Entry stringlengths 6 10 | Entry Name stringlengths 5 11 | Sequence stringlengths 2 35.2k | EC number stringlengths 7 118 ⌀ | Cofactor stringlengths 38 1.77k ⌀ | Gene Ontology (biological process) stringlengths 18 11.3k ⌀ | Gene Ontology (cellular component) stringlengths 17 1.75k ⌀ | Gene Ontology (molecular function) stringlengths 24 2.09k ⌀ | Pfam stringlengths 8 232 ⌀ | Gene3D stringlengths 10 250 ⌀ | Protein families stringlengths 9 237 ⌀ | Post-translational modification stringlengths 16 8.52k ⌀ | Subcellular location [CC] stringlengths 29 6.18k ⌀ | Catalytic activity stringlengths 64 35.7k ⌀ | Kinetics stringlengths 69 11.7k ⌀ | Pathway stringlengths 27 908 ⌀ | pH dependence stringlengths 64 955 ⌀ | Temperature dependence stringlengths 70 1.16k ⌀ | Function [CC] stringlengths 17 15.3k ⌀ | Organism stringlengths 8 196 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P04066 | FUCO_HUMAN | MRAPGMRSRPAGPALLLLLLFLGAAESVRRAQPPRRYTPDWPSLDSRPLPAWFDEAKFGVFIHWGVFSVPAWGSEWFWWHWQGEGRPQYQRFMRDNYPPGFSYADFGPQFTARFFHPEEWADLFQAAGAKYVVLTTKHHEGFTNWPSPVSWNWNSKDVGPHRDLVGELGTALRKRNIRYGLYHSLLEWFHPLYLLDKKNGFKTQHFVSAKTMPELYDLVNSYKPDLIWSDGEWECPDTYWNSTNFLSWLYNDSPVKDEVVVNDRWGQNCSCHHGGYYNCEDKFKPQSLPDHKWEMCTSIDKFSWGYRRDMALSDVTEESE... | 3.2.1.51 | null | fucose metabolic process [GO:0006004]; glycolipid catabolic process [GO:0019377]; glycosaminoglycan catabolic process [GO:0006027]; glycoside catabolic process [GO:0016139] | azurophil granule lumen [GO:0035578]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; intracellular membrane-bounded organelle [GO:0043231]; lysosomal lumen [GO:0043202]; lysosome [GO:0005764] | alpha-L-fucosidase activity [GO:0004560] | PF01120;PF16757; | 3.20.20.80;2.60.40.1180; | Glycosyl hydrolase 29 family | null | SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:9741689}. | CATALYTIC ACTIVITY: Reaction=an alpha-L-fucoside + H2O = an alcohol + L-fucose; Xref=Rhea:RHEA:12288, ChEBI:CHEBI:2181, ChEBI:CHEBI:15377, ChEBI:CHEBI:28349, ChEBI:CHEBI:30879; EC=3.2.1.51; Evidence={ECO:0000255|PROSITE-ProRule:PRU10054}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12289; Evidence={ECO:0000305... | null | null | null | null | FUNCTION: Alpha-L-fucosidase is responsible for hydrolyzing the alpha-1,6-linked fucose joined to the reducing-end N-acetylglucosamine of the carbohydrate moieties of glycoproteins. {ECO:0000269|PubMed:9741689}. | Homo sapiens (Human) |
P04070 | PROC_HUMAN | MWQLTSLLLFVATWGISGTPAPLDSVFSSSERAHQVLRIRKRANSFLEELRHSSLERECIEEICDFEEAKEIFQNVDDTLAFWSKHVDGDQCLVLPLEHPCASLCCGHGTCIDGIGSFSCDCRSGWEGRFCQREVSFLNCSLDNGGCTHYCLEEVGWRRCSCAPGYKLGDDLLQCHPAVKFPCGRPWKRMEKKRSHLKRDTEDQEDQVDPRLIDGKMTRRGDSPWQVVLLDSKKKLACGAVLIHPSWVLTAAHCMDESKKLLVRLGEYDLRRWEKWELDLDIKEVFVHPNYSKSTTDNDIALLHLAQPATLSQTIVPICL... | 3.4.21.69 | null | blood coagulation [GO:0007596]; negative regulation of apoptotic process [GO:0043066]; negative regulation of blood coagulation [GO:0030195]; negative regulation of coagulation [GO:0050819]; negative regulation of inflammatory response [GO:0050728]; positive regulation of establishment of endothelial barrier [GO:190314... | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; Golgi lumen [GO:0005796] | calcium ion binding [GO:0005509]; serine-type endopeptidase activity [GO:0004252] | PF14670;PF00594;PF00089; | 4.10.740.10;2.10.25.10;2.40.10.10; | Peptidase S1 family | PTM: The vitamin K-dependent, enzymatic carboxylation of some Glu residues allows the modified protein to bind calcium.; PTM: N- and O-glycosylated. Partial (70%) N-glycosylation of Asn-371 with an atypical N-X-C site produces a higher molecular weight form referred to as alpha. The lower molecular weight form, not N-g... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25618265}. Golgi apparatus {ECO:0000269|PubMed:22531345, ECO:0000269|PubMed:25748729}. Endoplasmic reticulum {ECO:0000269|PubMed:22531345, ECO:0000269|PubMed:25748729}. | CATALYTIC ACTIVITY: Reaction=Degradation of blood coagulation factors Va and VIIIa.; EC=3.4.21.69; | null | null | null | null | FUNCTION: Protein C is a vitamin K-dependent serine protease that regulates blood coagulation by inactivating factors Va and VIIIa in the presence of calcium ions and phospholipids (PubMed:25618265). Exerts a protective effect on the endothelial cell barrier function (PubMed:25651845). {ECO:0000269|PubMed:25618265, ECO... | Homo sapiens (Human) |
P04074 | AT1A1_SHEEP | MGKGVGRDKYEPAAVSEHGDKKKAKKERDMDELKKEVSMDDHKLSLDELHRKYGTDLNRGLTTARAAEILARDGPNALTPPPTTPEWVKFCRQLFGGFSMLLWIGAVLCFLAYGIQAATEEEPQNDNLYLGVVLSAVVIITGCFSYYQEAKSSKIMESFKNMVPQQALVIRNGEKMSINAEEVVVGDLVEVKGGDRIPADLRIISANGCKVDNSSLTGESEPQTRSPDFTNENPLETRNIAFFSTNCVEGTARGIVVYTGDRTVMGRIATLASGLEGGQTPIAAEIEHFIHIITGVAVFLGVSFFILSLILEYTWLEAVI... | 7.2.2.13 | null | intracellular potassium ion homeostasis [GO:0030007]; intracellular sodium ion homeostasis [GO:0006883]; potassium ion import across plasma membrane [GO:1990573]; proton transmembrane transport [GO:1902600]; regulation of sodium ion transport [GO:0002028]; sodium ion export across plasma membrane [GO:0036376] | axon [GO:0030424]; basolateral plasma membrane [GO:0016323]; melanosome [GO:0042470]; membrane [GO:0016020]; plasma membrane [GO:0005886]; sarcolemma [GO:0042383]; sodium:potassium-exchanging ATPase complex [GO:0005890] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; metal ion binding [GO:0046872]; P-type sodium:potassium-exchanging transporter activity [GO:0005391] | PF13246;PF00689;PF00690;PF00122; | 3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IIC subfamily | PTM: Phosphorylation on Tyr-10 modulates pumping activity. Phosphorylation of Ser-941 by PKA modulates the response of ATP1A1 to PKC (By similarity). Dephosphorylation by protein phosphatase 2A (PP2A) following increases in intracellular sodium, leading to increase catalytic activity (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8VDN2}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:P06685}; Multi-pass membrane protein {ECO:0000255}. Cell membrane, sarcolemma {ECO:0000250|UniProtKB:P05023}; Multi-pass membrane protein {ECO:0000255}. Cell pr... | CATALYTIC ACTIVITY: Reaction=ATP + H2O + K(+)(out) + Na(+)(in) = ADP + H(+) + K(+)(in) + Na(+)(out) + phosphate; Xref=Rhea:RHEA:18353, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29101, ChEBI:CHEBI:29103, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.13; | null | null | null | null | FUNCTION: This is the catalytic component of the active enzyme, which catalyzes the hydrolysis of ATP coupled with the exchange of sodium and potassium ions across the plasma membrane. This action creates the electrochemical gradient of sodium and potassium ions, providing the energy for active transport of various nut... | Ovis aries (Sheep) |
P04075 | ALDOA_HUMAN | MPYQYPALTPEQKKELSDIAHRIVAPGKGILAADESTGSIAKRLQSIGTENTEENRRFYRQLLLTADDRVNPCIGGVILFHETLYQKADDGRPFPQVIKSKGGVVGIKVDKGVVPLAGTNGETTTQGLDGLSERCAQYKKDGADFAKWRCVLKIGEHTPSALAIMENANVLARYASICQQNGIVPIVEPEILPDGDHDLKRCQYVTEKVLAAVYKALSDHHIYLEGTLLKPNMVTPGHACTQKFSHEEIAMATVTALRRTVPPAVTGITFLSGGQSEEEASINLNAINKCPLLKPWALTFSYGRALQASALKAWGGKKEN... | 4.1.2.13 | null | actin filament organization [GO:0007015]; ATP biosynthetic process [GO:0006754]; binding of sperm to zona pellucida [GO:0007339]; fructose 1,6-bisphosphate metabolic process [GO:0030388]; fructose metabolic process [GO:0006000]; glycolytic process [GO:0006096]; muscle cell cellular homeostasis [GO:0046716]; protein hom... | actin cytoskeleton [GO:0015629]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; ficolin-1-rich granule lumen [GO:1904813]; I band [GO:0031674]; M band [GO:0031430]; membrane [GO:0016020]; nucleus [GO:0005634]; platelet alpha granule lumen [... | actin binding [GO:0003779]; cadherin binding [GO:0045296]; cytoskeletal protein binding [GO:0008092]; fructose binding [GO:0070061]; fructose-bisphosphate aldolase activity [GO:0004332]; identical protein binding [GO:0042802]; RNA binding [GO:0003723]; tubulin binding [GO:0015631] | PF00274; | 3.20.20.70; | Class I fructose-bisphosphate aldolase family | null | SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, I band {ECO:0000250|UniProtKB:P00883}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000250|UniProtKB:P00883}. Note=In skeletal muscle, accumulates around the M line and within the I band, colocalizing with FBP2 on both sides of the Z line in the absence of Ca(2+).... | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate = D-glyceraldehyde 3-phosphate + dihydroxyacetone phosphate; Xref=Rhea:RHEA:14729, ChEBI:CHEBI:32966, ChEBI:CHEBI:57642, ChEBI:CHEBI:59776; EC=4.1.2.13; Evidence={ECO:0000269|PubMed:14766013, ECO:0000269|PubMed:2204832}; PhysiologicalDirection=left-to-right;... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=52 uM for fructose 1,6-bisphosphate (at 30 degrees Celsius) {ECO:0000269|PubMed:14766013}; KM=24 uM for fructose-l,6-bisphosphate {ECO:0000269|PubMed:2204832}; | PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 4/4. | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermal denaturation midpoint (Tm) is 54.4 degrees Celsius. {ECO:0000269|PubMed:14766013}; | FUNCTION: Catalyzes the reversible conversion of beta-D-fructose 1,6-bisphosphate (FBP) into two triose phosphate and plays a key role in glycolysis and gluconeogenesis (PubMed:14766013). In addition, may also function as scaffolding protein (By similarity). {ECO:0000250, ECO:0000269|PubMed:14766013}. | Homo sapiens (Human) |
P04079 | GUAA_ECOLI | MTENIHKHRILILDFGSQYTQLVARRVRELGVYCELWAWDVTEAQIRDFNPSGIILSGGPESTTEENSPRAPQYVFEAGVPVFGVCYGMQTMAMQLGGHVEASNEREFGYAQVEVVNDSALVRGIEDALTADGKPLLDVWMSHGDKVTAIPSDFITVASTESCPFAIMANEEKRFYGVQFHPEVTHTRQGMRMLERFVRDICQCEALWTPAKIIDDAVARIREQVGDDKVILGLSGGVDSSVTAMLLHRAIGKNLTCVFVDNGLLRLNEAEQVLDMFGDHFGLNIVHVPAEDRFLSALAGENDPEAKRKIIGRVFVEVFD... | 6.3.5.2 | null | glutamine metabolic process [GO:0006541]; GMP biosynthetic process [GO:0006177] | cytosol [GO:0005829] | ATP binding [GO:0005524]; GMP synthase (glutamine-hydrolyzing) activity [GO:0003922]; GMP synthase activity [GO:0003921]; identical protein binding [GO:0042802] | PF00117;PF00958;PF02540; | 3.30.300.10;3.40.50.880;3.40.50.620; | null | null | null | CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-glutamine + XMP = AMP + diphosphate + GMP + 2 H(+) + L-glutamate; Xref=Rhea:RHEA:11680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57464, ChEBI:CHEBI:58115, ChEBI:CHEBI:58359, ChEBI:CHEBI:456215; EC=6.3.5.2; Evide... | null | PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1. | null | null | FUNCTION: Catalyzes the synthesis of GMP from XMP. | Escherichia coli (strain K12) |
P04080 | CYTB_HUMAN | MMCGAPSATQPATAETQHIADQVRSQLEEKENKKFPVFKAVSFKSQVVAGTNYFIKVHVGDEDFVHLRVFQSLPHENKPLTLSNYQTNKAKHDELTYF | null | null | adult locomotory behavior [GO:0008344]; negative regulation of peptidase activity [GO:0010466]; negative regulation of proteolysis [GO:0045861] | collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; ficolin-1-rich granule lumen [GO:1904813]; nucleolus [GO:0005730]; nucleus [GO:0005634]; secretory granule lumen [... | cysteine-type endopeptidase inhibitor activity [GO:0004869]; endopeptidase inhibitor activity [GO:0004866]; protease binding [GO:0002020]; RNA binding [GO:0003723] | PF00031; | 3.10.450.10; | Cystatin family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11139332}. Nucleus {ECO:0000269|PubMed:11139332}. | null | null | null | null | null | FUNCTION: This is an intracellular thiol proteinase inhibitor. Tightly binding reversible inhibitor of cathepsins L, H and B. | Homo sapiens (Human) |
P04083 | ANXA1_HUMAN | MAMVSEFLKQAWFIENEEQEYVQTVKSSKGGPGSAVSPYPTFNPSSDVAALHKAIMVKGVDEATIIDILTKRNNAQRQQIKAAYLQETGKPLDETLKKALTGHLEEVVLALLKTPAQFDADELRAAMKGLGTDEDTLIEILASRTNKEIRDINRVYREELKRDLAKDITSDTSGDFRNALLSLAKGDRSEDFGVNEDLADSDARALYEAGERRKGTDVNVFNTILTTRSYPQLRRVFQKYTKYSKHDMNKVLDLELKGDIEKCLTAIVKCATSKPAFFAEKLHQAMKGVGTRHKALIRIMVSRSEIDMNDIKAFYQKMYG... | null | null | actin cytoskeleton organization [GO:0030036]; adaptive immune response [GO:0002250]; alpha-beta T cell differentiation [GO:0046632]; arachidonic acid secretion [GO:0050482]; cell surface receptor signaling pathway [GO:0007166]; cellular response to glucocorticoid stimulus [GO:0071385]; cellular response to hydrogen per... | adherens junction [GO:0005912]; apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome membrane [GO:0031901]; endosome [... | cadherin binding involved in cell-cell adhesion [GO:0098641]; calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; calcium-dependent protein binding [GO:0048306]; lipid binding [GO:0008289]; phosphatidylserine binding [GO:0001786]; phospholipase A2 inhibitor activity [GO:0019834]; phos... | PF00191; | 1.10.220.10; | Annexin family | PTM: Phosphorylated by protein kinase C, EGFR and TRPM7 (PubMed:15485879, PubMed:2457390). Phosphorylated in response to EGF treatment (PubMed:2532504). {ECO:0000269|PubMed:15485879, ECO:0000269|PubMed:2457390, ECO:0000269|PubMed:2532504}.; PTM: Sumoylated. {ECO:0000250|UniProtKB:P10107}.; PTM: Proteolytically cleaved ... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10772777, ECO:0000269|PubMed:19625660}. Cytoplasm {ECO:0000269|PubMed:10772777, ECO:0000269|PubMed:17008549, ECO:0000269|PubMed:19625660}. Cell projection, cilium {ECO:0000250|UniProtKB:P46193}. Cell membrane {ECO:0000269|PubMed:10772777}. Membrane {ECO:0000269|PubMed:1... | null | null | null | null | null | FUNCTION: Plays important roles in the innate immune response as effector of glucocorticoid-mediated responses and regulator of the inflammatory process. Has anti-inflammatory activity (PubMed:8425544). Plays a role in glucocorticoid-mediated down-regulation of the early phase of the inflammatory response (By similarit... | Homo sapiens (Human) |
P04084 | PA2HA_VIPAE | NLFQFGDMILQKTGKEAVHSYAIYGCYCGWGGQGRAQDATDRCCFAQDCCYGRVNDCNPKTATYTYSFENGDIVCGDNDLCLRAVCECDRAAAICLGENVNTYDKNYEYYSISHCTEESEQC | null | null | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Heterodimer: postsynaptic neurotoxin. {ECO:0000269|PubMed:23554559}.; FUNCTION: Monomer: Acidic phospholipase A2 homolog that is non-toxic. {ECO:0000269|PubMed:23554559}. | Vipera ammodytes meridionalis (Eastern sand viper) |
