ER) of eukaryotes, N-linked glycans are first assembled on the lipid carrier dolichyl pyrophosphate. The GlcNAc(2)Man(9)Glc(3) oligosaccharide is transferred to selected asparagine residues of nascent polypeptides. Defects along the biosynthetic pathway of N-glycans are associated with severe multisystemic syndromes called congenital disorders of glycosylation (CDG). The characteristic biochemical feature of CDG is defective glycosylation of glycoproteins due to mutations in genes required for the biosynthesis of N-linked oligosaccharides. Defects of the assembly of dolichyl-linked oligosaccharides or their transfer on to nascent glycoproteins form type I forms of CDG, whereas CDG type II comprises all defects of the trimming and elongation of N-linked oligosaccharides.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:184"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Conjugation</name> <rdfs:comment>Protein involved in the temporary fusion of two gametes or two cells leading to the transfer of genetic material. This process is seen in bacteria, ciliate protozoa and certain fungi.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:746"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:186"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Copper</name> <rdfs:comment>Protein which binds at least one copper atom, or protein whose function is copper-dependent. Copper is a trace metallic element, chemical symbol Cu.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:188"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Copulatory plug</name> <rdfs:comment>Protein involded in the formation of the copulatory plug, a plug composed of a number of proteins which are secreted by the seminal vesicle under the influence of testosterone. Found in rodents.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7620"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:189"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Core protein</name> <rdfs:comment>Protein directly associated with the nucleic acid inside the nucleocapsid (core). Core proteins are found mainly in icosahedral DNA and RNA viruses.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19012"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:190"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Covalent protein-DNA linkage</name> <name>DNA-protein covalent cross-linking</name> <rdfs:comment>Protein covalently attached to the end of a viral replicating DNA and which is necessary for DNA replication.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:18142"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:191"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Covalent protein-RNA linkage</name> <name>RNA-protein covalent cross-linking</name> <rdfs:comment>Protein covalently attached to the end of a viral replicating RNA and which is necessary for RNA replication.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:18144"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:192"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Crown gall tumor</name> <rdfs:comment>Protein involved in crown gall tumor formation, a plant tumor caused by the bacterium Agrobacterium tumefaciens.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:885"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>CTQ</name> <name>Cysteine tryptophylquinone</name> <rdfs:comment>Protein which contains at least one cysteine tryptophylquinone (CTQ) cross-link modification. CTQ is formed by oxidation of the indole ring of a tryptophan to form tryptophylquinone followed by covalent cross-linking with a cysteine residue. In the quinohemoprotein amine dehydrogenase, CTQ mediates during the catalytic cycle electron transfer from the substrate to either a copper protein, azurin, or cytochrome c-550.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:193"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Cuticle</name> <rdfs:comment>Protein which is a component of the cuticle, the outer protective layer produced by epidermal cells that covers the body of many invertebrates.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:42302"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:194"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Cyanelle</name> <name>Muroplast</name> <name>Cyanoplast</name> <rdfs:comment>Protein encoded by the cyanelle genome or protein located in the cyanelle. Cyanelles are the plastids of glaucocystophyte algae. They are surrounded by a double membrane and, in between, a peptidoglycan wall. The cyanelle genome is of chloroplast size and contains genes for tRNAs, rRNAs and approx. 150 proteins, which is more than found in higher plant chloroplast genomes (this feature is also shared by other primitive plastids). Thylakoid membrane architecture and the presence of carboxysomes are cyanobacteria-like. Historically, the term cyanelle is derived from a classification as endosymbiotic cyanobacteria, and thus is not fully correct.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9842"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:195"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Cyclin</name> <rdfs:comment>Protein that belongs to the cyclin family or that contains a cyclin box-like domain. Cyclins are regulatory subunits of the cyclin-dependent protein kinases. They form kinase holoenzymes, with distinct biochemical characteristics and nonredundant biological functions, which mediate phosphorylation of cellular proteins, including key cell cycle regulatory molecules. In this way, the kinase holoenzymes promote the transit of cells through the division cycle. Cyclins accumulate during interphase of eukaryotic cell cycle and are destroyed at the end of mitosis. Cyclins are also encoded by viruses.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:196"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Cycloheximide resistance</name> <rdfs:comment>Protein that confers, on an organism, the ability to withstand cycloheximide, an antibiotic produced by Streptomyces griseus, which inhibits eukaryotic elongation during protein synthesis. The resistance is often due to mutations that prevent antibiotic binding to the protein.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:46"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:46677"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:197"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Cyclosporin</name> <rdfs:comment>Protein binding cyclosporin or protein whose function is inhibited by cyclosporin, e.g. cyclophilins. Cyclosporins are peptides obtained from certain hyphomycetes which have potent immuno-suppressant activity on humoral and cellular systems. Cyclosporin is used in transplant surgery to suppress the immune response.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:198"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Cysteine biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of cysteine, the amino acid with the highly reactive sulfhydryl group (-SH). It is derived from the amino acids methionine and serine. Cysteine plays a special role in shaping some proteins by forming disulfide bonds. In enzymes the unique reactivity of this group is frequently exploited at the catalytic site.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:28"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19344"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:199"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Cystinuria</name> <name>CSNU</name> <rdfs:comment>Protein which, if defective, causes cystinuria (CSNU), an autosomal recessive condition of persistent excessive urinary excretion of cystine and three other dibasic amino acids: lysine, ornithine, and arginine. CSNU arises from impaired reabsorption of these amino acids through the epithelial cells of the renal tubule and gastrointestinal tract. It is characterized by cystine stones in the kidney, ureter and bladder. Three clinical types of cystinuria have been described: cystinuria type-I (CSNU1), type-II (CSNU2) and type-III (CSNU3).</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:200"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Cytadherence</name> <rdfs:comment>Protein involved in cytadherence, the attachment of mycoplasma to the epithelium.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:20035"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:201"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Cytochrome c-type biogenesis</name> <rdfs:comment>Protein involved in the biogenesis of c-type cytochromes. Cytochromes c are electron­transfer proteins having one or several heme c groups, bound to the protein by one or, more commonly two, thioether bonds involving sulphydryl groups of cysteine residues.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:17004"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:202"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Cytokine</name> <rdfs:comment>Small secreted proteins from higher eukaryotes which affect the growth, division and functions of other cells, e.g. interleukins, lymphokines, TNF and interferons. Generally, growth factors are not classified as cytokines, though TGF is an exception. Chemokines are a subset of cytokines. They differ from classical hormones in that they are produced by a number of tissues or cell types rather than by specialized glands. They generally act locally in a paracrine or autocrine rather than endocrine manner.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5125"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:203"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Cytokinin biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of cytokinins, a class of plant hormones which promote cell division (e.g. kinetin, zeatin, benzyl adenine). They are also involved in cell growth, cell differentiation and in other physiological processes.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9691"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:204"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Cytolysis</name> <name>Cell lysis</name> <rdfs:comment>Protein involved in the rupture of cell membranes and loss of cytoplasm, e.g. exotoxin, cytolysin.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19835"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:205"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Cytosine metabolism</name> <rdfs:comment>Protein involved in the biochemical reactions with the pyrimidine base cytosine.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19858"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:206"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Cytoskeleton</name> <rdfs:comment>Protein which is a component or which is associated with the cytoskeleton, a dynamic three-dimensional structure that fills the cytoplasm of eukaryotic cells. The cytoskeleton is both a muscle and a skeleton, and is responsible for cell movement, cytokinesis, and the organization of the organelles within the cell. The major components of cytoskeleton are the microfilaments (of actin), microtubules (of tubulin) and intermediate filament systems in cells.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5856"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:208"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>D-amino acid</name> <rdfs:comment>Protein which contains at least one D-amino acid. All of the amino acids derived from natural proteins are of the L configuration. D-amino acids are found in nature, especially as components of certain peptide antibiotics and in walls of certain microorganisms.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:209"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Deafness</name> <rdfs:comment>Protein which, if defective, causes a partial or total inability to hear. The two principal types of deafness are conduction deafness and nerve deafness.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7605"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:211"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Defensin</name> <rdfs:comment>Families of microbicidal and cytotoxic peptides. Defensins have antibacterial, antifungal and antiviral properties. Defensins kills cells by forming voltage-regulated multimeric channels in the susceptible cell's membrane.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6952"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:212"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Dehydrin</name> <rdfs:comment>Protein which belongs to the plant dehydrin family. These plant proteins are expressed in response to dehydration, low temperature, osmotic stress, seed drying, and exposure to abscisic acid.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9414"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:213"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Dejerine-Sottas syndrome</name> <name>DSS</name> <rdfs:comment>Protein which, if defective, causes Dejerine-Sottas disease. DSS is a hereditary motor and sensory neuropathy (HMSN) of the Charcot-Marie-Tooth disease type 1 class. DSS is characterized by severe early onset, very slow nerve conduction velocities (less than 12m/sec) and raised cerebrospinal fluid protein concentrations (0.7 g/l). Clinical signs are delayed age of walking as well as areflexia.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7638"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:214"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Dental caries</name> <rdfs:comment>Protein involved in dental caries or important in the prevention of dental caries. Dental caries are localized destruction of the tooth surface, initiated by decalcification of the enamel and followed by enzymatic lysis of organic structures, the result of which is cavity formation. The cavity may penetrate the enamel and dentin, and reach the pulp. The disease may be caused by acids produced by bacteria which lead to decalcification, or by microorganisms that destroy the enamel protein, or by keratolytic microorganisms producing chelates that lead to decalcification.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:215"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Deoxyribonucleotide synthesis</name> <rdfs:comment>Protein involved in the synthesis of deoxyribonucleotides, the basic repeating units in DNA. Deoxyribonucleotides consist of a purine or a pyrimidine base bonded to deoxyribose, which in turn is bound to a phosphate group. They are synthesised by reduction of ribonucleoside diphosphates.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9263"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:216"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Detoxification</name> <rdfs:comment>Protein involved in degrading toxic compounds. Detoxification generally takes place in the liver or kidney and inactivates toxins, either by degradation or by conjugation of residues to a hydrophilic moiety in order to promote excretion.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6805"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9636"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:217"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Developmental protein</name> <rdfs:comment>Protein involved in development, the process whereby a multicellular organism develops from its early immature forms, e.g., zygote, larva, embryo, into an adult.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7275"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:218"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Diabetes insipidus</name> <rdfs:comment>Protein which, if defective, causes diabetes insipidus, a rare form of diabetes in which the kidney tubules do not reabsorb enough water resulting in excessive urine excretion (polyuria). Two types of diabetes insipidus are recognized: central or neurohypophyseal diabetes insipidus which is due to defects in the neurohypophyseal system and results in a deficient quantity of anti-diuretic hormone being produced or released; nephrogenic diabetes insipidus, a vasopressin unresponsive condition of polyuria and hyposthenuria.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:219"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Diabetes mellitus</name> <rdfs:comment>Protein which, if defective, causes diabetes mellitus, a disorder of impaired carbohydrate, protein, and fat metabolism due to insufficient secretion of insulin or to target tissue insulin resistance. Diabetes mellitus can be divided into two main types, type I or insulin-dependent diabetes mellitus (IDDM), and type II, or non insulin-dependent diabetes mellitus (NIDDM). Type I diabetes mellitus normally starts in childhood or adolescence and is caused by the body's own immune system which destroys the insulin-producing beta cells in the pancreas. Classical features are polydipsia, polyphagia and polyuria, due to hyperglycemia-induced osmotic diuresis. Type II diabetes mellitus normally starts in adulthood and is caused by a lack of sensitivity to the body's own insulin. It is usually characterized by a gradual onset with minimal or no symptoms of metabolic disturbance. Both forms of diabetes mellitus lead to secondary complications (notably cardiovascular, nephropathy, retinopathy, neuropathy). Two other major subcategories of diabetes mellitus are gestational diabetes and diabetes secondary to other medical conditions. In common usage, the term diabetes, when used alone, refers to diabetes mellitus and not diabetes insipidus.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:220"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Diaminopimelate biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of diaminopimelate, the ionic form of the amino acid diaminopimelic acid (DAP) which is found in the murein peptidoglycans of bacterial cell walls. Diaminopimelic acid is synthesised from aspartate.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19877"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:221"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Differentiation</name> <rdfs:comment>Protein involved in differentiation, the developmental process of a multicellular organism by which cells become specialized for particular functions. Differentiation requires selective expression of the genome; the fully differentiated state may be preceded by a stage in which the cell is already programmed for differentiation but is not yet expressing the characteristic phenotype determination. Also used for fungal conidiation proteins.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:30154"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:222"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Digestion</name> <rdfs:comment>Protein involved in the process whereby nutrients are rendered soluble and capable of being absorbed by the organism or cell, by action of various hydrolytic enzymes that break down proteins, carbohydrates, fats, etc.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7586"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:903"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Direct protein sequencing</name> <rdfs:comment>Protein, whose amino acid sequence has been partially (more than one residue) or completely determined experimentally by Edman degradation or by mass spectrometry.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:225"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Disease mutation</name> <rdfs:comment>Protein for which at least one variant, responsible for a disease, is described in the feature table of its Swiss-Prot entry.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:226"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>DNA condensation</name> <rdfs:comment>Protein involved in DNA condensation. In most eukaryotes, the chromosomal packing involves the wrapping of DNA around a core of histones to form nucleosomes. Adjacent nucleosomes are packaged together via Histone 1 and nucleosomes are organised into a 30nm chromatin fibre. DNA condensation takes place as cells enter mitosis or when germ cells enter meiosis.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7076"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:227"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>DNA damage</name> <rdfs:comment>Protein induced by DNA damage or protein involved in the response to DNA damage. Drug- or radiation-induced injuries in DNA introduce deviations from its normal double-helical conformation. These changes include structural distortions which interfere with replication and transcription, as well as point mutations which disrupt base pairs and exert damaging effects on future generations through changes in DNA sequence. Response to DNA damage results in either repair or tolerance.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6974"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:229"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>DNA integration</name> <rdfs:comment>Protein involved in DNA integration, a process that mediates the insertion of viral genetic material, or other duplex DNA, into a chromosome, or another replicon, in order to form a covalently linked DNA, continuous with the host DNA. The latter is subsequently replicated as part of the replicon, and may express some or all of its genes.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6313"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:231"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>DNA packaging</name> <rdfs:comment>Protein involved in the packaging of replicated viral DNA into the viral capsid and of mature bacteriophage DNA into proheads.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6323"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:233"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>DNA recombination</name> <rdfs:comment>Protein involved in DNA recombination, i.e. any process in which DNA molecules are cleaved and the fragments are rejoined to give a new combination.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6310"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:234"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>DNA repair</name> <rdfs:comment>Protein involved in the repair of DNA, the various biochemical processes by which damaged DNA can be restored. DNA repair embraces, for instance, not only the direct reversal of some types of damage (such as the enzymatic photoreactivation of thymine dimers), but also multiple distinct mechanisms for excising damaged base; termed nucleotide excision repair (NER), base excision repair (BER) and mismatch repair (MMR); or mechanisms for repairing double-strand breaks.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6281"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:235"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>DNA replication</name> <rdfs:comment>Protein involved in DNA replication, i.e. the duplication of DNA by making a new copy of an existing molecule. The parental double-stranded DNA molecule is replicated semi conservatively, i.e. each copy contains one of the original strands paired with a newly synthesized strand that is complementary in terms of AT and GC base pairing.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6260"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:236"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>DNA replication inhibitor</name> <rdfs:comment>Protein involved in the inhibition of DNA replication.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:8156"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:237"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>DNA synthesis</name> <rdfs:comment>Protein involved in the synthesis of DNA from deoxyribonucleic acid monomers.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6259"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:238"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>DNA-binding</name> <rdfs:comment>Protein which binds to DNA, typically to pack or modify the DNA, or to regulate gene expression. Among those proteins that recognize specific DNA sequences, there are a number of characteristic conserved motifs believed to be essential for specificity. Many DNA-binding domains are described in PROSITE.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:3677"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:241"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Down's syndrome</name> <rdfs:comment>Protein which, if defective, causes Down's syndrome, a condition due to the presence of three copies of chromosome 21 (trisomy 21), characterized by some degree of mental retardation, short stature and poor muscle tone. Common (1 in 700 live births); incidence increases with maternal age. The cause is usually non-disjunction at meiosis but occasionally a translocation of fused chromosomes 21 and 14.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:242"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Dwarfism</name> <rdfs:comment>Protein which, if defective, causes dwarfism, a skeletal growth defect resulting in the condition of being undersized.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:244"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Early protein</name> <rdfs:comment>Phage or viral protein expressed in the first phase of the lytic cycle.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:245"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>EGF-like domain</name> <rdfs:comment>Protein containing at least one EGF-like domain, a sequence of about thirty to forty amino-acid residues long found in the sequence of epidermal growth factor (EGF). It has been shown to be present, in a more or less conserved form, in a large number of proteins. The EGF-like domain contains six cysteines which form disulfide bonds within the domain (C1-C3, C2-C4, C5-C6).</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:248"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Ehlers-Danlos syndrome</name> <name>EDS</name> <rdfs:comment>Protein which, if defective, causes Ehlers-Danlos syndrome (EDS), a genetically and phenotypically heterogeneous group of connective-tissue disorders. It affects primarily the skin, ligaments, joints, and blood vessels. Typical features include skin hyperextensibility, joint hypermobility, easy bruisability, friability of tissues with bleeding and poor wound healing. Inheritance can be autosomal dominant, autosomal recessive, or X-linked recessive.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:252"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Embryo</name> <rdfs:comment>Protein which is expressed in the embryo, a stage of development in a multicelled organism between the time that the female sex cell is fertilized and the point at which the developping organism becomes free-living. Specifically, in vertebrates, the developmental stage after which the long axis appears to the moment all major anatomical structures form (in some mammals, the developing embryo is known as a fetus after it achieves the main features of the adult form). In higher plants, this is the rudimentary plant encased in a viable seed before germination. In primitive plants, the young sporophyte that develops from the union of male and female sex cells.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:254"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Endocytosis</name> <rdfs:comment>Protein involved in endocytosis, a process by which extracellular materials are taken up into a cell by invagination of the plasma membrane to form vesicles enclosing these materials.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6897"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:255"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Endonuclease</name> <rdfs:comment>Phosphodiesterase capable of cleaving at phosphodiester internal bonds within a DNA or RNA substrate.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:4519"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:256"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Endoplasmic reticulum</name> <rdfs:comment>Protein whose subcellular location is the endoplasmic reticulum, a membrane system continuous with the outer nuclear membrane. It consists of flattened, single-membrane vesicles whose inner compartments, the cisternae, interconnect to form channels throughout the cytoplasm. The rough-surface portion is studded with ribosomes.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5783"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:257"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Endorphin</name> <rdfs:comment>Morphine-like peptides produced by the brain in response to neurotransmitters. They bind to neuron receptors that mediate the action of opiates and induce analgesia and sedation.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7218"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:259"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Enterobactin biosynthesis</name> <name>Enterochelin biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of enterobactin, a compound that transports iron from the bacterial environment into the cell cytoplasm.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9239"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:261"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Envelope protein</name> <rdfs:comment>Protein of the viral envelope, a lipoprotein membrane which forms the outermost layer of the virion in certain viruses.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19031"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:263"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Epidermolysis bullosa</name> <rdfs:comment>Heterogeneous group of mechano-bullous disorders characterized by fragility of the cutaneous basement membrane zone (BMZ). It manifests with blistering and erosion of the skin and mucous membranes as a result of mechanical trauma. In addition to skin involvement, various extracutaneous manifestations can be associated with distinct subtypes. EB is classified in 3 broad categories: in the simplex forms (EBS), tissue separation is intraepidermal; in the junctional forms (JEB) blistering occurs within the lamina lucida of BMZ; in the dystrophic forms (DEB), tissue separation occurs below the lamina densa on the dermal side of the BMZ. A variant form of EBS is MD-EBS in which mild blistering of the skin is associated with late-onset muscular dystrophy; two distinct variants of JEB are: the generalized atrophic benign epidermolysis bullosa (GABEB) in which life-long blistering of the skin is associated with hair and tooth abnormalities; epidermolysis bullosa with pyloric atresia (EB-PA), in which perinatal or neonatal blistering of the skin is associated with congenital pyloric atresia.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:887"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Epilepsy</name> <rdfs:comment>Protein which, if defective, causes epilepsy, any of a group of disorders characterized by paroxysmal transient disturbances of the electrical activity of the brain that may be manifested as episodic impairment or loss of consciousness, abnormal motor phenomena, psychic or sensory disturbances, or perturbation of the autonomic nervous system. Epilepsy is classified as either symptomatic or idiopathic according to whether the cause is known or unknown. Both of these types can be classified into partial and generalized epilepsy, depending on whether the seizures are due to limited or to widespread brain lesions, respectively.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:895"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>ERV</name> <name>Endogenous retrovirus</name> <name>Fossil virus</name> <rdfs:comment>Protein encoded by proviral genes of endogenous retroviruses. Retroviral replication has two particularities. First, extracellular retroviruses have RNA genomes, but when a retrovirus infects a host cell, viral reverse transcriptase (RT) makes a DNA copy of the viral genome. And then the integration of the viral genome into the DNA of the host is mediated by the viral enzyme integrase (IN). The integrated DNA form of a retrovirus is referred to as a provirus. Proviral genes are expressed by cellular mechanisms. Retroviruses that enter the germline are referred to as endogenous retroviruses (ERVs) to distinguish them from horizontally transmitted, not passed on to host progeny, "exogenous" retroviruses. Amplification of ERV copy number via retrotransposition or reinfection has given rise to numerous ERV sequences in the vertebrate genomes. As much as 8% of the human genome, and 10% of the mouse genome, consists of sequences derived from ERV insertions.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:264"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Erythrocyte</name> <name>Red blood cell</name> <name>Red blood corpuscle</name> <rdfs:comment>Protein found in erythrocytes, the vertebrate blood cells containing the gas-transporting protein, hemoglobin, which transports oxygen from the lungs to tissues, and carbon dioxide from the tissues to the lungs.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:265"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Erythrocyte maturation</name> <name>Red blood cell maturation</name> <name>Red blood corpuscle maturation</name> <rdfs:comment>Protein involved in the maturation of erythrocytes, the predominant type of cells present in vertebrate blood and which contain the gas-transporting protein, hemoglobin.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:266"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Ethylene biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of ethylene (C2H4), an unsaturated hydrocarbon gas mainly produced in plants. It has developmental effects as a hormone, including growth inhibition, regulation of fruit development, leaf abscission and aging.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9693"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:267"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Excision nuclease</name> <rdfs:comment>Enzyme which excises abnormal or mismatched nucleotides from a DNA strand.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:4518"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6289"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:268"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Exocytosis</name> <rdfs:comment>Protein involved in exocytosis, a process by which a material is transported out of a cell using a vesicle that first engulfs the material and then is extruded through an opening in the cell membrane. The exocyst protein complex plays an important role in exocytosis by directing exocytic vesicles to their precise sites of fusion in the plasma membrane.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6887"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:270"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Exopolysaccharide synthesis</name> <rdfs:comment>Protein involved in the synthesis of exopolysaccharide (EPS), a high molecular-weight polymer composed of saccharide subunits. An example is succinoglycan (EPS I) of Rhizobium meliloti, that is important for invasion of the nodules that it elicits on its host, Medicago sativa.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:271"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:271"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Exosome</name> <rdfs:comment>Protein which is a component of the exosome, a complex of proteins that includes 3->5 exoribonucleases and that plays a major role in diverse RNA processing and degradation pathways in eukaryotes and archaea.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:178"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:272"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Extracellular matrix</name> <rdfs:comment>Protein found in the extracellular matrix. The extracellular matrix consists of any material produced by cells and secreted into the surrounding medium, but this term generally applies to the non-cellular components of animal tissues. The extracellular matrix forms a supportive meshwork around cells and is largely composed of collagen, laminin, fibronectin and glycosaminoglycans. It can influence the properties of the cells that it supports. In certain tissues, specific modifications to the extracellular matrix occur. For instance, the matrix of bone is mineralized to resist compression.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5578"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:273"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Eye lens protein</name> <rdfs:comment>Protein found in the lens, a transparent body at the front of the vertebrate eye.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5212"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:274"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>FAD</name> <name>Flavin adenine dinucleotide</name> <rdfs:comment>Protein involved in flavin adenine dinucleotide synthesis or protein which contains at least one FAD as prosthetic group/cofactor (flavoprotein) such as many oxidation-reduction enzymes. FAD is an electron carrier molecule that functions as a hydrogen acceptor. The generic term "flavin" derives from the Latin word flavius ("yellow") because of the brilliant yellow color they exhibit as solids and in neutral aqueous solutions.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:277"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Feather</name> <rdfs:comment>Protein present in any of the flat light waterproof epidermal structures which form the plumage of birds.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:278"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Fertilization</name> <rdfs:comment>Protein involved in fertilization, the union of two haploid cells, the gametes, to form a diploid cell, the zygote.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7338"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:279"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Fiber protein</name> <rdfs:comment>Protein found in bacteriophage tail fibers and in the fibers of adenoviruses, or involved in its synthesis or assembly. In bacteriophages, the distal tip specifies the host-range due to its interaction with the bacterial lipopolysaccaride receptor. In adenoviruses, fiber proteins have a number of functions including assembly of virus particles, attachment to the cell membrane during infection, and type-and group-specific antigenicity. Also found in some bacteria.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:280"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Fibrinolysis</name> <rdfs:comment>Protein involved in fibrin degradation leading to the dissolving of blood clots.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:30195"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:281"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Fimbria</name> <rdfs:comment>Protein found in fimbria or pilus, or involved in its assembly or retraction. Pili are hollow, hair-like projection from the bacterial surface. The major constituent is a protein, pilin. Bacteria can have two kinds of pili: a low number of long F (conjugation, sex) pili and/or short pili (or fimbria) found in large numbers (up to hundreds). Short pili play a crucial role in processes such as adherence to other cell and twitching/retractive motility.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9289"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:282"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Flagellum</name> <rdfs:comment>Protein present in or involved in the biogenesis or function of flagella, a long whip-like or feathery structure which propels the cell through a liquid medium. It is produced either singly or in groups by the motile cells of many bacteria and unicellular eukaryotes, and by the motile male gametes of many eukaryotic organisms. The flagella of unicellular eukaryotes and motile male gametes of many eukaryotic organisms commonly have a characteristic axial '9+2' microtubular array (axoneme) and bends are generated along the length of the flagellum by restricted sliding of the nine outer doublets. In prokaryotes, the flagellum is made of polymerized flagellin and is rotated by the basal motor.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19861"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:283"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Flagellar rotation</name> <rdfs:comment>Protein involved in the movement of the flagella.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:1539"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:284"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Flavonoid biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of flavonoids, polyphenolic compounds possessing 15 carbon atoms; two benzene rings joined by a linear three carbon chain, a C6-C3-C6 skeleton. C6 presents a benzene ring, C3 often is part of of an oxygen-containing ring. Flavonoids are coloured phenolic pigments originally considered vitamins (Vitamins P, C2) but not shown to have any nutritional role. They are responsible for the red/purple colours of many higher plants.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9813"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:285"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Flavoprotein</name> <rdfs:comment>Enzymes which contain one or more flavin nucleotides (FAD or FMN) as redox cofactors. Flavoproteins are involved, for example, in the oxidative degradation of pyruvate, fatty acids and amino acids, and in the process of electron transport.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:286"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Flight</name> <rdfs:comment>Protein which stimulates or which is involved in flight, the act of passing through the air by the use of wings.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:287"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Flowering</name> <rdfs:comment>Protein involved in the transition from vegetative to reproductive development in plants.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9908"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:288"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>FMN</name> <name>Flavin adenine mononucleotide</name> <name>Riboflavin 5'-phosphate</name> <rdfs:comment>Protein involved in flavin adenine mononucleotide synthesis or protein which contains at least one FMN as prosthetic group/cofactor (flavoproteins), such as many oxidation-reduction enzymes. FMN is an electron carrier molecule that functions as a hydrogen acceptor. The generic term "flavin" derives from the Latin word flavius ("yellow") because of the brilliant yellow color they exhibit as solids and in neutral aqueous solutions.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:289"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Folate biosynthesis</name> <name>Pteroylglutamic acid biosynthesis</name> <name>Folacin biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of folate, the ionic form of folic acid (Latin folium, 'leaf'), first found in spinach leaves. Folate is converted in a two-step reduction into its coenzyme form tetrahydrofolate, often abbreviated FH4 or THF, which acts as a carrier of one-carbon units at several oxidation levels in a variety of biosyntheses.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6760"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:290"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Folate-binding</name> <name>Pteroylglutamic acid-binding</name> <name>Folacin-binding</name> <rdfs:comment>Protein that binds folate, the ionic form of folic acid.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5542"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:291"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Formylation</name> <rdfs:comment>A protein in which either the N-terminal N-formylmethionine has not been processed by the methionyl-tRNA formyltransferase or which is posttranslationally modified by the attachment of at least one formyl group.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:292"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Fruit ripening</name> <rdfs:comment>Protein involved in fruit ripening. The fruit is the matured ovary of a plant, enclosing the seed(s). The plant hormone ethylene stimulates fruit ripening.