P04085 | PDGFA_HUMAN | MRTLACLLLLGCGYLAHVLAEEAEIPREVIERLARSQIHSIRDLQRLLEIDSVGSEDSLDTSLRAHGVHATKHVPEKRPLPIRRKRSIEEAVPAVCKTRTVIYEIPRSQVDPTSANFLIWPPCVEVKRCTGCCNTSSVKCQPSRVHHRSVKVAKVEYVRKKPKLKEVQVRLEEHLECACATTSLNPDYREEDTGRPRESGKKRKRKRLKPT | null | null | actin cytoskeleton organization [GO:0030036]; angiogenesis [GO:0001525]; animal organ morphogenesis [GO:0009887]; cell activation [GO:0001775]; cell projection assembly [GO:0030031]; cell-cell signaling [GO:0007267]; embryonic lung development [GO:1990401]; hair follicle development [GO:0001942]; lung alveolus developm... | cell surface [GO:0009986]; endoplasmic reticulum lumen [GO:0005788]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796]; Golgi membrane [GO:0000139]; microvillus [GO:0005902]; platelet alpha granule lumen [GO:0031093]; platelet-derived growth factor complex [GO:1990265] | collagen binding [GO:0005518]; growth factor activity [GO:0008083]; identical protein binding [GO:0042802]; platelet-derived growth factor binding [GO:0048407]; platelet-derived growth factor receptor binding [GO:0005161]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803] | PF00341;PF04692; | 2.10.90.10; | PDGF/VEGF growth factor family | null | SUBCELLULAR LOCATION: Secreted. Note=Released by platelets upon wounding. | null | null | null | null | null | FUNCTION: Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Required for normal lung alveolar septum formation during embryogenesis, normal development of the gastrointestina... | Homo sapiens (Human) |
P04088 | INHBB_PIG | MDGLPGRALGAACLLLLAAGWLGPEAWGSPTPPPSPAAPPPPPPPGALGGSQDTCTSCGGFRRPEELGRLDGDFLEAVKRHILNRLQMRGRPNITHAVPKAAMVTALRKLHAGKVREDGRVEIPHLDGHASPGADGQERVSEIISFAETDGLASSRVRLYFFISNEGNQNLFVVQASLWLYLKLLPYVLEKGSRRKVRVKVYFQEPGHGDRWDVVEKRVDLKRSGWHTLPLTEAIQALFERGERRLNLDVQCDGCQELAVVPVFVDPGEESHRPFVVVQARLVDSRHRIRKRGLECDGRTNLCCRQQFFIDFRLIGWSDW... | null | null | activin receptor signaling pathway [GO:0032924]; cellular response to insulin stimulus [GO:0032869]; cellular response to starvation [GO:0009267]; fat cell differentiation [GO:0045444]; negative regulation of follicle-stimulating hormone secretion [GO:0046882]; negative regulation of hepatocyte growth factor production... | extracellular space [GO:0005615]; perinuclear region of cytoplasm [GO:0048471] | cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; hormone activity [GO:0005179]; protein homodimerization activity [GO:0042803] | PF00019;PF00688; | 2.60.120.970;2.10.90.10; | TGF-beta family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, eryth... | Sus scrofa (Pig) |
P04089 | PTHY_RAT | MMSASTMAKVMILMLAVCLLTQADGKPVKKRAVSEIQLMHNLGKHLASVERMQWLRKKLQDVHNFVSLGVQMAAREGSYQRPTKKEENVLVDGNSKSLGEGDKADVDVLVKAKSQ | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; bone mineralization [GO:0030282]; bone resorption [GO:0045453]; calcium ion homeostasis [GO:0055074]; cell-cell signaling [GO:0007267]; homeostasis of number of cells within a tissue [GO:0048873]; intracellular calcium ion homeostas... | extracellular space [GO:0005615] | hormone activity [GO:0005179]; parathyroid hormone receptor binding [GO:0031856]; peptide hormone receptor binding [GO:0051428]; receptor ligand activity [GO:0048018]; type 1 parathyroid hormone receptor binding [GO:0031857] | PF01279; | null | Parathyroid hormone family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: PTH elevates calcium level by dissolving the salts in bone and preventing their renal excretion. Stimulates [1-14C]-2-deoxy-D-glucose (2DG) transport and glycogen synthesis in osteoblastic cells (By similarity). {ECO:0000250}. | Rattus norvegicus (Rat) |
P04090 | REL2_HUMAN | MPRLFFFHLLGVCLLLNQFSRAVADSWMEEVIKLCGRELVRAQIAICGMSTWSKRSLSQEDAPQTPRPVAEIVPSFINKDTETINMMSEFVANLPQELKLTLSEMQPALPQLQQHVPVLKDSSLLFEEFKKLIRNRQSEAADSSPSELKYLGLDTHSRKKRQLYSALANKCCHVGCTKRSLARFC | null | null | female pregnancy [GO:0007565]; positive regulation of angiogenesis [GO:0045766]; positive regulation of gene expression [GO:0010628]; regulation of catalytic activity [GO:0050790] | extracellular region [GO:0005576] | hormone activity [GO:0005179] | PF00049; | 1.10.100.10; | Insulin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Relaxin is an ovarian hormone that acts with estrogen to produce dilatation of the birth canal in many mammals. May be involved in remodeling of connective tissues during pregnancy, promoting growth of pubic ligaments and ripening of the cervix. | Homo sapiens (Human) |
P04094 | PENK_RAT | MAQFLRLCIWLLALGSCLLATVQADCSQDCAKCSYRLVRPGDINFLACTLECEGQLPSFKIWETCKDLLQVSKPEFPWDNIDMYKDSSKQDESHLLAKKYGGFMKRYGGFMKKMDELYPVEPEEEANGGEILAKRYGGFMKKDADEGDTLANSSDLLKELLGTGDNRAKDSHQQESTNNDEDSTSKRYGGFMRGLKRSPQLEDEAKELQKRYGGFMRRVGRPEWWMDYQKRYGGFLKRFAESLPSDEEGESYSKEVPEMEKRYGGFMRF | null | null | aggressive behavior [GO:0002118]; behavioral fear response [GO:0001662]; cellular response to cAMP [GO:0071320]; cellular response to oxidative stress [GO:0034599]; cellular response to transforming growth factor beta stimulus [GO:0071560]; cellular response to virus [GO:0098586]; cellular response to vitamin D [GO:007... | axon [GO:0030424]; axon terminus [GO:0043679]; cell body fiber [GO:0070852]; chromaffin granule lumen [GO:0034466]; dendrite [GO:0030425]; extracellular region [GO:0005576]; neuronal cell body [GO:0043025]; neuronal dense core vesicle lumen [GO:0099013]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; symmetric ... | opioid peptide activity [GO:0001515]; opioid receptor binding [GO:0031628]; receptor ligand activity [GO:0048018] | PF01160; | null | Opioid neuropeptide precursor family | PTM: Proenkephalin-A is cleaved by CTSL to generate Met-enkephalin. {ECO:0000250|UniProtKB:P01211}.; PTM: [Met-enkephalin]: Processed and degraded by ACE. {ECO:0000250|UniProtKB:P01210}.; PTM: [Leu-enkephalin]: Processed and degraded by ACE. {ECO:0000250|UniProtKB:P01210}.; PTM: [Met-enkephalin-Arg-Gly-Leu]: Probably c... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19164277}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule lumen {ECO:0000250|UniProtKB:P01211}. | null | null | null | null | null | FUNCTION: [Met-enkephalin]: Neuropeptide that competes with and mimic the effects of opiate drugs. They play a role in a number of physiologic functions, including pain perception and responses to stress. {ECO:0000250|UniProtKB:P01210}.; FUNCTION: [Leu-enkephalin]: Neuropeptide that competes with and mimic the effects ... | Rattus norvegicus (Rat) |
P04095 | PR2C2_MOUSE | MLPSLIQPCSWILLLLLVNSSLLWKNVASFPMCAMRNGRCFMSFEDTFELAGSLSHNISIEVSELFTEFEKHYSNVSGLRDKSPMRCNTSFLPTPENKEQARLTHYSALLKSGAMILDAWESPLDDLVSELSTIKNVPDIIISKATDIKKKINAVRNGVNALMSTMLQNGDEEKKNPAWFLQSDNEDARIHSLYGMISCLDNDFKKVDIYLNVLKCYMLKIDNC | null | null | blood vessel endothelial cell migration [GO:0043534]; cell projection organization [GO:0030030]; female pregnancy [GO:0007565]; mammary gland development [GO:0030879]; myoblast differentiation [GO:0045445]; negative regulation of myoblast differentiation [GO:0045662]; neuroblast proliferation [GO:0007405]; positive reg... | endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615] | growth factor activity [GO:0008083]; hormone activity [GO:0005179]; prolactin receptor binding [GO:0005148] | PF00103; | 1.20.1250.10; | Somatotropin/prolactin family | PTM: N-glycosylated and sialylated. {ECO:0000269|PubMed:10537154}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10537154, ECO:0000269|PubMed:16876275}. Endoplasmic reticulum {ECO:0000269|PubMed:16876275}. | null | null | null | null | null | FUNCTION: May have a role in embryonic development. It is likely to provide a growth stimulus to target cells in maternal and fetal tissues during the development of the embryo at mid-gestation. May play a role during wound healing and in the hair follicle cycle as a growth factor and/or an angiogenesis factor. May pla... | Mus musculus (Mouse) |
P04104 | K2C1_MOUSE | MSLQCSSRSLCRGGGGSRNFSSGSAGLVSFQRRSTSSSMRRSGGGGGGRFSGGGFCGSSGSGFGSKSLMNLGGGRSISKSVAGGGGSFCGGFGGGSYGGGGFGGGSYGGGGFGGGSFGGGGFGGSGFGGGLGGGGGFGSGGGFGGGRFGSMGPVCPPGGIQEVTINQSLLQPLNVEVDPQIQKVKSQEREQIKSLNDKFASFIDKVRFLEQQNQVLQTKWELLQQVDTTTRTQNLDPFFENYISILRRKVDSLKSDQSRMDSELKNMQDLVEEYRTKYEDEINKRTNAENEFVTIKKDVDSAYMTKVELQAKADALQQDI... | null | null | complement activation, lectin pathway [GO:0001867]; establishment of skin barrier [GO:0061436]; intermediate filament organization [GO:0045109]; keratinization [GO:0031424]; negative regulation of inflammatory response [GO:0050728]; protein heterotetramerization [GO:0051290] | collagen-containing extracellular matrix [GO:0062023]; cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; keratin filament [GO:0045095] | carbohydrate binding [GO:0030246]; protein heterodimerization activity [GO:0046982]; structural constituent of skin epidermis [GO:0030280] | PF00038;PF16208;PF16210; | 1.20.5.170;1.20.5.500;1.20.5.1160; | Intermediate filament family | PTM: Undergoes deimination of some arginine residues (citrullination). {ECO:0000269|PubMed:11841545}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P04264}. Cytoplasm {ECO:0000250|UniProtKB:P04264}. | null | null | null | null | null | FUNCTION: May regulate the activity of kinases such as PKC and SRC via binding to integrin beta-1 (ITB1) and the receptor of activated protein C kinase 1 (RACK1). In complex with C1QBP is a high affinity receptor for kininogen-1/HMWK (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
P04105 | TBAN_PHYPO | MREIISIHIGQAGAQVGNACWELYCLEHGINPDGQMPSDKSVGGGDDAFNTFFSETSSGKHVPRAIYLDLEPTVIDEIRTGTYRQLFHPEQLITGKEDAANNYARGHYTVGKEIVDLCLDRVRKLADQCSGLQGFLVFHSVGGGTGSGFGSLLLERLSVDYGKKSKLDFCVYPSPQVSTAVVEPYNSVLSTHGLLEHTDVAFMLDNEAIYDLCKKSLDIDRPSYANLNRLVAQVISSLTTSLRFDGALNVDINEFQTNLVPYPRIHFMLASYAPVISAEKAFHEQLSVAELTNTVFEPSSMMAKCDPRHGKYMACCLMYR... | 3.6.5.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363}; | microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278] | cytoplasm [GO:0005737]; microtubule [GO:0005874]; nucleus [GO:0005634]; spindle [GO:0005819] | GTP binding [GO:0005525]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; structural constituent of cytoskeleton [GO:0005200] | PF00091;PF03953; | 1.10.287.600;3.30.1330.20;3.40.50.1440; | Tubulin family | PTM: Acetylation of alpha chains at Lys-40 stabilizes microtubules and affects affinity and processivity of microtubule motors. This modification has a role in multiple cellular functions, ranging from cell motility, cell cycle progression or cell differentiation to intracellular trafficking and signaling (By similarit... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, spindle. Nucleus. Note=Mitosis in the slime mold Plasmodium differs from the process in many eukaryotes. The tubulin chains must be transported to the nuclei for intranuclear assembly of the spindle. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P68363}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P6836... | null | null | null | null | FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers a... | Physarum polycephalum (Slime mold) |
P04114 | APOB_HUMAN | MDPPRPALLALLALPALLLLLLAGARAEEEMLENVSLVCPKDATRFKHLRKYTYNYEAESSSGVPGTADSRSATRINCKVELEVPQLCSFILKTSQCTLKEVYGFNPEGKALLKKTKNSEEFAAAMSRYELKLAIPEGKQVFLYPEKDEPTYILNIKRGIISALLVPPETEEAKQVLFLDTVYGNCSTHFTVKTRKGNVATEISTERDLGQCDRFKPIRTGISPLALIKGMTRPLSTLISSSQSCQYTLDAKRKHVAEAICKEQHLFLPFSYKNKYGMVAQVTQTLKLEDTPKINSRFFGEGTKKMGLAFESTKSTSPPK... | null | null | artery morphogenesis [GO:0048844]; cholesterol efflux [GO:0033344]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; cholesterol transport [GO:0030301]; establishment of localization in cell [GO:0051649]; fertilization [GO:0009566]; flagellated sperm motility [GO:0030317]; in utero embr... | chylomicron [GO:0042627]; chylomicron remnant [GO:0034360]; clathrin-coated endocytic vesicle membrane [GO:0030669]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]; endocytic vesicle lumen [GO:0071682]; endoplasmic reticulum exit site [GO:0070971]; endoplasmic reticulum lumen [GO:0005788]; en... | cholesterol transfer activity [GO:0120020]; heparin binding [GO:0008201]; lipase binding [GO:0035473]; low-density lipoprotein particle receptor binding [GO:0050750]; phospholipid binding [GO:0005543] | PF12491;PF06448;PF09172;PF01347; | 2.20.80.10;2.20.50.20;1.25.10.20; | null | PTM: Palmitoylated; structural requirement for proper assembly of the hydrophobic core of the lipoprotein particle. {ECO:0000269|PubMed:10679026}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22580899}. Secreted {ECO:0000269|PubMed:22580899, ECO:0000269|PubMed:26224785}. Lipid droplet {ECO:0000269|PubMed:28183703}. | null | null | null | null | null | FUNCTION: Apolipoprotein B is a major protein constituent of chylomicrons (apo B-48), LDL (apo B-100) and VLDL (apo B-100). Apo B-100 functions as a recognition signal for the cellular binding and internalization of LDL particles by the apoB/E receptor. | Homo sapiens (Human) |
P04115 | FIBG_PETMA | MGRIGTPVFLAFLSALTCSLQVHAQVRDLKQCSNDPEFGRYCPTTCGVADVLSKYAKGVDEDSSFIDSVLTQLAAKHGIVEGNVNIVNEDVRITRDEAQIIKDSGQKTVQKILEEVRILEQIGVSHDAQIQELSEMWRVNQQFVTRLQQQLVDIRQTCSRSCQDTTANKISPITGKDCQQVVDNGGKDSGLYYIKPLKAKQPFLVFCEIENGNGWTVIQHRHDGSVNFTRDWVSYREGFGYLAPTLTTEFWLGNEKIHLLTGQQAYRLRIDLTDWENTHRYADYGHFKLTPESDEYRLFYSMYLDGDAGNAFDGFDFGDD... | null | null | platelet activation [GO:0030168]; protein polymerization [GO:0051258] | fibrinogen complex [GO:0005577] | metal ion binding [GO:0046872]; signaling receptor binding [GO:0005102] | PF08702;PF00147; | 1.20.5.50;3.90.215.10;4.10.530.10; | null | PTM: Conversion of fibrinogen to fibrin is triggered by thrombin, which cleaves fibrinopeptides A and B from alpha and beta chains, and thus exposes the N-terminal polymerization sites responsible for the formation of the soft clot. The soft clot is converted into the hard clot by factor XIIIA which catalyzes the epsil... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:12501189}. | null | null | null | null | null | FUNCTION: Together with fibrinogen alpha (FGA) and fibrinogen beta (FGB), polymerizes to form an insoluble fibrin matrix. Has a major function in hemostasis as one of the primary components of blood clots. {ECO:0000250|UniProtKB:E9PV24}. | Petromyzon marinus (Sea lamprey) |