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9835"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:293"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Fruiting body</name> <rdfs:comment>Protein involved in fruiting body formation or expressed in fruiting bodies, any specialized reproductive structure that produces spores or gametes in fungi, slime molds, algae, etc. Fruiting bodies are distinct in size, shape and coloration for each species.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:294"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Fucose metabolism</name> <rdfs:comment>Protein involved in the biochemical reactions with fucose. L-fucose (6-deoxy-L-galactose) is present in some algae and identified in the chains of glycoproteins; it is the only polysaccharides of certain bacterias.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:119"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6004"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:295"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Fungicide</name> <name>Anti-fungal</name> <rdfs:comment>Protein capable of killing or inhibiting growth of fungi.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6805"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:50832"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:296"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Fusion protein</name> <rdfs:comment>Protein involved either in fungal nuclear or cell fusion, or in fusion of viral and cellular membranes.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:298"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Galactitol metabolism</name> <name>Dulcitol metabolism</name> <rdfs:comment>Protein involved in the biochemical reactions with galactitol. This sugar alcohol is derived from galactose. It can be found in certain bacteria, yeasts, fungi and plants. In humans, the congenital galactosemic cataracts are due to an accumulation of galactitol within the lens.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19402"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:299"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Galactose metabolism</name> <rdfs:comment>Protein involved in the biochemical reactions with the monosaccharide galactose. This optical isomer (epimer) of glucose is a constituent of various oligosaccharides (e.g. lactose, raffinose), polysaccharides (e.g. galactans, agar, gum arabic) and also of sphingolipids (galactocerebrosides).</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:119"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6012"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:301"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Gamma-carboxyglutamic acid</name> <name>1-carboxyglutamic acid</name> <rdfs:comment>Protein which possesses at least one gamma-carboxyglutamic acid, a posttranslationally modified glutamate residue found in blood coagulation proteins and in the proteins of calcified tissues. Gamma-carboxyglutamyl residues are good chelators of calcium ions.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:302"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Gap protein</name> <rdfs:comment>A group of insect proteins which are crucial for the development of proper embryonic segmentation. These are the first proteins that define the coarsest subdivisions. Generally, gap gene mutations are lethal and eliminate a large block of contiguous segments from the embryo.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:217"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:303"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Gap junction</name> <rdfs:comment>Protein component of gap junctions which are specialized regions of the plasma membrane formed by a cluster of channels allowing small molecules to diffuse from the cytosol of one cell to that of an adjacent cell. A current model of the gap junction consists of a cluster of gap-junction channels. Both membranes contain connexon hemichannels, composed of a hexamer of an integral membrane protein which is often referred to as connexin. The junction of two adjacent connexons forms a gap-junction channel.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5921"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:304"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Gas vesicle</name> <rdfs:comment>Protein component of, or involved in the formation of, gas vesicles, which are a rigid, hollow structure found in five phyla of the Bacteria and two groups of the Archaea, but mostly restricted to planktonic microorganisms, in which they provide buoyancy. By regulating their relative gas vesicle content, aquatic microbes are able to perform vertical migrations. The gas vesicle is impermeable to liquid water, but is highly permeable to gases and is normally filled with air. Two proteins have been shown to be present in the gas vesicle: GVPa, which makes the ribs that form the structure, and GVPc, which binds to the outside of the ribs and stiffens the structure against collapse.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:305"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Gaseous exchange</name> <rdfs:comment>Protein involved in the exchange of gases.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7585"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:306"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Gastrulation</name> <rdfs:comment>Protein involved in gastrulation, a stage in early embryogenesis in which the gut cavity is formed and the three primary layers of the animal body (ecto-, meso- and endoderm) are placed in position for further development.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7369"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:307"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Gaucher disease</name> <rdfs:comment>Protein which, if defective, causes Gaucher disease, the most prevalent sphingolipid storage disorder caused by a recessively inherited deficiency of the enzyme glucocerebrosidase. Most common in Ashkenazi Jews, it is associated with hepatosplenomegaly (enlargement of liver and spleen) and, in severe early onset forms of the disease, with neurological dysfunction.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7040"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:308"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Genetically modified food</name> <rdfs:comment>Any protein used in a biotechnological process that results in the modification of a naturally occurring food (crop or livestock). Examples include proteins introduced to enable herbicide or insect resistance or proteins that act in fruit ripening.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:309"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Germination</name> <rdfs:comment>Protein involved in germination, the growth of a plant embryo, and the emergence of a young shoot and a root. Food reserves for germination come from endosperm tissue within the seed and/or from the seed leaves (cotyledons). Germination ends when the plant no longer depends on the food stored in the seed (beginning of photosynthesis in green plants). The term germination is also used for the emergence of thallus, hypha etc. from a spore.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9844"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:310"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Glucagon family</name> <rdfs:comment>Protein which belongs to the glucagon family. Glucagon is a hormone synthesised by the alpha cells of the pancreas when blood glucose level is low and which stimulates the breakdown of glycogen to glucose in the liver. This family also includes homologous proteins that have a different biological activity.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:311"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Gluconate utilization</name> <rdfs:comment>Protein involved in the biochemical pathway(s) in which gluconate is the carbon source.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19521"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:312"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Gluconeogenesis</name> <rdfs:comment>Protein involved in the biosynthesis of "new" glucose from such noncarbohydrate precursors as pyruvate, lactate, certain amino acids and intermediates of the tricarboxylic acid cycle.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6094"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:313"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Glucose metabolism</name> <rdfs:comment>Protein involved in the biochemical reactions with the 6-carbon aldose sugar glucose.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:119"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6006"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:314"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Glutamate biosynthesis</name> <name>Glutamic acid biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of the acidic amino acid glutamate. Glutamate is a component of proteins and can also act as a neurotransmitter in the central nervous system.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6537"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:315"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Glutamine amidotransferase</name> <rdfs:comment>Enzyme that catalyzes the removal of the ammonia group from glutamine and transfers it to a substrate to form a new carbon-nitrogen group. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides or as domains in larger multifunctional proteins. There exist two classes of glutamine amidotransferases domains: I and II.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6541"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:316"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Glutaricaciduria</name> <name>Glutaric aciduria</name> <name>GA</name> <rdfs:comment>Protein which, if defective, causes glutaricaciduria (GA), a metabolic disorder characterized by the excretion of glutaric acid in the urine. Type I GA is caused by the deficiency of glutaryl-CoA dehydrogenase, a mitochondrial enzyme involved in the metabolism of lysine, hydroxylysine and tryptophan. Type II GA differs from type I in that multiple acyl-CoA dehydrogenase deficiencies result in a large excretion not only of glutaric acid but also of lactic, ethylmalonic, butyric, isobutyric, 2-methyl-butyric, and isovaleric acids. GA II can result from a deficiency of any one of 3 mitochondrial molecules: the alpha and beta subunits of electron transfer flavoprotein and electron transfer flavoprotein-ubiquinone oxidoreductase.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6118"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:317"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Glutathione biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of the tripeptide glutathione (Gamma-Glu-Cys-Gly). Glutathione sulphydryl group is kept largely in the reduced state; this allows it to act as a sulphydryl buffer, reducing any disulphide bonds formed within cytoplasmic proteins to cysteines. Glutathione is also important as a cofactor for the enzyme glutathione peroxidase, in the uptake of amino acids and participates in leucotriene synthesis. Glutathione contains an unusual peptide linkage between the carboxyl group of the glutamate side chain and the amine group of cysteine.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6750"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:318"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Glutathionylation</name> <rdfs:comment>Protein which is posttranslationally modified by the attachment of a glutathione molecule by a disulfide bond.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:319"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Glycerol metabolism</name> <rdfs:comment>Protein involved in the biochemical reactions with the 3-carbon sugar alcohol glycerol. Glycerol is primarily of interest as the central structural component of the major classes of biological lipids, triglycerides and phosphatidyl phospholipids. It is also an important intermediate in carbohydrate and lipid metabolism.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6071"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:320"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Glycogen biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of glycogen, a branched polymer of D-glucose (mostly -(1-4) linked, but with some -(1-6) linked residues at branch points). Glycogen is the major short term storage polymer of animal cells and is particularly abundant in liver and to a lesser extent in muscles.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5978"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:321"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Glycogen metabolism</name> <rdfs:comment>Protein involved in the biochemical reactions with glycogen, a branched polymer of D-glucose (mostly -(1-4) linked, but with some -(1-6) linked residues at branch points). Glycogen is the major short term storage polymer of animal cells and is particularly abundant in liver and to a lesser extent in muscles.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:119"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5977"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:322"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Glycogen storage disease</name> <rdfs:comment>Protein which, if defective, causes glycogen storage disease, a group of inherited metabolic disorders involving the enzymes responsible for the synthesis and degradation of glycogen. At least thirteen types of this disease have been described.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5977"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:323"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Glycolate pathway</name> <name>C2 cycle</name> <name>Photorespiration pathway</name> <name>Photosynthetic carbon oxydation cycle</name> <rdfs:comment>Protein involved in the glycolate pathway, synthesis of the amino acids serine and glycine from glycolate via a glyoxylate intermediate.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9854"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:324"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Glycolysis</name> <rdfs:comment>Protein involved in the anaerobic enzymatic conversion of glucose to lactate or pyruvate, resulting in energy stored in the form of adenosine triphosphate (ATP), as occurs in skeletal muscle and in embryonic tissue.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6096"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:325"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Glycoprotein</name> <rdfs:comment>Protein containing one or more covalently linked carbohydrate residues.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:327"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Glycosome</name> <rdfs:comment>Protein present in the glycosome, a microbody-like organelle found in all members of the protist order Kinetoplastida examined. Nine enzymes involved in glucose and glycerol metabolism are associated with these organelles. These enzymes are involved in pathways which, in other organisms, are usually located in the cytosol.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:20015"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:329"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Glyoxylate bypass</name> <name>Glyoxylate cycle</name> <rdfs:comment>Protein involved in the glyoxylate bypass, an alternate route in bacteria, plants, and fungi which bypasses the CO2-evolving steps of the tricarboxylic acid cycle, thus permiting the utilization of fatty acids or acetate, in the form of acetyl-CoA, as sole carbon source, particularly for the net biosynthesis of carbohydrate from fatty acids. The glyoxylate bypass is especially prominent in plant seeds.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6097"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:330"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Glyoxysome</name> <rdfs:comment>Protein present in the glyoxysome, a membrane-surrounded plant cell organelle, especially found in germinating seeds, and involved in the breakdown and conversion of fatty acids to acetyl-CoA for the glyoxylate bypass. Since it is also rich in catalase, the glyoxysome may be related to the microbodies or peroxisomes or derived from them.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9514"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:331"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>GM2-gangliosidosis</name> <rdfs:comment>Protein which, if defective, causes GM2-gangliosidosis, a group of inherited diseases characterized by the accumulation of GM2 ganglioside (N-acetylgalactosaminyl-galactosyl-(n-acetylneuraminyl)-glucosyl-ceramide) in central nervous system lysosomes and variably in other tissues. Subtypes include Tay-Sachs disease and Sandhoff disease.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6687"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:333"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Golgi stack</name> <name>Golgi apparatus</name> <name>Golgi complex</name> <rdfs:comment>Protein found in the Golgi apparatus, an organelle present in eukaryotic cells that appears as a stack of 6-8 plate-like membranous compartments and associated vesicles and vacuoles, often located near the centrosome. It has four functionally distinct compartments: cis, medial and trans Golgi stacks, and the trans Golgi network (TGN). The first three are involved in posttranslational modifications of proteins (e.g., N- or O-glycosylation, sulfation, processing of acid hydrolases), while the TGN is involved in sorting the proteins to their final destination (e.g., to lysosomes, to secretory vesicles, or to plasma membrane).</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5794"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:334"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Gonadal differentiation</name> <rdfs:comment>Protein involved in gonadal differentiation, the progressive restriction of the developmental potential and increasing specialization of function which takes place during the embryonic development and leads to the formation of gamete-producing glands, such as ovary or testis.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7506"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:335"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Gout</name> <rdfs:comment>Protein which, if defective, causes gout, a recurrent acute arthritis of peripheral joints caused by the precipitation of monosodium urate crystals. The arthritis occurs secondary to an inherited abnormality of purine metabolism.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:337"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>GPI-anchor biosynthesis</name> <name>Glycosylphosphatidylinositol anchor biosynthesis</name> <rdfs:comment>Protein involved in the synthesis or the attachment to a protein of a GPI-anchor (glycosylphosphatidylinositol anchor), a complex oligoglycan linked to a phosphotidylinositol molecule which attaches the C-terminus of some extracellular membrane proteins to the lipid bilayer of a membrane. The core glycolipid is composed of a tetraglycan: three mannose units and one glucosamine linked to a phosphatidylinositol. The terminal mannose is linked to the protein via an ethanolamine attached to the C-terminal of the mature protein. The core structure is conserved from protozoa to humans. There are, however, marked differences in the glycosyl side chains attached to the core glycolipid.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:338"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Growth arrest</name> <name>Cellular quiescence</name> <rdfs:comment>Protein involved in growth arrest, a phenomenon occurring when a cell does not proceed through the cell cycle.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:131"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7050"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:339"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Growth factor</name> <rdfs:comment>Protein which, by binding to a cell-surface receptor, triggers an intracellular signal-transduction pathway leading to differentiation, proliferation, or other cellular response.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:8083"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:340"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Growth factor binding</name> <rdfs:comment>Protein other than a receptor that binds to a cell's growth factor.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19838"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:341"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Growth regulation</name> <rdfs:comment>Protein involved in growth regulation, which usually implies the control of the rate of division rather than that of the size of an individual cell.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:1558"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:342"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>GTP-binding</name> <rdfs:comment>Protein which binds guanosine 5'-triphosphate (GTP), a ribonucleotide guanosine (a purine base guanine linked to the sugar D-ribofuranose) that carries three phosphate groups esterified to the sugar moiety.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5525"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:343"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>GTPase activation</name> <rdfs:comment>GTPase-activating protein (GAP) by itself does not hydrolyze GTP but, by binding to a GTPase, accelerates its intrinsic GTPase activity.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5096"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:344"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Guanine-nucleotide releasing factor</name> <rdfs:comment>Protein which catalyzes the release of GDP (guanosine 5'-diphosphate).</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:345"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>HDL</name> <rdfs:comment>Protein or apolipoprotein associated with High-Density Lipoproteins (HDL), a class of proteins involved in lipid (cholesterol, phospholipids and triacylglycerol) metabolism in the body fluids. HDL are formed in the liver and are involved in reverse cholesterol transport, the transport of cholesterol from peripherical tissues to the liver. Apolipoproteins are proteins which are specifically associated with lipoproteins, which is not the case for all the proteins associated with HDL or with the other lipoprotein classes.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5319"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:346"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Heat shock</name> <rdfs:comment>Protein involved in the response to heat shock. E.g., the induced heat shock proteins, switched on by an abrupt increase of the temperature, which stabilize and repair partially denatured cell proteins.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6457"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6986"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:348"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Hemagglutinin</name> <rdfs:comment>Protein which causes agglutination of erythrocytes or other cell types: In viruses, a protein which is responsible for attaching the virus to cell receptors and for initiating infection.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:349"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Heme</name> <name>Haeme</name> <rdfs:comment>Protein containing at least one heme, an iron atom coordinated to a protoporphyrin IX. In myoglobin and hemoglobin, one of the coordination positions of iron is occupied by oxygen or other ligands, such as carbon monoxide. Hemes are also found in cytochromes of the electron-transport chain where they bind electrons, in reducing peroxides (catalases and peroxidases), and act as terminal components in multienzyme systems involved in hydroxylation. Cytochrome c is the only common heme protein in which the heme is covalently bound.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:350"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Heme biosynthesis</name> <name>Haeme biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of heme, an iron atom coordinated to a protoporphyrin IX.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6783"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:351"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Hemoglobin-binding</name> <name>Haemoglobin-binding</name> <rdfs:comment>Protein which bind hemoglobin, a gas-carrying protein found in red blood cells.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:30492"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:352"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Hemolymph</name> <name>Haemolymph</name> <rdfs:comment>Protein characteric of the hemolymph, the fluid which flows through the hemocoel of invertebrates which have open circulatory systems, like mollusks, arthropods, and tunicates. The fluid is like a combination of blood and lymph in vertebrates.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:353"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Hemolymph clotting</name> <name>Hemolymph coagulation</name> <name>Haemolymph clotting</name> <rdfs:comment>Protein involved in the coagulation of hemolymph, the circulatory fluid of invertebrate animals which is functionally comparable to the blood and lymph of vertebrates.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7596"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:354"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Hemolysis</name> <name>Haemolysis</name> <rdfs:comment>Protein involved in hemolysis, the disruption of the integrity of the red cell membrane, thus causing the release of hemoglobin.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:204"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19836"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:355"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Hemophilia</name> <name>Haemophilia</name> <rdfs:comment>Protein which, if defective, causes hemophilia, a genetic disease characterized by uncontrollable bleeding due to a sex-linked recessive deficiency of blood-clotting factor (usually of Factor VIII).</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:356"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Hemostasis</name> <rdfs:comment>Protein involved in the arrest of bleeding through blood clotting and contraction of blood vessels.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7599"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:358"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Heparin-binding</name> <rdfs:comment>Protein which binds heparin, a highly sulfated glycosaminoglycan which consists of repeating units of disaccharides composed of D-glucosamine, D-glucuronic acid or L-iduronic acid. This anticoagulant is found in the granules of mast cells.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:8201"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:359"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Herbicide resistance</name> <rdfs:comment>Protein that confers, on plants, bacteria or other microorganisms, the ability to withstand herbicide action. Herbicides are chemicals that selectively kill plants. Herbicide resistance occurs usually as a result of mutation or amplification of a gene, e.g. 3-phosphoshikimate 1-carboxyvinyltransferase.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9635"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:360"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Hereditary hemolytic anemia</name> <name>Hereditary haemolytic anemia</name> <rdfs:comment>Protein which, if defective, causes hereditary hemolytic anemia, a hereditary disease characterized by the premature destruction of red blood cells.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:361"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Hereditary multiple exostoses</name> <rdfs:comment>Protein which, if defective, causes hereditary multiple exostoses (EXT). It is an autosomal dominant disease characterized by the formation of cartilage-capped benign tumors (exostoses), developing from the juxtaepiphyseal regions of the long bones and often accompanied by skeletal deformities and short stature.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:362"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Hereditary nonpolyposis colorectal cancer</name> <name>HNPCC</name> <name>Lynch's syndrome</name> <rdfs:comment>Protein which, if defective, causes hereditary non-polyposis colorectal cancer (HNPCC), also known as Lynch's syndrome. It is an autosomal dominant syndrome wich confers an increased risk for colorectal and endometrial cancers as well as others tumors. Clinically, HNPCC is often divided into two subgroups: type I, characterized by a hereditary predisposition to colorectal cancer, a young age of onset, and carcinoma observed in the proximal colon; type II, characterized by an increased risk for cancers in certain tissues such as the uterus, ovary, breast, stomach, small intestine, skin, and larynx in addition to the colon.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:890"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Hereditary spastic paraplegia</name> <name>HSP</name> <rdfs:comment>Protein which, if defective, causes hereditary spastic paraplegias (HSPs). HSPs are a diverse class of hereditary degenerative spinal cord disorders characterized by a slow, gradual, progressive weakness and spasticity (stiffness) of the legs. Initial symptoms may include difficulty with balance, weakness and stiffness in the legs, muscle spasms, and dragging the toes when walking. In some forms of the disorder, bladder symptoms (such as incontinence) may appear, or the weakness and stiffness may spread to other parts of the body. Rate of progression and the severity of symptoms are quite variable.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:363"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Hermansky-Pudlak syndrome</name> <name>HPS</name> <rdfs:comment>Protein which, if defective, causes Hermansky-Pudlak syndrome (HPS), a rare autosomal recessive disorder characterized by oculocutaneous albinism and storage pool deficiency due to an absence of platelet dense bodies. Lysosomal ceroid lipofuscinosis, pulmonary fibrosis and granulomatous colitis are occasional manifestations of the disease.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:364"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Heterocyst</name> <rdfs:comment>Protein which is implicated in heterocyst formation. A heterocyst is a differentiated cyanobacterial cell that carries out nitrogen fixation. The heterocysts function as the sites for nitrogen fixation under aerobic conditions. They are formed in response to a lack of fixed nitrogen (NH4 or NO3). The morphological differentiation is accompanied by biochemical alterations. The mature heterocysts contain no functional photosystem II and cannot produce oxygen. Instead, they contain only photosystem I, which enables them to carry out cyclic photophosphorylation and ATP regeneration. These changes provide the appropriate conditions for the functioning of the oxygen-sensitive nitrogenase.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:365"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Hexon protein</name> <rdfs:comment>Major coat protein of adenoviruses. Adenovirus capsids have three principal protein components: the hexon, the penton, and the fiber. Hexon consists of three subunits together forming two major components of different morphological symmetry. A triangular top with three towers of density is superimposed on a more bulky pseudo-hexagonal base. The symmetry of the top is in accord with the trimeric nature of hexon, but that of the base derives from the molecular function, which is to provide a densely packed impenetrable protective outer layer for the virion.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:167"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5198"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19012"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:366"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Hexon-associated protein</name> <rdfs:comment>Protein associated with hexon proteins in adenoviruses.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:367"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Hirschsprung disease</name> <name>HSCR</name> <rdfs:comment>Hirschsprung's disease (HSCR); a genetic disorder of neural crest development characterized by the absence of intramural ganglion cells in the hindgut; often resulting in intestinal obstruction.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:368"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Histidine biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of the weakly basic amino acid histidine.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:105"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:369"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Histidine metabolism</name> <rdfs:comment>Protein involved in the biochemical reactions with the weakly basic amino acid histidine.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6547"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:370"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Holoprosencephaly</name> <rdfs:comment>A clinically variable and genetically heterogeneous malformation in which the developing forebrain fails to correctly separate into right and left hemispheres.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:371"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Homeobox</name> <name>Homeodomain</name> <rdfs:comment>Protein which contains at least one homeobox, a conserved sequence originally detected, on the nucleotide level, in many of the genes which give rise to homeotic and segmentation mutants in Drosophila. The homeobox, also termed homeodomain, consists of about 60 amino acids and is involved in DNA-binding.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:3677"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:372"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Hormone</name> <rdfs:comment>Protein which functions as a hormone, a biochemical substance secreted by specialized cells that affects the metabolism or behavior of other cells which possess functional receptors for the hormone. Hormones may be hydrophilic, like insulin, in which case the receptors are on the cell surface, or lipophilic, like the steroids, where the receptor can be intracellular.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5179"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:374"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Hybridoma</name> <rdfs:comment>Protein sequenced from a hybridoma, an artificially produced hybrid cell line created by fusion of a lymphocyte and a myeloma cell. These cells can multiply indefinitely in culture and produce monoclonal antibodies.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:376"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Hydrogen peroxide</name> <rdfs:comment>Protein involved in hydrogen peroxide (H(2)O(2)) decomposition, e.g., catalase. H(2)O(2) is generated by the body as a byproduct of aerobic cellular respiration.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:4601"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:377"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Hydrogenosome</name> <rdfs:comment>Protein characteristic of the hydrogenosome, a redox organelle of anaerobic unicellular eukaryotes which contains hydrogenase and produces hydrogen by glycolysis.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:42566"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:378"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Hydrolase</name> <rdfs:comment>Enzyme which catalyzes hydrolysis reaction, i.e. the addition of the hydrogen and hydroxyl ions of water to a molecule with its consequent splitting into two or more simpler molecules.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:16787"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:379"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Hydroxylation</name> <rdfs:comment>Protein which is posttranslationally modified by the attachment of at least one hydroxyl (-OH) group.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:380"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Hyperlipidemia</name> <rdfs:comment>Protein which, if defective, causes hyperlipidemia, a condition characterized by the elevation of lipids in the bloodstream. There are different types of hyperlipidemias: type I (lipoprotein lipase deficiency), IIa (hypercholesterolemia; LDL receptor deficiency), IIb (combined hyperlipidemia), III (dysbetalipoproteinemia), IV (hypertriglyceridemia) and V (mixed hyperlipidemia).</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:381"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Hypersensitive response</name> <rdfs:comment>Protein mediating a hypersensitive response, e.g., harpin.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9626"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:382"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Hypotensive agent</name> <name>Antihypertensive agents</name> <rdfs:comment>Protein which can cause hypotension, i.e. low blood pressure or a sudden drop in blood pressure.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:8217"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:383"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Hypothalamus</name> <rdfs:comment>Protein released by the hypothalamus, a region of the brain below the thalamus, which is derived from the forebrain and involved in the control of the pituitary gland, body temperature and motivated behaviour such as eating and drinking. The hypothalamus also regulates other glands such as the ovaries, parathyroids and thyroid.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:384"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Hypothetical protein</name> <rdfs:comment>Predicted protein for which there is no experimental evidence that it is expressed in vivo.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:385"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Hypusine</name> <rdfs:comment>Protein which is posttranslationally modified on at least one lysine residue to form hypusine (N-epsilon-(4-aminobutyl)lysine). This spermidine-dependent reaction is catalyzed by deoxyhypusine synthase and deoxyhypusine hydroxylase. eIF-5A is the only protein in eukaryotes and archaebacteria known to contain hypusine.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:386"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Hypusine biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of hypusine, an amino acid formed by the two posttranslational steps in the modification of a lysine: (i) deoxyhypusine synthase catalyzes the transfer of a 4-aminobutyl moiety from spermidine to a specific lysine residue to form a deoxyhypusine residue, N-epsilon-(4-aminobutyl)lysine, and (ii) deoxyhypusine hydroxylase catalyzes the hydroxylation of the deoxyhypusine residue to form hypusine (N-epsilon-(4-amino-2-hydroxybutyl)lysine).</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:8612"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:387"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Ice nucleation</name> <rdfs:comment>Protein which promote the nucleation of ice. The proteins catalyzes the formation of ice crystals in extracellular fluid at relatively high temperatures (up to -2 degrees Celsius) to protect the organism from damage by intracellular ice formation.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:50825"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9405"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:388"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>IgA-binding protein</name> <rdfs:comment>Protein binding to immunoglobulin A, the major class of antibodies found in external secretions such as saliva, tears, gastric fluid, milk and mucosal secretions.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19862"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:389"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>IgE-binding protein</name> <rdfs:comment>Protein binding to immunoglobulin E, the antibody class involved in local inflammatory reactions, reactions to parasites, and also in allergic responses.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19863"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:390"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>IgG-binding protein</name> <rdfs:comment>Protein binding to immunoglobulin G, the main type of immunoglobulin produced towards the end of a primary immune response and in a secondary response.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19864"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:391"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Immune response</name> <rdfs:comment>Protein involved in the reaction of the immune system to an antigen, which includes the production of antibodies (humoral response), the cellular response (destruction of cells displaying foreign antigens on their cell surface by cytotoxic T-cells, or the stimulation of B-lymphocytes to produce antibodies by T-helper cells), the complement activation and in some cases the development of immunological tolerance.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6955"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:393"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Immunoglobulin domain</name> <name>Immunoglobulin fold</name> <rdfs:comment>Protein which contains at least one immunoglobulin domain, a characteristic beta-sheet fold of the immunoglobulin domain which has been found in many other proteins of diverse biological function.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:394"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Immunoglobulin V region</name> <rdfs:comment>Protein encoded by a variable region gene (V gene / V segment). The variable region is the region of the immunoglobulin (Ig) which varies greatly in amino acid sequence among different immunoglobulins of the same class. Each immunoglobulin molecules is a tetramer of two identical light chains and two identical heavy chains linked by disulfide bonds. The light chain has one variable region (VL) and one constant region (CL) domain, whereas the heavy chain has one variable region (VH) and three or four constant region domains (CH1 to CH4). The V regions confer the antigenic specificity, and are associated with the antigen-binding site. Variable and constant regions are encoded by separated genes, called V genes and C genes respectively, which join during cell differentiation.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:393"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:3823"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:395"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Inflammatory response</name> <rdfs:comment>Protein involved in the localized protective response to tissue damage, microbial infection, or the presence of foreign matter. It is characterized by swelling, redness, heat and pain and involves a complex series of events including vascular changes and accumulation of blood cells, such as neutrophil leucocytes and mononuclear phagocytes, at the site of injury.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6954"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:398"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Inositol biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of inositol, a cyclic hexahydric alcohol. It occurs in various forms, of which myo-inositol, a constituent of phospholipids, is the most important.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6021"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:399"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Insect immunity</name> <rdfs:comment>Protein involved in insect immunity, i.e. in the capacity an insect has in responding to invasive or pathogenic effects of microorganisms. An important part of the innate immune response of insects is the synthesis of antibacterial peptides and proteins, which effectively lyse bacteria or are bacteriostatic.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6952"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:400"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Insulin family</name> <rdfs:comment>Protein that belongs to the insulin family. This family groups a number of hormones and growth factors.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:401"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Integrin</name> <rdfs:comment>Protein of the integrin family of cell surface heterodimeric receptors that mediate cell-to-cell as well as cell-to-matrix adhesion. Each subunit has a large N-terminal extracellular domain followed by a transmembrane domain and a short C-terminal cytoplasmic region. Some subclasses of integrins share a common beta chain while having different alpha chains.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7229"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:402"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Interferon induction</name> <name>IFN induction</name> <rdfs:comment>Protein induced by interferon(s). Interferons are a class of cytokines which mediate, by binding to specific cell-surface receptors, a broad range of activities such as resistance to viral infection, modulation of the immune response and regulation of proliferation of normal and malignant cells.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6955"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:403"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Intermediate filament</name> <rdfs:comment>Intermediate filaments (IF) are proteins which are primordial components of the cytoskeleton and the nuclear envelope. They generally form filamentous structures 8 to 14 nm wide and intermediate in size between microtubules and microfilaments. This family of protein includes cytokeratins, vimentin, desmin, glial fibrillary acidic protein, neurofilament proteins and nestin. All IF proteins are structurally similar in that they consist of: a central rod domain which is arranged in coiled-coiled alpha-helices, with at least two short characteristic interruptions; an N-terminal non-helical domain (head) of variable length; and an C-terminal domain (tail) which is also non-helical and shows extreme length variation between different IF proteins.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5882"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:404"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Intron homing</name> <name>Intron transposition</name> <rdfs:comment>Endonucleases involved in intron homing, a genetic event leading to the transfer of an intron DNA sequence. This type of intron mobility depends on site-specific restriction endonucleases encoded by the mobile introns.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6314"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:405"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Iodination</name> <rdfs:comment>Protein which is posttranslationally modified by the replacement of at least one hydrogen by iodine.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:872"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Ionic channel inhibitor</name> <rdfs:comment>Protein which interferes with the function of ionic channels, which are hydrophilic channels across the lipid bilayer through which specific inorganic ions can diffuse down their electrochemical gradients.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:8200"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:408"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Iron</name> <rdfs:comment>Protein which binds at least one iron atom, or protein whose function is iron-dependent. Iron is a metal, chemical symbol Fe.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:409"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Iron storage</name> <rdfs:comment>Protein involved in the storage of iron.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:408"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6879"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:411"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Iron-sulfur</name> <rdfs:comment>Protein which binds at least one iron-sulfur cluster, e.g. 2Fe-2S, 3Fe-4S, 4Fe-4S.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:408"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:412"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Isoleucine biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of the hydrophobic amino acid isoleucine.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:100"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9097"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:413"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Isomerase</name> <rdfs:comment>Enzyme that catalyzes the 1,1-, 1,2- or 1,3-hydrogen shift. The 1,1-hydrogen shift is an inversion at an asymmetric carbon center (racemases, epimerases). The 1,2-hydrogen shift involved a hydrogen transfer between two adjacent carbon atoms, one undergoing oxidation, the other reduction (aldose-ketose isomerases). The 1,3-hydrogen shifts are allylic or azaallylic (when nitrogen is one of the three atoms) isomerizations.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:16853"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:414"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Isoprene biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of isoprene, an important organic unit of 5 carbons in plants. It is used to build up isoprenoids, including carotenoids, terpenes and natural rubber.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:8299"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:415"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Karyogamy</name> <rdfs:comment>Protein involved in the fusion of the nuclei of two gametes after cytoplasmic fusion.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:880"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Kelch repeat</name> <rdfs:comment>Protein containing at least one Kelch repeat.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:416"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Keratin</name> <rdfs:comment>Fibrous proteins rich in cysteine and the chief constituent of horn, nails, hair, epidermis and feathers. Two major conformational groups have been characterized, alpha-keratin, whose peptide backbone forms an alpha-helix, and beta-keratin, whose backbone forms a zigzag or pleated sheet structure.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5882"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:417"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Keratinization</name> <rdfs:comment>Protein involved in keratinization, the process in which the cytoplasm of the outermost cells of the vertebrate epidermis is replaced by keratin. Keratinization occurs in the stratum corneum, feathers, hair, claws, nails, hooves, and horns.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:420"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Kringle</name> <rdfs:comment>Protein containing at least one kringle domain, a triple-looped, disulfide cross-linked domain of approximately 80 amino acids in length and involved in protein-protein interactions.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:421"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Lactation</name> <rdfs:comment>Protein involved in lactation, the secretion of milk by mammary glands.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7595"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:422"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Lactose biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of lactose, a disaccharide of glucose and galactose present in milk.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5989"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:423"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Lactose metabolism</name> <rdfs:comment>Protein involved in the biochemical reactions with lactose, a disaccharide of glucose and galactose, found in milk.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5988"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:424"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Laminin EGF-like domain</name> <rdfs:comment>Protein containing at least one laminin EGF-like domain. Laminins are the major noncollagenous components of basement membranes. Their subunits contain consecutive repeats of about 60 amino acids, which include 8 conserved cysteines that form disulfide bonds (C1-C3, C2-C4, C5-C6, C7-C8). The tertiary structure of this domain is remotely similar, in its N-terminal, to that of the EGF-like module.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:425"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Lantibiotic</name> <rdfs:comment>Lanthionine-containing peptide antibiotics are peptides produced by Gram-positive bacteria which cause cell death of other Gram-positive bacteria.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:78"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5102"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19835"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:426"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Late protein</name> <rdfs:comment>Phage or viral protein expressed in a later phase of the lytic cycle, during viral nucleic acid replication and particle assembly.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:427"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>LDL</name> <rdfs:comment>Protein constituent of the low-density lipoproteins or protein which binds LDLs. LDLs are plasma lipoproteins rich in cholesterol esters, synthesized from the very low-density lipoprotein (VLDL), and which transport cholesterol to peripheral tissue and regulate de novo cholesterol synthesis.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5319"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:428"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Leader peptide</name> <rdfs:comment>Short peptide sequences translated from bacterial leader RNA sequences which are involved in translation attenuation, a mechanism that modulates mRNA translation.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:901"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Leber congenital amaurosis</name> <rdfs:comment>Protein which, if defective, causes Leber congenital amaurosis, a clinically and genetically heterogeneous type of blindness transmitted as an autosomal recessive trait and occurring at or shortly after birth. It is associated with an atypical form of diffuse pigmentation and commonly with optic atrophy and attenuation of the retinal vessels.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:429"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Leber hereditary optic neuropathy</name> <rdfs:comment>Protein which, if defective, causes Leber hereditary optic neuropathy, a maternally inherited disease resulting from a deficit of ATP and leading to acute bilateral blindness, predominantly in young men. It is characterized by degeneration of the optic nerve and papillomacular bundle.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:430"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Lectin</name> <rdfs:comment>Protein which specifically bind carbohydrates. Lectins are obtained particularly from seeds of leguminous plants but also from other plant and animal sources. They contain binding sites for specific mono-and oligosaccharides. They agglutinate cells by binding to specific sugar residues in membrane glycoproteins.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5529"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:431"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Leigh syndrome</name> <rdfs:comment>Protein which, if defective, causes Leigh syndrome, a neurodegenerative disorder characterized by the subacute onset of psychomotor retardation, hypotonia, ataxia, weakness, vision loss, eye movement abnormalities, seizures, dysphagia, and lactic acidosis. Pathological features include spongy degeneration of the neuropile of the basal ganglia, thalamus, brain stem, and spinal cord. The syndrome is caused by a variety of defects of enzymes involved in energy metabolism, including cytochrome c oxidase (COX), the mitochondrial encoded ATP6 subunit of ATP synthase, and the X-linked E1-alpha subunit of pyruvate dehydrogenase.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:432"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Leucine biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of the hydrophobic amino acid leucine.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:100"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9098"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:433"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Leucine-rich repeat</name> <name>LRR</name> <rdfs:comment>Protein containing at least one leucine-rich repeat (LRR).</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:434"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Leukotriene biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of leukotrienes, eicosanoid hormones first isolated from leukocytes. They are thought to mediate the allergic response that causes lung constriction and muscle contraction in asthma.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19370"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:435"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Li-Fraumeni syndrome</name> <name>LFS</name> <name>Sarcoma family syndrome of Li and Fraumeni</name> <name>SBLA syndrome</name> <rdfs:comment>Protein which, if defective, causes Li-Fraumeni syndrome (LFS), an autosomal dominant familial cancer predisposition syndrome associated with soft-tissue sarcoma, breast cancer, leukemia, osteosarcoma, melanoma, and cancer of the colon, pancreas, adrenal cortex and brain. Individuals with LFS are at increased risk for developing multiple primary cancers.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:436"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Ligase</name> <rdfs:comment>Enzyme that catalyzes the joining of two molecules coupled with the breakdown of a pyrophosphate bond in ATP or a similar triphosphate. Sometimes the terms "synthase", "synthetase" or "carboxylase" are also used for this class of enzymes.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:16874"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:437"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Light-harvesting polypeptide</name> <name>Light-harvesting complex</name> <rdfs:comment>Proteins which form part of the antenna complex, a light-harvesting system found in photosynthetic bacteria which absorb light radiation and transfer the excitation energy to the reaction centres.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:30076"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:438"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Lignin biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of lignin, a polymer of phenylpropanoid subunits found in the walls of plant cells such as xylem and sclerenchyma fibres. Lignin imparts strength to the wall and protects against degradation by microorganisms.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9809"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:439"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Lignin degradation</name> <rdfs:comment>Protein involved in the breakdown of lignin, a polymer of phenylpropanoid subunits found in the walls of plant cells such as xylem and sclerenchyma fibres. It imparts strength to the wall and protects against degradation by microorganisms.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9808"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:440"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>LIM domain</name> <name>LIM motif</name> <rdfs:comment>Protein which contains at least one LIM domain, a conserved cysteine-rich domain of approximately 60 amino acids with seven conserved cysteines and a histidine. The LIM domain binds two zinc ions and seems to be involved in protein-protein interactions.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:442"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Lipid degradation</name> <rdfs:comment>Protein involved in the breakdown of lipids, a diverse class of compounds, insoluble in water but soluble in organic solvents, and which include fats, oils, triacylglycerols, fatty acids, glycolipids, phospholipids and steroids.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:16042"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:443"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Lipid metabolism</name> <rdfs:comment>Protein involved in the biochemical reactions of lipids. Lipids are a diverse class of compounds which are insoluble in water but soluble in organic solvents. They include fats, oils, triacylglycerols, fatty acids, glycolipids, phospholipids and steroids.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6629"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:444"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Lipid synthesis</name> <rdfs:comment>Protein involved in the synthesis of lipids, a diverse class of compounds which are insoluble in water but soluble in organic solvents. They include fats, oils, triacylglycerols, fatty acids, glycolipids, phospholipids and steroids.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:8610"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:446"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Lipid-binding</name> <rdfs:comment>Protein which binds one or more lipids.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:8289"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:447"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Lipocalin</name> <rdfs:comment>Protein which belongs to the lipocalin family. Lipocalins transport small hydrophobic molecules such as steroids, bilins, retinoids and lipids. They share limited regions of sequence homology and a common tertiary structure architecture.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6810"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:448"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Lipopolysaccharide biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of lipopolysaccharides (LPS), the main constituents of the outer cell wall of Gram-negative bacteria. LPS are composed of lipid molecules joined to polysaccharides and are highly immunogenic.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9103"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:449"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Lipoprotein</name> <rdfs:comment>Protein which is posttranslationally modified by the attachment of at least one lipid or fatty acid, e.g. farnesyl, palmitate and myristate.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:450"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Lipoyl</name> <rdfs:comment>Protein which contains at least one lipoyl-binding domain. Lipoic acid is an essential cofactor for E2 acyltransferases and some other proteins.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:451"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Lissencephaly</name> <rdfs:comment>Protein which, if defective, causes lissencephaly, a brain malformation characterized by the absence (agyria) or reduction (pachygyria) of brain surface convolutions (gyri). Lissencephaly means "smooth brain".</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:452"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Lithium</name> <rdfs:comment>Protein whose function is lithium-dependent. Lithium is an alkali metal, chemical symbol Li.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:454"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Long QT syndrome</name> <name>LQTS</name> <rdfs:comment>Protein which, if defective, causes the long QT syndrome, a heart disease which manifests itself by a prolonged QT interval on the ECG and, clinically, by a propensity for tachyarrhythmias, causing syncopes and sudden cardiac death. LQTS may be drug-induced, but mutations in genes coding for cardiac ion-channels are the cause of the hereditary forms: Romano-Ward syndrome (RWS), and Jervell and Lange-Nielsen Syndrome (JLNS).</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:886"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>LTQ</name> <name>Lysine tyrosylquinone</name> <name>Lysine topaquinone</name> <rdfs:comment>Protein which contains at least one lysine tyrosylquinone (LTQ) cross-link modification. LTQ is formed by oxidation of the phenol ring of a tyrosine to form tyrosylquinone (topaquinone) followed by covalent cross-linking with a lysine residue.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:455"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Luminescence</name> <rdfs:comment>Protein involved in luminescence, the property of giving off light without emitting a corresponding degree of heat.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:8218"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:456"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Lyase</name> <rdfs:comment>Enzyme that catalyzes the cleavage of C-C, C-O, C-S, C-N or other bonds by other means than by hydrolysis or oxidation, with two substrates in one reaction direction, and one in the other. In the latter direction, a molecule (of carbon dioxide, water, etc) is eliminated, thus creating a new double bond or a new ring.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:16829"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:457"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Lysine biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of the essential basic amino acid lysine.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9085"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:458"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Lysosome</name> <rdfs:comment>Protein found in the lysosome, a membrane-limited organelle present in all eukaryotic cells, which contains a large number of hydrolytic enzymes that are used for the intracellular degradation of macromolecules.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5764"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:459"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Macrophage</name> <rdfs:comment>Protein found in macrophages, a type of large phagocytic mononuclear white blood cell, widely distributed in tissue, and which ingests invading microorganisms and also scavenges damaged cells and cellular debris. The macrophages of the connective tissue are also called histiocytes.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:460"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Magnesium</name> <rdfs:comment>Protein which binds at least one magnesium atom, or protein whose function is magnesium-dependent. Magnesium is a metallic element, chemical symbol Mg.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:287"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:461"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Malaria</name> <rdfs:comment>Protein involved in malaria, a human disease caused by Plasmodium, a parasitic protozoan that grows by sexual reproduction in the Anopheles mosquito.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:462"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Maltose metabolism</name> <rdfs:comment>Protein involved in the biochemical reactions with maltose, a disaccharide of glucose. Maltose is produced by the hydrolysis of starch.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:23"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:463"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Mandelate pathway</name> <rdfs:comment>Enzyme involved in the mandelate pathway. These enzymes enable various microorganisms to grow using D(-)-, L(+)- or DL-mandelate (2-hydroxy-2-phenylacetate) as the sole source of carbon and energy.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:464"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Manganese</name> <rdfs:comment>Protein which binds at least one manganese atom, or protein whose function is manganese-dependent. Manganese is a metallic element, chemical symbol Mn.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:30145"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:465"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Mannose-binding</name> <rdfs:comment>Protein which binds mannose, a 6-carbon aldose sugar, that is found in many glycoproteins and polysaccharides.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:430"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5537"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:466"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Maple syrup urine disease</name> <rdfs:comment>Protein which, if defective, cause maple syrup urine disease, an autosomal recessive disorder characterized by mental and physical retardation, feeding problems and a maple syrup odour to the urine.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5947"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:467"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Mast cell degranulation</name> <rdfs:comment>Protein involved in mast cell degranulation. Mast cell is a large, ovoid cell of hematopoietic lineage, with a centrally located nucleus and numerous large, intensely basophilic granules. The binding of an antigen to its specific immunoglobulin-E antibody on the mast cell surface triggers the release of the MC granules. Mast cells are involved in hypersensitivity reactions.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:468"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Matrix protein</name> <rdfs:comment>Protein that is associated with the matrix in a viral structure or in a sea urchin embryo spicule.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5198"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:469"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Meiosis</name> <rdfs:comment>Protein involved in meiotic processes or in regulation of meiosis. Meiosis is the nuclear division which results in the daughter nuclei each containing half the number of chromosomes of the parent. It comprises two distinct nuclear divisions, the first and second meiotic divisions (which may be separated by cell division), the actual reduction in chromosome number takes place during the first division.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7126"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:470"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Melanin biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of melanin. Melanins are brown or black pigments found in skin, hair, feathers, etc. They are irregular polymeric structures produced from tyrosine. Melanins can be divided into 3 groups: allomelanins in the plant kingdom, and eumelanins and phaeomelanins in the animal kingdom.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6583"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:867"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>MELAS syndrome</name> <rdfs:comment>Protein which, if defective, causes mitochondrial encephalomyopathy with lactic acidosis and stroke-like episodes (MELAS) syndrome, a genetically heterogenious disorder, characterized by episodic vomiting, seizures, and recurrent cerebral insults resembling strokes and causing hemiparesis, hemianopsia, or cortical blindness.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:471"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Melatonin biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of melatonin (N-acetyl 5-methoxytryptamine), a neurohormone synthesized by lower plants and in the pineal gland in animals. In humans, it is involved in the regulation of sleep, mood, puberty, ovarian cycles and in the establishment of circadian rhythms. In lower vertebrates, it causes aggregation of pigment in melanophores, and thus lightens skin.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5184"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7622"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:30187"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:472"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Membrane</name> <rdfs:comment>Protein which is membrane-bound or membrane-associated. A membrane is the layer which forms the boundary of cells and intracellular organelles. It is composed of two oriented lipid layers in which proteins are embedded and acts as a selective permeability barrier.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:16020"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:473"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Membrane attack complex</name> <rdfs:comment>Component of the membrane attack complex which groups the complement plasma glycoproteins C5b, C6, C7, C8 and polymeric C9 on biological membranes. The complex forms transmembrane channels which displace lipid molecules and other constituents, thus disrupting the phospholipid bilayer of target cells leading to cell lysis by osmotic leakage. The formation of the membrane attack complex is the terminal step in the complement cascade.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5579"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:474"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Menaquinone biosynthesis</name> <name>Vitamin K2 biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of menaquinone, a derivative of 2-methyl-1,4-naphthoquinone in which the 3-position is substituted with a variable-length polyisoprene chain. In mammals, menaquinone is an important component of the blood coagulation system. Mammals need to obtain this vitamin by their diet or from the bacterial flora of the gut.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9234"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:475"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Mercuric resistance</name> <rdfs:comment>Protein that confers bacteria or other microorganisms the ability to withstand mercury salts.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:46689"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:476"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Mercury</name> <rdfs:comment>Protein which binds mercury and/or is involved in the cleavage of carbon-mercury bonds. Mercury is the only liquid metallic element, chemical symbol is Hg.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:477"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Merozoite</name> <rdfs:comment>Protein expressed in the merozoite stage of sporozoite parasites, a stage in the life cycle produced by schizogony or asexual reproduction in which the nucleus of a cell undergoes division several times. This results in a multinucleate schizont which subsequently gives rise to a number of uninucleate cells called merozoites.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:478"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Metachromatic leukodystrophy</name> <name>Metachromatic leucodystrophy</name> <rdfs:comment>Protein which, if defective, causes metachromatic leukodystrophy, a disease characterized by intralysosomal or myelin membrane storage of cerebroside-3-sulfate. Whereas storage occurs in many cells, the disease almost exclusively affects oligodendrocytes. Patients suffer from a progressive demyelination, which causes a variety of neurological symptoms, including gait disturbances, ataxias, optical atrophy, dementia, seizures and spastic tetraparesis.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:479"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Metal-binding</name> <rdfs:comment>Protein which binds metals.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:480"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Metal-thiolate cluster</name> <rdfs:comment>Protein which binds at least a cluster composed of metal coordinated via cysteinyl thiolate bridges to cysteine ligands.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:479"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:46872"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:481"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Metalloenzyme inhibitor</name> <rdfs:comment>Protein that inhibits metalloenzymes, enzymes which contains metal ions.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:4857"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:483"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Metalloprotease inhibitor</name> <name>Metallopeptidase inhibitor</name> <rdfs:comment>Protein that inhibits metalloproteases, which are peptide hydrolases that use a metal in the catalytic mechanism.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:481"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:8191"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:484"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Methanogenesis</name> <rdfs:comment>Protein involved in methanogenesis, the energy yielding formation of methane by methanogenic bacteria.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:15948"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:485"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Methanol utilization</name> <rdfs:comment>Protein involved in the utilization of methanol.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:15945"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:486"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Methionine biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of the hydrophobic amino acid methionine, an essential amino acid in human diets which contains a thioether linkage.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9086"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:487"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Methotrexate resistance</name> <rdfs:comment>Protein that confers the ability to withstand methotrexate, an inhibitor of dehydrofolate reductase (DHFR). Methotrexate resistance occurs usually as a result of mutation or amplification of the DHFR gene.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:46"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:488"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Methylation</name> <rdfs:comment>Protein which is posttranslationally modified by the attachment of at least one methyl group.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:490"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>MHC I</name> <rdfs:comment>Protein of the major histocompatibility complex (MHC) class I which is involved in the induction of strong immune reaction. MHC I is involved in immune responses against virus-infected cells and rejection of transplanted tissue.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:30106"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19883"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19885"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:491"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>MHC II</name> <rdfs:comment>Protein of the major histocompatibility complex (MHC) class II which is involved in the induction of strong immune reaction. MHC II is involved in the control the expression of surface structures on lymphocytes and macrophages.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:45012"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19884"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19886"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:492"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Microsome</name> <rdfs:comment>Protein found in microsomes, a heterogenous set of vesicles 20-200nm in diameter and formed from the endoplasmic reticulum when cells are disrupted. The vesicles are isolated by differential centrifugation and are composed of three structural features: rough vesicles, smooth vesicles and ribosomes. Numerous enzyme activities are associated with the microsomal fraction.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5792"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:493"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Microtubule</name> <rdfs:comment>Protein associated with or component of the microtubule. The microtubule is formed by the arrangement of 13 parallel protofilaments arising from end-to-end aggregation of the tubulin alpha/beta-dimers. Microtubules are associated with various other proteins (MAPs, dynein, kinesin) and are involved in structures responsible for cellular movement such as flagella or cilia. Microtubules of the ciliary axoneme are more permanent than cytoplasmic and spindle microtubules. Microtubule formation is inhibited by agents such as colchicine, vinblastine or vincristine.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:494"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Milk</name> <rdfs:comment>Protein found in milk, a fluid secreted by female mammals to provide food for their offspring. It consists of water, proteins, soluble carbohydrates, electrolytes, lipids and vitamins.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:495"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Mineral balance</name> <rdfs:comment>Protein that influences the equilibrium of minerals present in bone, e.g., fetuin.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:30500"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:496"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Mitochondrion</name> <rdfs:comment>Protein encoded by or localized in the mitochondrion, a semiautonomous, self-reproducing organelle that occurs in the cytoplasm of all cells of most, but not all, eukaryotes. Each mitochondrion is surrounded by a double limiting membrane. The inner membrane is highly invaginated, and its projections are called cristae. Mitochondria are the sites of the reactions of oxidative phosphorylation, which result in the formation of ATP. The size and coding capacity of the mitochondrial DNA varies considerably in different organisms, and encodes rRNAs, tRNAs and essential mitochondrial proteins.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5739"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:497"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Mitogen</name> <rdfs:comment>Protein which can induce mitosis of certain eukaryotic cells, i.e. it stimulates cellular proliferation.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:8083"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:74"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:8283"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:498"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Mitosis</name> <rdfs:comment>Protein involved in mitosis, the nuclear division in eukaryotic cells involving the exact duplication and separation of the chromosome threads so that each daughter nucleus carries a chromosome complement identical to that of the parent nucleus. Mitosis is divided into four substages: prophase, metaphase, anaphase and telophase.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:132"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7067"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:499"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Mobility protein</name> <rdfs:comment>Protein involved in the conjugative transfer of plasmid DNA. These proteins provide the function of nicking the DNA at a certain point, guiding the 5' end of the nicked strand into the recipient cell, recircularization, and perhaps the priming of complementary strand synthesis in the recipient.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:184"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:500"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Molybdenum</name> <rdfs:comment>Protein which binds molybdenum (or molybdopterin) or protein involved in the transport of molybdenum, a metallic element, chemical symbol Mo. It plays an essential role in the active site of all eukaryotic Mo-containing enzymes. In plants, Mo enzymes are important for nitrate assimilation, phytohormone synthesis, and purine catabolism. Mo is often coordinated to the sulfur atoms of a pterin derivative (molybdopterin [MPT]), thereby forming the active Molybdenum cofactor (Moco), which is highly conserved in eukaryotes, eubacteria, and archaebacteria.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:30151"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:501"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Molybdenum cofactor biosynthesis</name> <name>Molybdopterin biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of the molybdenum cofactor (Moco), a molybdenum atom coordinated to the sulfur atoms of a pterin derivative (molybdopterin [MPT]). It is highly conserved in eukaryotes, eubacteria, and archaebacteria. In prokaryotes, two operons are directly associated with biosynthesis of the pterin moiety and its side chain while additional loci play a role in the acquisition of molybdenum and/or activation of the cofactor.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6777"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:502"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Monoclonal antibody</name> <rdfs:comment>Antibody produced by a single clone of B cells and thus consisting of a population of identical antibody molecules all specicfic for a single antigenic determinant. They are produced from cultured hybridoma cell lines for research and commercial purposes.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:3823"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:504"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Morphogen</name> <rdfs:comment>Diffusible protein that influence morphogenesis or embryonic development. These proteins carry information relating, for example, to a position in the embryo, and thus, determine the differentiation that cells perceiving this information will undergo. They are thought to act as a function of a threshold of their concentration.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:16015"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9653"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:505"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Motor protein</name> <rdfs:comment>Protein that walks or slides along microtubules or microfilaments using the energy provided by ATP or GTP hydrolysis, e.g. dyneins, myosins and kinesins. Or protein which mediates motility by other non enzymatic processes, e.g. prestin, a bidirectional voltage-to-force converter.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:3774"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:507"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>mRNA processing</name> <name>Messenger RNA processing</name> <rdfs:comment>Protein involved in the processing of the primary mRNA transcript to yield a functional mRNA. This includes 5' capping, 3' cleavage and polyadenylation, as well as mRNA splicing and RNA editing.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6397"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:508"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>mRNA splicing</name> <name>Messenger RNA splicing</name> <rdfs:comment>Protein involved in the process by which nonsense sequences or intervening sequences (introns) are removed from pre-mRNA to generate a functional mRNA (messenger RNA) that contains only exons. This process occurs in the nucleus before the fuctional mRNA is sent to the cytoplasm.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:507"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:398"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:510"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Mucopolysaccharidosis</name> <rdfs:comment>Protein which, if defective, causes mucopolysaccharidosis. These inherited diseases are characterized by excessive accumulation and secretion of oligomucopoloysaccharide due to the deficiency of enzymes involved in the degradation of glycosaminoglycans (mucopolysaccharides). They are progressive and often display a wide spectrum of clinical severity within one enzyme deficiency.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:30203"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:511"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Multifunctional enzyme</name> <rdfs:comment>Protein that contains at least two distinct enzymatic activities.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:3824"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:512"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Multigene family</name> <rdfs:comment>Member of a family of related proteins encoded by a set of similar genes. Multigene families are believed to have arisen by duplication and variation of a single ancestral gene. Examples of multigene families include those that encode the actins, hemoglobins, immunoglobulins, tubulins, interferons, histones etc.