P04116 | MYPR_BOVIN | MGLLECCARCLVGAPFASLVATGLCFFGVALFCGCGHEALTGTEKLIETYFSKNYQDYEYLINVIHAFQYVIYGTASFFFLYGALLLAEGFYTTGAVRQIFGDYKTTICGKGLSATVTGGQKGRGSRGQHQAHSLERVCHCLGKWLGHPDKFVGITYALTVVWLLVFACSAVPVYIYFNTWTTCQSIAAPSKTSASIGTLCADARMYGVLPWNAFPGKVCGSNLLSICKTAEFQMTFHLFIAAFVGAAATLVSLLTFMIAATYNFAVLKLMGRGTKF | null | null | astrocyte development [GO:0014002]; axon development [GO:0061564]; axon ensheathment [GO:0008366]; cell maturation [GO:0048469]; central nervous system myelination [GO:0022010]; inflammatory response [GO:0006954]; long-chain fatty acid biosynthetic process [GO:0042759]; myelination [GO:0042552]; positive regulation of ... | myelin sheath [GO:0043209]; plasma membrane [GO:0005886] | structural constituent of myelin sheath [GO:0019911] | PF01275; | null | Myelin proteolipid protein family | PTM: Palmitoylated; contains four to five bound palmitate, probably attached in a non-stoichiometric manner. {ECO:0000269|PubMed:1281423, ECO:0000269|PubMed:1695508, ECO:0000269|PubMed:6642431}. | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Myelin membrane {ECO:0000250}. Note=Colocalizes with SIRT2 in internodal regions, at paranodal axoglial junction and Schmidt-Lanterman incisures of myelin sheat. {ECO:0000250}. | null | null | null | null | null | FUNCTION: This is the major myelin protein from the central nervous system. It plays an important role in the formation or maintenance of the multilamellar structure of myelin. | Bos taurus (Bovine) |
P04117 | FABP4_MOUSE | MCDAFVGTWKLVSSENFDDYMKEVGVGFATRKVAGMAKPNMIISVNGDLVTIRSESTFKNTEISFKLGVEFDEITADDRKVKSIITLDGGALVQVQKWDGKSTTIKRKRDGDKLVVECVMKGVTSTRVYERA | null | null | brown fat cell differentiation [GO:0050873]; cellular response to lithium ion [GO:0071285]; cellular response to tumor necrosis factor [GO:0071356]; cholesterol homeostasis [GO:0042632]; fatty acid metabolic process [GO:0006631]; fatty acid transport [GO:0015908]; long-chain fatty acid transport [GO:0015909]; negative ... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | fatty acid binding [GO:0005504]; hormone receptor binding [GO:0051427]; long-chain fatty acid binding [GO:0036041]; long-chain fatty acid transporter activity [GO:0005324] | PF00061; | 2.40.128.20; | Calycin superfamily, Fatty-acid binding protein (FABP) family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17516629, ECO:0000269|PubMed:17761196}. Nucleus {ECO:0000269|PubMed:17516629, ECO:0000269|PubMed:17761196}. Note=Depending on the nature of the ligand, a conformation change exposes a nuclear localization motif and the protein is transported into the nucleus (PubMed:1... | null | null | null | null | null | FUNCTION: Lipid transport protein in adipocytes. Binds both long chain fatty acids and retinoic acid. Delivers long-chain fatty acids and retinoic acid to their cognate receptors in the nucleus. {ECO:0000269|PubMed:12077340, ECO:0000269|PubMed:16574478, ECO:0000269|PubMed:17516629}. | Mus musculus (Mouse) |
P04118 | COL_HUMAN | MEKILILLLVALSVAYAAPGPRGIIINLENGELCMNSAQCKSNCCQHSSALGLARCTSMASENSECSVKTLYGIYYKCPCERGLTCEGDKTIVGSITNTNFGICHDAGRSKQ | null | null | digestion [GO:0007586]; lipid catabolic process [GO:0016042]; lipid metabolic process [GO:0006629]; response to bacterium [GO:0009617]; response to food [GO:0032094] | extracellular region [GO:0005576] | enzyme activator activity [GO:0008047]; lipase binding [GO:0035473] | PF01114;PF02740; | 2.10.80.10; | Colipase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | null | null | null | null | null | FUNCTION: Colipase is a cofactor of pancreatic lipase. It allows the lipase to anchor itself to the lipid-water interface. Without colipase the enzyme is washed off by bile salts, which have an inhibitory effect on the lipase. {ECO:0000269|PubMed:17401110, ECO:0000269|PubMed:26494624}.; FUNCTION: Enterostatin has a bio... | Homo sapiens (Human) |
P04135 | VME1_CVPPU | MKILLILACVIACACGERYCAMKSDTDLSCRNSTASDCESCFNGGDLIWHLANWNFSWSIILIVFITVLQYGRPQFSWFVYGIKMLIMWLLWPVVLALTIFNAYSEYQVSRYVMFGFSIAGAIVTFVLWIMYFVRSIQLYRRTKSWWSFNPETKAILCVSALGRSYVLPLEGVPTGVTLTLLSGNLYAEGFKIAGGMNIDNLPKYVMVALPSRTIVYTLVGKKLKASSATGWAYYVKSKAGDYSTEARTDNLSEQEKLLHMV | null | null | null | host cell cytoplasm [GO:0030430]; host cell Golgi membrane [GO:0044178]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | structural constituent of virion [GO:0039660] | PF01635; | null | Alphacoronaviruses M protein family | null | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04201}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04201}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_04201}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_04201}. Note=Largely embedded in the lipid bilayer. {ECO:0000255... | null | null | null | null | null | FUNCTION: Component of the viral envelope that plays a central role in virus morphogenesis and assembly via its interactions with other viral proteins. {ECO:0000255|HAMAP-Rule:MF_04201, ECO:0000255|PROSITE-ProRule:PRU01275, ECO:0000269|PubMed:11152504}. | Porcine transmissible gastroenteritis coronavirus (strain Purdue) (TGEV) |
P04141 | CSF2_HUMAN | MWLQSLLLLGTVACSISAPARSPSPSTQPWEHVNAIQEARRLLNLSRDTAAEMNETVEVISEMFDLQEPTCLQTRLELYKQGLRGSLTKLKGPLTMMASHYKQHCPPTPETSCATQIITFESFKENLKDFLLVIPFDCWEPVQE | null | null | cell population proliferation [GO:0008283]; cellular response to granulocyte macrophage colony-stimulating factor stimulus [GO:0097011]; cellular response to lipopolysaccharide [GO:0071222]; dendritic cell differentiation [GO:0097028]; embryonic placenta development [GO:0001892]; epithelial fluid transport [GO:0042045]... | extracellular region [GO:0005576]; extracellular space [GO:0005615]; granulocyte macrophage colony-stimulating factor receptor complex [GO:0030526]; intracellular membrane-bounded organelle [GO:0043231]; plasma membrane [GO:0005886] | cytokine activity [GO:0005125]; granulocyte macrophage colony-stimulating factor receptor binding [GO:0005129]; growth factor activity [GO:0008083] | PF01109; | 1.20.1250.10; | GM-CSF family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1737041, ECO:0000269|PubMed:3925454}. | null | null | null | null | null | FUNCTION: Cytokine that stimulates the growth and differentiation of hematopoietic precursor cells from various lineages, including granulocytes, macrophages, eosinophils and erythrocytes. {ECO:0000269|PubMed:3925454}. | Homo sapiens (Human) |
P04147 | PABP_YEAST | MADITDKTAEQLENLNIQDDQKQAATGSESQSVENSSASLYVGDLEPSVSEAHLYDIFSPIGSVSSIRVCRDAITKTSLGYAYVNFNDHEAGRKAIEQLNYTPIKGRLCRIMWSQRDPSLRKKGSGNIFIKNLHPDIDNKALYDTFSVFGDILSSKIATDENGKSKGFGFVHFEEEGAAKEAIDALNGMLLNGQEIYVAPHLSRKERDSQLEETKAHYTNLYVKNINSETTDEQFQELFAKFGPIVSASLEKDADGKLKGFGFVNYEKHEDAVKAVEALNDSELNGEKLYVGRAQKKNERMHVLKKQYEAYRLEKMAKYQ... | null | null | mRNA processing [GO:0006397]; mRNA transport [GO:0051028]; regulation of nuclear-transcribed mRNA poly(A) tail shortening [GO:0060211]; regulation of translational initiation [GO:0006446] | cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; intracellular non-membrane-bounded organelle [GO:0043232]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904]; ribosome [GO:0005840] | molecular condensate scaffold activity [GO:0140693]; mRNA 3'-UTR binding [GO:0003730]; mRNA binding [GO:0003729]; poly(A) binding [GO:0008143]; poly(U) RNA binding [GO:0008266]; promoter-specific chromatin binding [GO:1990841]; ribonuclease inhibitor activity [GO:0008428] | PF00658;PF00076; | 3.30.70.330;1.10.1900.10; | Polyadenylate-binding protein type-1 family | null | SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Predominantly cytoplasmic. Rapidly shuttles between the nucleus and the cytoplasm. Can be exported from the nucleus through at least 2 distinct pathways, the main being dependent on the exportin CRM1, and the second requiring MEX67 and ongoing mRNA export. Import is mediat... | null | null | null | null | null | FUNCTION: Binds the poly(A) tail of mRNA. Appears to be an important mediator of the multiple roles of the poly(A) tail in mRNA biogenesis, stability and translation. In the nucleus, interacts with the nuclear cleavage factor IA (CFIA), which is required for both mRNA cleavage and polyadenylation. Is also required for ... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P04150 | GCR_HUMAN | MDSKESLTPGREENPSSVLAQERGDVMDFYKTLRGGATVKVSASSPSLAVASQSDSKQRRLLVDFPKGSVSNAQQPDLSKAVSLSMGLYMGETETKVMGNDLGFPQQGQISLSSGETDLKLLEESIANLNRSTSVPENPKSSASTAVSAAPTEKEFPKTHSDVSSEQQHLKGQTGTNGGNVKLYTTDQSTFDILQDLEFSSGSPGKETNESPWRSDLLIDENCLLSPLAGEDDSFLLEGNSNEDCKPLILPDTKPKIKDNGDLVLSSPSNVTLPQVKTEKEDFIELCTPGVIKQEKLGTVYCQASFPGANIIGNKMSAIS... | null | null | adrenal gland development [GO:0030325]; apoptotic process [GO:0006915]; astrocyte differentiation [GO:0048708]; cell division [GO:0051301]; cellular response to dexamethasone stimulus [GO:0071549]; cellular response to glucocorticoid stimulus [GO:0071385]; cellular response to steroid hormone stimulus [GO:0071383]; cel... | centrosome [GO:0005813]; chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; mitochondrial matrix [GO:0005759]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; spindle [GO:0005819]; synapse [GO:0045202] | core promoter sequence-specific DNA binding [GO:0001046]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor... | PF02155;PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR3 subfamily | PTM: Acetylation by CLOCK reduces its binding to glucocorticoid response elements and its transcriptional activity. {ECO:0000269|PubMed:19141540, ECO:0000269|PubMed:21980503}.; PTM: Increased proteasome-mediated degradation in response to glucocorticoids (PubMed:11555652). Isoform Alpha-B appears to be more susceptible... | SUBCELLULAR LOCATION: [Isoform Alpha]: Cytoplasm {ECO:0000269|PubMed:15769988, ECO:0000269|PubMed:17635946, ECO:0000269|PubMed:18838540, ECO:0000269|PubMed:27120390, ECO:0000269|PubMed:8621628}. Nucleus {ECO:0000269|PubMed:15769988, ECO:0000269|PubMed:17635946, ECO:0000269|PubMed:18838540, ECO:0000269|PubMed:27120390, ... | null | null | null | null | null | FUNCTION: Receptor for glucocorticoids (GC) (PubMed:27120390). Has a dual mode of action: as a transcription factor that binds to glucocorticoid response elements (GRE), both for nuclear and mitochondrial DNA, and as a modulator of other transcription factors (PubMed:28139699). Affects inflammatory responses, cellular ... | Homo sapiens (Human) |
P04152 | UMUC_ECOLI | MFALCDVNAFYASCETVFRPDLWGKPVVVLSNNDGCVIARNAEAKALGVKMGDPWFKQKDLFRRCGVVCFSSNYELYADMSNRVMSTLEELSPRVEIYSIDEAFCDLTGVRNCRDLTDFGREIRATVLQRTHLTVGVGIAQTKTLAKLANHAAKKWQRQTGGVVDLSNLERQRKLMSALPVDDVWGIGRRISKKLDAMGIKTVLDLADTDIRFIRKHFNVVLERTVRELRGEPCLQLEEFAPTKQEIICSRSFGERITDYPSMRQAICSYAARAAEKLRSEHQYCRFISTFIKTSPFALNEPYYGNSASVKLLTPTQDSR... | null | null | DNA damage response [GO:0006974]; error-prone translesion synthesis [GO:0042276]; SOS response [GO:0009432]; translesion synthesis [GO:0019985] | cytosol [GO:0005829]; DNA polymerase V complex [GO:0009355]; membrane [GO:0016020]; plasma membrane [GO:0005886] | ATP-dependent activity, acting on DNA [GO:0008094]; damaged DNA binding [GO:0003684]; DNA-directed DNA polymerase activity [GO:0003887]; single-stranded DNA binding [GO:0003697] | PF13438;PF00817;PF11799;PF11798; | 3.30.70.270;3.40.1170.60;1.10.150.20;3.30.1490.100; | DNA polymerase type-Y family | null | null | null | null | null | null | null | FUNCTION: Involved in UV protection and mutation. Poorly processive, error-prone DNA polymerase involved in translesion repair (PubMed:10801133). Essential for induced (or SOS) mutagenesis. Able to replicate DNA across DNA lesions (thymine photodimers and abasic sites, translesion synthesis) in the presence of activate... | Escherichia coli (strain K12) |
P04155 | TFF1_HUMAN | MATMENKVICALVLVSMLALGTLAEAQTETCTVAPRERQNCGFPGVTPSQCANKGCCFDDTVRGVPWCFYPNTIDVPPEEECEF | null | null | carbohydrate metabolic process [GO:0005975]; cell differentiation [GO:0030154]; cell population proliferation [GO:0008283]; maintenance of gastrointestinal epithelium [GO:0030277]; negative regulation of cell population proliferation [GO:0008285]; response to immobilization stress [GO:0035902]; response to iron ion [GO... | extracellular region [GO:0005576]; extracellular space [GO:0005615] | growth factor activity [GO:0008083] | PF00088; | 4.10.110.10; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15924415, ECO:0000269|PubMed:3041593}. | null | null | null | null | null | FUNCTION: Stabilizer of the mucous gel overlying the gastrointestinal mucosa that provides a physical barrier against various noxious agents. May inhibit the growth of calcium oxalate crystals in urine. {ECO:0000269|PubMed:16308573}. | Homo sapiens (Human) |
P04156 | PRIO_HUMAN | MANLGCWMLVLFVATWSDLGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHSQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPIIHFGSDYEDRYYRENMHRYPNQVYYRPMDEYSNQNNFVHDCVNITIKQHTVTTTTKGENFTETDVKMMERVVEQMCITQYERESQAYYQRGSSMVLFSSPPVILLISFLIFLIVG | null | null | calcium-mediated signaling using intracellular calcium source [GO:0035584]; cell cycle [GO:0007049]; cellular response to amyloid-beta [GO:1904646]; cellular response to copper ion [GO:0071280]; cellular response to xenobiotic stimulus [GO:0071466]; dendritic spine maintenance [GO:0097062]; intracellular copper ion hom... | cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extrinsic component of membrane [GO:0019898]; Golgi apparatus [GO:0005794]; inclusion body [GO:0016234]; ... | amyloid-beta binding [GO:0001540]; aspartic-type endopeptidase inhibitor activity [GO:0019828]; ATP-dependent protein binding [GO:0043008]; copper ion binding [GO:0005507]; cupric ion binding [GO:1903135]; cuprous ion binding [GO:1903136]; glycosaminoglycan binding [GO:0005539]; identical protein binding [GO:0042802]; ... | PF00377;PF11587; | 1.10.790.10; | Prion family | PTM: The glycosylation pattern (the amount of mono-, di- and non-glycosylated forms or glycoforms) seems to differ in normal and CJD prion. {ECO:0000269|PubMed:12214108}. | SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:19936054}. Golgi apparatus {ECO:0000250|UniProtKB:P04925}. Note=Targeted to lipid rafts via association with the heparan sulfate chains of GPC1. Colocates, in the presence of Cu(2+), to vesicles in para- and perinuclear regions, where bot... | null | null | null | null | null | FUNCTION: Its primary physiological function is unclear. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May promote myelin homeostasis through acting as an agonist for ADGRG6 receptor. May play a role in iron uptake and iron homeostasis. Soluble ... | Homo sapiens (Human) |