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:514"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Muscle protein</name> <rdfs:comment>Characteristic protein of a muscle cell. The major ones are myosin and actin, which are responsible for the contraction and relaxation of muscles.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7517"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:515"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Mutator protein</name> <rdfs:comment>Protein which is encoded by a mutator gene (mutator). Generally, these are genes within which certain mutations cause an increase in frequency of spontaneous mutations in other genes. Mutator proteins are therefore thought to be responsible for inaccurate DNA replication.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:516"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Myelin</name> <rdfs:comment>Characteristic protein of the myelin, a lipid-rich sheath of specialized glial cells that wrap their plasma membrane in a tight spiral around the axons in both the central and peripheral vertebrate nervous systems. The myelin sheath serves as an electrical insulator which increases the transmission of nerve impulses.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:517"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Myogenesis</name> <rdfs:comment>Protein involved in the differentiation and development of the muscle. Myogenesis is controlled by myogenic factors, a family of muscle-specific transcription factors that contain a conserved helix-loop-helix domain which is homologous to the myc family of proteins.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7519"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:518"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Myosin</name> <rdfs:comment>A motor protein which uses the energy provided by the hydrolysis of ATP to drive movements along actin filaments. Different types of myosin are found in eukaryotic cells.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:505"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:16459"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:519"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Myristate</name> <name>n-tetradecanoate</name> <rdfs:comment>Protein which is posttranslationally modified by the attachment of at least one myristate group. The myristate (14-carbon saturated fatty acid) group is attached through an amide bond to the N-terminal glycine residue of the mature form of a protein or to an internal lysine residue. Myristoylproteins may be cytoplasmic or membrane-associated.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:449"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:520"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>NAD</name> <name>Nicotinamide adenine dinucleotide</name> <name>Nicotinic adenine dinucleotide</name> <rdfs:comment>Enzymes which use NAD(H) as an electron acceptor or as a cofactor. Nicotinamide adenine dinucleotide, an important redox coenzyme that participates in a variety of enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NAD+) and reduced (NADH). NAD also functions as an ADP-ribose donor in ADP-ribosylation reactions.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:521"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>NADP</name> <name>Nicotinamide adenine dinucleotide phosphate</name> <name>Nicotinic adenine dinucleotide phosphate</name> <rdfs:comment>Enzymes which use NADP(H) as an electron acceptor or as a cofactor. Nicotinamide adenine dinucleotide phosphate, a redox coenzyme that participates in a variety of enzymatic reactions in which it serves as an electron carrier by being alternately oxidized (NADP+) and reduced (NADPH). Analogue of NAD, but NADPH is used extensively in biosynthetic, rather than catabolic pathways as well as in photosynthesis.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:523"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Neurodegeneration</name> <rdfs:comment>Protein which, if defective, causes neurodegeneration.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:8219"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:524"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Neurogenesis</name> <rdfs:comment>Protein involved in neurogenesis, which involves the differentiation and development of the nervous system.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7399"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:525"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Neuronal ceroid lipofuscinosis</name> <name>CLN</name> <name>NCL</name> <rdfs:comment>Protein which, if defective, causes neuronal ceroid lipofuscinosis (CLN or NCL), a group of autosomal recessive, progressive encephalopathies in children. They are characterized by psychomotor deterioration, visual failure, and the accumulation of autofluorescent lipopigment in neurons and other cell types. The main childhood forms are the infantile type (Santavuori-Haltia disease), the late infantile type (Jansky-Bielschowsky disease), and the juvenile type (Batten disease). Clinical onset is usually between the ages of 5 and 10. Biochemically, the disease is characterized by lysosomal accumulation of hydrophobic material, mainly ATP synthase subunit c.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:527"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Neuropeptide</name> <rdfs:comment>Peptides released by neurons as intercellular messengers. Many neuropeptides are also hormones released by non-neuronal cells. They have direct synaptic effects (peptide neurotransmitters) or indirect modulatory effects on the nervous system (peptide neuromodulators).</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7218"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:529"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Neurotransmitter</name> <rdfs:comment>Protein, released by the axon terminal in response to an electrical impulse, which travels across the synapse to either excite or inhibit the target cell.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7268"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:530"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Neurotransmitter biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of neurotransmitters. The proteins are released by the axon terminal in response to an electrical impulse and travel across the synapse to either excite or inhibit the target cell.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7268"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:42136"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:531"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Neurotransmitter degradation</name> <rdfs:comment>Protein involved in the breakdown of neurotransmitters. The proteins are released by the axon terminal in response to an electrical impulse and travel across the synapse to either excite or inhibit the target cell.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:42135"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:533"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Nickel</name> <rdfs:comment>Protein which binds at least one nickel atom, or protein whose function is nickel-dependent. Nickel is a metal, chemical symbol Ni.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:16151"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:534"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Nitrate assimilation</name> <rdfs:comment>Protein involved in the uptake, from the environment, of nitrates, inorganic or organic salts and esters of nitric acid. This includes the uptake and transport into cells by nitrate transporters, with the sequential reduction to nitrite and ammonium, catalysed by the enzymes nitrate reductase and nitrate reductase, respectively.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:42128"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:535"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Nitrogen fixation</name> <rdfs:comment>Protein involved in nitrogen fixation, the reduction of gaseous nitrogen to ammonia. This process is carried out only by prokaryotes who are either free-living or form symbiotic associations with plants or other organisms (e.g. termites, protozoa).</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9399"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:536"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Nodulation</name> <rdfs:comment>Protein involved in nodulation, the formation of nitrogen-fixing nodules on roots of both leguminous plants and the Parasponia genus.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9877"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:537"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Noncapsid protein</name> <rdfs:comment>Viral protein which does not form part of the capsid. The later is the external protein coat that protects the nucleic acid of a virus.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19012"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:866"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Nonsense-mediated mRNA decay</name> <name>NMD</name> <rdfs:comment>Protein involved in nonsense-mediated messenger RNA (mRNA) decay, a critical process of selective degradation of mRNAs that contain premature stop codons.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:184"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:538"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Nonstructural protein</name> <rdfs:comment>Viral proteins that are encoded by nonstructural genes and usually have an unknown function. Some of these proteins may play structural roles within the infected cell during replication or act in virus regulation.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19012"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:906"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Nuclear pore complex</name> <name>NPC</name> <name>Nuclear pore</name> <rdfs:comment>Protein associated predominantly with the nuclear pore complex (NPC). NPCs constitute the exclusive means of nucleocytoplasmic transport in eukaryotes during interphase. NPCs allow the passive diffusion of ions and small molecules (up to about 20 kDa or 5 nm) and the active, nuclear transport receptor (karyopherin: importin and exportin)-mediated bidirectional transport of macromolecules such as proteins, RNAs, ribonucleoprotein (RNPs), and ribosomal subunits (up to about 10 MDa) across the double-membrane nuclear envelope. NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. The NPC is composed of at least 30 distinct subunits, shows 8-fold rotational symmetry with specialized structures on the cyto- and nucleoplasmic side and in the nuclear envelope embedded core. The MW varies from about 44-60 MDa in S. cerevisiae to 60-120 MDa in vertebrates, yet the overall architecture is conserved.</rdfs:comment> <rdfs:seeAlso rdf:resource="http://npd.hgu.mrc.ac.uk/compartments/nuc_pore.html"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:539"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Nuclear protein</name> <rdfs:comment>Protein located in the nucleus of a cell.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5634"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:540"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Nuclease</name> <rdfs:comment>Enzyme that degrades nucleic acids into shorter oligonucleotides or single nucleotide subunits by hydrolyzing sugar-phosphate bonds in the nucleic acid backbone.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:378"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:4518"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:541"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Nucleocapsid</name> <rdfs:comment>Protein characteristic of the viral nucleocapsid, a protein-nucleic acid complex which forms part or all of a virion. The nucleocapsid consists of a capsid (external protein coat) plus an enclosed nucleic acid. Depending on the virus, the nucleocapsid could either be a naked core or be surrounded by a membranous envelope.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19013"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:542"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Nucleomorph</name> <rdfs:comment>Protein encoded by the nucleomorph genome or protein located in the nucleomorph. Nucleomorphs are vestigial endosymbiont found in cryptomonads and chlorachniophytes algae. These organisms respectively retain an enslaved red or green algal nucleus.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:543"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Nucleoprotein</name> <rdfs:comment>Viral protein conjugated with nucleic acid (DNA or RNA).</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:3676"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19012"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:544"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Nucleosome core</name> <rdfs:comment>Protein characteristic of the nucleosome, a repeating structural unit in chromatin that packages DNA to give the chromatin a 'beads-on-a-string' appearance. Each repeat consists of approximately 146 base pairs of DNA wound around a disk-shaped protein core which is composed of two of each of the nucleosomal histones H2A, H2B, H3 and H4.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:158"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:786"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:545"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Nucleotide biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of a nucleotide, a phosphate ester of a nucleoside consisting of a purine or pyrimidine base linked to ribose or deoxyribose phosphates.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9165"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:546"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Nucleotide metabolism</name> <rdfs:comment>Protein involved in the biochemical reactions of nucleotides. Nucleotides are phosphate esters of a nucleoside consisting of a purine or pyrimidine base linked to ribose or deoxyribose phosphates.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9117"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:547"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Nucleotide-binding</name> <rdfs:comment>Protein which binds a nucleotide, a phosphate ester of a nucleoside consisting of a purine or pyrimidine base linked to ribose or deoxyribose phosphates.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:166"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:549"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Nylon degradation</name> <rdfs:comment>Protein involved in the degradation of nylon, a polymer whose main chain comprises recurrent amide groups. These compounds are generally formed from combinations of diamines, diacids and amino acids.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19876"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:550"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Obesity</name> <rdfs:comment>Protein which, if defective, causes obesity, a disorder characterized by excessive deposition of fat.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:551"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Oil body</name> <rdfs:comment>Protein characteristic of oil bodies, the sites of lipid storage in plant seed cells. They originate as vesicles formed from the endoplasmic reticulum and are coated by a phospholipid monolayer and a set of tightly associated proteins.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:12511"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:552"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Olfaction</name> <rdfs:comment>Protein involved in olfaction, the process of smelling.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7608"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:553"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Oncogene</name> <name>Oncoprotein</name> <rdfs:comment>Protein encoded by an oncogene, which is responsible for cellular transformations in culture or for cancer induction in animals.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:8151"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:554"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>One-carbon metabolism</name> <rdfs:comment>Protein involved in the biochemical reactions with one-carbon groups, e.g., methyl and formyl groups.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6730"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:896"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Oogenesis</name> <rdfs:comment>Protein involved in egg development and maturation. A process whereby primordial germ cells form mature ova.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:221"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:555"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Opioid peptide</name> <rdfs:comment>Endogenous peptides with opiate-like activity.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:1515"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:556"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Organic radical</name> <rdfs:comment>Protein which is posttranslationally modified by the formation of a stable radical. E.g., P09373 is posttranslationally interconverted, under anaerobic conditions, from an inactive to an active form that carries a stable radical localized to a specific glycine at the C-terminal region of the polypeptidic chain.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:892"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Osteogenesis</name> <name>Ossification</name> <rdfs:comment>Protein involved in osteogenesis, the mechanism of bone formation wether intramembranous or endochondral. In intramembranous ossification, bone is formed by differentiation of mesenchymal cells into osteoblasts with absence of a cartilaginous model. The flat bones of the skull, the sternum, and the scapula are examples of bones that develop by intramembranous ossification. The term endochondral refers to the close association of the developing bone with the pre-existing hyaline cartilage model of that bone. The long bones of the limbs (including the phalanges) and the ribs develop by endochondral ossification.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:557"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Outer membrane</name> <rdfs:comment>Protein characteristic of the outer membrane of organelles like mitochondria, chloroplasts and some eubacteria which are surrounded by a double membrane: the outer membrane and the inner membrane.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:472"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19867"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:558"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Oxidation</name> <rdfs:comment>Protein which is posttranslationally modified by oxidation of a residue.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:560"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Oxidoreductase</name> <rdfs:comment>Enzyme that catalyzes the oxidation of one compound with the reduction of another.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:16491"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:562"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Pair-rule protein</name> <rdfs:comment>A protein encoded by a pair-rule gene. These are developmental genes in Drosophila involved in delimiting segments in the early embryos. Mutations in pair rule genes affect every alternate segment.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:217"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7275"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7366"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:563"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Paired box</name> <rdfs:comment>Protein which contains a paired box domain, a conserved domain of about 120 amino acids, which is generally located in the N-terminal section of various proteins.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:564"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Palmitate</name> <name>n-hexadecanoate</name> <rdfs:comment>Protein which is posttranslationally modified by the attachment of at least one palmitate group. The palmitate (16-carbon saturated fatty acid) group is usually attached to cysteine via a thioester bond. Lysine, serine and threonine may also serve as palmitate acceptors. Many palmitoylproteins are membrane associated either directly through the palmitate moiety or as transmembrane proteins anchored by the fatty acid. However, a few are actually secreted from cells.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:449"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:565"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Pancreas</name> <rdfs:comment>Protein characteristic of or secreted by the pancreas, a gland associated with gut in most vertebrates, which secretes hormones, insulin and glucagon from endocrine glands and digestive enzymes from exocrine glands.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:566"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Pantothenate biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of pantothenate.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:15940"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:907"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Parkinson's disease</name> <name>Paralysis agitans</name> <rdfs:comment>Protein which, if defective, causes classic Parkinson's disease. Parkinson's disease is a complex multifactorial neurodegenerative disorder, usually occurring in late life, although an early onset and a juvenile form are known. Typical features are masklike facies, tremor of resting muscles, a slowing of voluntary movements (bradykinesia), festinating gait and postural instability. The signs and symptoms of the disease are the consequence of a striatal deficiency of dopamine, resulting from neuronal death in the substantia nigra. Parkinson's disease is characterized by the presence of Lewy bodies, intraneuronal inclusions found in many brain regions which are not entirely specific to, but are a highly sensitive marker for, Parkinson’s disease.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:908"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Parkinsonism</name> <rdfs:comment>Protein which, if defective, causes parkinsonism. Parkinsonism refers to disorders, both genetic and non-genetic, characterized by four primary parkinsonian symptoms: tremor, rigidity, postural instability and bradykinesia, resulting from the loss or dysfunction of dopamine-producing neurons in the substantia nigra. Lewy bodies, intraneuronal accumulations of aggregated proteins, may or may not be present in the brain of the patients.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:569"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Pentaxin</name> <name>Pentraxin</name> <rdfs:comment>Protein which belongs to the pentaxin family. Pentaxins have a pentameric configuration of five non-covalently bound identical subunits organized as a planar disc-like subunit. Members have been recognized in a range of evolutionarily diverse species from crabs to higher mammals.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:570"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Pentose shunt</name> <name>Hexose monophosphate pathway</name> <name>Pentose phosphate pathway</name> <name>Phosphogluconate oxidative pathway</name> <rdfs:comment>Protein involved in the pentose shunt, the biochemical pathway in which glucose-6-phosphate is oxidized to 6-phosphogluconate with the the production of NADPH. Then 6-phosphogluconate is converted to ribulose-5-phosphate and CO2 and a second molecule of NADH. This pathway is an important source of NADPH and ribose-5-phosphate.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6098"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:572"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Peptidoglycan-anchor</name> <rdfs:comment>Surface protein of a Gram-positive bacteria which is anchored to the cell wall envelope by a transpeptidation mechanism which requires a C-terminal sorting signal with a conserved LPXTG motif. An amide bond is created between the carboxyl-group of the conserved threonine and the amino-group of peptidoglycan cross-bridges.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:573"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Peptidoglycan synthesis</name> <name>Murein synthesis</name> <name>Pseudomurein synthesis</name> <rdfs:comment>Protein involved in the synthesis of peptidoglycan which consists of a glycosaminoglycan formed by alternating residues of D-glucosamine and either muramic acid {2-amino-3-O-[(R)-1-carboxyethyl]-2-deoxy-D-glucose} or L-talosaminuronic acid (2-amino-2-deoxy-L-taluronic acid), which are usually N-acetylated or N-glycoloylated. The carboxyl group of the muramic acid is commonly substituted by a peptide containing residues of both L- and D-amino acids, whereas that of L-talosaminuronic acid is substituted by a peptide consisting of L-amino acids only. These peptide units may be cross-linked by a peptide bond, thereby giving rise to a giant macromolecule that forms the rigid cell wall (sacculus or murein sacculus). This macromolecule is known to occur as a monomolecular layer between the inner and outer membrane in Gram-negative bacteria and as a multimolecular layer, often associated covalently or non-covalently with various additional compounds (teichoic acids, neutral polysaccharides. etc.) in Gram-positive bacteria. In the archaebacteria, several organisms contain a peptidoglycan, also called pseudomurein, which differs in certain respects from those of the eubacteria.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:133"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9252"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:574"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Periplasmic</name> <rdfs:comment>Protein located in the space between the inner membrane and the outer membrane (cell wall) of Gram negative bacteria and some eukaryotic algae. Also used for proteins located in the region between the plasma membrane and the cell wall in fungi.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:42597"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:575"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Peroxidase</name> <rdfs:comment>Enzyme that catalyzes the oxidation of a substrate by reducing peroxide to water. These enzymes are often located in peroxisomes.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:560"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:4601"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:576"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Peroxisome</name> <rdfs:comment>Protein found in the peroxisome or involved in its biosynthesis. The peroxisome is a small eukaryotic organelle limited by a single membrane, specialized for carrying out oxidative reactions. Contains mainly peroxidases, several other oxidases and catalase. The catalase regulates the contents of the produced toxic hydrogen peroxide thus protecting the cell. Beta-oxidation of fatty acids is another major function of peroxisomes. In plants and fungi this degradation occurs only in this cellular compartment.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5777"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:577"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>PHA biosynthesis</name> <name>Poly(3-hydroxyalkanoate) biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of poly(3-hydroxyalkanoates) (PHA). In Pseudomonas oleovorans large amounts of this polyester are synthesized when cells are grown under nitrogen-limiting conditions. When nitrogen is further supplied in the medium, the accumulated PHA is degraded.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:42621"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:578"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Phage lysis protein</name> <rdfs:comment>Phage protein involved in the lysis of the bacterial cell wall allowing the release of mature, newly formed phages.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:16998"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19835"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:579"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Phage maturation</name> <rdfs:comment>Protein involved in phage maturation, the formation of complete phage viruses ready for release.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19067"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:580"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Phage recognition</name> <rdfs:comment>Protein involved in phage recognition. Necessary for adsorption of the virion into the host cell.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9597"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:46718"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:581"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Phagocytosis</name> <rdfs:comment>Protein that renders the organism resistant to phagocytosis, the process by which a cell is engulfed and broken down by another for purposes of defense or sustenance.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6909"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:582"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Pharmaceutical</name> <rdfs:comment>Protein which is used as a pharmaceutical drug, e.g. to treat specific diseases.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:583"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>PHB biosynthesis</name> <name>Poly-hydroxybutyrate biosynthesis</name> <name>Poly-beta-hydroxybutyrate biosynthesis</name> <name>Poly-(3-hydroxybutyrate) biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of poly-hydroxybutyrate (PHB). It accumulates in a variety of bacteria as an energy source. This polyester is thermoplastic with biodegradable properties.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:42619"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:584"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Phenylalanine biosynthesis</name> <rdfs:comment>Protein involved in the biosynthesis of the aromatic amino acid phenylalanine.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:57"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9094"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:585"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Phenylalanine catabolism</name> <rdfs:comment>Protein involved in the degradation of the aromatic amino acid phenylalanine.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6559"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:586"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Phenylketonuria</name> <rdfs:comment>Protein which, if defective, causes phenylketonuria, an autosomal recessive disorder in which the body is unable to break down the amino acid phenylalanine. The resulting buildup of phenylalanine in the body causes mental retardation, mental disturbances, eczema and skin pigmentation.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6559"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:587"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Phenylpropanoid metabolism</name> <rdfs:comment>Protein involved in the biochemical reactions with phenylpropanoids.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9698"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:588"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Pheromone</name> <rdfs:comment>Proteins which acts as a pheromone. Pheromones are odours of conspecifics which elicit an adaptive behavioral response, e.g. insect sex pheromones. Generally, they are comprised of mixtures of compounds and behavioral responsiveness to them is largely instinctual, sexually-dimorphic, and attributable to a specialized component(s) of the olfactory system.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5186"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:589"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Pheromone response</name> <name>Pheromone response pathway</name> <rdfs:comment>Protein involved in the pheromone response.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19236"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:590"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Pheromone-binding</name> <rdfs:comment>Protein which binds pheromones, the odours of conspecifics which elicit an adaptive behavioral response, e.g. insect sex pheromones.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5550"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:591"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Phorbol-ester binding</name> <rdfs:comment>Protein which contains at least one phorbol ester/diacylglycerol binding domain. Phorbol ester is an analogue of diacyl glycerol (DAG) and is a potent tumor promoter that cause a variety of physiological changes when administered to both cells and tissues. Phorbol esters can stimulate protein kinase C (PKC) directly.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19992"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:593"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Phospholipase A2 inhibitor</name> <rdfs:comment>Protein which inhibits phospholipase A2 (EC 3.1.1.4) (PA2), an enzyme which releases fatty acids from the second carbon group of glycerol. Phospholipase A2 inhibitors are widely distributed in venoms and digestive secretions.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19834"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:594"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Phospholipid biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of phospholipids, the major lipid component of most cellular membranes. Phospholipids are usually composed of two fatty acid chains esterified to two of the carbons of glycerol phosphate, the phosphate being esterified to a hydroxyl group of another hydrophilic compound, such as choline, ethanolamine or serine.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:8654"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:595"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Phospholipid degradation</name> <rdfs:comment>Protein involved in the breakdown of phospholipids, the major lipid component of most cellular membranes. Phospholipids are usually composed of two fatty acid chains esterified to two of the carbons of glycerol phosphate, the phosphate being esterified to a hydroxyl group of another hydrophilic compound, such as choline, ethanolamine or serine.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6644"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:596"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Phosphopantetheine</name> <name>Pantetheine 4'phosphate</name> <rdfs:comment>Protein which contains at least one phosphopantetheine as the prosthetic group. In acyl carrier proteins (ACP) for example, it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:597"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Phosphorylation</name> <rdfs:comment>Protein which is posttranslationally modified by the attachment of at least one phosphate group usually on serine, threonine or tyrosine residues, but also on aspartic acid or histidine residues.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:598"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Phosphotransferase system</name> <name>Phosphoenolpyruvate-dependent sugar phosphotransferase system</name> <name>PTS</name> <name>Sugar phosphotransferase system</name> <rdfs:comment>Protein involved in the phosphotransferase system, the major carbohydrate transport system in bacteria. This phosphotransferase system catalyzes the transfer of the phosphoryl group from phosphoenolpyruvate to incoming sugar substrates concomitant with their translocation across the cell membrane.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9401"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:599"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Photoprotein</name> <rdfs:comment>Luminescent proteins, which are involved in the phenomenon of light emission in certain living organisms. E.g., green fluorescent protein which is unique among fluorescent proteins in that its chromophore is not a separately synthesized prostethic group but is composed of modified amino acid residues within its polypeptide chain.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:8218"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:600"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Photoreceptor</name> <rdfs:comment>Protein found or involved in the function of photoreceptor cells, e.g. rod and cone cells. Photoreceptors are sensitive and respond to light stimuli, e.g. rhodopsin in retina and phytochrome in plants.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:8020"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7601"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:601"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Photorespiration</name> <rdfs:comment>Protein involved in oxygen consumption, which takes place in plants during the light period: in the presence of O(2) the enzyme rubisco catalyzes the oxidative fragmentation of ribulose 1,5-biphosphate to 3-phospho-D-glycerate and 2-phospho-glycolate in the chloroplast. 2-phosphoglycolate can then be recycled via reactions in peroxisomes, mitochondria as well as chloroplasts, where for every 2 molecules of phosphoglycolate, one molecule of 3-phosphoglycerate is formed and one molecule of CO(2) is lost.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9853"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:602"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Photosynthesis</name> <rdfs:comment>Protein involved in photosynthesis, the process in which light energy is absorbed by photosynthetic pigments (e.g. chlorophyll) and converted to chemical energy (usually ATP and NADPH, =light reaction). This energy is subsequently used as an energy source for the reduction of carbon dioxide to carbohydrate (=Calvin cycle). The general reaction is: CO(2) + 2H(2)A = (CH(2)O) + 2A + H(2)O, where 2H(2)A is any reduced compound that can serve as an electron donor. In plants, algae and cyanobacteria H(2)O serves as a reductant, generating O(2). Non-oxygenic organisms use other electron donors, for example H(2)S in purple sulfur bacteria, generating sulfur.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:15979"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:603"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Photosystem I</name> <name>PSI</name> <name>P700</name> <rdfs:comment>Protein involved in photosystem I (PSI), a complex that uses light energy to mediate electron flow in the chloroplast thylakoid membrane of plants and in cyanobacteria. In linear electron flow, PSII is coupled to PSI and produces a pH gradient, ATP and NADPH. In cyclic electron flow, PSI generates a pH gradient and ATP. PSI is excited best by light at about 700 nm, and is thus sometimes called P700. PSI is an iron-sulfur type reaction center (RC), sharing a common ancestor with the RCs of Heliobacteriaceae, green sulfur and green non-sulfur bacteria.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9522"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:604"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Photosystem II</name> <name>PSII</name> <name>P680</name> <rdfs:comment>Protein involved in photosystem II (PSII), a complex that uses light energy to mediate electron flows in the chloroplast thylakoid membrane of plants and in cyanobacteria. PSII splits water, releasing hydrogen ions and molecular oxygen. PSII cannot use photons of a wavelength greater than 680 nm, and is thus sometimes called P680. PSII is a quinone type rection center (RC), sharing a common ancestor with the RCs of purple bacteria.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9523"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:605"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Phycobilisome</name> <rdfs:comment>Protein found in phycobilisome, an accessory light energy harvesting structure on the outer face of the thylakoid membranes in cyanobacteria and red algae. Phycobilisomes are mainly composed of phycobiliproteins (such as allophycocyanin, phycocyanin and phycoerythrin) together with linker polypeptides.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:30089"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:606"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Phytochrome</name> <rdfs:comment>Protein of the phytochrome family. The plant phytochrome acts as a regulatory photoreceptor which mediates red-light effects on a wide variety of physiological and molecular responses. It can undergo a reversible photochemical conversion between a biologically inactive red light-absorbing form and the active far-red light-absorbing form. In higher plants the tetrapyrrole chromophore is attached to a cysteine which is located in a highly conserved region.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:600"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:8020"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9585"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:607"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Phytochrome signaling pathway</name> <rdfs:comment>Protein involved in the relay of information from the activated phytochrome molecule to target genes. Different phytochromes use both separate and common early signaling pathways. These pathways converge downstream in a process of signal integration that regulates photomorphogenesis and the circadian clock. This provides the means by which information from specific wavelengths of light may be amplified and coordinated.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:608"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Pigment</name> <rdfs:comment>Protein which binds or transport pigments, any coloring matter in animals, plants or microorganisms.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:609"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Pituitary</name> <rdfs:comment>Protein characteristic of the pituitary gland (hypophysis), an endocrine gland at the base of the hypothalamus, which secretes a number of hormones (pituitary hormones), such as vasopressin (antidiuretic hormone), oxytocin, adrenocorticotropin (ACTH), somatotropin (growth hormone, GH), prolactin and gonadotropin.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:610"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Placenta</name> <rdfs:comment>Protein characteristic of the placenta, a structure formed on the wall of the uterus during pregnancy and which allows the exchange of nutrients, wastes and oxygen between the mother's blood and the fetus' blood. The placenta also provides the endocrine secretion of various hormones, which are believed to be involved in the maintenance of pregnancy.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:611"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Plant defense</name> <rdfs:comment>Protein involved in plant defense, either as part of preexisting, developmentally regulated defense barriers (such as thionins, defensins or hydroxyproline-rich glycoproteins fortifying the cell wall) or as components of the defense responses induced upon pathogen infection during hypersensitive cell death (HR), local acquired resistance (LAR) or systemic acquired resistance (SAR). This includes proteins involved in various pathways, such as the gene-for-gene resistance, the salicylic acid (SA)-dependant resistance, the jasmonate (JA) and/or ethylene (ET)-dependant resistance and the induced systemic resistance (ISR), as well as the final products of those pathways such as the pathogenesis-related proteins.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:613"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Plasma</name> <rdfs:comment>Protein secreted in the plasma, an acellular fluid in which blood cells are suspended. A variety of proteins are present in the blood plasma, including serum albumin, immunoglobulins, fibrinogens and other blood coagulation factors, protease inhibitors and complement components.