P04157 | PTPRC_RAT | MYLWLKLLAFSLALLGPEVFVTGQGTTDDGLDTTEIVLLPQTDPLPARTTEFTPPSISERGNGSSETTYLPGFSSTLMPHLTPQPDSQTPSARGADTQTLSSQADLTTLTAAPSGETDPPGVPEESTVPETFPGGTPILARNSTAPSPTHTSNVSTTDISSGANLTTPAPSTLGFASNTTTSTEIATPQTKPSCDEKFGNVTVRYIYDDSSKNFNANLEGDKKPKCEYTDCEKELKNLPECSQKNVTLSNGSCTPDKIINLDVPPGTHNFNLTNCTPDIEANTSICLEWKIKNKFTCDIQKISYNFRCTPEMKTFALDKH... | 3.1.3.48 | null | alpha-beta T cell proliferation [GO:0046633]; B cell differentiation [GO:0030183]; B cell proliferation [GO:0042100]; B cell receptor signaling pathway [GO:0050853]; bone marrow development [GO:0048539]; calcium-mediated signaling using intracellular calcium source [GO:0035584]; cell cycle phase transition [GO:0044770]... | bleb [GO:0032059]; cell periphery [GO:0071944]; cell surface [GO:0009986]; cytoplasmic side of plasma membrane [GO:0009898]; external side of plasma membrane [GO:0009897]; focal adhesion [GO:0005925]; membrane microdomain [GO:0098857]; membrane raft [GO:0045121]; plasma membrane [GO:0005886] | ankyrin binding [GO:0030506]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; protein kinase binding [GO:0019901]; protein kinase regulator activity [GO:0019887]; protein tyrosine phosphatase activity [GO:0004725]; signaling receptor binding [GO:0005102]; spectrin binding [GO:0030507]; ... | PF12567;PF00041;PF12453;PF00102; | 2.60.40.10;3.90.190.10; | Protein-tyrosine phosphatase family, Receptor class 1/6 subfamily | PTM: Heavily N- and O-glycosylated.; PTM: The cytoplasmic domain contains potential phosphorylation sites. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P08575}; Single-pass type I membrane protein {ECO:0000255}. Membrane raft {ECO:0000250|UniProtKB:P08575}. Synapse {ECO:0000250|UniProtKB:P08575}. Note=Colocalized with DPP4 in membrane rafts. {ECO:0000250|UniProtKB:P08575}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044}; | null | null | null | null | FUNCTION: Protein tyrosine-protein phosphatase required for T-cell activation through the antigen receptor. Acts as a positive regulator of T-cell coactivation upon binding to DPP4. The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the first one. Upon T-ce... | Rattus norvegicus (Rat) |
P04166 | CYB5B_RAT | MATPEASGSGRNGQGSDPAVTYYRLEEVAKRNTAEETWMVIHGRVYDITRFLSEHPGGEEVLLEQAGADATESFEDVGHSPDAREMLKQYYIGDVHPNDLKPKDGDKDPSKNNSCQSSWAYWIVPIVGAILIGFLYRHFWADSKSS | null | null | nitric oxide biosynthetic process [GO:0006809] | intracellular membrane-bounded organelle [GO:0043231]; mitochondrial outer membrane [GO:0005741]; nitric-oxide synthase complex [GO:1903958] | enzyme activator activity [GO:0008047]; heme binding [GO:0020037]; metal ion binding [GO:0046872]; nitrite reductase (NO-forming) activity [GO:0050421]; ubiquinol-cytochrome-c reductase activity [GO:0008121] | PF00173; | 3.10.120.10; | Cytochrome b5 family | null | SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:6840088}. | null | null | null | null | null | FUNCTION: Cytochrome b5 is a membrane-bound hemoprotein functioning as an electron carrier for several membrane-bound oxygenases. | Rattus norvegicus (Rat) |
P04167 | CP2B2_RAT | MEPSILLLLALLVGFLLLLVRGHPKSRGNFPPGPRPLPLLGNLLQLDRGGLLNSFMQLREKYGDVFTVHLGPRPVVMLCGTDTIKEALVGQAEDFSGRGTIAVIEPIFKEYGVIFANGERWKALRRFSLATMRDFGMGKRSVEERIQEEAQCLVEELRKSQGAPLDPTFLFQCITANIICSIVFGERFDYTDRQFLRLLELFYRTFSLLSSFSSQVFEFFSGFLKYFPGAHRQISKNLQEILDYIGHIVEKHRATLDPSAPRDFIDTYLLRMEKEKSNHHTEFHHENLMISLLSLFFAGTETGSTTLRYGFLLMLKYPHV... | 1.14.14.1 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; | epoxygenase P450 pathway [GO:0019373]; nicotine metabolic process [GO:0018933]; response to calcium ion [GO:0051592]; response to metal ion [GO:0010038]; response to organic cyclic compound [GO:0014070]; xenobiotic metabolic process [GO:0006805] | cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231] | arachidonic acid epoxygenase activity [GO:0008392]; aromatase activity [GO:0070330]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity [GO:0016491]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as on... | PF00067; | 1.10.630.10; | Cytochrome P450 family | PTM: Phosphorylation is accompanied by a decrease in enzyme activity. {ECO:0000269|PubMed:2583091}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57... | null | null | null | null | FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. | Rattus norvegicus (Rat) |
P04176 | PH4H_RAT | MAAVVLENGVLSRKLSDFGQETSYIEDNSNQNGAISLIFSLKEEVGALAKVLRLFEENDINLTHIESRPSRLNKDEYEFFTYLDKRTKPVLGSIIKSLRNDIGATVHELSRDKEKNTVPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYTEEEKQTWGTVFRTLKALYKTHACYEHNHIFPLLEKYCGFREDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMYTPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEK... | 1.14.16.1 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:10331871}; | L-phenylalanine catabolic process [GO:0006559]; L-phenylalanine metabolic process [GO:0006558]; tyrosine biosynthetic process [GO:0006571]; tyrosine biosynthetic process, by oxidation of phenylalanine [GO:0019293] | null | amino acid binding [GO:0016597]; identical protein binding [GO:0042802]; iron ion binding [GO:0005506]; phenylalanine 4-monooxygenase activity [GO:0004505] | PF01842;PF00351; | 1.10.800.10; | Biopterin-dependent aromatic amino acid hydroxylase family | PTM: Phosphorylation at Ser-16 increases basal activity and facilitates activation by the substrate phenylalanine. {ECO:0000250|UniProtKB:P00439}. | null | CATALYTIC ACTIVITY: Reaction=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-phenylalanine + O2 = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + L-tyrosine; Xref=Rhea:RHEA:20273, ChEBI:CHEBI:15379, ChEBI:CHEBI:15642, ChEBI:CHEBI:58095, ChEBI:CHEBI:58315, ChEBI:CHEBI:59560; EC=1.14.16.1; Evidence={ECO:000025... | null | PATHWAY: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 1/6. | null | null | FUNCTION: Catalyzes the hydroxylation of L-phenylalanine to L-tyrosine. {ECO:0000250|UniProtKB:P00439}. | Rattus norvegicus (Rat) |
P04177 | TY3H_RAT | MPTPSAPSPQPKGFRRAVSEQDAKQAEAVTSPRFIGRRQSLIEDARKEREAAAAAAAAAVASSEPGNPLEAVVFEERDGNAVLNLLFSLRGTKPSSLSRAVKVFETFEAKIHHLETRPAQRPLAGSPHLEYFVRFEVPSGDLAALLSSVRRVSDDVRSAREDKVPWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQVYRQRRKLIAEIAFQYKHGEPIPHVEYTAEEIATWKEVYVTLKGLYATHACREHLEGFQLLERYCGYREDSIPQLEDVSRFLKERTGFQLRPVAGLLSARDFLASLAFRVFQCTQYIRHASS... | 1.14.16.2 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:9228951}; | aminergic neurotransmitter loading into synaptic vesicle [GO:0015842]; animal organ morphogenesis [GO:0009887]; catecholamine biosynthetic process [GO:0042423]; cellular response to alkaloid [GO:0071312]; cellular response to glucose stimulus [GO:0071333]; cellular response to growth factor stimulus [GO:0071363]; cellu... | axon [GO:0030424]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytoplasmic vesicle [GO:0031410]; cytoplasmic vesicle membrane [GO:0030659]; dendrite [GO:0030425]; melanosome membrane [GO:0033162]; mitochondrion [GO:0005739]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; ... | amino acid binding [GO:0016597]; dopamine binding [GO:0035240]; enzyme binding [GO:0019899]; ferric iron binding [GO:0008199]; ferrous iron binding [GO:0008198]; identical protein binding [GO:0042802]; monooxygenase activity [GO:0004497]; oxygen binding [GO:0019825]; protein domain specific binding [GO:0019904]; small ... | PF00351;PF21417;PF12549; | 3.30.70.260;1.10.800.10; | Biopterin-dependent aromatic amino acid hydroxylase family | PTM: Phosphorylated on Ser-19, Ser-31 and Ser-40 by several protein kinases with different site specificities. Phosphorylation at Ser-31 and Ser-40 leads to an increase of TH activity. Phosphorylation at Ser-40 activates the enzyme and also counteracts the feedback inhibition of TH by catecholamines (By similarity). Ph... | SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P24529}. Nucleus {ECO:0000269|PubMed:21392500}. Cell projection, axon {ECO:0000250|UniProtKB:P24529}. Cytoplasm {ECO:0000269|PubMed:15496595, ECO:0000269|PubMed:21392500}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000269|Pub... | CATALYTIC ACTIVITY: Reaction=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-tyrosine + O2 = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + L-dopa; Xref=Rhea:RHEA:18201, ChEBI:CHEBI:15379, ChEBI:CHEBI:15642, ChEBI:CHEBI:57504, ChEBI:CHEBI:58315, ChEBI:CHEBI:59560; EC=1.14.16.2; Evidence={ECO:0000269|PubMed:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=96 uM for phenylalanine {ECO:0000269|PubMed:10933781}; KM=210 uM for tryptophan {ECO:0000269|PubMed:11922614}; KM=16 uM for tyrosine {ECO:0000269|PubMed:10933781}; | PATHWAY: Catecholamine biosynthesis; dopamine biosynthesis; dopamine from L-tyrosine: step 1/2. {ECO:0000250|UniProtKB:P07101}. | null | null | FUNCTION: Catalyzes the conversion of L-tyrosine to L-dihydroxyphenylalanine (L-Dopa), the rate-limiting step in the biosynthesis of cathecolamines, dopamine, noradrenaline, and adrenaline. Uses tetrahydrobiopterin and molecular oxygen to convert tyrosine to L-Dopa (By similarity). In addition to tyrosine, is able to c... | Rattus norvegicus (Rat) |
P04178 | SODC_PIG | MATKAVCVLKGDGPVQGTIYFELKGEKTVLVTGTIKGLAEGDHGFHVHQFGDNTQGCTSAGPHFNPESKKHGGPKDQERHVGDLGNVTAGKDGVATVYIEDSVIALSGDHSIIGRTMVVHEKPDDLGRGGNEESTKTGNAGSRLACGVIGITQ | 1.15.1.1 | COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250}; Note=Binds 1 copper ion per subunit. {ECO:0000250}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | auditory receptor cell stereocilium organization [GO:0060088]; embryo implantation [GO:0007566]; glutathione metabolic process [GO:0006749]; heart contraction [GO:0060047]; hydrogen peroxide biosynthetic process [GO:0050665]; intracellular iron ion homeostasis [GO:0006879]; locomotory behavior [GO:0007626]; muscle cell... | cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; dendrite cytoplasm [GO:0032839]; extracellular space [GO:0005615]; mitochondrion [GO:0005739]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; peroxisome [GO:0005777]; protein-containing complex [GO:0032991] | copper ion binding [GO:0005507]; protein phosphatase 2B binding [GO:0030346]; protein-folding chaperone binding [GO:0051087]; superoxide dismutase activity [GO:0004784]; zinc ion binding [GO:0008270] | PF00080; | 2.60.40.200; | Cu-Zn superoxide dismutase family | PTM: Palmitoylation helps nuclear targeting and decreases catalytic activity. {ECO:0000250}.; PTM: Succinylation, adjacent to copper catalytic site, probably inhibits activity. Desuccinylation by SIRT5 enhances activity. {ECO:0000250|UniProtKB:P00441}. | SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18421; EC=1.15.1.1; | null | null | null | null | FUNCTION: Destroys radicals which are normally produced within the cells and which are toxic to biological systems. | Sus scrofa (Pig) |
P04179 | SODM_HUMAN | MLSRAVCGTSRQLAPVLGYLGSRQKHSLPDLPYDYGALEPHINAQIMQLHHSKHHAAYVNNLNVTEEKYQEALAKGDVTAQIALQPALKFNGGGHINHSIFWTNLSPNGGGEPKGELLEAIKRDFGSFDKFKEKLTAASVGVQGSGWGWLGFNKERGHLQIAACPNQDPLQGTTGLIPLLGIDVWEHAYYLQYKNVRPDYLKAIWNVINWENVTERYMACKK | 1.15.1.1 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:10852710, ECO:0000269|PubMed:11580280, ECO:0000269|PubMed:1394426, ECO:0000269|PubMed:19265433, ECO:0000269|PubMed:9537987, ECO:0000269|PubMed:9537988}; Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000269|PubMed:10852710, ECO:0000269|PubMed:11580... | acetylcholine-mediated vasodilation involved in regulation of systemic arterial blood pressure [GO:0003069]; cellular response to ethanol [GO:0071361]; cellular response to oxidative stress [GO:0034599]; detection of oxygen [GO:0003032]; erythrophore differentiation [GO:0048773]; glutathione metabolic process [GO:00067... | extracellular exosome [GO:0070062]; mitochondrial matrix [GO:0005759]; mitochondrial nucleoid [GO:0042645]; mitochondrion [GO:0005739] | DNA binding [GO:0003677]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; manganese ion binding [GO:0030145]; oxygen binding [GO:0019825]; superoxide dismutase activity [GO:0004784] | PF02777;PF00081; | 1.10.287.990;3.55.40.20; | Iron/manganese superoxide dismutase family | PTM: Nitrated under oxidative stress. Nitration coupled with oxidation inhibits the catalytic activity. {ECO:0000269|PubMed:10334867, ECO:0000269|PubMed:16399855}.; PTM: Acetylation at Lys-122 decreases enzymatic activity. Deacetylated by SIRT3 upon exposure to ionizing radiations or after long fasting (By similarity).... | SUBCELLULAR LOCATION: Mitochondrion matrix. | CATALYTIC ACTIVITY: Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:18421; EC=1.15.1.1; Evidence={ECO:0000269|PubMed:10334867, ECO:0000269|PubMed:10852710, ECO:0000269|PubMed:11580280, ECO:0000269|PubMed:19265433, ECO:0000269|PubMed:... | null | null | null | null | FUNCTION: Destroys superoxide anion radicals which are normally produced within the cells and which are toxic to biological systems. {ECO:0000269|PubMed:10334867}. | Homo sapiens (Human) |
P04180 | LCAT_HUMAN | MGPPGSPWQWVTLLLGLLLPPAAPFWLLNVLFPPHTTPKAELSNHTRPVILVPGCLGNQLEAKLDKPDVVNWMCYRKTEDFFTIWLDLNMFLPLGVDCWIDNTRVVYNRSSGLVSNAPGVQIRVPGFGKTYSVEYLDSSKLAGYLHTLVQNLVNNGYVRDETVRAAPYDWRLEPGQQEEYYRKLAGLVEEMHAAYGKPVFLIGHSLGCLHLLYFLLRQPQAWKDRFIDGFISLGAPWGGSIKPMLVLASGDNQGIPIMSSIKLKEEQRITTTSPWMFPSRMAWPEDHVFISTPSFNYTGRDFQRFFADLHFEEGWYMWLQ... | 2.3.1.43; 3.1.1.47 | null | cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; cholesterol transport [GO:0030301]; high-density lipoprotein particle remodeling [GO:0034375]; lipid metabolic process [GO:0006629]; lipoprotein biosynthetic process [GO:0042158]; phosphatidylcholine biosynthetic process [GO:0006656]; pho... | extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; high-density lipoprotein particle [GO:0034364] | 1-alkyl-2-acetylglycerophosphocholine esterase activity [GO:0003847]; apolipoprotein A-I binding [GO:0034186]; phosphatidylcholine-sterol O-acyltransferase activity [GO:0004607]; platelet-activating factor acetyltransferase activity [GO:0047179]; sterol esterase activity [GO:0004771] | PF02450; | 3.40.50.1820; | AB hydrolase superfamily, Lipase family | PTM: O- and N-glycosylated. O-glycosylation on Thr-431 and Ser-433 consists of sialylated galactose beta 1-->3N-acetylgalactosamine structures. N-glycosylated sites contain sialylated triantennary and/or biantennary complex structures. {ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:7613477}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10222237, ECO:0000269|PubMed:19065001, ECO:0000269|PubMed:3458198, ECO:0000269|PubMed:8016111, ECO:0000269|PubMed:8820107}. Note=Secreted into blood plasma (PubMed:10222237, PubMed:3458198, PubMed:8820107). Produced in astrocytes and secreted into cerebral spinal fluid... | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + a sterol = a 1-acyl-sn-glycero-3-phosphocholine + a sterol ester; Xref=Rhea:RHEA:21204, ChEBI:CHEBI:15889, ChEBI:CHEBI:35915, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=2.3.1.43; Evidence={ECO:0000255|PROSITE-ProRule:PRU10037, ECO:0000269|PubMed:1022... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.97 mM for LDL {ECO:0000269|PubMed:10329423}; KM=0.4 mM for HDL(2) {ECO:0000269|PubMed:10329423}; KM=0.1 mM for HDL(3) {ECO:0000269|PubMed:10329423}; KM=12.8 uM for 1-O-alkyl-2-acetyl-sn-glycero-3-phosphocholine {ECO:0000269|PubMed:8016111}; KM=125.5 uM for (24S)-... | null | null | null | FUNCTION: Central enzyme in the extracellular metabolism of plasma lipoproteins. Synthesized mainly in the liver and secreted into plasma where it converts cholesterol and phosphatidylcholines (lecithins) to cholesteryl esters and lysophosphatidylcholines on the surface of high and low density lipoproteins (HDLs and LD... | Homo sapiens (Human) |
P04181 | OAT_HUMAN | MFSKLAHLQRFAVLSRGVHSSVASATSVATKKTVQGPPTSDDIFEREYKYGAHNYHPLPVALERGKGIYLWDVEGRKYFDFLSSYSAVNQGHCHPKIVNALKSQVDKLTLTSRAFYNNVLGEYEEYITKLFNYHKVLPMNTGVEAGETACKLARKWGYTVKGIQKYKAKIVFAAGNFWGRTLSAISSSTDPTSYDGFGPFMPGFDIIPYNDLPALERALQDPNVAAFMVEPIQGEAGVVVPDPGYLMGVRELCTRHQVLFIADEIQTGLARTGRWLAVDYENVRPDIVLLGKALSGGLYPVSAVLCDDDIMLTIKPGEHG... | 2.6.1.13 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:9514741}; | arginine catabolic process to glutamate [GO:0019544]; arginine catabolic process to proline via ornithine [GO:0010121]; L-proline biosynthetic process [GO:0055129]; visual perception [GO:0007601] | cytoplasm [GO:0005737]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654] | identical protein binding [GO:0042802]; ornithine aminotransferase activity [GO:0004587]; pyridoxal phosphate binding [GO:0030170] | PF00202; | 3.90.1150.10;3.40.640.10; | Class-III pyridoxal-phosphate-dependent aminotransferase family | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:23076989}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-ornithine = L-glutamate + L-glutamate 5-semialdehyde; Xref=Rhea:RHEA:25160, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:46911, ChEBI:CHEBI:58066; EC=2.6.1.13; Evidence={ECO:0000269|PubMed:1737786, ECO:0000269|PubMed:23076989}; PhysiologicalDirection=left-to-right; X... | null | PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-ornithine: step 1/1. {ECO:0000305|PubMed:1737786, ECO:0000305|PubMed:23076989}. | null | null | FUNCTION: Catalyzes the reversible interconversion of L-ornithine and 2-oxoglutarate to L-glutamate semialdehyde and L-glutamate. {ECO:0000269|PubMed:1737786, ECO:0000269|PubMed:23076989}. | Homo sapiens (Human) |
P04182 | OAT_RAT | MLSKLASLQTVAALRRGLRTSVASATSVATKKTEQGPPSSEYIFERESKYGAHNYHPLPVALERGKGIYMWDVEGRQYFDFLSAYGAVSQGHCHPKIIEAMKSQVDKLTLTSRAFYNNVLGEYEEYITKLFNYNKVLPMNTGVEAGETACKLARRWGYTVKGIQKYKAKIVFAVGNFWGRTLSAVSSSTDPTSYDGFGPFMPGFETIPYNDLPALERALQDPNVAAFMVEPIQGEAGVIVPDPGYLTGVRELCTRHQVLFIADEIQTGLARTGRWLAVDHENVRPDIVLLGKALSGGLYPVSAVLCDDDIMLTIKPGEHG... | 2.6.1.13 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; | arginine catabolic process to glutamate [GO:0019544]; arginine catabolic process to proline via ornithine [GO:0010121]; L-proline biosynthetic process [GO:0055129]; ornithine metabolic process [GO:0006591] | cytoplasm [GO:0005737]; mitochondrial matrix [GO:0005759]; nucleoplasm [GO:0005654] | identical protein binding [GO:0042802]; N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity [GO:0003992]; ornithine aminotransferase activity [GO:0004587]; pyridoxal phosphate binding [GO:0030170] | PF00202; | 3.90.1150.10;3.40.640.10; | Class-III pyridoxal-phosphate-dependent aminotransferase family | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:P04181}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-ornithine = L-glutamate + L-glutamate 5-semialdehyde; Xref=Rhea:RHEA:25160, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:46911, ChEBI:CHEBI:58066; EC=2.6.1.13; Evidence={ECO:0000250|UniProtKB:P04181}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25161; Eviden... | null | PATHWAY: Amino-acid biosynthesis; L-proline biosynthesis; L-glutamate 5-semialdehyde from L-ornithine: step 1/1. {ECO:0000250|UniProtKB:P04181}. | null | null | FUNCTION: Catalyzes the reversible interconversion of L-ornithine and 2-oxoglutarate to L-glutamate semialdehyde and L-glutamate. {ECO:0000250|UniProtKB:P04181}. | Rattus norvegicus (Rat) |
P04183 | KITH_HUMAN | MSCINLPTVLPGSPSKTRGQIQVILGPMFSGKSTELMRRVRRFQIAQYKCLVIKYAKDTRYSSSFCTHDRNTMEALPACLLRDVAQEALGVAVIGIDEGQFFPDIVEFCEAMANAGKTVIVAALDGTFQRKPFGAILNLVPLAESVVKLTAVCMECFREAAYTKRLGTEKEVEVIGGADKYHSVCRLCYFKKASGQPAGPDNKENCPVPGKPGEAVAARKLFAPQQILQCSPAN | 2.7.1.21 | null | DNA synthesis involved in mitotic DNA replication [GO:1904860]; nucleobase-containing compound metabolic process [GO:0006139]; phosphorylation [GO:0016310]; protein homotetramerization [GO:0051289]; thymidine biosynthetic process [GO:0046105]; thymidine metabolic process [GO:0046104] | cytosol [GO:0005829]; nucleus [GO:0005634] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; thymidine kinase activity [GO:0004797]; zinc ion binding [GO:0008270] | PF00265; | 3.30.60.20;3.40.50.300; | Thymidine kinase family | PTM: Phosphorylated on Ser-13 in mitosis. Phosphorylation of Ser-13 by CDK1 during mitosis reduces homotetramerization and catalytic efficiency when DNA replication is complete and intracellular TK1 is still present at a high level (PubMed:14697231, PubMed:9575153). {ECO:0000269|PubMed:14697231, ECO:0000269|PubMed:9575... | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=ATP + thymidine = ADP + dTMP + H(+); Xref=Rhea:RHEA:19129, ChEBI:CHEBI:15378, ChEBI:CHEBI:17748, ChEBI:CHEBI:30616, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.1.21; Evidence={ECO:0000269|PubMed:14697231, ECO:0000269|PubMed:22385435}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:1... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.4 uM for thymidine {ECO:0000269|PubMed:22385435}; KM=0.54 uM for thymidine {ECO:0000269|PubMed:14697231}; KM=0.52 uM for AZT {ECO:0000269|PubMed:22385435}; Vmax=26.6 umol/min/mg enzyme toward thymidine {ECO:0000269|PubMed:22385435}; Vmax=10 umol/min/mg enzyme tow... | null | null | null | FUNCTION: Cell-cycle-regulated enzyme of importance in nucleotide metabolism (PubMed:9575153). Catalyzes the first enzymatic step in the salvage pathway converting thymidine into thymidine monophosphate (PubMed:22385435). Transcriptional regulation limits expression to the S phase of the cell cycle and transient expres... | Homo sapiens (Human) |
P04184 | KITH_MOUSE | MSYINLPTVLPSSPSKTRGQIQVILGPMFSGKSTELMRRVRRFQIAQYKCLVIKYAKDTRYSNSFSTHDRNTMDALPACMLRDVTQESLGVAVIGIDEGQFFPDIVDFCEMMANEGKTVIVAALDGTFQRKAFGSILNLVPLAESVVKLTAVCMECFREAAYTKRLGLEKEVEVIGGADKYHSVCRLCYFKKSSAQTAGSDNKNCLVLGQPGEALVVRKLFASQQVLQYNSAN | 2.7.1.21 | null | DNA synthesis involved in mitotic DNA replication [GO:1904860]; phosphorylation [GO:0016310]; protein homotetramerization [GO:0051289]; thymidine biosynthetic process [GO:0046105]; thymidine metabolic process [GO:0046104] | cytosol [GO:0005829]; nucleus [GO:0005634] | ATP binding [GO:0005524]; identical protein binding [GO:0042802]; thymidine kinase activity [GO:0004797]; zinc ion binding [GO:0008270] | PF00265; | 3.30.60.20;3.40.50.300; | Thymidine kinase family | PTM: Phosphorylated on Ser-13 in mitosis. Phosphorylation of Ser-13 by CDK1 during mitosis reduces homotetramerization and catalytic efficiency when DNA replication is complete and intracellular TK1 is still present at a high level. {ECO:0000250|UniProtKB:P04183}.; PTM: Polyubiquitinated. Postmitosis, ubiquitination le... | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=ATP + thymidine = ADP + dTMP + H(+); Xref=Rhea:RHEA:19129, ChEBI:CHEBI:15378, ChEBI:CHEBI:17748, ChEBI:CHEBI:30616, ChEBI:CHEBI:63528, ChEBI:CHEBI:456216; EC=2.7.1.21; Evidence={ECO:0000250|UniProtKB:P04183}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19130; Evidence={ECO:0000250|... | null | null | null | null | FUNCTION: Cell-cycle-regulated enzyme of importance in nucleotide metabolism. Catalyzes the first enzymatic step in the salvage pathway converting thymidine into thymidine monophosphate. Transcriptional regulation limits expression to the S phase of the cell cycle and transient expression coincides with the oscillation... | Mus musculus (Mouse) |
P04186 | CFAB_MOUSE | MESPQLCLVLLVLGFSSGGVSATPVLEARPQVSCSLEGVEIKGGSFQLLQGGQALEYLCPSGFYPYPVQTRTCRSTGSWSDLQTRDQKIVQKAECRAIRCPRPQDFENGEFWPRSPFYNLSDQISFQCYDGYVLRGSANRTCQENGRWDGQTAICDDGAGYCPNPGIPIGTRKVGSQYRLEDIVTYHCSRGLVLRGSQKRKCQEGGSWSGTEPSCQDSFMYDSPQEVAEAFLSSLTETIEGADAEDGHSPGEQQKRKIVLDPSGSMNIYLVLDGSDSIGSSNFTGAKRCLTNLIEKVASYGVRPRYGLLTYATVPKVLVR... | 3.4.21.47 | null | B cell proliferation [GO:0042100]; complement activation [GO:0006956]; complement activation, alternative pathway [GO:0006957]; proteolysis [GO:0006508]; response to bacterium [GO:0009617] | classical-complement-pathway C3/C5 convertase complex [GO:0005601]; extracellular exosome [GO:0070062] | serine-type endopeptidase activity [GO:0004252] | PF00084;PF00089;PF00092; | 2.40.10.120;2.10.70.10;3.40.50.410; | Peptidase S1 family | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Cleavage of Arg-|-Ser bond in complement component C3 alpha-chain to yield C3a and C3b, and Arg-|-Xaa bond in complement component C5 alpha-chain to yield C5a and C5b.; EC=3.4.21.47; | null | null | null | null | FUNCTION: Factor B which is part of the alternate pathway of the complement system is cleaved by factor D into 2 fragments: Ba and Bb. Bb, a serine protease, then combines with complement factor 3b to generate the C3 or C5 convertase. | Mus musculus (Mouse) |
P04187 | GRAB_MOUSE | MKILLLLLTLSLASRTKAGEIIGGHEVKPHSRPYMALLSIKDQQPEAICGGFLIREDFVLTAAHCEGSIINVTLGAHNIKEQEKTQQVIPMVKCIPHPDYNPKTFSNDIMLLKLKSKAKRTRAVRPLNLPRRNVNVKPGDVCYVAGWGRMAPMGKYSNTLQEVELTVQKDRECESYFKNRYNKTNQICAGDPKTKRASFRGDSGGPLVCKKVAAGIVSYGYKDGSPPRAFTKVSSFLSWIKKTMKSS | 3.4.21.79 | null | apoptotic process [GO:0006915]; defense response to bacterium [GO:0042742]; granzyme-mediated programmed cell death signaling pathway [GO:0140507]; killing of cells of another organism [GO:0031640]; natural killer cell mediated cytotoxicity [GO:0042267]; protein maturation [GO:0051604]; proteolysis involved in protein ... | cytolytic granule [GO:0044194]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]; extracellular space [GO:0005615]; intracellular membrane-bounded organelle [GO:0043231] | serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236] | PF00089; | 2.40.10.10; | Peptidase S1 family, Granzyme subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P10144}. Cytolytic granule {ECO:0000250|UniProtKB:P10144}. Note=Delivered into the target cell by perforin. {ECO:0000250|UniProtKB:P10144}. | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: -Asp-|-Xaa- >> -Asn-|-Xaa- > -Met-|-Xaa-, -Ser-|-Xaa-.; EC=3.4.21.79; Evidence={ECO:0000269|PubMed:35705808}; | null | null | null | null | FUNCTION: Abundant protease in the cytosolic granules of cytotoxic T-cells and NK-cells which activates caspase-independent pyroptosis when delivered into the target cell through the immunological synapse (PubMed:35705808). It cleaves after Asp (PubMed:35705808). Once delivered into the target cell, acts by catalyzing ... | Mus musculus (Mouse) |
P04189 | SUBT_BACSU | MRSKKLWISLLFALTLIFTMAFSNMSAQAAGKSSTEKKYIVGFKQTMSAMSSAKKKDVISEKGGKVQKQFKYVNAAAATLDEKAVKELKKDPSVAYVEEDHIAHEYAQSVPYGISQIKAPALHSQGYTGSNVKVAVIDSGIDSSHPDLNVRGGASFVPSETNPYQDGSSHGTHVAGTIAALNNSIGVLGVAPSASLYAVKVLDSTGSGQYSWIINGIEWAISNNMDVINMSLGGPTGSTALKTVVDKAVSSGIVVAAAAGNEGSSGSTSTVGYPAKYPSTIAVGAVNSSNQRASFSSAGSELDVMAPGVSIQSTLPGGTY... | 3.4.21.62 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:9811547}; Note=Binds 2 calcium ions per subunit. {ECO:0000269|PubMed:9811547}; | proteolysis [GO:0006508]; sporulation resulting in formation of a cellular spore [GO:0030435] | extracellular space [GO:0005615] | metal ion binding [GO:0046872]; serine-type endopeptidase activity [GO:0004252] | PF05922;PF00082; | 3.30.70.80;3.40.50.200; | Peptidase S8 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7589571}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.; EC=3.4.21.62; Evidence={ECO:0000269|PubMed:7589571}; | null | null | null | null | FUNCTION: An extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides. {ECO:0000269|PubMed:7589571}. | Bacillus subtilis (strain 168) |
P04190 | BLA2_BACCE | MKKNTLLKVGLCVGLLGTIQFVSTISSVQASQKVEKTVIKNETGTISISQLNKNVWVHTELGSFNGEAVPSNGLVLNTSKGLVLVDSSWDDKLTKELIEMVEKKFQKRVTDVIITHAHADRIGGIKTLKERGIKAHSTALTAELAKKNGYEEPLGDLQTVTNLKFGNMKVETFYPGKGHTEDNIVVWLPQYNILVGGCLVKSTSAKDLGNVADAYVNEWSTSIENVLKRYRNINAVVPGHGEVGDKGLLLHTLDLLK | 3.5.2.6 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:20677753, ECO:0000269|PubMed:24059435, ECO:0000269|PubMed:26482303, ECO:0000269|PubMed:7588620, ECO:0000269|PubMed:9761898}; Note=Binds 2 Zn(2+) ions per subunit. The enzyme can also function with only 1 Zn(2+) ion (PubMed:9761898). {ECO:000026... | antibiotic catabolic process [GO:0017001]; response to antibiotic [GO:0046677] | periplasmic space [GO:0042597] | beta-lactamase activity [GO:0008800]; zinc ion binding [GO:0008270] | PF00753; | 3.60.15.10; | Metallo-beta-lactamase superfamily, Class-B beta-lactamase family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a beta-lactam + H2O = a substituted beta-amino acid; Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627, ChEBI:CHEBI:140347; EC=3.5.2.6; Evidence={ECO:0000250|UniProtKB:P25910}; | null | null | null | null | FUNCTION: Confers resistance to the different beta-lactams antibiotics (penicillin, cephalosporin and carbapenem) via the hydrolysis of the beta-lactam ring. Active on cephalosporin and penicillin. {ECO:0000269|PubMed:3930467}. | Bacillus cereus |