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:614"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Plasmid</name> <rdfs:comment>Protein encoded on a plasmid, a self-replicating circular DNA that is found in a variety of bacterial, archaeal, fungal, algal and plant species, and can be transferred from one organism to another. Plasmids often carry antibiotic-resistant genes and are widely used in molecular biology as vectors of genes and in cloning.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:615"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Plasmid copy control</name> <rdfs:comment>Protein involved in the plasmid copy control, the ability of a plasmid to control its own copy number in a cell. Copy number is a function of the rate at which DNA synthesis is initiated.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6276"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:616"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Plasmid partition</name> <rdfs:comment>Protein involved in plasmid partition, the process whereby newly replicated plasmids are distributed properly to daughter cells during cell division.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:30541"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:617"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Plasminogen activation</name> <rdfs:comment>Protein involved in the plasminogen activation which occurs when an heterogeneous group of proteolytic enzymes convert plasminogen to plasmin.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:8243"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:618"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Plastoquinone</name> <rdfs:comment>Protein which interacts with plastoquinone, a substituted quinone called plastoquinone because it appeared concentrated in the chloroplasts of higher plants. Plastoquinone transfers electrons from the photosystem II reaction center to the cytochrome bf complex and carries protons across the photosynthetic membrane.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:16655"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6118"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9523"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:619"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Platelet</name> <rdfs:comment>Protein which interacts or which is characteristic of platelets. These are anucleate discoid cells found in large numbers in the bloodstream, which bind to fibrinogen at the site of a wound in order to begin the clotting process. Platelets are formed in the bone marrow.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:620"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Polyamine biosynthesis</name> <rdfs:comment>Protein involved in polyamine biosynthesis. The polyamines, e.g. putrescine, cadaverine, agmatine, spermidine and spermine, are wide-spread in all organisms, and have been shown to play a role in the regulation of growth and differentiation of virtually all types of cells.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6596"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:621"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Polymorphism</name> <rdfs:comment>Protein for which there is at least one variant not directly responsible for a disease.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:622"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Polyneuropathy</name> <rdfs:comment>Protein which, if defective, causes polyneuropathy, a disease involving a number of peripheral nerves. The various forms are categorized by the type of nerve affected (e.g. sensory, motor or autonomic), by the distribution of nerve injury (e.g. distal vs. proximal), by the nerve component primarily affected (e.g., demyelinating vs. axonal), by etiology or by a pattern of inheritance.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:623"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Polyprotein</name> <rdfs:comment>Protein that is cleaved to produce several functional polypeptides.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:624"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Polysaccharide degradation</name> <rdfs:comment>Protein involved in polysaccharide degradation, the breakdown of polysaccharides.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:119"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:272"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:627"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Porphyrin biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of porphyrins which are compounds that contain the porphin structure, e.g. four pyrrole rings connected by methine bridges in a cyclic configuration to which a variety of side chains are attached. Porphyrins often chelate metal ions (Fe, Mg, Co, Zn, Cu, Ni). Examples are, heme proteins (which contain iron porphyrins) like myoglobin, hemoglobin, cytochromes, or related macrocycles including chlorophylls (which have a central magnesium ion) and pheophytins (which are metal free) and vitamin B-12 (which has cobalt).</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6779"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:628"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Postsynaptic membrane</name> <rdfs:comment>Protein characteristic of the postsynaptic membrane. In a chemical synapse, the postsynaptic membrane is the membrane that receives a signal (binds neurotransmitter) from the presynaptic cell and responds via depolarisation or hyperpolarisation. The postsynaptic membrane is separated from the presynaptic membrane by the synaptic cleft.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7268"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:630"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Potassium</name> <rdfs:comment>Protein which binds at least one potassium, or protein whose function is potassium-dependent. Potassium is an alkali metal, chemical symbol K.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:632"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Potassium channel inhibitor</name> <rdfs:comment>Protein which interferes with the function of potassium channels which are membrane proteins forming a channel in a biological membrane selectively permeable to potassium ions. They are found in various venoms from snakes, scorpions and spiders.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:872"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19870"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:633"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Potassium transport</name> <rdfs:comment>Protein involved in the transport of potassium ions.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:630"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6813"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:634"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>PQQ</name> <name>Pyrroloquinoline quinone</name> <name>Methoxatin</name> <rdfs:comment>Protein which is modified by linkage to a pyrroloquinoline quinone (PQQ) cofactor.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:884"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>PQQ biosynthesis</name> <name>Pyrroloquinoline quinone biosynthesis</name> <rdfs:comment>Protein involved in the biosynthesis of the cofactor pyrroloquinoline quinone (PQQ).</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:18189"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:635"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Pregnancy</name> <rdfs:comment>Protein which plays a role in pregnancy, the condition of having a developing embryo or fetus in the body, after union of an ovum and spermatozoon.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7565"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:636"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Prenylation</name> <rdfs:comment>Protein which is posttranslationally modified by the attachment of at least one prenyl group (farnesyl or geranylgeranyl) usually on cysteine residues which are at or near the C-terminal extremity.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:449"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:637"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Prenyltransferase</name> <rdfs:comment>Enzyme that catalyzes the transfer of an isoprenoid (farnesyl or geranylgeranyl) usually on cysteine residues, which are three residues away from the C-terminal extremity.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:4659"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:905"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Primary microcephaly</name> <rdfs:comment>Protein which, if defective, causes primary microcephaly. This is a neurodevelopmental condition characterized by a head circumference more than 3 standard deviations below the age-related mean, and absence of other syndromic features or significant neurological deficits. Brain weight is markedly reduced and the cerebral cortex is disproportionately small. Primary microcephaly is also known as true microcephaly or microcephaly vera.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:639"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Primosome</name> <rdfs:comment>Component of the complex involved in the synthesis of RNA primer sequences used in DNA replication. Main components are primases and replicative DNA helicases that move as a unit along the replication fork.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6269"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5658"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:640"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Prion</name> <rdfs:comment>Protein of that is able to form a prion, a self-propagating protein conformation. This class of proteins includes the members of the prion family which can form proteinaceous infectious particles responsible for transmissible spongiform encephalopathies (TSE) in many animals , such as Kuru and Creutzfeldt-Jakob syndrome in humans, scrapies in sheep and BSE in cattle. Prion diseases can present themselves as sporadic, genetic or infectious disorders and are associated with the accumulation of an abnormal isoform (PrPSc) of a cellular protein (PrPC) in affected brains. In sporadic and infectious forms, the conversion of PrPC into PrPSc involves a conformational change whereby the alpha-helical content diminishes and the amount of beta-sheet increases. Unlike PrPC, PrPSc is insoluble and partly resistant to protease digestion, yielding a shorter 141 amino-acid fragment. In brain, PrPSc is often present as aggregated amyloid fibrils which are totally resistant to protease digestion and cannot be eliminated by the cells.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:641"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Proline biosynthesis</name> <rdfs:comment>Protein involved in the biosynthesis of the cyclic amino acid proline. The structure of proline differs from the structure of other amino acids in that its side chain is bonded to the nitrogen of the amino group as well as to the carbon atom. This makes the amino group a secondary amine, and because of this, proline is also described as an imino acid. The presence of proline residues strongly influences the secondary structure of proteins.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:28"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6561"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:642"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Proline metabolism</name> <rdfs:comment>Protein involved in a biochemical reaction with the cyclic amino acid proline. The structure of proline differs from the structure of other amino acids in that its side chain is bonded to the nitrogen of the amino group as well as to the carbon atom. This makes the amino group a secondary amine, and because of this, proline is also described as an imino acid. The presence of proline residues strongly influences the secondary structure of proteins.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6560"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:645"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Protease</name> <name>Peptidase</name> <name>Peptide hydrolase</name> <name>Proteinase</name> <rdfs:comment>Enzyme which hydrolyzes peptide bonds.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:378"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:8233"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:646"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Protease inhibitor</name> <rdfs:comment>Protein which inhibits or antagonizes the biosynthesis of proteases or their activity.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:4866"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:647"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Proteasome</name> <name>Macropain</name> <name>Prosome</name> <rdfs:comment>Protein which is part of the proteasome, a large protein complex in the cytosol that is responsible for degrading proteins which have been marked for destruction by ubiquitination or by some other means.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5829"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:648"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Protein biosynthesis</name> <rdfs:comment>Protein involved in the biosynthesis of proteins from mRNA molecules. This process, called translation, is carried out by ribosomes, where activated amino acids are added to the nascent polypeptide chain.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6412"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:649"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Protein kinase inhibitor</name> <rdfs:comment>Protein which inhibits the activity of a protein kinase.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:4860"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:904"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Protein phosphatase</name> <name>Phosphoprotein phosphatase</name> <rdfs:comment>Enzyme that catalyzes the hydrolysis of phosphate monoesters bonds of phosphoserines, phosphothreonines, phosphotyrosines or phosphoaspartic acids. While many protein phosphatases inhibit the activities of phosphorylation cascades, some activate them.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:378"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:4721"/> <rdfs:seeAlso rdf:resource="http://bioinf.man.ac.uk/phosphabase/"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:650"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Protein phosphatase inhibitor</name> <rdfs:comment>Protein which inhibits the activity of a protein phosphatase.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:4864"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:651"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Protein splicing</name> <rdfs:comment>Protein which undergoes protein self-splicing, a posttranslational modification involving the excision of an intervening protein sequence (intein) from a protein precursor and the concomitant ligation of the flanking protein fragments (exteins) to form a mature extein protein and the free intein.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:68"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:652"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Protein synthesis inhibitor</name> <rdfs:comment>Protein which blocks the synthesis of proteins (translation) through various mechanisms, including hydrolysis of cellular tRNA, and inactivation of the 60S subunits of eukaryotic ribosome.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:17148"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:654"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Proteoglycan</name> <rdfs:comment>Protein containing one or more covalently linked and usually sulfated glycosaminoglycans, (e.g., chondroitin sulfate, dermatan sulfate, heparan sulfate, heparin, keratan sulfate). Glycosaminoglycans are polysaccharides made of repeating disaccharides (usually 40-100 times), which consist of uronic acid (or galactose) and hexosamines. Aggrecan, for example, is the major component in articular cartilage.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:655"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Prothrombin activator</name> <rdfs:comment>Protein which activates prothrombin, the inactive precursor of thrombin. For example, staphylocoagulase, an extracellular protein produced by Staphylococcus aureus, forms a complex with prothrombin which can clot fibrinogen without any proteolytic cleavage of prothrombin.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:30567"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:656"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Proto-oncogene</name> <rdfs:comment>Protein whose normal cellular gene can be converted into a cancer-promoting oncogene by mutation. An oncogene protein product has abnormal activity and/or is expressed at abnormal levels, which leads to cell death or gives rise to cancer.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:8151"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:657"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Pseudohermaphroditism</name> <rdfs:comment>Protein which, if defective, causes pseudohermaphroditism, a condition in humans in which the individual has gonads of one sex but shows ambiguous morphologic criteria of sex.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7530"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:658"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Purine biosynthesis</name> <rdfs:comment>Protein involved in the biosynthesis of purine, a nitrogenous heterocyclic base, e.g. adenine, guanine, hypoxanthine and xanthine. De novo synthesis involves a complex, energy-expensive pathway that yields inosine 5'-monophosphate (IMP), a purine ribonucleotide. AMP and GMP are then formed from IMP in separate pathways. Adenine and guanine are found in both DNA and RNA. Hypoxanthine and xanthine are important intermediates in the synthesis and degradation of the purine nucleotides.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6164"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:659"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Purine metabolism</name> <rdfs:comment>Protein involved in a biochemical reaction with purines. Purines are nitrogenous heterocyclic bases, e.g. adenine, guanine, hypoxanthine and xanthine. The degradation of purines leads to uric acid, which is excreted in primates, birds and some other animals. In many other vertebrates uric acid is degraded further to the excretory product allantoin.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6144"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:660"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Purine salvage</name> <rdfs:comment>Protein involved in the biosynthesis of purine nucleotides from free purines salvaged from their catabolism. This process is less expensive energetically and exerts feedback control on the de novo synthesis.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6166"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:661"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Putrescine biosynthesis</name> <name>1,4-diaminobutane biosynthesis</name> <name>1,4-butanediamine biosynthesis</name> <rdfs:comment>Protein involved in the biosynthesis of putrescine, a foul-smelling polyamine. This metabolic precursor of the polyamines spermine and spermidine is often produced during breakdown of some of the amino acids by bacteria.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9446"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:662"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Pyridine nucleotide biosynthesis</name> <rdfs:comment>Protein involved in the biosynthesis of the pyridine nucleotides NAD and NADP. NAD may be synthesized de novo from aspartate and dihydroxyacetone phosphate or from tryptophan. NAD may also be synthesized from nicotinamide or nicotinic acid. NADP is formed via the phosphorylation of NAD by NAD+ kinase.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19363"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:663"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Pyridoxal phosphate</name> <rdfs:comment>Protein which uses at least one pyridoxal phosphate as cofactor or protein required for its synthesis. This coenzyme, derived from vitamin B6, is important in amino acid metabolism, e.g., in reactions involving transamination, decarboxylation, racemization, elimination or replacement.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:664"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Pyridoxine biosynthesis</name> <name>Pyridoxol biosynthesis</name> <name>Vitamin B6 biosynthesis</name> <rdfs:comment>Protein involved in the biosynthesis of pyridoxine, a precursor to the coenzyme pyridoxal phosphate.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:8615"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:665"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Pyrimidine biosynthesis</name> <rdfs:comment>Protein involved in the biosynthesis of pyrimidine, a nitrogenous heterocyclic base, e.g. uracil, thymine, cytosine and orotic acid. Pyrimidines are synthesized from carbamoyl phosphate and aspartate. Ribose-5-phosphate is then attached to yield pyrimidine ribonucleotides. Cytosine is found in both DNA and RNA. Uracil is found only in RNA. Thymine is normally found in DNA. Sometimes tRNA contains some thymine as well as uracil.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6221"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:666"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Pyrogen</name> <rdfs:comment>Protein producing fever. The major endogenous pyrogen in mammals is probably interleukin-1, which is produced by activated macrophages and acts on the hypothalamic thermoregulatory centre.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6954"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:667"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Pyrokinin</name> <rdfs:comment>Protein of the pyrokinin family. Pyrokinin is an insect neuropeptide of 8 to 16 amino acids, which mediates visceral muscle contractile activity (myotropic activity).</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:527"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5184"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7218"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:668"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Pyropoikilocytosis</name> <name>HPP</name> <rdfs:comment>Protein which, if defective, causes hereditary pyropoikilocytosis (HPP), a recessively inherited hemolytic anemia characterized by microspherocytosis, poikilocytosis (deformation of the erythrocytes), and an unusual thermal sensitivity of red cells. Frequently associated with abnormalities in alpha-spectrin, one of the principal structural proteins of the erythrocyte membrane skeleton.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:360"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:873"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Pyrrolidone carboxylic acid</name> <name>Pyroglutamic acid</name> <name>Pyro-Glu</name> <rdfs:comment>Protein which is posttranslationally modified by the cyclization of a N-terminal glutamine.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:669"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Pyrrolysine</name> <rdfs:comment>Protein which contains a pyrrolysine, a naturally occurring amino acid so far only found in some archaeal proteins. Pyrrolysine is a lysine in amide-linkage to (4R,5R)-4-substituted-pyrroline-5-carboxylate.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:670"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Pyruvate</name> <rdfs:comment>Protein which uses at least one pyruvate as cofactor (pyruvoyl) or substrate, or protein required for pyruvate synthesis or degradation. Pyruvate is an intermediate compound in the metabolism of carbohydrates, proteins and fats.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:671"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Queuosine biosynthesis</name> <name>Nucleoside Q biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of queuosine (nucleoside Q), a modified guanosine derivative found only in tRNAs for aspartic acid, asparagine, histidine and tyrosine. It can pair with either C or U.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:8616"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:672"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Quinate metabolism</name> <rdfs:comment>Protein involved in the biochemical reactions of quinate. Quinate is the ionized form of quinic acid which is found in plants, e.g. in cinchona bark.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19630"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:874"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Quinone</name> <rdfs:comment>Protein which interacts with quinones. Quinones are aromatic dicarbonyl compounds, where the two carbonyl groups are usually in the para position. Most naturally occuring quinones contain a long isoprenoid side chain, and are divided in two major structural groups, the naphtoquinones and benzoquinones; the number of isoprene units depends on the organism. These highly hydrophobic molecules are mainly involved in electron transport, as electron carriers in redox reactions. For example, ubiquinone (coenzyme Q) and menaquinone (vitamin K2) are essential components of the respiratory electron transport chain. Plastoquinone, found in chloroplasts and in cyanobacteria, functions as one of the carrier molecules of the electron transport chain in photosynthesis. Phylloquinone (vitamin K1) is the major form of vitamin K found in plants. Chlorobiumquinone, demethylmenaquinone, alpha-tocopherolquinone, rhodoquinone, epoxyubiquinone and caldariellaquinone are other quinones found in several species.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:673"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Quorum sensing</name> <rdfs:comment>Protein whose expression is quorum sensing (QS)-dependent. QS is a phenomenon whereby the accumulation of signaling molecules enables a single cell to sense the number of bacteria (cell density). The bacterial reponse to QS includes adaptation to availability of nutrients, defence against other microorganisms which may compete for the same nutrients and the avoidance of toxic compounds potentially dangerous for the bacteria.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9372"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:674"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Reaction center</name> <rdfs:comment>Protein which is a component of the reaction center, a system consisting of proteins and cofactors which facilitate light energy and electron transfer in plants. The system also acts as a light-driven electron pump across the photosynthetic membrane of photosynthetic bacteria.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:30090"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:675"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Receptor</name> <rdfs:comment>Protein which binds to, or responds to, a ligand with high specificity.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:4872"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:676"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Redox-active center</name> <rdfs:comment>Protein which possesses at least one active center which mediates its participation in redox reactions, usually via reversible oxidation of a cysteine residue leading to a cysteine-sulfenic acid that can either be stabilized, or react with an unmodified cysteine residue and form a stable but reversible disulfide bond.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:677"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Repeat</name> <rdfs:comment>Protein which contains a stretch of amino acids present in multiple copies.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:678"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Repressor</name> <rdfs:comment>Protein which interferes with transcription, usually by binding to specific sites on DNA. Also used for proteins which repress translation.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:680"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Restriction system</name> <name>Restriction-modification system</name> <rdfs:comment>Protein involved in the restriction system present in many bacteria and archaea. This defense mechanism is composed principally of a restriction endonuclease and a methylase. The restriction endonuclease cuts the invading DNA of viruses (or phages) at a specific recognition site. The bacterial DNA is protected by the methylase which adds a methyl group to a specific nucleotide, immediately following replication, in the same target site as the restriction enzyme.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9307"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:681"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Retinal protein</name> <rdfs:comment>Protein found in the retina or, in the case of bacteriorhodopsin, in the purple membrane of halobacteria, and which acts as a photoreceptor and which binds a retinal chromophore.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:600"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7602"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:682"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Retinitis pigmentosa</name> <rdfs:comment>Protein which, if defective, causes retinitis pigmentosa, a hereditary progressive degeneration of the neuroepithelium of the retina,</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7601"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:683"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Retinol-binding</name> <name>Vitamin A-binding</name> <rdfs:comment>Protein which binds retinol, one of the active form of Vitamin A, a fat-soluble vitamin derived from carotenes. It is a precursor of retinal, the light-absorbing group of visual pigments. Vitamin A is also required for growth.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19841"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:684"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Rhamnose metabolism</name> <name>6-deoxy-L-mannose metabolism</name> <rdfs:comment>Protein involved in the biochemical reactions of rhamnose. Rhamnose is a methylpentose sugar structurally derived from mannose. The L-isomer occurs naturally as a component of many plant glycosides and in lipopolysaccharides of some gram-negative bacteria.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19299"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:685"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Rhizomelic chondrodysplasia punctata</name> <name>RCDP</name> <rdfs:comment>Protein which, if defective, causes rhizomelic chondrodysplasia punctata (RCDP). This lethal autosomal recessive disease is characterized by proximal limb shortening, severely disturbed endochondrial bone formation, and mental retardation. At the cellular level, the biogenesis of most peroxisomal proteins is normal, but a specific subset of at least four peroxisomal matrix proteins fail to be imported from the cytosol. Type 1 RCDP (RCDP1) is the most common form, caused by mutations in the PEX7 gene, which encodes the PTS2-receptor peroxin-7. In RCDP type 2 and type 3 the RCDP phenotype results from a deficiency of the peroxisomal enzymes dihydroxyacetone phosphate synthase (RCDP2), and dihydroxyacetone phosphate acyltransferase (RCDP3), which are both involved in the biosynthesis of plasmalogens.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:686"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Riboflavin biosynthesis</name> <name>Vitamin B2 biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of riboflavin (Vitamin B2), which consists of ribose attached to a flavin moiety. It is synthesized by all green plants and most microorganisms and occurs free in milk, the retina, whey and urine. It is found in most cells as a component of the coenzymes flavin adenine dinucleotide (FAD) and flavin mononucleotide (FMN).</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9231"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:687"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Ribonucleoprotein</name> <rdfs:comment>Proteins conjugated with ribonucleic acid (RNA). Ribonucleoprotein are involved in a wide range of cellular processes. Besides ribosomes, in eukaryotic cells both initial RNA transcripts in the nucleus (hnRNA) and cytoplasmic mRNAs exist as complexes with specific sets of proteins. Processing (splicing) of the former is carried out by small nuclear RNPs (snRNPs). Other examples are the signal recognition particle responsible for targetting proteins to endoplasmic reticulum and a complex involved in termination of transcription.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:30529"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:688"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Ribosomal frameshift</name> <rdfs:comment>Protein produced by programmed ribosomal frameshifting, a translational recoding mechanism which causes the ribosome to alter its reading of the genetic code to produce an alternative product not directly encoded by the mRNA.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:689"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Ribosomal protein</name> <rdfs:comment>Protein of the ribosome, large ribonucleoprotein particles where the translation of messenger RNA (mRNA) into protein occurs. They are both free in the cytoplasm and attached to membranes of eukaryotic and prokaryotic cells. Ribosomes are also present in all plastids and mitochondria, where they translate organelle-encoded mRNA.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:687"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:3735"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:690"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Ribosome biogenesis</name> <rdfs:comment>Protein involved in the synthesis of ribosomes.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7046"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:691"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>RNA editing</name> <rdfs:comment>Protein which is derived from an RNA which has been modified by RNA editing, a process that changes the nucleotide sequence of an RNA from that of the DNA template encoding it. RNA editing can be due to nucleotide conversion, insertion and/or deletion.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:692"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>RNA repair</name> <rdfs:comment>Protein involved in the repair of RNA, the various biochemical processes by which damaged RNA can be restored.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:42245"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:693"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>RNA replication</name> <rdfs:comment>Protein involved in the replication of RNAs, thus resulting in the duplication of RNA by making a new copy of an existing molecule.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6410"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:694"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>RNA-binding</name> <rdfs:comment>Protein which binds to RNA.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:3723"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:697"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Rotamase</name> <rdfs:comment>Enzyme (EC 5.2.1.8) which accelerates the folding of proteins by catalyzing the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:413"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:3755"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6457"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:698"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>rRNA processing</name> <name>Ribosomal RNA processing</name> <rdfs:comment>Protein involved in the processing of the primary rRNA transcript to yield a functional rRNA. This includes the cleavage and other modifications.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6364"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:699"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>rRNA-binding</name> <rdfs:comment>Protein which binds to ribosomal RNA.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:694"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19843"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:700"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Rubredoxin</name> <rdfs:comment>Rubredoxin is a small protein (or domain) which serves as an electron transfer protein. The protein contains around 50 amino acids and binds one iron atom via the sulfur atoms of four cysteine residues. The iron-sulfur complex shows tetrahedral symmetry.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:701"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>S-layer</name> <rdfs:comment>Protein of the paracrystalline mono-layered assembly which coats the surface of bacteria and archaea.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:134"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:702"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>S-nitrosylation</name> <rdfs:comment>Protein which is posttranslationally modified by the attachment of a nitric oxide group on the sulfur atom of one or more cysteine residues.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:703"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Sarcoplasmic reticulum</name> <rdfs:comment>Protein found in a special form of agranular reticulum located in the sarcoplasm of striated muscle. The agranular reticulum comprises and comprising a system of smooth-surfaced tubules which form a plexus around each myofibril.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:16529"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:704"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Schiff base</name> <rdfs:comment>Enzyme which forms a covalent enzyme-substrate complex, a Schiff's base or ketimine between the amino group of a lysine residue of the enzyme and the carbonyl group of the substrate.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:456"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:705"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>SCID</name> <name>Severe combined immunodeficiency disease</name> <name>Severe congenital immunodeficiency disease</name> <rdfs:comment>Protein which, if defective, causes severe combined (or congenital) immunodeficiency disease. An heterogeneous group of inherited disorders characterized by gross functional impairment of the immune system.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:706"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Seed</name> <rdfs:comment>Protein found in the encapsulated embryos of flowering plants. The encapsulated embryos of flowering plants.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:707"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Seed embryo</name> <rdfs:comment>Protein found in the part of the seed that will eventually grow into the plant upon germination.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:706"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:709"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Segmentation polarity protein</name> <name>Segment polarity protein</name> <rdfs:comment>Protein involved in the division of the embryo into segments and which is responsible for determining the internal polarity of the segments. Segment polarity gene mutations are lethal and change the pattern and, often the polarity, of every segment.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:217"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7367"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:710"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Selectin</name> <rdfs:comment>Cell adhesion proteins of the selectin superfamily which have an N-terminal lectin domain followed by an epidermal growth factor-like domain, a variable number (between 2 and 9) of complement regulatory elements, a single transmembrane region and a short cytoplasmic anchor. These integral membrane glycoproteins may be involved in the selective trafficking of blood-borne components of the immune system. Selectins mediate the binding of leukocytes to the vascular endothelium.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:430"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5529"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:711"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Selenium</name> <rdfs:comment>Protein which binds at least one selenium, or protein whose function is selenium-dependent. Selenium is a nonmetallic trace element, chemical symbol Se.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:712"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Selenocysteine</name> <name>3-selenyl-L-alanine</name> <rdfs:comment>Protein which contains a selenocysteine, a naturally occurring amino acid in both eukaryotic and prokaryotic organisms.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:711"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:713"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Self-incompatibility</name> <rdfs:comment>Protein involved in the sporophytic self-incompatibility system, which is to say the inability of pollen grains to fertilize flowers of the same plant or a close relative. This mechanism ensures out-breeding in certain plant species.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:714"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Semen</name> <rdfs:comment>Protein found in semen, the fluid secreted from testes and accessory glands that carries the male germ cells (spermatozoa).</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:715"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Seminal vesicle</name> <rdfs:comment>Protein secreted by the seminal vesicles, a pair of glands in male vertebrates which are united with the excretory duct and secrete the fluid component of semen; can also serve for temporary storage of semen. Some insects also have seminal vesicles, for example Drosophila.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:716"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Sensory transduction</name> <rdfs:comment>Protein involved in sensory transduction, the process by which a cell converts an extracellular signal, such as light, taste, sound, touch or smell, into electric signals.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7600"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:717"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Septation</name> <rdfs:comment>Protein involved in septation, the formation of a separating wall (septum) between daughter cells during cell division.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:132"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:917"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:718"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Serine biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of the amino acid serine, a constituent of proteins and precursor of several metabolites, including cysteine, glycine and choline. Serine is mostly formed from 3-phosphoglycerate in a 3-step reaction pathway.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:28"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6564"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:719"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Serine esterase</name> <rdfs:comment>Enzyme which catalyzes the hydrolysis of esters and is characterized by a catalytically active serine residue in its active site.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:378"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:4759"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:720"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Serine protease</name> <name>Serine endopeptidase</name> <name>Serine peptidase</name> <name>Serine proteinase</name> <rdfs:comment>Proteolytic enzyme with a serine residue (Ser) in its active site. The reactivity of the serine residue is ensured by the vicinity of a histidine and an aspartate residue (catalytic triad), all three residues are required for the charge relay system to take place.