P04191 | AT2A1_RABIT | MEAAHSKSTEECLAYFGVSETTGLTPDQVKRHLEKYGHNELPAEEGKSLWELVIEQFEDLLVRILLLAACISFVLAWFEEGEETITAFVEPFVILLILIANAIVGVWQERNAENAIEALKEYEPEMGKVYRADRKSVQRIKARDIVPGDIVEVAVGDKVPADIRILSIKSTTLRVDQSILTGESVSVIKHTEPVPDPRAVNQDKKNMLFSGTNIAAGKALGIVATTGVSTEIGKIRDQMAATEQDKTPLQQKLDEFGEQLSKVISLICVAVWLINIGHFNDPVHGGSWIRGAIYYFKIAVALAVAAIPEGLPAVITTCLA... | 7.2.2.10 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613, ECO:0000269|PubMed:15448704, ECO:0000269|PubMed:15618517, ECO:0000269|PubMed:18075584, ECO:0000269|PubMed:23455424}; | calcium ion import into sarcoplasmic reticulum [GO:1990036]; calcium ion transport [GO:0006816]; intracellular calcium ion homeostasis [GO:0006874]; negative regulation of striated muscle contraction [GO:0045988]; positive regulation of ATPase-coupled calcium transmembrane transporter activity [GO:1901896]; positive re... | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; H zone [GO:0031673]; I band [GO:0031674]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]; sarcoplasmic reticulum [GO:0016529]; sarcoplasmic reticulum m... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; calcium ion binding [GO:0005509]; P-type calcium transporter activity [GO:0005388] | PF13246;PF00689;PF00690;PF00122;PF00702; | 3.40.1110.10;2.70.150.10;1.20.1110.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IIA subfamily | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:12585965}; Multi-pass membrane protein {ECO:0000269|PubMed:10864315, ECO:0000269|PubMed:12167852, ECO:0000269|PubMed:15192230, ECO:0000269|PubMed:15229613, ECO:0000269|PubMed:15448704, ECO:0000269|PubMed:15618517, ECO:0000269|PubMed:16710301, ECO:... | CATALYTIC ACTIVITY: Reaction=ATP + Ca(2+)(in) + H2O = ADP + Ca(2+)(out) + H(+) + phosphate; Xref=Rhea:RHEA:18105, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29108, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=7.2.2.10; Evidence={ECO:0000269|PubMed:10914677, ECO:0000269|PubMed:11438520, ECO:000026... | null | null | null | null | FUNCTION: Key regulator of striated muscle performance by acting as the major Ca(2+) ATPase responsible for the reuptake of cytosolic Ca(2+) into the sarcoplasmic reticulum. Catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen (PubMed:10914677, P... | Oryctolagus cuniculus (Rabbit) |
P04196 | HRG_HUMAN | MKALIAALLLITLQYSCAVSPTDCSAVEPEAEKALDLINKRRRDGYLFQLLRIADAHLDRVENTTVYYLVLDVQESDCSVLSRKYWNDCEPPDSRRPSEIVIGQCKVIATRHSHESQDLRVIDFNCTTSSVSSALANTKDSPVLIDFFEDTERYRKQANKALEKYKEENDDFASFRVDRIERVARVRGGEGTGYFVDFSVRNCPRHHFPRHPNVFGFCRADLFYDVEALDLESPKNLVINCEVFDPQEHENINGVPPHLGHPFHWGGHERSSTTKPPFKPHGSRDHHHPHKPHEHGPPPPPDERDHSHGPPLPQGPPPLL... | null | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:16436387}; | angiogenesis [GO:0001525]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; chemotaxis [GO:0006935]; cytolysis by host of symbiont cells [GO:0051838]; defense response to fungus [GO:0050832]; fibrinolysis [GO:0042730]; heme transport [GO:0015886]; negative regulation of angiogenesis... | blood microparticle [GO:0072562]; cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; endolysosome [GO:0036019]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; plasma membrane [GO:0005886]; platelet alpha granule lumen [GO:0031093] | cysteine-type endopeptidase inhibitor activity [GO:0004869]; heme binding [GO:0020037]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; immunoglobulin binding [GO:0019865]; metal ion binding [GO:0046872]; serine-type endopeptidase inhibitor activity [GO:0004867]; signaling receptor bind... | PF00031; | 3.10.450.10; | null | PTM: Proteolytic cleavage produces several HRG fragments which are mostly disulfide-linked and, therefore, not released. Cleavage by plasmin is inhibited in the presence of heparin, zinc ions or in an acidic environment. Cleavage reduces binding of HRG to heparan sulfate, but enhances the ability of HRG to bind and tet... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21215706}. | null | null | null | null | null | FUNCTION: Plasma glycoprotein that binds a number of ligands such as heme, heparin, heparan sulfate, thrombospondin, plasminogen, and divalent metal ions. Binds heparin and heparin/glycosaminoglycans in a zinc-dependent manner. Binds heparan sulfate on the surface of liver, lung, kidney and heart endothelial cells. Bin... | Homo sapiens (Human) |
P04197 | MYB_DROME | MASASTENGEELMNYGSNSDSEESEYSENEDTQVCDKDSQQNSNADSGYPLDSPELQDSKTTGQKGQNKSGKTSIGAVHPNYGFGKRWSKSEDVLLKQLVETHGENWEIIGPHFKDRLEQQVQQRWAKVLNPELIKGPWTRDEDDMVIKLVRNFGPKKWTLIARYLNGRIGKQCRERWHNHLNPNIKKTAWTEKEDEIIYQAHLELGNQWAKIAKRLPGRTDNAIKNHWNSTMRRKYDVERRSVNASGSDLKSSRTHLITLIKSGGISKCMNNMQHNKESGGEAVNKSENADGASVTAVKGGDLAQESQDDHQKGSNLAH... | null | null | centriole replication [GO:0007099]; centrosome cycle [GO:0007098]; chromosome condensation [GO:0030261]; eggshell chorion gene amplification [GO:0007307]; Golgi organization [GO:0007030]; mitotic cell cycle [GO:0000278]; mitotic cytokinesis [GO:0000281]; negative regulation of cell size [GO:0045792]; positive regulatio... | euchromatin [GO:0000791]; Myb complex [GO:0031523]; nucleus [GO:0005634]; polytene chromosome [GO:0005700] | DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA bindi... | PF09316;PF13921;PF00249; | 1.10.10.60; | null | null | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: DNA-binding protein that specifically recognizes the sequence 5'-YAAC[GT]G-3'. Component of the DREAM complex, a multiprotein complex that can both act as a transcription activator or repressor depending on the context. In follicle cells, the complex plays a central role in the site-specific DNA replication a... | Drosophila melanogaster (Fruit fly) |
P04198 | MYCN_HUMAN | MPSCSTSTMPGMICKNPDLEFDSLQPCFYPDEDDFYFGGPDSTPPGEDIWKKFELLPTPPLSPSRGFAEHSSEPPSWVTEMLLENELWGSPAEEDAFGLGGLGGLTPNPVILQDCMWSGFSAREKLERAVSEKLQHGRGPPTAGSTAQSPGAGAASPAGRGHGGAAGAGRAGAALPAELAHPAAECVDPAVVFPFPVNKREPAPVPAAPASAPAAGPAVASGAGIAAPAGAPGVAPPRPGGRQTSGGDHKALSTSGEDTLSDSDDEDDEEEDEEEEIDVVTVEKRRSSSNTKAVTTFTITVRPKNAALGPGRAQSSELIL... | null | null | negative regulation of gene expression [GO:0010629]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of gene expression [GO:0010628]; positive regulation of miRNA transcription [GO:1902895]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transc... | chromatin [GO:0000785]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; kinase binding [GO:0019900]; protein dimerization activity [GO:0046... | PF00010;PF01056; | 4.10.280.10; | null | PTM: Phosphorylated by GSK3-beta which may promote its degradation (PubMed:24391509). Phosphorylated by AURKA (PubMed:27837025). {ECO:0000269|PubMed:24391509, ECO:0000269|PubMed:27837025}. | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Positively regulates the transcription of MYCNOS in neuroblastoma cells. {ECO:0000269|PubMed:24391509}. | Homo sapiens (Human) |
P04201 | MAS_HUMAN | MDGSNVTSFVVEEPTNISTGRNASVGNAHRQIPIVHWVIMSISPVGFVENGILLWFLCFRMRRNPFTVYITHLSIADISLLFCIFILSIDYALDYELSSGHYYTIVTLSVTFLFGYNTGLYLLTAISVERCLSVLYPIWYRCHRPKYQSALVCALLWALSCLVTTMEYVMCIDREEESHSRNDCRAVIIFIAILSFLVFTPLMLVSSTILVVKIRKNTWASHSSKLYIVIMVTIIIFLIFAMPMRLLYLLYYEYWSTFGNLHHISLLFSTINSSANPFIYFFVGSSKKKRFKESLKVVLTRAFKDEMQPRRQKDNCNTVT... | null | null | G protein-coupled receptor signaling pathway [GO:0007186]; hippocampus development [GO:0021766]; male gonad development [GO:0008584]; negative regulation of protein phosphorylation [GO:0001933]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of cell population prolifera... | cell surface [GO:0009986]; plasma membrane [GO:0005886] | angiotensin receptor activity [GO:0001595]; angiotensin type II receptor activity [GO:0004945]; G protein-coupled receptor activity [GO:0004930]; peptide binding [GO:0042277] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16611642}; Multi-pass membrane protein {ECO:0000269|PubMed:16611642}. | null | null | null | null | null | FUNCTION: Receptor for angiotensin 1-7 (By similarity). Acts specifically as a functional antagonist of AGTR1 (angiotensin-2 type 1 receptor), although it up-regulates AGTR1 receptor levels. Positive regulation of AGTR1 levels occurs through activation of the G-proteins GNA11 and GNAQ, and stimulation of the protein ki... | Homo sapiens (Human) |
P04202 | TGFB1_MOUSE | MPPSGLRLLPLLLPLPWLLVLTPGRPAAGLSTCKTIDMELVKRKRIEAIRGQILSKLRLASPPSQGEVPPGPLPEAVLALYNSTRDRVAGESADPEPEPEADYYAKEVTRVLMVDRNNAIYEKTKDISHSIYMFFNTSDIREAVPEPPLLSRAELRLQRLKSSVEQHVELYQKYSNNSWRYLGNRLLTPTDTPEWLSFDVTGVVRQWLNQGDGIQGFRFSAHCSCDSKDNKLHVEINGISPKRRGDLGTIHDMNRPFLLLMATPLERAQHLHSSRHRRALDTNYCFSSTEKNCCVRQLYIDFRKDLGWKWIHEPKGYHAN... | null | null | adaptive immune response based on somatic recombination of immune receptors built from immunoglobulin superfamily domains [GO:0002460]; animal organ morphogenesis [GO:0009887]; animal organ regeneration [GO:0031100]; aortic valve morphogenesis [GO:0003180]; ATP biosynthetic process [GO:0006754]; branch elongation invol... | axon [GO:0030424]; blood microparticle [GO:0072562]; cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; microvillus [GO:0005902]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; secretory g... | antigen binding [GO:0003823]; cytokine activity [GO:0005125]; deubiquitinase activator activity [GO:0035800]; enzyme binding [GO:0019899]; growth factor activity [GO:0008083]; identical protein binding [GO:0042802]; protein serine/threonine kinase activator activity [GO:0043539]; protein-containing complex binding [GO:... | PF00019;PF00688; | 2.60.120.970;2.10.90.10; | TGF-beta family | PTM: Transforming growth factor beta-1 proprotein: The precursor proprotein is cleaved in the Golgi apparatus by FURIN to form Transforming growth factor beta-1 (TGF-beta-1) and Latency-associated peptide (LAP) chains, which remain non-covalently linked, rendering TGF-beta-1 inactive. {ECO:0000250|UniProtKB:P01137}.; P... | SUBCELLULAR LOCATION: [Latency-associated peptide]: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P01137}.; SUBCELLULAR LOCATION: [Transforming growth factor beta-1]: Secreted {ECO:0000250|UniProtKB:P01137}. | null | null | null | null | null | FUNCTION: Transforming growth factor beta-1 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-1 (TGF-beta-1) chains, which constitute the regulatory and active subunit of TGF-beta-1, respectively. {ECO:0000250|UniProtKB:P01137}.; FUNCTION: [Latency-associated peptide]: Re... | Mus musculus (Mouse) |
P04216 | THY1_HUMAN | MNLAISIALLLTVLQVSRGQKVTSLTACLVDQSLRLDCRHENTSSSPIQYEFSLTRETKKHVLFGTVGVPEHTYRSRTNFTSKYNMKVLYLSAFTSKDEGTYTCALHHSGHSPPISSQNVTVLRDKLVKCEGISLLAQNTSWLLLLLLSLSLLQATDFMSL | null | null | angiogenesis [GO:0001525]; cell-cell adhesion [GO:0098609]; cell-cell signaling [GO:0007267]; cytoskeleton organization [GO:0007010]; focal adhesion assembly [GO:0048041]; heterotypic cell-cell adhesion [GO:0034113]; integrin-mediated signaling pathway [GO:0007229]; negative regulation of axonogenesis [GO:0050771]; neg... | apical plasma membrane [GO:0016324]; axolemma [GO:0030673]; cell surface [GO:0009986]; dendrite [GO:0030425]; dendrite membrane [GO:0032590]; endoplasmic reticulum [GO:0005783]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; focal adhesion [GO:00059... | GPI anchor binding [GO:0034235]; GTPase activator activity [GO:0005096]; integrin binding [GO:0005178] | PF00047; | 2.60.40.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor, GPI-anchor {ECO:0000250}. | null | null | null | null | null | FUNCTION: May play a role in cell-cell or cell-ligand interactions during synaptogenesis and other events in the brain. | Homo sapiens (Human) |
P04217 | A1BG_HUMAN | MSMLVVFLLLWGVTWGPVTEAAIFYETQPSLWAESESLLKPLANVTLTCQAHLETPDFQLFKNGVAQEPVHLDSPAIKHQFLLTGDTQGRYRCRSGLSTGWTQLSKLLELTGPKSLPAPWLSMAPVSWITPGLKTTAVCRGVLRGVTFLLRREGDHEFLEVPEAQEDVEATFPVHQPGNYSCSYRTDGEGALSEPSATVTIEELAAPPPPVLMHHGESSQVLHPGNKVTLTCVAPLSGVDFQLRRGEKELLVPRSSTSPDRIFFHLNAVALGDGGHYTCRYRLHDNQNGWSGDSAPVELILSDETLPAPEFSPEPESGRA... | null | null | null | blood microparticle [GO:0072562]; collagen-containing extracellular matrix [GO:0062023]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; ficolin-1-rich granule lumen [GO:1904813]; plasma membrane [GO:0005886]; platelet alpha granule lumen [GO:0031093]; secretory ... | null | PF13895; | 2.60.40.10; | null | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | null | Homo sapiens (Human) |
P04218 | OX2G_RAT | MGSPVFRRPFCHLSTYSLLWAIAAVALSTAQVEVVTQDERKLLHTTASLRCSLKTTQEPLIVTWQKKKAVGPENMVTYSKAHGVVIQPTYKDRINITELGLLNTSITFWNTTLDDEGCYMCLFNMFGSGKVSGTACLTLYVQPIVHLHYNYFEDHLNITCSATARPAPAISWKGTGSGIENSTESHSHSNGTTSVTSILRVKDPKTQVGKEVICQVLYLGNVIDYKQSLDKGFWFSVPLLLSIVSLVILLVLISILLYWKRHRNQERGESSQGMQRMK | null | null | cell-cell adhesion [GO:0098609]; heterotypic cell-cell adhesion [GO:0034113]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of interleukin-6 production [GO:0032715]; negative regulation of macrophage activation [GO:0043031]; negative regulation of macrophage migration [GO:190552... | axon [GO:0030424]; cell body [GO:0044297]; cell surface [GO:0009986]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886] | cell-cell adhesion mediator activity [GO:0098632]; protein binding involved in heterotypic cell-cell adhesion [GO:0086080] | PF00047; | 2.60.40.10; | null | null | SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Costimulates T-cell proliferation. May regulate myeloid cell activity in a variety of tissues. | Rattus norvegicus (Rat) |
P04223 | HA1K_MOUSE | MAPCMLLLLLAAALAPTQTRAGPHSLRYFHTAVSRPGLGKPRFISVGYVDDTQFVRFDSDAENPRYEPRVRWMEQVEPEYWERNTQIAKGNEQIFRVNLRTALRYYNQSAGGSHTFQRMYGCEVGSDWRLLRGYEQYAYDGCDYIALNEDLKTWTAADMAALITKHKWEQAGDAERDRAYLEGTCVEWLRRYLQLGNATLPRTDSPKAHVTRHSRPEDKVTLRCWALGFYPADITLTWQLNGEELTQDMELVETRPAGDGTFQKWASVVVPLGKEQYYTCHVYHQGLPEPLTLRWEPPPSTVSNTVIIAVLVVLGAAIVT... | null | null | antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-dependent [GO:0002485]; antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen ... | external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; MHC class I protein complex [GO:0042612]; phagocytic vesicle membrane [GO:0030670] | beta-2-microglobulin binding [GO:0030881]; peptide antigen binding [GO:0042605]; peptide binding [GO:0042277]; protein-containing complex binding [GO:0044877]; signaling receptor binding [GO:0005102] | PF07654;PF00129;PF06623; | 2.60.40.10;3.30.500.10; | MHC class I family | null | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Involved in the presentation of foreign antigens to the immune system. | Mus musculus (Mouse) |