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:645"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:4252"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:721"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Serine protease homolog</name> <rdfs:comment>Protein which is related to serine proteases but seems to have no proteolytic activity.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:722"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Serine protease inhibitor</name> <name>Serine endopeptidase inhibitor</name> <name>Serine peptidase inhibitor</name> <name>Serine proteinase inhibitor</name> <rdfs:comment>Protein which inhibits serine proteases, a group of proteolytic enzymes which are characterized by a catalytically active serine residue in their active site.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:646"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:4867"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:724"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Serotonin biosynthesis</name> <name>5-hydroxytryptamine</name> <name>5-HT</name> <rdfs:comment>Protein involved in the synthesis of the biochemical messenger and regulator serotonin which is formed by the hydroxylation and subsequent decarboxylation of L-tryptophan. In humans, serotonin mediates several important physiological functions, including neurotransmission, gastrointestinal motility, hemostasis and cardiovascular integrity.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6587"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:725"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Serpin</name> <rdfs:comment>Serpins (SERine Proteinase INhibitors) are a large family of structurally related proteins found in animals, plants, and viruses. Most serpins function as suicide substrate inhibitors of serine proteases, trapping their target enzymes as stable covalent acyl-enzyme complexes. The mechanism of inhibition requires cleavage of the serpin by the enzyme, followed by a profound conformational change in the serpin structure.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:722"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:4867"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:726"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Sexual differentiation</name> <rdfs:comment>Protein involved in both the determination of cells to become sexual tissue in embryonic development and in the process by which male and female tissue becomes structurally and functionally specialized during embryonic development.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7548"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:727"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>SH2 domain</name> <rdfs:comment>Protein with at least one Src homology 2 (SH2) domain. The SH2 domain, which was first identified in the oncoproteins Src and Fps, is about 100 amino-acid residues long. It functions as a regulatory module of intracellular signaling cascades by interacting with high affinity to phosphotyrosine-containing target peptides in a sequence-specific and strictly phosphorylation-dependent manner.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:728"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>SH3 domain</name> <rdfs:comment>Protein with at least one Src homology 3 (SH3) domain It is a small protein domain of about 50 amino-acid residues first identified as a conserved sequence in the non-catalytic part of several cytoplasmic protein tyrosine kinases (e.g. Src). Since then, it has been found in a great variety of other intracellular or membrane-associated proteins. The SH3 module might mediate the assembly of specific protein complexes by binding to proline-rich peptides.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:729"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>SH3-binding</name> <rdfs:comment>Protein with at least one SH3-binding site and which mediates the binding to the Src homology 3 (SH3) region, a module present in a large group of proteins, including cytoskeletal elements and signaling proteins.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:730"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Sialic acid</name> <rdfs:comment>Family of naturally occurring N-and O-acyl derivatives of the deoxyamino sugar neuraminic acid. They are widely distributed in bacteria and animal tissue as components of polysaccharides, glycoproteins and glycolipids.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:731"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Sigma factor</name> <rdfs:comment>Initiation factors that bind to bacterial DNA-dependent RNA polymerases and promote attachment to specific initiation sites on DNA. Following attachment, the sigma factor is released.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:16987"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6355"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:732"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Signal</name> <name>Signal sequence</name> <name>Signal peptide</name> <rdfs:comment>Protein which has a signal sequence, a peptide usually present at the N-terminus of proteins and which is destined to be either secreted or part of membrane components. The signal sequence (usually 20-30 amino acids long) interacts with the signal recognition particle and directs the ribosome to the endoplasmic reticulum where co-translational insertion takes place. Signal peptides are highly hydrophobic but have some positively charged amino acids. Normally, the signal sequence is removed from the growing peptide chain by specific peptidases (signal peptidases) located on the cisternal face of the endoplasmic reticulum.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:733"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Signal recognition particle</name> <rdfs:comment>Protein of the signal recognition particle (SRP) which is a cytosolic ribonucleoprotein complex that induces elongation arrest of nascent presecretory and membrane proteins until the ribosome becomes associated with the rough endoplasmic reticulum. It consists of a 7S RNA and at least six polypeptide subunits. One of the SRP proteins (srp54) binds GTP and in association with 7S RNA and srp19 has GTPase activity.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5786"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:734"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Signal transduction inhibitor</name> <rdfs:comment>Protein which inhibits signal transduction, the process by which extracellular signals induce intracellular responses. Usually a hormone or neurotransmitter binds to a cell surface receptor which is coupled to a second messenger system, such as that involving cAMP, or to an ion channel. The final downstream consequence of signal transduction is a change in the cell's function, such as a modification in glucose uptake or in cell division. Such a change may be the result of an activation or an inhibition event.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7165"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:736"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Signalosome</name> <name>COP9 signalosome</name> <name>CSN</name> <name>COP9 complex</name> <name>COP9 signalosome complex</name> <rdfs:comment>Protein of the signalosome complex, a multifunctional protein complex essential for development and possibly involved in the regulation of protein degradation.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:8180"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:737"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Silk</name> <rdfs:comment>Protein found in silk, a strong, soft, lustrous fiber made of fibroin, a structural protein consisting almost entirely of stacked antiparallel beta pleated sheets. It is produced by certain spiders and by the larvae of certain bombycine moths.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:738"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Sodium channel inhibitor</name> <rdfs:comment>Protein which interferes with the function of sodium channels which are membrane proteins forming a channel in a biological membrane selectively permeable to sodium ions. They are found in various venoms from snakes, scorpions and spiders.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:872"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19871"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:742"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>SOS response</name> <name>SOS response system</name> <name>SOS system</name> <name>SOS repair system</name> <rdfs:comment>Protein involved in an SOS response, which implies the coordinated activation of diverse unlinked genes (ca. 20 in E.coli) involved in DNA repair, error-prone DNA replication, etc., in response to severe DNA damage. The SOS system is tightly regulated and its expression only occurs when absolutely required.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:234"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6281"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9432"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:743"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Sperm</name> <rdfs:comment>Protein found in sperm or spermatozoa; any male gamete produced by an animal.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:744"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Spermatogenesis</name> <rdfs:comment>Protein involved in sperm cell development. A process whereby primordial germ cells form mature spermatozoa, which includes spermatocytogenesis (successive mitotic and meiotic divisions) and spermiogenesis (a metamorphic change).</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:221"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7283"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:745"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Spermidine biosynthesis</name> <name>N-(3-aminopropyl)-1,4-butanediamine</name> <rdfs:comment>Protein involved in the synthesis of spermidine, a widely distributed polyamine which acts as a growth factor for some microorganisms and stabilizes the membrane structure of bacteria, as well as the structure of ribosomes, some viruses and the DNA of many organisms.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:8295"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:746"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Sphingolipid metabolism</name> <rdfs:comment>Protein involved in the biochemical reactions of sphingolipids. These are structurally complex saponifiable lipids which contain a fatty acid covalently linked to the amino alcohol sphingosine (or a related base), as backbone structure, to which is attached a polar head group. They are synthesized in the Golgi complex and are important membrane components in both plant and animal cells. They are present in especially large amounts in brain and nerve tissue.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:443"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6665"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:747"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Spliceosome</name> <rdfs:comment>Protein of the spliceosome, a very large complex of small nuclear RNA/protein particles (snRNPs) which assemble with pre-mRNA to achieve RNA splicing.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:508"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5681"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:748"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Sporozoite</name> <rdfs:comment>Protein expressed in the sporozoite stage which is the infectious stage of the malaria parasite. Malaria is transmitted by mosquitos to the vertebrate host. This term also refers to the motile infectious stage of other sporozoans (parasitic protozoans).</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:749"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Sporulation</name> <rdfs:comment>Protein involved in the production of spores, i.e. sporulation.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:30435"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:750"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Starch biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of starch, the carbohydrate storage of plants. Starch consists of amylose (a linear alpha(1-4)-glucan) and amylopectin (an alpha(1-4)-glucan with alpha(1-6)-branch points). Starch (glucans and amylopectins) is synthesised via the ADP-glucose pathway by three key enzymes: ADP-glucose pyrophosphorylase, starch synthases and starch branching enzymes. The randomly branched glucan molecules are then specifically debranched via a debranching enzyme in order to produce amylopectins. Amylopectins are branched in highly ordered clusters and are crystalline in nature, but also contain covalently bound phosphate.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19252"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:751"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Stargardt disease</name> <name>SD</name> <rdfs:comment>Protein which, if defective, causes Stargardt disease (SD). SD is a hereditary degeneration of the macula lutea occurring between the ages of six and twenty, marked by rapid loss of visual accuity and by abnormal appearance and pigmentation of the macular aerea.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:752"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Steroid biosynthesis</name> <rdfs:comment>In vivo synthesis of steroids (steroidogenesis), a large group of complex polycyclic lipids that consist of a 17-carbon ring system. Examples are bile acids, sterols, various hormones and saponins.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:444"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6694"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:753"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Steroid metabolism</name> <rdfs:comment>Protein involved in the biochemical reactions of steroids. Steroids are a large group of complex tetracyclic lipids that consist of a 17-carbon-ring system. Examples are bile acids, sterols, various hormones and saponins.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:443"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:8202"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:754"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Steroid-binding</name> <rdfs:comment>Protein which binds steroids.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5496"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:755"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Steroidogenesis</name> <rdfs:comment>Biosynthesis of steroid hormones which takes place in the mitochondria of the adrenal cortex. Oxidation of two adjacent carbon atoms in the side chain of cholesterol, followed by the cleavage between them, produces pregnenolone, a precursor of all other steroid hormones. The hydroxylation and oxygenation reactions are catalyzed by cytochrome P450 and mixed-functions oxidases that use NADPH and O2.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6700"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:756"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Sterol biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of sterols, any steroid alcohol which are components of cell membranes in plants, animals and fungi.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:752"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:16126"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:757"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Stickler syndrome</name> <name>STL</name> <rdfs:comment>Protein which, if defective, causes Stickler syndrome (STL), also known as hereditary progressive arthro-ophthalmopathy. It is a genetically and phenotypically heterogeneous disorder with ocular, oro-facial, auditory and skeletal manifestations. Clinical features include high myopia, vitreo-retinal degeneration, retinal detachment, cleft palate, midfacial hypoplasia, osteoarthritis, and sensorineural hearing loss. Inheritance is autosomal dominant.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:758"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Storage protein</name> <rdfs:comment>Protein which is a source of nutrients for the development or growth of an organism.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:45735"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:759"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Streptomycin biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of streptomycin, an antibiotic substance produced by the soil actinomycete Streptomyces griseus. The three parts of the molecule (streptidine-6-P, dTDP-dihydrostreptose and N-methyl-glucosamine) are synthesized by separate biochemical pathways and the subunits brought together at the end. The final intermediate in the pathway, streptomycin P, becomes biologically active upon removal of the phosphate. The synthesis of the key streptomycin biosynthesis enzymes is mainly regulated by differing levels of factor A. Streptomycin binds to the small subunit of ribosomes of prokaryotic cells and causes inhibition and misreading.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:45"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19872"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:760"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Structural protein</name> <rdfs:comment>Proteins that serve as supporting filaments, cables or sheets, to give biological structures strength or protection.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5198"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:761"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Submandibular gland</name> <rdfs:comment>Protein found in the submandibular gland, one of two salivary glands in the neck, located in the space bound by the two bellies of the digastric muscle and the angle of the mandible. It discharges through the submandibular duct. The secretory units are predominantly serous although a few mucous alveoli, some with serous demilunes, occur.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:765"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Sulfation</name> <name>Sulfatation</name> <rdfs:comment>Protein which is posttranslationally modified by the attachment of at least one sulfate group to a tyrosine residue. Serine and threonine may also serve as sulfate group acceptors.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:766"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Superantigen</name> <rdfs:comment>Antigens, mostly from bacterial toxins, that interact with a set of T-lymphocytes bearing a set of products of the V_T receptor genes. As a consequence superantigens activate large numbers of T cells. Staphylococcal enterotoxins are the best known superantigens, which stimulate CD4 T cells in humans.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:48"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:767"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Surface film</name> <rdfs:comment>Protein found in the film of pulmonary surfactants which cover the alveolar surface of the mammalian lung. These surfactants are composed of 90 % phospholipids and 10 % proteins.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:50828"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:768"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Sushi</name> <rdfs:comment>Protein which contains at least one sushi domain, a motif of approximately 60 amino acids characterized by a framework of four conserved half-cystine residues (1-3 and 2-4 disulfide-bonded) and several other highly conserved residues including proline, tryptophan, tyrosine/phenylalanine and cysteine. This type of structure, also designated SCR (Short Consensus Repeat), is predominantly present in proteins associated with the complement system.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:770"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Synapse</name> <rdfs:comment>Protein required for the well of the synapses. Synapses are the communicating cell-cell junctions that allow signals to pass from a nerve cell to a target cell. In a chemical synapse, the signal is carried by a neurotransmitter which diffuses across a narrow synaptic cleft and activates a receptor on the postsynaptic membrane of the target cell. The target may be a dendrite, cell body, neuronal axon, a specialized region of a muscle or a secretory cell. In an electrical synapse, a direct connection is made between the cytoplasms of two cells via gap junctions.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:45202"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:771"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Synaptosome</name> <rdfs:comment>Protein found in synaptosomes, the pinched-off nerve endings and their contents of vesicles and cytoplasm together with the attached subsynaptic area of the membrane of the postsynaptic cell. They are largely artificial structures produced by fractionation after selective centrifugation of nervous tissue homogenates.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19717"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:772"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Systemic lupus erythematosus</name> <name>SLE</name> <rdfs:comment>Protein involved in the systemic lupus erythematosus (SLE), a chronic autoimmune disease where the immune system is over-active and produces too many abnormal antibodies that react with the patient’s own tissues. The exact cause of lupus is not known, but heredity, environment and hormonal changes may be involved. The immune complex deposition in many tissues leads to the manifestations of the disease. Immune complexes can be deposited in glomeruli, skin, lungs, synovium, mesothelium, and other places. Many SLE patients develop renal complications.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:773"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>T-cell</name> <name>B-lymphocyte</name> <name>B lymphocyte</name> <name>Thymus dependent lymphocytes</name> <rdfs:comment>Protein expressed in T-cell, a class of lymphocytes so named because they are of thymic origin and have been through thymic processing. T-cells are involved primarily in cell-mediated immune response such as graft rejection. When T cells recognize a graft as foreign, this stimulates the cells to undergo blastic transformation, when the T cells, which are small lymphocytes, enlarge into lymphoblasts. The lymphoblasts divide repeatedly and differentiate into a number of T cell subsets: cytotoxic lymphocytes, helper lymphocytes, T memory cells and suppressor lymphocytes.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:775"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Tachykinin</name> <rdfs:comment>Protein of a family of biologically active neuropeptide hormones sharing a common conserved C-terminal sequence, -Phe-Xaa-Gly-Leu-Met-NH2, where Xaa is either an aromatic or a branched aliphatic amino acid. Members of this family have been found in mammals, amphibians and mollusks.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:527"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5102"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:776"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Taste-modifying protein</name> <name>TMP</name> <name>Sweet-taste protein</name> <rdfs:comment>Protein that function as a natural sweetener or flavor enhancer. TMPs are found in the fruit or seed of several plants and show no primary sequence similarity. TMPs interact with taste receptors in a potent and specific manner. TMPs are natural and have been used by some cultures for centuries. West Africans have long used TMPs to improve flavor and suppress bitterness of food and drink.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:876"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Taxol biosynthesis</name> <name>Paclitaxel biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of taxol, a complex diterpenoid isolated from the bark of yew (Taxus) species. Taxol is a potent antimitotic agent with activity against a number of leukamias and solid tumors. It has become a chemotherapeutic drug under the generic name of paclitaxel.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:42617"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:777"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Teichoic acid biosynthesis</name> <name>C polysaccharide biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of teichoic acid, a polymer of mainly glycerol phosphate or ribitol phosphate substituted extensively with amino acids and/or sugars. Teichoic acid occurs in the cell wall of Gram-positive bacteria.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19350"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:778"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Tellurium resistance</name> <rdfs:comment>Protein that confers resistance to tellurium.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:46690"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:779"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Telomere</name> <rdfs:comment>Protein involved in telomere replication, length regulation, structure, etc. The telomere is a nucleoprotein structure comprising the terminal section of a eukaryotic chromosome. It has a specialized structure which is replicated by a special process, thereby counteracting the tendency of a chromosome to be shortened during each round of replication.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:158"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7004"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:781"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:780"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Terminal addition</name> <rdfs:comment>Protein involved in the random addition of deoxynucleoside 5'-triphosphate to the 3'end of a DNA initiator.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:3912"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6304"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:781"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Testis</name> <rdfs:comment>Protein characteristic of the male reproductive gland producing spermatozoa.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:782"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Testosterone</name> <rdfs:comment>Protein induced by the testosterone, the major androgenic hormone produced by the interstitial (Leydig) cells of the testes in response to stimulation by the luteinizing hormone of the anterior pituitary.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:783"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Tetrahydrobiopterin biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of tetrahydrobiopterin, the reduced form of dihydrobiopterin, a reduced pteridine derivative related to folic acid. It is a coenzyme for the enzyme phenylalanine-4-hydroxylase which is involved in phenylalanine degradation.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6729"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:784"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Thiamine biosynthesis</name> <name>Thiamin biosynthesis</name> <name>Vitamin B1 biosynthesis</name> <name>Aneurin biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of thiamine, a water-soluble vitamin member of the vitamin B complex. It occurs in cells largely as its active coenzyme form thiamine pyrophosphate, formerly called cocarboxylase. Thiamine is necessary in the diet of most vertebrates and some microorganisms. Its deficiency causes beriberi in man and polyneuritis in birds. Thiamine pyrophosphate serves as coenzyme in aldehyde-group transfers.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9228"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:785"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Thiamine catabolism</name> <name>Thiamin catabolism</name> <name>Vitamin B1 catabolism</name> <name>Aneurin catabolism</name> <rdfs:comment>Protein involved in the degradation of thiamine, a water-soluble vitamin which is a member of the vitamin B complex. It occurs in cells largely as its active coenzyme form thiamine pyrophosphate, formerly called cocarboxylase. Thiamine is necessary in the diet of most vertebrates and some microorganisms. Its deficiency causes beriberi in man and polyneuritis in birds. Thiamine pyrophosphate serves as a coenzyme in aldehyde-group transfers.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9230"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:786"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Thiamine pyrophosphate</name> <name>Thiamin pyrophosphate</name> <name>TPP</name> <name>Thiamin diphosphate</name> <name>TDP</name> <rdfs:comment>Protein which contains at least one thiamine pyrophosphate, the active form of vitamin B1 (thiamine). It is a required coenzyme for the pyruvate decarboxylase, pyruvate dehydrogenase and ketoglutarate dehydrogenase reactions.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:787"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Thick filament</name> <rdfs:comment>Protein found in, or associated with, the thick filaments which are formed by bipolar myosin-II filaments (12-14nm in diameter, 1.6mm long) found striated muscle. Myosin filaments elsewhere are often referred to as 'thick filaments', although their length may be considerably less. The myosin heads project from the thick filament in a regular fashion.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:514"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6941"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5863"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:882"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Thioester bond</name> <name>Thiolester bond</name> <rdfs:comment>Protein which is posttranslationally modified by the formation of a thioester crosslink between two amino acids in the polypeptidic chain(s), usually formed between a cysteine side chain and the carboxamide group of an asparagine or glutamine side chain.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:883"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Thioether bond</name> <rdfs:comment>Protein which is posttranslationally modified by the formation of a thioether crosslink between two amino acids in the polypeptidic chain(s), usually formed between a cysteine side chain and the side chain of a serine or a threonine.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:788"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Thiol protease</name> <name>Thiol peptidase</name> <name>Thiol proteinase</name> <name>Sulfhydryl protease</name> <rdfs:comment>Proteolytic enzyme with a cysteine residue (Cys) in its active site. There are many families of thiol proteases. The most well known one is the papain family (C1 in MEROPS classification) which is known to exist in most eukaryotes.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:645"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:8234"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:789"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Thiol protease inhibitor</name> <name>Thiol peptidase inhibitor</name> <name>Thiol proteinase inhibitor</name> <rdfs:comment>Protein which inhibits the activity of a thiol protease, a class of proteases that contains an active site cysteine residue (Cys), e.g. papain, cathepsins, etc.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:646"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:4869"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:790"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Thionin</name> <rdfs:comment>Member of the plant thionin family. Thionins are small basic plant proteins generally toxic to animal cells and consist of a polypeptide chain of forty five to fifty amino acids with three to four internal disulfide bonds.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:791"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Threonine biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of the essential amino acid threonine.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:28"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9088"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:888"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Threonine protease</name> <rdfs:comment>Proteolytic enzyme with a threonine residue (Thr) in its active site. The prototype members of this class of enzymes are the proteasome catalytic subunits.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:645"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:8233"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:792"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Thrombophilia</name> <name>Recurrent venous thrombosis</name> <rdfs:comment>Protein which, if defective, causes thrombophilia, a disorder of the hemopoietic system in which the individuals are prone to serious spontaneous thrombosis.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:793"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Thylakoid</name> <rdfs:comment>Protein located in or on the thylakoid, a membranous cisterna of the chloroplast. Thylakoids stack up to form the grana or stay as single cisternae and interconnect the grana. The thylakoid contains the photosynthetic pigments, reaction centers and electron-transport chain. Thylakoid, where photosynthesis occurs, are also found in cyanelles and in photosynthetic bacteria where they are the extensive invaginations of the plasma membrane.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9579"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:794"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Thymus</name> <rdfs:comment>Protein secreted by the thymus. In mammals the thymus is just anterior to the heart within the rib cage; in other vertebrates it is in rather undefined regions of the neck or within the gill chamber in teleost fish. The thymus is the site of the production of T-lymphocytes and regresses as the animal matures.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:795"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Thyroid hormone</name> <rdfs:comment>Protein precursor of thyroid hormones which are secreted by the thymus gland and participate in the development of the lymphoid system as well as the maturation of the cellular immune response. Also used for proteins which bind thyroid hormones or thyroid hormone receptor antagonists.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:372"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6590"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:893"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Thyroid hormones biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of thyroid hormones.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:796"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Tight junction</name> <rdfs:comment>Protein which is a component of the tight junction or are associated with it. These specialized regions of the plasma membrane prevent the diffusion of dissolved molecules between adjacent epithelial cells, seal off body cavities such as intestine or stomach lumen and prevent the diffusion of membrane proteins and glycolipids between the apical and basolateral regions of the plasma membrane.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5923"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:797"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Tissue remodeling</name> <rdfs:comment>Protein involved in tissue remodeling. As an example the matrix-degrading plasminogen activators (PAs) and matrix metalloproteinases (MMPs) are general proteolytic enzyme systems which mediate tissue remodeling and tissue destruction in a variety of physiological and pathological conditions, including ovulation, angiogenesis, implantation, tumor invasion and inflammatory diseases such as rheumatoid arthritis (RA).</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:798"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>TonB box</name> <rdfs:comment>Protein with a TonB box. In Escherichia coli the TonB protein interacts with outer membrane receptor proteins that carry out high-affinity binding and energy-dependent uptake of specific substrates into the periplasmic space. These substrates are either poorly permeable through the porin channels or are encountered at very low concentrations. In the absence of TonB these receptors bind their substrates but do not carry out active transport. TonB also interacts with some colicins and is involved in the energy dependent, irreversible steps of bacteriophages phi-80 and T1 infection.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:799"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Topoisomerase</name> <rdfs:comment>Enzymes capable of altering the degree of supercoiling of double-stranded DNA molecules. Various topoisomerases can increase or relax supercoiling, convert single-stranded rings to intertwined double-stranded rings, tie and untie knots in single stranded and duplex rings or catenate and decatenate duplex rings. Any enzyme that cleaves only one strand of a DNA duplex and then reseals it is classified as a type I topoisomerase (Topo I). Type II topoisomerases (Topo II) change DNA topology by breaking and rejoining double-stranded DNA.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:413"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:3916"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:800"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Toxin</name> <rdfs:comment>Naturally-produced poisonous protein that damages or kills other cells. Eukaroytic toxins (mostly from snake, scorpion, spider, anemonia or conus shells) are generally secreted in the venom of the animal. Bacterial toxins are frequently the major cause of the pathogenicity of the organism in question.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9405"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:801"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>TPQ</name> <name>Topaquinone</name> <rdfs:comment>Protein which is posttranslationally modified on a tyrosine residue to form TPQ. This modification of a strictly conserved active-site tyrosine residue proceeds via the hydroxylation of tyrosine to Topa (Trihydroxyphenylalanine) and then to TPQ (Topaquinone). It is a self-processing pathway requiring only the protein, copper and molecular oxygen. TPQ is the redox cofactor of most copper-containing amine oxidases.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:802"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>TPR repeat</name> <name>Tetratricopeptide repeat</name> <rdfs:comment>Protein with at least one TPR repeat. The TPR repeat of typically 34 amino acids was first described in the yeast cell division control protein 23 (CDC23) and later found to occur in a large number of proteins. A function for this repeat seems to be protein-protein interaction.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:803"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Trans-acting factor</name> <rdfs:comment>Protein which regulates transcription by binding to the DNA sequences, in the vicinity of the structural portion of a gene, which are required for gene expression. These DNA sequences, e.g. promoter sequences or operators are called cis-acting elements.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:3700"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:804"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Transcription</name> <rdfs:comment>Protein involved in the transfer of genetic information from DNA to messenger RNA (mRNA) by DNA-directed RNA polymerase.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6350"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:805"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Transcription regulation</name> <rdfs:comment>Protein involved in the regulation of the transcription process.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:804"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6355"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:806"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Transcription termination</name> <rdfs:comment>Protein involved in transcription termination.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:805"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6353"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:807"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Transducer</name> <rdfs:comment>Protein which converts an input signal into an output signal of a different form.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:4871"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7165"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:808"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Transferase</name> <rdfs:comment>Enzyme that transfers a chemical group, e.g. a methyl group or a glycosyl group from one compound (donor) to another compound (acceptor).</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:16740"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:809"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Transit peptide</name> <rdfs:comment>Proteins which have an N-terminal presequence which directs them to an organelle (chloroplast, mitochondria, microbody, cyanelle). The transit peptide is required for their transport across the relevant membranes from their site of synthesis in the cytoplasm.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:810"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Translation regulation</name> <rdfs:comment>Protein involved in the regulation of peptide formation on ribosomes, directed by messenger RNA (mRNA).</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6417"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6445"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:812"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Transmembrane</name> <rdfs:comment>Protein with at least one transmembrane domain, a membrane-spanning alpha-helical or beta-sheet (in the case of porins) domain embedded in a membrane.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:16021"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:813"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Transport</name> <rdfs:comment>Protein involved in the transport of a molecule (metabolite, protein, etc), a ion or an electron across cell membranes, inside the cell or in a tissue fluid.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6810"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:814"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Transposable element</name> <name>Transposon</name> <rdfs:comment>Protein encoded by a transposable element, or transposon, a mobile DNA segment that can replicate and insert a copy at another site within the genome. Simple transposons only contains genes needed for insertion. More complex types also carry genes with functions unrelated to insertion, e.g. genes for resistance to antibiotics or heavy metals.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6313"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:815"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Transposition</name> <rdfs:comment>Protein involved in the movement of a specific DNA sequence - generally known as a transposable element or transposon - to another location within the genome by replication of the sequence and insertion of the copy at its target site, at random or at some specific site. Proteins necessary for the transposition, such as the enzyme transposase, are usually encoded by the transposable element itself.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6313"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:816"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Tricarboxylic acid cycle</name> <name>TCA cycle</name> <name>Citric acid cycle</name> <name>Krebs cycle</name> <rdfs:comment>Protein involved in the tricarboxylic acid cycle, a series of metabolic reactions in aerobic cellular respiration, which occurs in the mitochondria of animals and plants and in which acetyl-CoA, formed from pyruvate produced during glycolysis, is completely oxidized to CO2 via the interconversion of various carboxylic acids. It results in the reduction of NAD and FAD to NADH and FADH2, whose reducing power is then used indirectly in the synthesis of ATP by oxidative phosphorylation. The TCA cycle also provides intermediates for many other biosynthetic processes.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6099"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:817"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Trimethoprim resistance</name> <rdfs:comment>Protein that confers, on bacteria or other microorganisms, the ability to withstand the antibacterial agent trimethroprim that inhibits dihydrofolate reductase (DHFR), an enzyme required for de novo glycine and purine synthesis.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:46"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:46677"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:818"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Triplet repeat expansion</name> <rdfs:comment>Protein encoded by a gene which has a triplet repeat expansion, i.e. the increase of triplet (trinucleotide) repeats within the gene sequence. The length of such repeats is frequently polymorphic, and there is often a correlation between repeat length and disease severity.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:621"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:819"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>tRNA processing</name> <name>Transfer RNA processing</name> <name>tRNA biosynthesis</name> <rdfs:comment>Protein involved in the processing of the primary tRNA transcript to yield a functional tRNA. Transcription of tRNA genes results in a large precursor molecule which may even contain sequences for several tRNA molecules. This primary transcript is subsequently processed by cleavage and by modification of the appropriate bases.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:8033"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:820"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>tRNA-binding</name> <name>Transfer RNA binding</name> <rdfs:comment>Protein which binds transfer RNA, for example some ribosomal proteins or some aminoacyl-tRNA synthetases.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:694"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:49"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:821"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Trypanosomiasis</name> <rdfs:comment>Protein involved in trypanosomiasis, a human or animal disease caused by Trypanosoma, a genus of parasitic flagellate protozoa. Such diseases include African sleeping sickness, Nagana and American Chagas' disease.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:822"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Tryptophan biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of the aromatic amino acid tryptophan (Trp) in bacteria, fungi and plants from chorismate. Trp is needed to synthesize proteins and as a precursor to niacin, serotonin and melatonin.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:57"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:162"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:823"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Tryptophan catabolism</name> <rdfs:comment>Protein involved in the degradation of the aromatic amino acid tryptophan (Trp).</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6569"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:824"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>TTQ</name> <name>Tryptophan tryptophylquinone</name> <rdfs:comment>Protein which contains at least one tryptophan tryptophylquinone (TTQ) cross-link modification. TTQ, the cofactor of methylamine dehydrogenase (MADH), is formed by oxidation of the indole ring of a tryptophan to form tryptophylquinone followed by covalent cross-linking with another tryptophan residue. MADH converts primary amines to their corresponding aldehydes plus ammonia. During the catalytic cycle, TTQ mediates electron transfer from the substrate to a copper protein, amicyanin. These electrons are transferred to the respiratory chain via a C-type cytochrome.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:825"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Tumor antigen</name> <name>Cancer antigen</name> <rdfs:comment>Protein on the surfaces of tumor cells detected by cell-mediated immunity. Different categories of tumor antigens which induce cytotoxic T lymphocyte (CTL) responses in vitro and in vivo, have been identified. These are, namely, "cancer testis" (CT) antigens expressed in different tumours and normal testis, melanocyte differentiation antigens, point mutations of normal genes, self antigens that are overexpressed in malignant tissues and viral antigens.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:48"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:826"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Tungsten</name> <rdfs:comment>Protein which binds at least one tungsten atom, or protein whose function is tungsten-dependent. Tungsten is a metallic element, chemical symbol W.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:902"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Two-component regulatory system</name> <name>Two-component system</name> <name>Phosphorelay system</name> <name>Phospho-relay system</name> <name>Two-component sensory transduction system</name> <name>Two-component signal transduction system</name> <rdfs:comment>Protein involved in a system responding to environmental changes characterized usually by a sensor kinase in the cell membrane that phosphorylates itself in response to a signal and a response regulator to which the phosphoryl group is transferred. The responder is typically a DNA-binding protein that regulates transcription. Several of these systems are quite complex, involving many proteins in a signaling cascade or contributing to several responses simultaneously. They are involved in a variety processes such as chemotaxis, osmoregulation, magnesium transport, pH tolerance, sporulation, or response of virulent species to host cell's environments.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:716"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:827"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Tyrosine biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of the aromatic amino acid tyrosine. In microorganisms and plants, tyrosine is synthesized from chorismate via a simple pathway using prephenate as an intermediate. In rat, this nonessential amino acid is produced by hydroxylating the essential amino acid phenylalanine.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:57"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6571"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:828"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Tyrosine catabolism</name> <rdfs:comment>Protein involved in the degradation of the aromatic amino acid tyrosine. In mammals, tyrosine degradation is catalyzed by a series of 5 enzymatic reactions which yield acetoacetate (ketogenic) and the Krebs cycle intermediate fumarate (glucogenic).</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6572"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:830"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Ubiquinone</name> <name>Coenzyme Q</name> <name>CoQ</name> <rdfs:comment>Protein involved in ubiquinone synthesis or protein which interacts with ubiquinone. This fat soluble benzoquinone has a long isoprenoid side chain, which varies in length depending on the species. For example, S.cerevisiae has CoQ-6, E.coli has CoQ-8, rat and R.capsulatus have CoQ-9 and S.pombe, G.suboxydans and humans have CoQ-10. Ubiquinone is a carrier of hydrogen atoms (protons plus electrons) and functions as an ubiquitous coenzyme in redox reactions, where it is first reduced to the enzyme-bound intermediate radical semiquinone and in a second reduction to ubiquinol (Dihydroquinone; CoQH2). Ubiquinone is not tightly bound or covalently linked to a protein complex but is very mobile.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:831"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Ubiquinone biosynthesis</name> <name>Coenzyme Q biosynthesis</name> <name>CoQ biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of ubiquinone which involves the conversion of chorismate into 4-hydroxy-benzoate, to which is added six to ten isoprene units to form polyprenyl phenol. The addition of a further oxygen atom at C3, followed by the transfer of three methyl groups from S-adenosine methionine gives rise to ubiquinol, which is further reduced to ubiquinone (6-polyprenyl-2,3-dimethoxy-5-methyl-1,4-benzoquinone).</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6744"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:832"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Ubl conjugation</name> <name>Ubiquitin conjugation</name> <name>Ubiquitination</name> <name>Ubiquitinylation</name> <name>Sumoylation</name> <name>Ubiquitin-like modifier conjugation</name> <rdfs:comment>Protein which is posttranslationally modified by the attachment of at least one ubiquitin-like modifier protein, such as ubiquitin, SUMO, APG12, URM1 or RUB1. Ubiquitin, for example, is linked through a thioester bond between its C-terminus and the epsilon group of a lysine residue present on either another ubiquitin-like modifier protein or a target protein.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:833"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Ubl conjugation pathway</name> <name>Ubiquitin conjugation pathway</name> <name>Ubiquitin-like modifier conjugation pathway</name> <rdfs:comment>Protein involved in ubiquitin-like modifier processing, activation, conjugation or deconjugation such as Ubl-activating enzymes (E1s), Ubl-conjugating enzymes (E2s), Ubl-protein ligases (E3s), some thiol proteases (Ubiquitin carboxyl-terminal hydrolases (UCH), Ubiquitin-specific processing proteases (UBP) and ubiquitin-like proteases) and the ubiquitin-like modifier proteins. Besides signaling proteolysis, ubiquitination for example can be a signal for trafficking, kinase activation and other nonproteolytic fates.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:834"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Unfolded protein response</name> <name>UPR</name> <name>ER stress response</name> <name>ER stress pathway</name> <rdfs:comment>Protein involved in the unfolded protein response. An accumulation of unfolded proteins in the ER lumen triggers a stress response, resulting in the transcriptional induction in the nucleus of a set of genes, whose products are involved in protein folding, assembly and modification as well as in phospholipid biosynthesis. The unfolded protein response (UPR) is the intracellular pathway that mediates signaling from the endoplasmic reticulum (ER) to the nucleus. UPR is also tightly linked to ER-associated protein degradation (ERAD). UPR is a ubiquitous mechanism observed in all eukaryotes from humans to yeast.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6986"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:835"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Urea cycle</name> <name>Krebs-Henseleit cycle</name> <rdfs:comment>Protein involved in the urea cycle. This is a metabolic pathway in which ammonia, produced during amino acid degradation, is converted to urea in the liver, through a series of reactions that are distributed between the mitochondrial matrix and the cytosol.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:50"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:836"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Usher syndrome</name> <rdfs:comment>Protein which, if defective, causes Usher syndrome, an autosomal recessive disorder characterized by sensorineural hearing loss and retinitis pigmentosa leading to visual impairment. There are three clinical subtypes: Usher syndrome type 1 (USH1), characterized by congenital profound deafness, constant vestibular dysfunction, and prepubertal onset of retinitis pigmentosa; Usher syndrome type 2 (USH2), associated with moderate to severe hearing loss, normal vestibular function, and onset of retinitis pigmentosa during the second decade of life; and Usher syndrome type 3 (USH3), characterized by progressive hearing loss, variable vestibular function, and adult onset retinitis pigmentosa.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:837"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Vanadium</name> <rdfs:comment>Protein whose function is vanadium-dependent. Vanadium is a transition metal, chemical symbol V.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:838"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Vasoactive</name> <rdfs:comment>Protein which is vasoactive, i.e. has a constricting or dilating effect on the caliber of blood vessels.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:839"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Vasoconstrictor</name> <rdfs:comment>Protein which constricts the caliber of blood vessels.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:838"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:8217"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:840"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Vasodilator</name> <rdfs:comment>Protein which dilates the caliber of blood vessels.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:838"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:8217"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:899"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Viral immunoevasion</name> <name>Viral host defense evasion</name> <name>Viral immune evasion</name> <name>Immunoevasin</name> <rdfs:comment>Viral protein involved in host immune evasion thereby optimizing viral growth and dissemination. Viral immune evasion strategies are typical of viruses which persist in their host throughout life. For example: Herpesviridae, Adenoviridae, Poxviridae and Retroviridae have developed subversions of the MHC class I antigen-presentation pathway. In order to reduce the effectiveness of cytotoxic T-lymphocytes immunity, they express proteins that either down-modulate MHC class I expression (degradation or mislocalization) or interfere with the antigen binding/presentation process (down-regulation of the expression of the transporter associated with antigen processing TAP). Some proteins of these virus families also down-regulate other molecules involved in immune recognition.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:842"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Viral occlusion body</name> <rdfs:comment>Protein component of the viral occlusion body, a crystalline protein matrix which surrounds the nucleocapsids of some insect viruses (baculoviridae, entomopoxvirinae, cypovirus). Viral occlusion bodies are produced either in the nucleus (baculoviridae) or in the cytoplasm (poxvirinae and cypovirus) of the infected cells and confer resistance to adverse environmental conditions on viruses. They are made from polyhedrin (nucleopolyhedrovirus, cypovirus), granulin (granulovirus), spheroidin and spherulin (entomopox-virinae) and are dissolved by the alkaline pH of the insect gut, thus resulting in the release of infectious virus particles.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19028"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:843"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Virulence</name> <rdfs:comment>Protein involved in virulence, the degree of pathogenicity within a group or species of microorganisms or viruses, as indicated by case fatality rates and/or the ability of the organism to invade the tissues of the host.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9405"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:844"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Vision</name> <rdfs:comment>Protein involved in vision, the special sense by which objects in the external environment are perceived by the light they give off or reflect, which stimulates the photoreceptors in the retina.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7601"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:845"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Vitamin A</name> <name>Retinol</name> <rdfs:comment>Protein which interacts with any form of the fat-soluble vitamin A. There are three active forms of vitamin A: retinol, retinal (retinaldehyde) and retinoic acid, which are all derived from the plant beta-carotene (provitamin A). Vitamin A is essential to night vision and is also required for epithelium differentiation, bone development, reproduction and the immune response. Symptoms associated with a deficiency of vitamin A are night blindness, changes in the eyes, poor bone development, weak tooth enamel and dry skin.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:846"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Vitamin B12</name> <name>Cobalamin</name> <rdfs:comment>Protein which contains at least one cobalamin as cofactor, e.g. methylmalonyl-CoA mutase, or which binds and/or transports cobalamin, such as intrinsic factor or transcobalamins. Cobalamin, which is synthesized by microorganisms, has equatorial sites occupied by a tetrapyrrol ring structure (corrin ring) with a cobalt(III) ion in the center, one axial site occupied by an intramolecularly-bound dimethylbenzimidazole and the other axial site occupied by a number of different ligands such as water (aquacobalamin), cyanide (cyanocobalamine=vitamin B12), glutathione (glutathionylcobalamine), 5'deoxyadenosine (adenosylcobalamine=coenzyme B12) or a methyl group (methylcobalamin). It is a prosthetic group of certain mammalian enzymes, where it is essential for the normal maturation and development of erythrocytes. A deficiency in the diet or more frequently the failure to absorb the vitamin give rise to pernicious anemia.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:847"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Vitamin C</name> <name>Ascorbic acid</name> <rdfs:comment>Protein which contains at least one vitamin C as cofactor. This water-soluble vitamin is a reducing agent in a number of reactions. As cofactor, it is required for the hydroxylation of proline residues in collagen, and in many other metabolic reactions such as in the catabolism of tyrosine and the synthesis of bile acids. Deficiency in vitamin C leads to the disease scurvy.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:848"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Vitamin D</name> <rdfs:comment>Protein which interacts with any form of the fat-soluble vitamin D or protein whose transcription is regulated by the biologically active form of vitamin D, i.e. 1,25-dihydroxy vitamin D3 (1,25 dihydroxycholecalciferol) also termed calcitriol. Active calcitriol is derived from ergosterol (produced in plants) and 7-dehydrocholesterol (produced in the skin). Ergocalciferol (vitamin D2) and cholecalciferol (vitamin D3) are formed by UV irradiation of ergosterol and 7-dehydrocholesterol, respectively, and processed by the same enzymatic pathway in the body to D2-calcitriol and D3-calcitriol. Deficiency in vitamin D leads to the disease rickets, in children, and osteomalacia, in adults.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:849"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Vitamin K</name> <rdfs:comment>Protein which undergoes vitamin-K dependent carboxylation of glutamate. There are two natural forms, which are phylloquinone (vitamin K1 or phytylmenaquinone) in green vegetables and menaquinone (vitamin K2 or menaquinone-n, depending of the number of isoprene units of the side-chain or MK-n) in intestinal bacteria, as well as one synthetic provitamin form, menadione (vitamin K3). In infants, the primary symptom of a deficiency of this fat-soluble vitamin is a hemorrhagic syndrome.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:850"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>VLDL</name> <rdfs:comment>Protein present in particles of Very Low-Density Lipoproteins or protein which interacts with them. VLDL are composed of 50% triacylglycerols, 12% cholesteryl esters, 7% free cholesterol, 18% phospholipids, and 10% proteins including apoB-100, apoC-I, apoC-II, apoC-III and apoE. Excess fatty acids or carbohydrate in the diet can be converted into triacylglycerols in the liver and packaged into VLDL. These lipoproteins are transported by the blood to muscle and adipose tissue, where activation of lipoprotein lipase by apoC-II causes the release of free fatty acids from the triacylglycerols of the VLDL.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5319"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:851"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Voltage-gated channel</name> <name>Voltage-gated ion channel</name> <name>Voltage-gated cation channel</name> <rdfs:comment>Protein which is a component of a voltage-gated channel. Voltage-gated ion channels are responsible for the electrical activity in a variety of cell types. They probably exist in all life forms.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:813"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5244"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:852"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>von Willebrand disease</name> <rdfs:comment>Protein which, if defective, causes von Willebrand disease, a hemorrhagic disorder in which the von Willebrand factor is either quantitatively or qualitatively abnormal. Usually inherited as an autosomal dominant trait though rare kindreds are autosomal recessive. Symptoms vary depending on severity and disease type but may include prolonged bleeding time, deficiency of factor VIII and impaired platelet adhesion.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:897"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Waardenburg syndrome</name> <name>WS</name> <rdfs:comment>Protein which, if defective, causes Waardenburg syndrome (WS), an autosomal dominant disorder, characterized by non progressive sensory-neural deafness, as well as pigmentary changes of the irides, hair and skin; each of these features may be uni- or bilateral. On the basis of the presence or absence of dystopia canthorum (lateral displacement of the inner corner of the eye), Waardenburg syndrome type I (WS1) and type II (WS2) are distinguished. Additionally, Waardenburg syndrome type III (WS3), also known as Klein-Waardenburg syndrome, is characterized by WS1 and upper-limb involvement including muscle hypoplasia with joint contractures. Waardenburg syndrome type IV (WS4), also known as Waardenburg-Shah syndrome, is characterized by features of WS2 and Hirschsprung disease.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:853"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>WD repeat</name> <name>WD-40 repeat</name> <name>Trp-Asp repeat</name> <rdfs:comment>Protein which contains at least one WD repeat, a conserved domain of about 40 amino acids in length. Most copies contain a central conserved Trp-Asp motif.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:854"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Whey</name> <rdfs:comment>Protein present in the whey, the fluid fraction of milk after precipitation of casein by acidification. It contains 4-5% lactose, 0.8% protein (whey protein) and 0.2-0.8% lactic acid.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:855"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Whooping cough</name> <rdfs:comment>Protein involved in the induction of whooping cough, a respiratory infection caused by the very small Gram-negative aerobic coccobacillus Bordetella pertussis. It is characterized by paroxysmal coughing often ending in a characteristic inspiratory gasp (whoop). The bacterium is a pathogen for humans and possibly for higher primates.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:856"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Williams-Beuren syndrome</name> <name>WBS</name> <rdfs:comment>Protein which, if defective, causes Williams-Beuren syndrome (WBS), a contiguous gene deletion syndrome involving genes from chromosome band 7q11.23. It is a rare developmental autosomal dominant disorder characterized by cardiovascular abnormalities, elfin face, mental and statural deficiency, characteristic dental malformation, and infantile hypercalcemia.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:879"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Wnt signaling pathway</name> <name>Wnt signalling pathway</name> <name>Wnt signal transduction pathway</name> <name>Wnt signaling cascade</name> <rdfs:comment>Protein involved in the Wnt signaling pathway. Wnts are a large family of cysteine-rich secreted glycoproteins that control development in organisms ranging from nematodes to mammals. Wnt genes are defined by sequence homology to the original members of the family, Wnt1 in the mouse and wingless (wg) in Drosophila. Wnt signaling is a very complex pathway which includes numerous ligands, receptors and transcriptional effectors. There is a well-characterized canonical pathway as well as diverse, less-characterized noncanonical pathways. Several components of Wnt signaling are implicated in the genesis of human cancer.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:16055"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:857"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Xeroderma pigmentosum</name> <rdfs:comment>Protein which, if defective, causes xeroderma pigmentosum, an autosomal recessive disease characterized by extreme photosensitivity to ultraviolet light and the development of multiple skin cancers. It is caused by a defect in the excisional repair of ultraviolet-damaged DNA.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:858"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Xylan degradation</name> <name>Xylan hydrolysis</name> <rdfs:comment>Protein involved in the hydrolysis of xylan to xylose and other sugars. Xylan is a major component of hemicellulose, which is the second most common plant material in nature. The structures of xylans are complex, and several enzymes are involved in their breakdown. Xylan degrading enzymes are produced by a variety of microorganisms.</rdfs:comment> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5975"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:859"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Xylose metabolism</name> <rdfs:comment>Protein involved in the biochemical reactions with the 5-carbon sugars xylose or xylulose. Xylose is the second most abundant sugar found in hardwood and agricultural residues.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:119"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5996"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:860"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Yolk</name> <rdfs:comment>Protein present in the yolk, the nutrient portion of an egg that supplies food to the developing embryo.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:861"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Zellweger syndrome</name> <name>Cerebrohepatorenal syndrome</name> <name>CHR syndrome</name> <name>ZWS</name> <rdfs:comment>Protein which, if defective, causes Zellweger syndrome, a fatal inherited human disease associated with severe abnormalities in the brain, liver and kidney and death soon after birth. This disease is characterized by the presence of empty peroxisomes in the cells due to impaired transport of peroxisomal proteins into the peroxisomes.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:862"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Zinc</name> <rdfs:comment>Protein which binds at least one zinc atom, or protein whose function is zinc-dependent. Zinc is a metallic trace element, chemical symbol Zn.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:863"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Zinc-finger</name> <rdfs:comment>Protein which contains at least one zinc-finger. A small, functional, independently folded domain that requires coordination of one or more zinc ions to stabilize its structure. Zinc-fingers vary widely in structure, as well as in function, which ranges from DNA or RNA binding to protein-protein interactions and membrane association.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:479"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:864"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Zinc transport</name> <rdfs:comment>Protein involved in the transport of zinc.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:813"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6829"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:865"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Zymogen</name> <name>Proenzyme</name> <rdfs:comment>The enzymatically inactive precursor of mostly proteolytic enzymes.</rdfs:comment> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:1"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>2Fe-2S</name> <rdfs:comment>Protein which contains at least one 2Fe-2S iron-sulfur cluster: 2 iron atoms complexed to 2 inorganic sulfides and 4 sulfur atoms of cysteines from the protein.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:411"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:3"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>3Fe-4S</name> <rdfs:comment>Protein which contains at least one 3Fe-4S iron-sulfur cluster: 3 iron atoms complexed to 4 inorganic sulfides and 3 sulfur atoms of cysteines from the protein. In a number of iron-sulfur proteins, the 4Fe-4S cluster can be reversibly converted by oxidation and loss of one iron ion to a 3Fe-4S cluster.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:411"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:4"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>4Fe-4S</name> <rdfs:comment>Protein which contains at least one 4Fe-4S iron-sulfur cluster: 4 iron atoms complexed to 4 inorganic sulfides and 4 sulfur atoms of cysteines from the protein. In a number of iron-sulfur proteins, the 4Fe-4S cluster can be reversibly converted by oxidation and loss of one iron ion to a 3Fe-4S cluster.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:411"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:12"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Acyltransferase</name> <rdfs:comment>Enzyme catalyzing the transfer of acyl- (RCO-) groups.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:808"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:8415"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:29"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Amino-acid transport</name> <name>Amino acid transport</name> <rdfs:comment>Protein involved in the transport of amino acids.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:813"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:15171"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6865"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:30"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Aminoacyl-tRNA synthetase</name> <name>Aminoacyl-tRNA synthase</name> <name>Aminoacyl-tRNA ligase</name> <name>Amino acid translase</name> <rdfs:comment>Enzyme that activates an amino acid for translation by forming an aminoacyladenylate intermediate and then links this activated amino acid to the corresponding tRNA molecule (amino acid-tRNA, aminoacyl-tRNA). In general, a specific aminoacyl-tRNA synthase is available for each amino acid.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:436"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:4812"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:31"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Aminopeptidase</name> <rdfs:comment>Enzyme that catalyzes the removal of amino acids from the N-terminus of peptides and proteins.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:645"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:4177"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:32"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Aminotransferase</name> <name>Transaminase</name> <rdfs:comment>Enzyme that catalyzes the transfer of an alpha-amino group from an amino acid to an alpha-keto acid. The amino group is usually covalently bound by the prosthetic group pyridoxal phosphate.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:808"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:8483"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:50"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Antiport</name> <rdfs:comment>Protein involved in the transport of a solute across a biological membrane coupled, directly, to the transport of a different solute in the opposite direction.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:813"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:15297"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:54"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Arabinose catabolism</name> <rdfs:comment>Protein involved in arabinose breakdown. Arabinose is a 5-carbon aldose sugar found in plant gums, pectins and bacterial cell wall polysaccharides.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:119"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19568"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:62"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Aspartic protease inhibitor</name> <name>Aspartic proteinase inhibitor</name> <name>Aspartyl protease inhibitor</name> <rdfs:comment>Protein which inhibits the catalytic activity of an aspartyl protease, a class of proteases that contains an active site aspartate residue (Asp), e.g. pepsin, HIV retropepsin, renin, etc.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:646"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19828"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:63"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Aspartyl esterase</name> <rdfs:comment>Enzyme which catalyzes the hydrolysis of esters and is characterized by a catalytically active aspartic acid residue in its active site.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:378"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:45330"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:64"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Aspartyl protease</name> <name>Acid protease</name> <name>Aspartic protease</name> <name>Aspartic proteinase</name> <name>Aspartate protease</name> <name>Aspartyl proteinase</name> <rdfs:comment>Proteolytic enzyme with an aspartate residue (Asp) in its active site. There are many families of aspartyl proteases. The most well known one is the pepsin family (A1 in MEROPS classification) which is known to exist in vertebrates, fungi, plants, retroviruses and some plant viruses.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:645"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:4190"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:77"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Bacteriochlorophyll biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of bacteriochlorophylls. These photosynthetic pigments are magnesium-porphyrin complexes with a long hydrophobic terpenoid side chain (the alcohol phytol). Biosynthesis of bacteriochlorophyll is a light-independent reaction.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:149"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:30494"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:84"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Basement membrane</name> <rdfs:comment>Protein which is a component of the basement membrane, an extracellular matrix found under epithelial cells and around smooth and striated muscle cells. This matrix contains intrinsic macromolecular components such as collagen, laminin, and sulfated proteoglycans.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:272"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5604"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:88"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Bile acid catabolism</name> <name>Bile salt catabolism</name> <rdfs:comment>Protein involved in degradation of bile acids. Bile acids, which exist mainly as bile salts, are a family of carboxylic acid derivatives of cholesterol which play an important role in the digestion and absorption of fat. They are made in the liver, stored in the gallblader, and secreted as needed into the intestines.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:753"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:30573"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:89"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Bile pigment</name> <name>Bilin chromophore</name> <rdfs:comment>Protein binding covalently at least one linear tetrapyrrole chromophore, e.g. bilirubin, biliverdin, bilifuscin, biliprasin, choleprasin, bilihumin, and bilicyanin. Bile pigments are produced by breaking down protoporphyrin IX derived from hemoglobin and other heme proteins.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:157"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:98"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Bradykinin</name> <rdfs:comment>Protein containing bradykinin or bradykinin-like peptides. Bradykinin is a vasoactive nonapeptide (RPPGFSPFR) formed by action of proteases on kininogens. It is a potent but short-lived agent of arteriolar dilation and increased capillary permeability. Bradykinin is also released from mast cells during asthma attacks, from gut walls as a gastrointestinal vasodilator, from damaged tissues as a pain signal, and may be a neurotransmitter. It is also a physiologically active component of the kallikrein-kinin system.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:840"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:108"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Calcium channel inhibitor</name> <rdfs:comment>Protein which interferes with the function of calcium channels which are membrane proteins forming a channel in a biological membrane selectively permeable to calcium ions. They are found in various venoms from snakes, scorpions and spiders.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:872"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19855"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:113"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Calvin cycle</name> <name>Calvin-Benson cycle</name> <name>Reductive pentose phosphate cycle</name> <rdfs:comment>Protein involved in the cycle of biochemical reactions responsible for photosynthetic CO(2) fixation in many photosynthetic bacteria and in the stroma of plant chloroplasts. The energy and reducing power for this reaction are provided by the ATP and NADPH produced during the light reactions of photosynthesis. The Calvin cycle is the only photosynthetic pathway in C3 plants. In C4 and CAM plants CO(2) is initially fixed into other organic acids that are subsequently decarboxylated to release CO(2) to the Calvin cycle. Non-photosynthetic organism (e.g. Rhizobium) also use the cycle to fix CO(2).</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:602"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19253"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:116"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>cAMP-binding</name> <name>Cyclic AMP-binding</name> <rdfs:comment>Protein which binds at least one cAMP. cAMP is the abbreviation for cyclic AMP, adenosine 3',5'-cyclic monophosphate.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:547"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:30552"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:121"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Carboxypeptidase</name> <rdfs:comment>Protein that hydrolyzes a C-terminal peptide bond in polypeptide chains.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:645"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:4180"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:123"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Cardiotoxin</name> <rdfs:comment>Protein which has a poisonous or deleterious effect upon the heart or other parts of the cardiovascular system.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:800"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9405"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:136"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Cellulose degradation</name> <rdfs:comment>Protein involved in the conversion of cellulose into D-glucose. Cellulose is the most abundant cell-wall and structural polysaccharide in plants and it is also found in some lower invertebrates. Cellulose is the major component of wood and thus of paper. Cotton is the purest natural form of cellulose. As a raw material, it forms the basis for many derivatives used in chromatography, ion exchange materials, explosives manufacturing and pharmaceutical preparations.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:624"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:30245"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:142"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>cGMP-binding</name> <name>Cyclic GMP-binding</name> <rdfs:comment>Protein which binds at least one cGMP. cGMP is the abbreviation for cyclic GMP, guanosine 3',5'-cyclic monophosphate.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:547"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:30553"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:145"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Chemotaxis</name> <rdfs:comment>Protein involved in the movement of a cell, or organism, along a concentration gradient of a chemotactic agent, such as a protein which causes, mediates or responds to chemotaxis. Chemotactic molecules such as sugars, peptides, cell metabolites, cell-wall or membrane lipids bind to cell surface receptors and trigger activation of intracellular signaling pathways, as well as remodeling of the cytoskeleton through the activation or inhibition of various actin-binding proteins.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:716"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6935"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:146"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Chitin degradation</name> <rdfs:comment>Protein involved in the breakdown of chitin, a linear polysaccharide consisting of (1->4)-beta-linked D-glucosamine residues, most of which are N-acetylated.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:624"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6032"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:869"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Chloride channel</name> <rdfs:comment>Protein which is part of an anion channel found in the plasma lemma and in intracellular membranes. These channels are permeable for various anions, such as iodide, bromide, but also for nitrates, phosphates and even negatively charged amino acids. They are called chloride channels, because chloride is the most abundant anion and the predominant permeating species in all organisms. They have been classified according to their gating mechanisms, which may depend on changes in the transmembrane electric field (voltage-dependent/gated chloride channels, e.g. ClC family), on a protein kinase/nucleotide mediated mechanism (CFTR), an increase in intracellular calcium (calcium activated chloride channels, e.g. CaCC), cell swelling (volume-regulated anion channels, e.g. VRAC) or binding of a ligand, e.g. glycine or - aminobutyric acid (GABA) activated channels. In contrast with cation channels, they are not involved in the initiation or spread of excitation, but in the regulation of excitability in nerve and muscle. They also participate in many housekeeping processes, such as volume regulation, pH regulation in organelles, electrogenesis and control of synaptic activity. The chloride channels are crucial for transepithelial transport and the control of water flow, and often provide unexpected permeation pathways for a large variety of anions.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:813"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:870"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Chloride channel inhibitor</name> <rdfs:comment>Protein which interferes with the function of chloride channels which are membrane proteins forming a channel in a biological membrane selectively permeable to chloride ions.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:872"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19869"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:148"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Chlorophyll</name> <rdfs:comment>Protein which interacts with chlorophyll, the major light-absorbing pigment in most oygenic green organisms. Higher plants contain chlorophyll a and chlorophyll b which are magnesium-porphyrin complexes esterified to a long hydrophobic terpenoid side chain (the alcohol phytol).