P04227 | HA2Q_MOUSE | GIVVYQSPGDIGQYTHEFDGDEWFYVDLDKKETVWMLPEFGQLTSFDPQGGLQNIATGKHNLGGWTKRSNFTPATNEAPQATVFPKSPVLLGQPNTLICFVDNIFPPVINITWLRNSKSVTDGVYETSFLVNRDHSFHKLSYLTFIPSDDDIYDCKVEHWGLDEPVLKHWEPEIPAPMSELTETVVCALGLSVGLVGIVVGTIFIIQGLRSGGTSRPPGPL | null | null | adaptive immune response [GO:0002250]; antigen processing and presentation [GO:0019882]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; antigen processing and presentation of peptide antigen [GO:0048002]; negative regulation of T cell proliferation [GO:0042130]; peptide ... | external side of plasma membrane [GO:0009897]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; MHC class II protein complex [GO:0042613]; plasma membrane [GO:0005886] | MHC class II protein complex binding [GO:0023026]; peptide antigen binding [GO:0042605]; protein-containing complex binding [GO:0044877] | PF07654;PF00993; | 2.60.40.10; | MHC class II family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. | null | null | null | null | null | null | Mus musculus (Mouse) |
P04228 | HA2D_MOUSE | MPCSRALILGVLALNTMLSLCGGEDDIEADHVGFYGTTVYQSPGDIGQYTHEFDGDELFYVDLDKKKTVWRLPEFGQLILFEPQGGLQNIAAEKHNLGILTKRSNFTPATNEAPQATVFPKSPVLLGQPNTLICFVDNIFPPVINITWLRNSKSVTDGVYETSFLVNRDHSFHKLSYLTFIPSDDDIYDCKVEHWGLEEPVLKHWEPEIPAPMSELTETVVCALGLSVGLVGIVVGTIFIIQGLRSGGTSRHPGPL | null | null | adaptive immune response [GO:0002250]; antigen processing and presentation [GO:0019882]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; antigen processing and presentation of peptide antigen [GO:0048002]; negative regulation of T cell proliferation [GO:0042130]; peptide ... | external side of plasma membrane [GO:0009897]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; MHC class II protein complex [GO:0042613]; plasma membrane [GO:0005886] | MHC class II protein complex binding [GO:0023026]; peptide antigen binding [GO:0042605]; protein-containing complex binding [GO:0044877] | PF07654;PF00993; | 2.60.40.10; | MHC class II family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. | null | null | null | null | null | null | Mus musculus (Mouse) |
P04233 | HG2A_HUMAN | MHRRRSRSCREDQKPVMDDQRDLISNNEQLPMLGRRPGAPESKCSRGALYTGFSILVTLLLAGQATTAYFLYQQQGRLDKLTVTSQNLQLENLRMKLPKPPKPVSKMRMATPLLMQALPMGALPQGPMQNATKYGNMTEDHVMHLLQNADPLKVYPPLKGSFPENLRHLKNTMETIDWKVFESWMHHWLLFEMSRHSLEQKPTDAPPKVLTKCQEEVSHIPAVHPGSFRPKCDENGNYLPLQCYGSIGYCWCVFPNGTEVPNTRSRGHHNCSESLELEDPSSGLGVTKQDLGPVPM | null | null | antigen processing and presentation [GO:0019882]; antigen processing and presentation of endogenous antigen [GO:0019883]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; chaperone cofactor-dependent protein refolding [GO:0051085]; immunoglobulin mediated immune response [... | cell surface [GO:0009986]; clathrin-coated endocytic vesicle membrane [GO:0030669]; cytoplasm [GO:0005737]; endocytic vesicle membrane [GO:0030666]; ER to Golgi transport vesicle membrane [GO:0012507]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; Golgi membrane [GO:0000139]; late e... | amyloid-beta binding [GO:0001540]; CD4 receptor binding [GO:0042609]; cytokine binding [GO:0019955]; cytokine receptor activity [GO:0004896]; identical protein binding [GO:0042802]; macrophage migration inhibitory factor binding [GO:0035718]; MHC class II protein binding [GO:0042289]; MHC class II protein binding, via ... | PF09307;PF08831;PF00086; | 1.10.870.10;4.10.800.10; | null | PTM: O-glycosylated with core 1 or possibly core 8 glycans (PubMed:22171320, PubMed:23234360). Contains chondroitin sulfate (PubMed:25326458). {ECO:0000269|PubMed:22171320, ECO:0000269|PubMed:23234360, ECO:0000269|PubMed:25326458}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type II membrane protein {ECO:0000305}. Endoplasmic reticulum membrane. Golgi apparatus, trans-Golgi network. Endosome. Lysosome. Secreted {ECO:0000269|PubMed:25326458, ECO:0000269|PubMed:36213313, ECO:0000269|PubMed:37453717}. Note=Transits through a numbe... | null | null | null | null | null | FUNCTION: Plays a critical role in MHC class II antigen processing by stabilizing peptide-free class II alpha/beta heterodimers in a complex soon after their synthesis and directing transport of the complex from the endoplasmic reticulum to the endosomal/lysosomal system where the antigen processing and binding of anti... | Homo sapiens (Human) |
P04234 | CD3D_HUMAN | MEHSTFLSGLVLATLLSQVSPFKIPIEELEDRVFVNCNTSITWVEGTVGTLLSDITRLDLGKRILDPRGIYRCNGTDIYKDKESTVQVHYRMCQSCVELDPATVAGIIVTDVIATLLLALGVFCFAGHETGRLSGAADTQALLRNDQVYQPLRDRDDAQYSHLGGNWARNK | null | null | adaptive immune response [GO:0002250]; alpha-beta T cell activation [GO:0046631]; cell surface receptor signaling pathway [GO:0007166]; positive thymic T cell selection [GO:0045059]; T cell receptor signaling pathway [GO:0050852] | alpha-beta T cell receptor complex [GO:0042105]; clathrin-coated endocytic vesicle membrane [GO:0030669]; cytoplasm [GO:0005737]; external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886]; T cell receptor complex [GO:0042101] | identical protein binding [GO:0042802]; transmembrane signaling receptor activity [GO:0004888] | PF16680;PF02189; | 2.60.40.10;1.10.287.770; | null | PTM: Phosphorylated on Tyr residues after T-cell receptor triggering by LCK in association with CD4/CD8. {ECO:0000269|PubMed:2470098}. | SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Part of the TCR-CD3 complex present on T-lymphocyte cell surface that plays an essential role in adaptive immune response. When antigen presenting cells (APCs) activate T-cell receptor (TCR), TCR-mediated signals are transmitted across the cell membrane by the CD3 chains CD3D, CD3E, CD3G and CD3Z. All CD3 cha... | Homo sapiens (Human) |
P04235 | CD3D_MOUSE | MEHSGILASLILIAVLPQGSPFKIQVTEYEDKVFVTCNTSVMHLDGTVEGWFAKNKTLNLGKGVLDPRGIYLCNGTEQLAKVVSSVQVHYRMCQNCVELDSGTMAGVIFIDLIATLLLALGVYCFAGHETGRPSGAAEVQALLKNEQLYQPLRDREDTQYSRLGGNWPRNKKS | null | null | adaptive immune response [GO:0002250]; cell surface receptor signaling pathway [GO:0007166]; positive thymic T cell selection [GO:0045059]; protein-containing complex assembly [GO:0065003]; T cell activation [GO:0042110] | alpha-beta T cell receptor complex [GO:0042105]; external side of plasma membrane [GO:0009897]; T cell receptor complex [GO:0042101] | identical protein binding [GO:0042802]; transmembrane signaling receptor activity [GO:0004888] | PF16680;PF02189; | 2.60.40.10;1.10.287.770; | null | PTM: Phosphorylated on Tyr residues after T-cell receptor triggering by LCK in association with CD4/CD8. {ECO:0000250|UniProtKB:P04234}. | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Part of the TCR-CD3 complex present on T-lymphocyte cell surface that plays an essential role in adaptive immune response. When antigen presenting cells (APCs) activate T-cell receptor (TCR), TCR-mediated signals are transmitted across the cell membrane by the CD3 chains CD3D, CD3E, CD3G and CD3Z. All CD3 cha... | Mus musculus (Mouse) |
P04244 | HBB_PANPO | MSFLSAEEKNLVSGLWGKVNVDEVGGEALGRLLVVYPWTQRFFQSFGDLSSADAIMSNAKVKAHGKKVLNSFSDGLKNIDDLKGAFAKLSELHCDKLHVDPENFRLLGNVLVCVLAHHFGHEFNPQVQAAFQKVVAGVASALAHRYH | null | null | hydrogen peroxide catabolic process [GO:0042744] | blood microparticle [GO:0072562]; haptoglobin-hemoglobin complex [GO:0031838]; hemoglobin complex [GO:0005833] | haptoglobin binding [GO:0031720]; heme binding [GO:0020037]; hemoglobin alpha binding [GO:0031721]; metal ion binding [GO:0046872]; organic acid binding [GO:0043177]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601] | PF00042; | 1.10.490.10; | Globin family | null | null | null | null | null | null | null | FUNCTION: Involved in oxygen transport from the lung to the various peripheral tissues. | Panthera pardus orientalis (Amur leopard) |
P04247 | MYG_MOUSE | MGLSDGEWQLVLNVWGKVEADLAGHGQEVLIGLFKTHPETLDKFDKFKNLKSEEDMKGSEDLKKHGCTVLTALGTILKKKGQHAAEIQPLAQSHATKHKIPVKYLEFISEIIIEVLKKRHSGDFGADAQGAMSKALELFRNDIAAKYKELGFQG | 1.11.1.-; 1.7.-.- | null | brown fat cell differentiation [GO:0050873]; enucleate erythrocyte differentiation [GO:0043353]; heart development [GO:0007507]; oxygen transport [GO:0015671]; removal of superoxide radicals [GO:0019430]; response to hormone [GO:0009725]; response to hydrogen peroxide [GO:0042542]; response to hypoxia [GO:0001666] | extracellular exosome [GO:0070062]; sarcoplasm [GO:0016528] | heme binding [GO:0020037]; metal ion binding [GO:0046872]; nitrite reductase activity [GO:0098809]; oxygen binding [GO:0019825]; oxygen carrier activity [GO:0005344]; peroxidase activity [GO:0004601] | PF00042; | 6.10.140.2100;6.10.140.2110; | Globin family | null | SUBCELLULAR LOCATION: Cytoplasm, sarcoplasm {ECO:0000250|UniProtKB:P02144}. | CATALYTIC ACTIVITY: Reaction=Fe(III)-heme b-[protein] + H2O + nitric oxide = Fe(II)-heme b-[protein] + 2 H(+) + nitrite; Xref=Rhea:RHEA:77711, Rhea:RHEA-COMP:18975, Rhea:RHEA-COMP:18976, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:16480, ChEBI:CHEBI:55376, ChEBI:CHEBI:60344; Evidence={ECO:00002... | null | null | null | null | FUNCTION: Monomeric heme protein which primary function is to store oxygen and facilitate its diffusion within muscle tissues. Reversibly binds oxygen through a pentacoordinated heme iron and enables its timely and efficient release as needed during periods of heightened demand (PubMed:10468637, PubMed:11304494). Depen... | Mus musculus (Mouse) |
P04253 | HCY2_LIMPO | TLHDKQIRVCHLFEQLSSATVIGDGDKHKHSDRLKNVGKLQPGAIFSCFHPDHLEEARHLYEVFWEAGDFNDFIEIAKEARTFVNEGLFAFAAEVAVLHRDDCKGLYVPPVQEIFPDKFIPSAAINEAFKKAHVRPEFDESPILVDVQDTGNILDPEYRLAYYREDVGINAHHWHWHLVYPSTWNPKYFGKKKDRKGELFYYMHQQMCARYDCERLSNGMHRMLPFNNFDEPLAGYAPHLTHVASGKYYSPRPDGLKLRDLGDIEISEMVRMRERILDSIHLGYVISEDGSHKTLDELHGTDILGALVESSYESVNHEYY... | null | null | oxygen transport [GO:0015671] | extracellular region [GO:0005576] | chloride ion binding [GO:0031404]; copper ion binding [GO:0005507]; oxidoreductase activity [GO:0016491]; oxygen carrier activity [GO:0005344] | PF03723;PF00372;PF03722; | 1.10.1280.10;2.60.40.1520;1.20.1370.10; | Tyrosinase family, Hemocyanin subfamily | null | SUBCELLULAR LOCATION: Secreted, extracellular space. | null | null | null | null | null | FUNCTION: Hemocyanins are copper-containing oxygen carriers occurring freely dissolved in the hemolymph of many mollusks and arthropods. | Limulus polyphemus (Atlantic horseshoe crab) |
P04255 | H2B1_CAEEL | MPPKPSAKGAKKAAKTVTKPKDGKKRRHARKESYSVYIYRVLKQVHPDTGVSSKAMSIMNSFVNDVFERIAAEASRLAHYNKRSTISSREIQTAVRLILPGELAKHAVSEGTKAVTKYTSSK | null | null | null | chromatin [GO:0000785]; nucleosome [GO:0000786]; nucleus [GO:0005634] | DNA binding [GO:0003677]; protein heterodimerization activity [GO:0046982]; protein-containing complex binding [GO:0044877]; structural constituent of chromatin [GO:0030527] | PF00125; | 1.10.20.10; | Histone H2B family | PTM: Monoubiquitination of Lys-117 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation. {ECO:0000250}.; PTM: GlcNAcylation at Ser-109 promotes monoubiquitination of Lys-117. It fluctuates in response to extracellular glucose, and associ... | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... | Caenorhabditis elegans |
P04256 | ROA1_RAT | MSKSESPKEPEQLRKLFIGGLSFETTDESLRSHFEQWGTLTDCVVMRDPNTKRSRGFGFVTYATVEEVDAAMNARPHKVDGRVVEPKRAVSREDSQRPGAHLTVKKIFVGGIKEDTEEHHLRDYFEQYGKIEVIEIMTDRGSGKKRGFAFVTFDDHDSVDKIVIQKYHTVNGHNCEVRKALCKQEMASASSSQRGRSGSGNFGGGRGGGFGGNDNFGRGGNFSGRGGFGGSRGGGGYGGSGDGYNGFGNDGSNFGGGGSYNDFGNYNNQSSNFGPMKGGNFGGRSSGPYGGGGQYFAKPRNQGGYGGSSSSSSYGSGRRF | null | null | alternative mRNA splicing, via spliceosome [GO:0000380]; amyloid fibril formation [GO:1990000]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellular response to glucose starvation [GO:0042149]; cellular response to organic substance [GO:0071310]; cellular response to potassium ion [GO:0035865]; ... | catalytic step 2 spliceosome [GO:0071013]; cytoplasm [GO:0005737]; intracellular non-membrane-bounded organelle [GO:0043232]; nucleoplasm [GO:0005654]; nucleoplasmic periphery of the nuclear pore complex [GO:1990826]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904]; spliceosomal complex [GO:0005681]; synap... | DNA binding [GO:0003677]; DNA/DNA annealing activity [GO:1990814]; G-rich strand telomeric DNA binding [GO:0098505]; miRNA binding [GO:0035198]; molecular condensate scaffold activity [GO:0140693]; mRNA 3'-UTR binding [GO:0003730]; mRNA binding [GO:0003729]; pre-mRNA binding [GO:0036002]; protein domain specific bindin... | PF11627;PF00076; | 3.30.70.330; | null | PTM: Sumoylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P09651}. Cytoplasm {ECO:0000250|UniProtKB:P09651}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs. Shuttles continuously between the nucleus and the cytoplasm along with mRNA. Component of ribonucleosomes. {ECO:0000250|UniProtKB:P09651}. | null | null | null | null | null | FUNCTION: Involved in the packaging of pre-mRNA into hnRNP particles, transport of poly(A) mRNA from the nucleus to the cytoplasm and modulation of splice site selection. Plays a role in the splicing of pyruvate kinase PKM by binding repressively to sequences flanking PKM exon 9, inhibiting exon 9 inclusion and resulti... | Rattus norvegicus (Rat) |
P04258 | CO3A1_BOVIN | EYEAYDVKSGVAGGGIAGYPGPAGPPGPPGPPGTSGHPGAPGAPGYQGPPGEPGQAGPAGPPGPPGAIGPSGKDGESGRPGRPGPRGFPGPPGMKGPAGMPGFPGMKGHRGFDGRNGEKGEPGAPGLKGENGVPGEDGAPGPMGPRGAPGERGRPGLPGAAGARGNDGARGSDGQPGPPGPPGTAGFPGSPGAKGEVGPAGSPGSSGAPGQRGEPGPQGHAGAPGPPGPPGSDGSPGGKGEMGPAGIPGAPGLIGARGPPGPPGTNGVPGQRGAAGEPGKNGAKGDPGPRGERGEAGSPGIAGPKGEDGKDGSPGEPGAN... | null | null | cerebral cortex development [GO:0021987]; extracellular matrix organization [GO:0030198]; negative regulation of neuron migration [GO:2001223]; positive regulation of Rho protein signal transduction [GO:0035025] | collagen trimer [GO:0005581]; collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | extracellular matrix structural constituent conferring tensile strength [GO:0030020] | PF01391; | null | Fibrillar collagen family | PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains. {ECO:0000269|PubMed:488906, ECO:0000269|PubMed:488910, ECO:0000269|PubMed:488911}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. | null | null | null | null | null | FUNCTION: Collagen type III occurs in most soft connective tissues along with type I collagen. Involved in regulation of cortical development. Is the major ligand of ADGRG1 in the developing brain and binding to ADGRG1 inhibits neuronal migration and activates the RhoA pathway by coupling ADGRG1 to GNA13 and possibly G... | Bos taurus (Bovine) |