</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:157"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:152"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Cholesterol biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of cholesterol, the major sterol of higher animals. It is a component of cell membranes, especially of the plasma membrane.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:756"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6695"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:153"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Cholesterol metabolism</name> <rdfs:comment>Protein which participates in the biochemical reactions where cholesterol is involved, including transport. Cholesterol is the major sterol of higher animals and an important component of cell membranes, especially of the plasma membrane.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:753"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:8203"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:183"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Conidiation</name> <rdfs:comment>Protein involved in conidiation, the production of conidia which are asexual fungal spores.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:749"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:30435"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:210"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Decarboxylase</name> <rdfs:comment>Enzyme that belongs to the lyase family and which catalyzes the spliting of CO(2) from the carboxylic group of amino acids, beta-keto acids and alpha-keto acids.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:456"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:16831"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:223"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Dioxygenase</name> <rdfs:comment>Enzyme that reduces molecular oxygen by incorporating both atoms into its substrate(s).</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:560"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:16702"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:224"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Dipeptidase</name> <rdfs:comment>Enzyme that hydrolyzes a dipeptide into its constituent amino acids.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:645"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:16805"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:228"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>DNA excision</name> <rdfs:comment>Protein involved in the repair of damages to one strand of DNA (loss of purines due to thermal fluctuations, formation of pyrimidine dimers by UV irradiation, for instance). The site of damage is recognized, excised by an endonuclease, the correct sequence is copied from the complementary strand by a polymerase and the ends of this correct sequence are joined to the rest of the strand by a ligase. In bacterial systems, the polymerase also acts as endonuclease. Excisase A and other proteins involved in recombination mediate DNA excision; a process whereby abnormal or mismatched nucleotides are enzymatically cut out of a strand of a DNA molecule.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:233"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6284"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:230"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>DNA invertase</name> <rdfs:comment>Specific recombinases which catalyze the inversion of a DNA segment within a nucleoprotein structure termed invertasome.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:233"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:3677"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6310"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:232"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>DNA priming</name> <rdfs:comment>Protein covalently linked to the 5' end of the genome of some viruses or bacteriophages and used as a primer in DNA replication.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:235"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6269"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:239"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>DNA-directed DNA polymerase</name> <rdfs:comment>Enzyme that catalyzes DNA synthesis by addition of deoxyribonucleotide units to a DNA chain using DNA as a template. They can also possess exonuclease activity and therefore function in DNA repair.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:808"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:3887"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:240"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>DNA-directed RNA polymerase</name> <rdfs:comment>Enzymes which catalyze RNA synthesis the by addition of ribonucleotide units to a RNA chain using DNA as a template. They can initiate a chain de novo. Prokaryotes have a single enzyme for the three RNA types that is subject to stringent regulatory mechanisms. Eukaryotes have type I that synthesizes all rRNA except the 5S component, type II that synthesizes mRNA and hnRNA and type III that synthesizes tRNA and the 5S component of rRNA.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:808"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:3899"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:243"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Dynein</name> <rdfs:comment>Large multimeric protein with ATPase activity, responsible for the movement of eukaryotic cilia and flagella (axonemal dynein) and for the intracellular retrograde motility of vesicles, organelles and chromosomes along microtubules (cytosolic dynein). Constitutes the side arms of the outer microtubule doublets in the ciliary axoneme and is responsible for the sliding. Also used for the dynein-associated microtubule-binding proteins (MTBs), e.g. dynactin.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:505"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:3774"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:30286"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:249"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Electron transport</name> <rdfs:comment>Protein involved in the transport of electrons, a process by which electrons are transported through a series of reactions from the reductant, or electron donor, to the oxidant, or electron acceptor, with concomitant energy conversion. Necessary for both photosynthesis and aerobic respiration.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:813"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6118"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:250"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Elliptocytosis</name> <rdfs:comment>Protein which, if defective, causes elliptocytosis, a disorder characterized by variable haemolytic anaemia and elliptical red blood cell shape. Caused by deficiency/dysfunction of red blood cell membrane proteins.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:360"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:251"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Elongation factor</name> <rdfs:comment>Protein that associates with ribosomes cyclically during the elongation phase of protein synthesis, and catalyze formation of the acyl bond between the incoming amino-acid residue and the peptide chain.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:648"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:3746"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:260"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Enterotoxin</name> <rdfs:comment>Toxin which, either when ingested or when produced by enterobacteria within the intestine, acts on the intestinal mucosa and induces diarrhea by perturbing ion and water transport systems.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:800"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9405"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:269"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Exonuclease</name> <rdfs:comment>Enzyme that degrades DNA or RNA by progressively splitting off single nucleotides from one end of the chain.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:378"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:4527"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:275"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Fatty acid biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of fatty acids, long chain organic acids of the general formula CH3(CnHx)COOH. They are constituents of lipids and can be saturated or unsaturated. The esterified forms are important both as energy storage molecules and structural molecules.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:444"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6633"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:276"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Fatty acid metabolism</name> <rdfs:comment>Protein involved in the biochemical reactions with fatty acids. Fatty acids are long chain organic acids of the general formula CH3(CnHx)COOH. They are constituents of lipids and can be saturated or unsaturated. The esterified forms are important both as energy storage molecules and structural molecules.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:443"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6631"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:297"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>G-protein coupled receptor</name> <name>GPCR</name> <name>7TM receptor</name> <rdfs:comment>Receptors which transduce extracellular signals across the cell membrane. At the external side they receive a ligand (a photon in case of opsins), and at the cytosolic side they activate a guanine nucleotide-binding (G) protein. These receptors are hydrophobic proteins that cross the membrane seven times.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:675"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:4930"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7186"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:300"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Galectin</name> <name>Galaptin</name> <name>S-lectin</name> <rdfs:comment>Protein that belongs to the galectin family or galectin-related protein. Galectins are a family of lectins that bind beta-galactosides by means of a carbohydrate recognition domain (CRD) that has many conserved sequence elements. In addition to galectins expressed in vertebrates (fish, birds, amphibians, and mammals), galectins have also been found in invertebrates (worms and insects) and even in protists (sponge and fungus). All galectins share a core sequence consisting of about 130 amino acids, many of which are highly conserved. As many of the galectin relatives may lack galactoside binding activity, therefore, they are referred as galectin-related proteins. Some of these proteins might even recognize other sugar structures instead.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:430"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:326"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Glycosidase</name> <rdfs:comment>Hydrolases which attack glycosidic bonds in carbohydrates, glycoproteins and glycolipids. The glycosidases are not highly specific. Usually they distinguish only the type of bond, e.g. O- or N-glycosidic, and its configuration (alpha or beta).</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:378"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:16798"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5975"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:328"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Glycosyltransferase</name> <rdfs:comment>Enzymes that catalyze the transfer of glycosyl (sugar) residues to an acceptor, both during degradation (cosubstrates= water or inorganic phosphate) and during biosynthesis of polysaccharides, glycoproteins and glycolipids. In biosynthetic glycosyl transfers, the common activated monomeric sugar intermediate is a nucleoside diphosphate sugar.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:808"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:16757"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:332"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>GMP biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of GMP. GMP is the abbreviation for the nucleotide guanosine 5'-monophosphate.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:658"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6177"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:336"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>GPI-anchor</name> <name>Glycosylphosphatidylinositol anchor</name> <name>Glycosylsphingolipidinositol anchor</name> <rdfs:comment>Protein bound to the lipid bilayer of a membrane through either a GPI-anchor (glycosylphosphatidylinositol anchor), a complex oligoglycan linked to a phosphatidylinositol group, or a GPI-like-anchor, a similar complex oligoglycan linked to a sphingolipidinositol group, resulting in the attachment of the C-terminus of the protein to the membrane.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:449"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:347"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Helicase</name> <rdfs:comment>Protein with an helicase activity. Helicases are ATPases that catalyze the unwinding of double-stranded nucleic acids. They are tightly integrated (or coupled) components of various macromolecular complexes which are involved in processes such as DNA replication, recombination, and nucleotide excision repair, as well as RNA transcription and splicing.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:378"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:4386"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:357"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Heparan sulfate</name> <rdfs:comment>Protein containing at least one heparan sulfate, a highly sulfated glycosaminoglycan, closely related to heparin, which consists of repeating units of disaccharides composed of iduronic acid, glucosamine and N-acetylglucosamine.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:654"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:373"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Hyaluronic acid</name> <rdfs:comment>Protein which binds hyaluronic acic, an acidic glycosaminoglycan which consists of repeating units of the disaccharide composed of D-glucuronic acid and N-acetyl-D-glucosamine. This linear polymer is present in cell coats and in the extracellular ground substance of the connective tissues of vertebrates; it also occurs in the synovial fluid in joints and in the vitreous humor of the eye.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:654"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5540"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:392"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Immunoglobulin C region</name> <rdfs:comment>Protein encoded by a constant region gene (C gene / C segment). The constant region is the region of the immunoglobulin (Ig) that is invariable in its amino acid sequence within any class of immunoglobulin. Each immunoglobulin is a tetramer of two identical light chains and two identical heavy chains linked by disulfide bonds. The light chain has one variable region (VL) and one constant region (CL) domain, whereas the heavy chain has one variable region (VH) and three or four constant region domains (CH1 to CH4). Variable and constant regions are encoded by separated genes, called V genes and C genes respectively, which join during cell differentiation.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:393"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:3823"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:396"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Initiation factor</name> <rdfs:comment>Protein which plays an important role in initiating the translation of a mRNA molecule into a polypeptide. Initiation factors help to form the complex between the mRNA and a ribosome.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:648"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:3743"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:397"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Inner membrane</name> <rdfs:comment>Protein found in or associated with the inner membrane. Mitochondria, chloroplasts and some eubacteria are surrounded by a double membrane. The outer membrane is freely permeable to most ions and metabolites, whereas the inner membrane is highly selective. The inner membrane is extensively folded and contains the components of the electron-transport chain, proton-translocating ATPases and specific transport systems.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:472"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:19866"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:406"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Ion transport</name> <rdfs:comment>Protein involved in the transport of ions. Such proteins are usually transmembrane and mediate a movement of ions across cell membranes. Transport may be passive (facilitated diffusion; down the electrochemical gradient), or active (against the electrochemical gradient). Active transport requires energy which may come from light, oxidation reactions, ATP hydrolysis, or cotransport of other ions or molecules.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:813"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6811"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:407"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Ionic channel</name> <rdfs:comment>Protein which is part of a transmembrane protein complex that forms a hydrophilic channel across the lipid bilayer through which specific inorganic ions can diffuse down their electrochemical gradients. The channels are usually gated and only open in response to a specific stimulus, such as a change in membrane potential (voltage-gated) or the binding of a ligand (ligand-gated channel).</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:406"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5216"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:410"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Iron transport</name> <rdfs:comment>Protein involved in the transport of iron.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:813"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6826"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:418"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Kinase</name> <name>Phosphotransferase</name> <rdfs:comment>Enzyme that catalyzes the transfer of phosphate (phosphoryl or pyrophosphoryl transfer) usually from ATP to a second substrate.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:808"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:16301"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:419"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Kinetoplast</name> <rdfs:comment>Protein encoded by the kinetoplast DNA or protein associated with it. The mitochondrial DNA of trypanosomatid protozoa is termed kinetoplast DNA (kDNA). kDNA is a massive network, composed of thousands of topologically interlocked DNA circles. Each cell contains one network condensed into a disk-shaped structure within the matrix of its single mitochondrion. The kDNA circles are of two types, maxicircles present in a few dozen copies and minicircles present in several thousand copies.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:496"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:20023"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:441"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Lipid A biosynthesis</name> <rdfs:comment>Protein involved in the synthesis of lipid A (endotoxin), the hydrophobic anchor of lipopolysaccharide (LPS). Lipid A is a glucosamine-based phospholipid that makes up the outer monolayer of the outer membranes of most Gram-negative bacteria.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:444"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9245"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:445"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Lipid transport</name> <rdfs:comment>Protein involved in the transport of lipids, a diverse class of compounds which are insoluble in water but soluble in organic solvents. They include fats, oils, triacylglycerols, fatty acids, glycolipids, phospholipids and steroids.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:813"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6869"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:482"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Metalloprotease</name> <name>Metallopeptidase</name> <rdfs:comment>Proteolytic enzyme which use a metal for its catalytic mechanism. Most metalloproteases are zinc-dependent, some use cobalt.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:645"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:8237"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:489"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Methyltransferase</name> <rdfs:comment>Enzyme that transfers methyl groups from one compound to another.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:808"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:8168"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:503"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Monooxygenase</name> <rdfs:comment>Enzymes that reduce molecular oxygen by incorporating one oxygen atom into its substrate and the other one in water.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:560"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:4497"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:506"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>mRNA capping</name> <name>Messenger RNA capping</name> <rdfs:comment>Protein involved in the modification (capping) of the 5' end of eukaryotic mRNAs. This modification occurs after the beginning of transcription in the nucleus, and consists of adding a guanosine nucleotide to the 5'-end of mRNAs and then, methylating the guanosine. Capping protects mRNAs at their termini against attack by phosphatases and other nucleases and promotes mRNA function at the level of initiation of translation.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:507"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6370"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:509"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>mRNA transport</name> <name>Messenger RNA transport</name> <rdfs:comment>Protein which is involved in the mechanism of export of mRNAs from the nucleus to the cytoplasm.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:813"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6397"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6406"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:528"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Neurotoxin</name> <rdfs:comment>Proteins, often exquisitely toxic, that inhibit neuronal function. Neurotoxins act typically against sodium channels or block or enhance synaptic transmission. Most venoms contain neurotoxic substances.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:800"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9405"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:532"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Neurotransmitter transport</name> <rdfs:comment>Protein involved in the transport of neurotransmitters. The proteins are released by the axon terminal in response to an electrical impulse and travel across the synapse to either excite or inhibit the target cell.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:813"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6836"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:548"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Nucleotidyltransferase</name> <rdfs:comment>Enzyme which transfers a nucleotide from one compound to another.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:808"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:16779"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:561"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Oxygen transport</name> <rdfs:comment>Protein involved in the transport of oxygen (e.g. hemoglobin and myoglobin).</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:813"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5344"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:15671"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:568"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Pathogenesis-related protein</name> <name>PR protein</name> <rdfs:comment>Protein induced in several plant species when they are infected by viruses, viroids, fungi or bacteria. The occurrence of these proteins is not pathogen-specific, but determined by the type of reaction of the host plant. They form a protective barrier against pathogens by collecting at infection sites and act to decrease susceptibility of plants. They may have anti-fungal or anti-bacterial activity.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:611"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9607"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:571"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Peptide transport</name> <rdfs:comment>Protein involved in the transport of peptides.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:813"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:15198"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6857"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:592"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Phosphate transport</name> <rdfs:comment>Protein involved in the transport of phosphate.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:813"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6817"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:612"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Plant toxin</name> <rdfs:comment>Protein produced by plants and which is toxic to animal or insect cells, e.g. thionins.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:800"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9405"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5576"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:626"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Porin</name> <rdfs:comment>Outer membrane protein which, in dimeric or trimeric form, constitutes a water-filled transmembrane channel ("pore"). This pore allows the passage of ions and numerous other, non-specific molecules through the membrane. Found in the mitochondrial outer membrane of eukaryotes and in many Gram-negative bacteria.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:406"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:15288"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5741"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:16021"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:629"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Postsynaptic neurotoxin</name> <rdfs:comment>Protein which acts as a neurotoxin at the postsynaptic membrane. They bind to acetylcholine receptors and so inhibit their activity.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:800"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7268"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9405"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:45211"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:631"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Potassium channel</name> <rdfs:comment>Protein which is part of a transmembrane protein complex that forms a hydrophilic channel across the lipid bilayer through which potassium ions can diffuse down their electrochemical gradient. The channels are gated and only open in response to a specific stimulus, such as a change in membrane potential (voltage-gated). They are important for the regulation of the resting membrane potential and for the control of the shape and frequency of action potentials.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:406"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:638"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Presynaptic neurotoxin</name> <rdfs:comment>Protein which acts as a neurotoxin at the presynaptic membrane and usually blocks neuromuscular transmission.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:528"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:7268"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9405"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:42734"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:643"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Prostaglandin biosynthesis</name> <rdfs:comment>Protein involved in the biosynthesis of prostaglandins. Prostaglandins are fatty acids composed of 20 carbons with a substituted cyclopentane ring. There are four major classes of prostaglandin, which differ in the position of the double bonds and/or the oxygen substituents on the ring: PGA, PGB, PGE, and PGF. They are found in many mammalian tissues.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:275"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:1516"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:644"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Prostaglandin metabolism</name> <rdfs:comment>Protein involved in a biochemical reaction with prostaglandins. Prostaglandins are fatty acids composed of 20 carbons with a substituted cyclopentane ring. There are four major classes of prostaglandin, which differ in the position of the double bonds and/or the oxygen substituents on the ring: PGA, PGB, PGE, and PGF. They are found in many mammalian tissues.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:276"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6693"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:653"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Protein transport</name> <rdfs:comment>Protein involved in the intracellular transport of proteins from one location to another. All proteins (except the ones synthesized in mitochondria and plastids) are synthesized on ribosomes in the cytosol. Most proteins remain in the cytosol. Proteins with a signal sequence either become plasma membrane components or are exported from the cell of origin.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:813"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:15031"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:679"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Respiratory chain</name> <name>Respiration chain</name> <name>Electron transport chain</name> <rdfs:comment>Protein involved in respiratory chain. In aerobic respiration electrons are transferred from metabolites to molecular oxygen through a series of redox reactions mediated by an electron transport chain. The resulting free energy is used for the formation of ATP and NAD. In anaerobic respiration analogous reactions take place with an inorganic compound other than oxygen as ultimate electron acceptor.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:249"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5746"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:695"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>RNA-directed DNA polymerase</name> <name>Reverse transcriptase</name> <rdfs:comment>Enzyme (EC 2.7.7.49) which synthesizes (-)DNA on a (+)RNA template. They are encoded by the pol gene of retroviruses and by certain retrovirus-like elements.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:808"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:3964"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:696"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>RNA-directed RNA polymerase</name> <rdfs:comment>Enzyme (EC 2.7.7.48) which synthesizes (+)RNA on a (-)RNA template. They are encoded by many viruses.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:808"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:3968"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:708"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Seed storage protein</name> <rdfs:comment>Protein required for the development or growth of seeds.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:758"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:45735"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:723"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Serine/threonine-protein kinase</name> <rdfs:comment>Protein which catalyzes the phosphorylation of serine or threonine residues on target proteins by using ATP as phosphate donor. Such phosphorylation may cause changes in the function of the target protein. Protein kinases share a conserved catalytic core common to both serine/ threonine and tyrosine protein kinases</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:418"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:4674"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:735"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Signal-anchor</name> <rdfs:comment>Single-pass transmembrane protein (type II, III, and IV) possessing a membrane-spanning domain which targets the protein to the ER membrane. Typical features of signal-anchors are the presence of positively charged residues on the amino terminal side followed by an apolar segment of approx. 20 residues. The amino-acid composition is not very different from typical signal sequences.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:812"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:894"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Sodium channel</name> <rdfs:comment>Protein which is part of a cation channel permeable for sodium found in the plasma membrane and in intracellular membranes. Sodium channels have been classified according to their gating mechanisms, which may depend on changes in the transmembrane electric field (voltage-gated sodium channels) or not (non-voltage-gated sodium channels, e.g. degenerins which are permeable also to lithium and potassium). Voltage-gated sodium channels, by opening in response to membrane depolarization, allow sodium entry and thus the propagation of depolarization along the plasma membrane of nerve, muscle and other electrically excitable cells. They play a role in different processes such as sensation, emotions, thought and movement. Another class of sodium channel is the degenerin/epithelial sodium channel (ENaC) superfamily, which is a group of proteins involved in diverse biological processes, including sodium homeostasis, salt taste, nociception, pain transduction, touch sensation and mechanotransduction.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:406"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:739"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Sodium transport</name> <rdfs:comment>Protein involved in the movement of sodium ions across energy-transducing cell membranes. Primary active sodium transport is coupled to an energy-yielding chemical reaction such as ATP hydrolysis. Secondary active transport utilizes the voltage and ion gradients produced by the primary transport to drive the cotransport of other ions or molecules. These may be transported in the same (symport) or opposite (antiport) direction.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:406"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6814"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:740"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Sodium/potassium transport</name> <rdfs:comment>Protein involved in the active transport system which simultaneously moves two potassium ions into the cell and three sodium ions out of the cell.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:739"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6813"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6814"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:741"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>SOS mutagenesis</name> <rdfs:comment>Protein involved in the DNA repair system also known as error-prone repair in which apurinic DNA molecules are repaired by the incorporation of a base that may be the wrong base but that permits replication.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:742"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6280"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:762"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Sugar transport</name> <rdfs:comment>Protein involved in the transfer of sugars across a biological membrane by a carrier protein.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:813"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5351"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:763"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Sulfate respiration</name> <name>Dissimilatory sulfate reduction</name> <rdfs:comment>Protein involved in sulfate respiration, which is the use of sulfate (or other oxidized compounds of sulfur) as the terminal electron acceptor in the anaerobic respiratory metabolism of sulfate-or sulfur-reducing bacteria.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:249"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:9061"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:764"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Sulfate transport</name> <rdfs:comment>Protein involved in the translocation of sulfate, or sulfate-containing compounds, such as thiosulfate, across a biological membrane.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:813"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:8272"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:769"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Symport</name> <rdfs:comment>Protein involved in the transport of solutes across a biological membrane in one direction, which depends on the transport of another solute in the same direction. One molecule can move up an electrochemical gradient because the movement of the other molecule is more favorable. Example: the sodium/glucose co-transport.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:813"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:15293"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:889"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Transcription antitermination</name> <rdfs:comment>Protein involved in transcription antitermination, the process whereby RNA polymerase is allowed to read through specific RNA secondary structures that normally terminate transcription.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:805"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:811"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Translocation</name> <rdfs:comment>Protein involved in the transport of proteins across a membrane. As an example translocation into the nucleus occurs via nuclear pores which allow rapid diffusion of small molecules. Larger molecules (maximum 9 nm) take longer. Translocation into the mitochondria or chloroplast occurs at sites of adhesion between the outer and inner membranes and is driven by ATP hydrolysis as well as the electrochemical gradient of the inner membrane.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:653"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6605"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:829"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Tyrosine-protein kinase</name> <rdfs:comment>Enzyme which catalyzes the transfer of the terminal phosphate of ATP to a specific tyrosine residue on its target protein. Many of these kinases play significant roles in development and cell division. Tyrosine-protein kinases can be divided into two subfamilies: receptor tyrosine kinases, which have an intracellular tyrosine kinase domain, a transmembrane domain and an extracellular ligand-binding domain; and non-receptor (cytoplasmic) tyrosine kinases, which are soluble, cytoplasmic kinases.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:418"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:4713"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:39"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Anion exchange</name> <rdfs:comment>Protein involved in the exchange of anions across a membrane. Anion exchange is a cellular transport function which contributes to the regulation of cell pH and volume by a functionally related anion exchanger protein family.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:406"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:15380"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:76"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Bacteriochlorophyll</name> <rdfs:comment>Protein interacting with bacteriochlorophyll, a photosynthetic pigment found in non-oxygenic photosynthetic bacteria. It is a magnesium-porphyrin complex esterified to a long hydrophobic terpenoid side chain (the alcohol phytol). It differs from chlorophyll of oxygenic organisms in the substituents around the tetrapyrrole nucleus of the molecule, and in the absorption spectra. Different bacteria have different species of bacteriochlorophyll.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:148"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:42314"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:80"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Bacteriocin transport</name> <rdfs:comment>Protein involved in the export of a bacteriocin (bacterial antibiotic).</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:653"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:107"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Calcium channel</name> <rdfs:comment>Cell membrane glycoprotein forming a channel in a biological membrane selectively permeable to calcium ions. Calcium is essential for a variety of bodily functions, such as neurotransmission, muscle contraction and proper heart function.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:407"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5262"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:109"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Calcium transport</name> <rdfs:comment>Protein involved in the transport of calcium ions. Calcium is essential for a variety of bodily functions, such as neurotransmission, muscle contraction and proper heart function.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:406"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6816"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:171"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Cobalt transport</name> <rdfs:comment>Protein involved in the transport of the trace element cobalt, which is a component of vitamin B12.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:406"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:15087"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6824"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:187"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Copper transport</name> <rdfs:comment>Protein involved in the transport of ions of the trace element copper.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:406"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:5375"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:6825"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:375"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Hydrogen ion transport</name> <rdfs:comment>Protein involved in the transport of hydrogen ions across a membrane. Used to power processes such as ATP synthesis and bacterial flagellar rotation.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:406"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:15078"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:15992"/> </rdf:Description> <rdf:Description rdf:about="urn:lsid:uniprot.org:keywords:625"> <rdf:type rdf:resource="urn:lsid:uniprot.org:ontology:Keyword"/> <name>Polysaccharide transport</name> <rdfs:comment>Protein involved in the transport of polysaccharides.</rdfs:comment> <rdfs:subClassOf rdf:resource="urn:lsid:uniprot.org:keywords:762"/> <owl:sameAs rdf:resource="urn:lsid:uniprot.org:go:15774"/> </rdf:Description> </rdf:RDF>