P04259 | K2C6B_HUMAN | MASTSTTIRSHSSSRRGFSANSARLPGVSRSGFSSISVSRSRGSGGLGGACGGAGFGSRSLYGLGGSKRISIGGGSCAISGGYGSRAGGSYGFGGAGSGFGFGGGAGIGFGLGGGAGLAGGFGGPGFPVCPPGGIQEVTVNQSLLTPLNLQIDPAIQRVRAEEREQIKTLNNKFASFIDKVRFLEQQNKVLDTKWTLLQEQGTKTVRQNLEPLFEQYINNLRRQLDNIVGERGRLDSELRNMQDLVEDLKNKYEDEINKRTAAENEFVTLKKDVDAAYMNKVELQAKADTLTDEINFLRALYDAELSQMQTHISDTSVVL... | null | null | ectoderm development [GO:0007398]; intermediate filament organization [GO:0045109]; keratinization [GO:0031424] | cytosol [GO:0005829]; extracellular exosome [GO:0070062]; keratin filament [GO:0045095] | structural constituent of cytoskeleton [GO:0005200]; structural constituent of skin epidermis [GO:0030280] | PF00038;PF16208; | 1.20.5.170;1.20.5.500;1.20.5.1160; | Intermediate filament family | null | null | null | null | null | null | null | null | Homo sapiens (Human) |
P04264 | K2C1_HUMAN | MSRQFSSRSGYRSGGGFSSGSAGIINYQRRTTSSSTRRSGGGGGRFSSCGGGGGSFGAGGGFGSRSLVNLGGSKSISISVARGGGRGSGFGGGYGGGGFGGGGFGGGGFGGGGIGGGGFGGFGSGGGGFGGGGFGGGGYGGGYGPVCPPGGIQEVTINQSLLQPLNVEIDPEIQKVKSREREQIKSLNNQFASFIDKVRFLEQQNQVLQTKWELLQQVDTSTRTHNLEPYFESFINNLRRRVDQLKSDQSRLDSELKNMQDMVEDYRNKYEDEINKRTNAENEFVTIKKDVDGAYMTKVDLQAKLDNLQQEIDFLTALYQ... | null | null | complement activation, lectin pathway [GO:0001867]; establishment of skin barrier [GO:0061436]; fibrinolysis [GO:0042730]; intermediate filament organization [GO:0045109]; keratinization [GO:0031424]; negative regulation of inflammatory response [GO:0050728]; peptide cross-linking [GO:0018149]; protein heterotetrameriz... | blood microparticle [GO:0072562]; collagen-containing extracellular matrix [GO:0062023]; cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; ficolin-1-rich granu... | carbohydrate binding [GO:0030246]; protein heterodimerization activity [GO:0046982]; signaling receptor activity [GO:0038023]; structural constituent of skin epidermis [GO:0030280] | PF00038;PF16208;PF16210; | 1.20.5.170;1.20.5.500;1.20.5.1160; | Intermediate filament family | PTM: Undergoes deimination of some arginine residues (citrullination). {ECO:0000269|PubMed:11841545, ECO:0000269|PubMed:8780679}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17956333}. Cytoplasm {ECO:0000269|PubMed:32179842}. | null | null | null | null | null | FUNCTION: May regulate the activity of kinases such as PKC and SRC via binding to integrin beta-1 (ITB1) and the receptor of activated protein C kinase 1 (RACK1). In complex with C1QBP is a high affinity receptor for kininogen-1/HMWK. {ECO:0000269|PubMed:17956333, ECO:0000269|PubMed:21544310}. | Homo sapiens (Human) |
P04268 | TPM1_CHICK | MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEERSKQLEDELVALQKKLKGTEDELDKYSESLKDAQEKLELADKKATDAESEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAQKDEEKMEIQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERAEERAELSESKCAELEEELKTVTNNLKSLEAQAEKYSQKEDKYEEEIKVLTDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMTSI | null | null | actin filament organization [GO:0007015]; cardiac muscle contraction [GO:0060048] | actin cytoskeleton [GO:0015629]; actin filament [GO:0005884]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | actin filament binding [GO:0051015]; cytoskeletal protein binding [GO:0008092]; identical protein binding [GO:0042802]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803] | PF00261; | 1.20.5.170;1.20.5.340; | Tropomyosin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P04692}. Note=Associates with F-actin stress fibers. {ECO:0000250|UniProtKB:P04692}. | null | null | null | null | null | FUNCTION: Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in sta... | Gallus gallus (Chicken) |
P04271 | S100B_HUMAN | MSELEKAMVALIDVFHQYSGREGDKHKLKKSELKELINNELSHFLEEIKEQEVVDKVMETLDNDGDGECDFQEFMAFVAMVTTACHEFFEHE | null | null | adaptive thermogenesis [GO:1990845]; axonogenesis [GO:0007409]; cell adhesion [GO:0007155]; central nervous system development [GO:0007417]; learning or memory [GO:0007611]; memory [GO:0007613]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of cell population prolifera... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; intracellular membrane-bounded organelle [GO:0043231]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; ruffle [GO:0001726]; sa... | calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; identical protein binding [GO:0042802]; ion binding [GO:0043167]; protein homodimerization activity [GO:0042803]; RAGE receptor binding [GO:0050786]; S100 protein binding [GO:0044548]; tau protein binding [GO:0048156]; zinc ion binding [G... | PF00036;PF01023; | 1.10.238.10; | S-100 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:9925766}. Nucleus {ECO:0000269|PubMed:9925766}. Secreted {ECO:0000250|UniProtKB:P50114}. Note=Secretion into the medium is promoted by interaction with isoform CLSTN3beta of CLSTN3. {ECO:0000250|UniProtKB:P50114}. | null | null | null | null | null | FUNCTION: Small zinc- and- and calcium-binding protein that is highly expressed in astrocytes and constitutes one of the most abundant soluble proteins in brain (PubMed:20950652, PubMed:6487634). Weakly binds calcium but binds zinc very tightly-distinct binding sites with different affinities exist for both ions on eac... | Homo sapiens (Human) |
P04272 | ANXA2_BOVIN | MSTVHEILCKLSLEGDHSTPPSAYGSVKAYTNFDAERDALNIETAIKTKGVDEVTIVNILTNRSNEQRQDIAFAYQRRTKKELASALKSALSGHLETVILGLLKTPAQYDASELKASMKGLGTDEDSLIEIICSRTNQELQEINRVYKEMYKTDLEKDIVSDTSGDFRKLMVALAKGRRAEDGSVIDYELIDQDARDLYDAGVKRKGTDVPKWISIMTERSVCHLQKVFERYKSYSPYDMLESIKKEVKGDLENAFLNLVQCIQNKPLYFADRLYDSMKGKGTRDKVLIRIMVSRSEVDMLKIRSEFKKKYGKSLYYYIQ... | null | null | biomineral tissue development [GO:0031214]; calcium ion import [GO:0070509]; calcium ion transmembrane transport [GO:0070588]; positive regulation of receptor-mediated endocytosis involved in cholesterol transport [GO:1905602] | basement membrane [GO:0005604]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endosome [GO:0005768]; extracellular membrane-bounded organelle [GO:0065010]; extracellular space [GO:0005615]; intracellular membrane-bounded organelle [GO:0043231]; melanosome [GO:0042470]; membrane [GO:0016020]; nucleus [GO:0005634]; plasm... | cadherin binding involved in cell-cell adhesion [GO:0098641]; calcium channel activity [GO:0005262]; calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; cytoskeletal protein binding [GO:0008092]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; phosphatidylserine binding [G... | PF00191; | 1.10.220.10; | Annexin family | PTM: ISGylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. Melanosome {ECO:0000250}. Note=In the lamina beneath the plasma membrane. | null | null | null | null | null | FUNCTION: Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids. It binds two calcium ions with high affinity. May be involved in heat-stress response. Inhibits PCSK9-enhanced LDLR degradation, probably reduces PCSK9 protein levels via a translational mechani... | Bos taurus (Bovine) |
P04273 | PRIO_MESAU | MANLSYWLLALFVAMWTDVGLCKKRPKPGGWNTGGSRYPGQGSPGGNRYPPQGGGTWGQPHGGGWGQPHGGGWGQPHGGGWGQPHGGGWGQGGGTHNQWNKPSKPKTNMKHMAGAAAAGAVVGGLGGYMLGSAMSRPMMHFGNDWEDRYYRENMNRYPNQVYYRPVDQYNNQNNFVHDCVNITIKQHTVTTTTKGENFTETDIKIMERVVEQMCTTQYQKESQAYYDGRRSSAVLFSSPPVILLISFLIFLMVG | null | null | amyloid fibril formation [GO:1990000]; calcium-mediated signaling using intracellular calcium source [GO:0035584]; cell cycle [GO:0007049]; cellular response to amyloid-beta [GO:1904646]; cellular response to copper ion [GO:0071280]; cellular response to xenobiotic stimulus [GO:0071466]; learning or memory [GO:0007611]... | cell surface [GO:0009986]; cytosol [GO:0005829]; dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; inclusion body [GO:0016234]; membrane raft [GO:0045121]; nuclear membrane [GO:0031965]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]; terminal bouton [GO:0043195] | amyloid-beta binding [GO:0001540]; aspartic-type endopeptidase inhibitor activity [GO:0019828]; copper ion binding [GO:0005507]; cupric ion binding [GO:1903135]; cuprous ion binding [GO:1903136]; glycosaminoglycan binding [GO:0005539]; identical protein binding [GO:0042802]; microtubule binding [GO:0008017]; molecular ... | PF00377;PF11587; | 1.10.790.10; | Prion family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P04156}; Lipid-anchor, GPI-anchor {ECO:0000250|UniProtKB:P04156}. Golgi apparatus {ECO:0000250|UniProtKB:P04925}. Note=Targeted to lipid rafts via association with the heparan sulfate chains of GPC1. Colocates, in the presence of Cu(2+), to vesicles in para- an... | null | null | null | null | null | FUNCTION: Its primary physiological function is unclear. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May promote myelin homeostasis through acting as an agonist for ADGRG6 receptor. May play a role in iron uptake and iron homeostasis. Soluble ... | Mesocricetus auratus (Golden hamster) |
P04274 | ADRB2_MESAU | MGPPGNDSDFLLTTNGSHVPDHDVTEERDEAWVVGMAILMSVIVLAIVFGNVLVITAIAKFERLQTVTNYFITSLACADLVMGLAVVPFGASHILMKMWNFGNFWCEFWTSIDVLCVTASIETLCVIAVDRYIAITSPFKYQSLLTKNKARMVILMVWIVSGLTSFLPIQMHWYRATHQKAIDCYHKETCCDFFTNQAYAIASSIVSFYVPLVVMVFVYSRVFQVAKRQLQKIDKSEGRFHSPNLGQVEQDGRSGHGLRRSSKFCLKEHKALKTLGIIMGTFTLCWLPFFIVNIVHVIQDNLIPKEVYILLNWLGYVNSA... | null | null | activation of adenylate cyclase activity [GO:0007190]; adenylate cyclase-activating adrenergic receptor signaling pathway [GO:0071880]; bone resorption [GO:0045453]; brown fat cell differentiation [GO:0050873]; cellular response to amyloid-beta [GO:1904646]; desensitization of G protein-coupled receptor signaling pathw... | apical plasma membrane [GO:0016324]; early endosome [GO:0005769]; Golgi apparatus [GO:0005794]; neuronal dense core vesicle [GO:0098992]; nucleus [GO:0005634]; receptor complex [GO:0043235] | adenylate cyclase binding [GO:0008179]; amyloid-beta binding [GO:0001540]; beta2-adrenergic receptor activity [GO:0004941]; norepinephrine binding [GO:0051380]; potassium channel regulator activity [GO:0015459]; protein homodimerization activity [GO:0042803]; protein-containing complex binding [GO:0044877] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family, Adrenergic receptor subfamily, ADRB2 sub-subfamily | PTM: Palmitoylated; may reduce accessibility of Ser-345 and Ser-346 by anchoring Cys-341 to the plasma membrane. Agonist stimulation promotes depalmitoylation and further allows Ser-345 and Ser-346 phosphorylation (By similarity). {ECO:0000250}.; PTM: Phosphorylated by PKA and BARK upon agonist stimulation, which media... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2547766}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P07550}. Early endosome {ECO:0000250|UniProtKB:P07550}. Golgi apparatus {ECO:0000250|UniProtKB:P07550}. Note=Colocalizes with VHL at the cell membrane. Activated receptors are internalized into endosomes... | null | null | null | null | null | FUNCTION: Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. The beta-2-adrenergic receptor binds epinephrine with an approximately 30-fold greater affinity than it does norepinephrine. {ECO:0000269|PubMed:2547766}. | Mesocricetus auratus (Golden hamster) |
P04275 | VWF_HUMAN | MIPARFAGVLLALALILPGTLCAEGTRGRSSTARCSLFGSDFVNTFDGSMYSFAGYCSYLLAGGCQKRSFSIIGDFQNGKRVSLSVYLGEFFDIHLFVNGTVTQGDQRVSMPYASKGLYLETEAGYYKLSGEAYGFVARIDGSGNFQVLLSDRYFNKTCGLCGNFNIFAEDDFMTQEGTLTSDPYDFANSWALSSGEQWCERASPPSSSCNISSGEMQKGLWEQCQLLKSTSVFARCHPLVDPEPFVALCEKTLCECAGGLECACPALLEYARTCAQEGMVLYGWTDHSACSPVCPAGMEYRQCVSPCARTCQSLHINEM... | null | null | blood coagulation [GO:0007596]; cell adhesion [GO:0007155]; cell-substrate adhesion [GO:0031589]; hemostasis [GO:0007599]; platelet activation [GO:0030168]; positive regulation of intracellular signal transduction [GO:1902533]; response to wounding [GO:0009611] | collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; platelet alpha granule [GO:0031091]; platelet alpha granule lumen [GO:0031093]; Weibel-Pa... | collagen binding [GO:0005518]; identical protein binding [GO:0042802]; immunoglobulin binding [GO:0019865]; integrin binding [GO:0005178]; protease binding [GO:0002020]; protein-folding chaperone binding [GO:0051087] | PF08742;PF01826;PF00092;PF16164;PF00093;PF00094; | 2.10.25.10;3.40.50.410; | null | PTM: All cysteine residues are involved in intrachain or interchain disulfide bonds.; PTM: N- and O-glycosylated. {ECO:0000269|PubMed:14760718, ECO:0000269|PubMed:19139490, ECO:0000269|PubMed:19159218}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10961880}. Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:10961880}. Note=Localized to storage granules. | null | null | null | null | null | FUNCTION: Important in the maintenance of hemostasis, it promotes adhesion of platelets to the sites of vascular injury by forming a molecular bridge between sub-endothelial collagen matrix and platelet-surface receptor complex GPIb-IX-V. Also acts as a chaperone for coagulation factor VIII, delivering it to the site o... | Homo sapiens (Human) |
P04276 | VTDB_RAT | MKRVLVLLLALAFGHALERGRDYEKDKVCQELSTLGKDDFRSLSLILYSRKFPSSTFEQVSQLVKEVVSLTEECCAEGADPNCYDTRTSELSIKSCESDAPFPVHPGTSECCTKEGLERKLCMAALSHQPQEFPAYVEPTNDEICEAFRKDPKGFADQFLFEYSSNYGQAPLPLLVGYTKSYLSMVGSCCTSAKPTVCFLKERLQMKQLLLLTTMSNRVCSQYAAYGKEKSRMSHLIKLAQKVPTANLEDVLPLAEDLTEILSRCCKSTSEDCMARELPEHTLKICGNLSKKNSKFEECCYETTPMGIFMCSYFMPTAEP... | null | null | female pregnancy [GO:0007565]; lactation [GO:0007595]; response to estradiol [GO:0032355]; response to nutrient levels [GO:0031667]; response to steroid hormone [GO:0048545]; vitamin D metabolic process [GO:0042359] | axon [GO:0030424]; blood microparticle [GO:0072562]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; perinuclear region of cytoplasm [GO:0048471] | actin binding [GO:0003779]; calcidiol binding [GO:1902118]; vitamin D binding [GO:0005499]; vitamin transmembrane transporter activity [GO:0090482] | PF00273;PF09164; | 1.10.246.10; | ALB/AFP/VDB family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3713442}. | null | null | null | null | null | FUNCTION: Involved in vitamin D transport and storage, scavenging of extracellular G-actin, enhancement of the chemotactic activity of C5 alpha for neutrophils in inflammation and macrophage activation. {ECO:0000250|UniProtKB:P02774}. | Rattus norvegicus (Rat) |
P04278 | SHBG_HUMAN | MESRGPLATSRLLLLLLLLLLRHTRQGWALRPVLPTQSAHDPPAVHLSNGPGQEPIAVMTFDLTKITKTSSSFEVRTWDPEGVIFYGDTNPKDDWFMLGLRDGRPEIQLHNHWAQLTVGAGPRLDDGRWHQVEVKMEGDSVLLEVDGEEVLRLRQVSGPLTSKRHPIMRIALGGLLFPASNLRLPLVPALDGCLRRDSWLDKQAEISASAPTSLRSCDVESNPGIFLPPGTQAEFNLRDIPQPHAEPWAFSLDLGLKQAAGSGHLLALGTPENPSWLSLHLQDQKVVLSSGSGPGLDLPLVLGLPLQLKLSMSRVVLSQG... | null | null | null | extracellular exosome [GO:0070062]; extracellular region [GO:0005576] | androgen binding [GO:0005497]; steroid binding [GO:0005496] | PF00054; | 2.60.120.200; | null | PTM: Variant Asn-356 contains one N-linked (GlcNAc...) at position 356. {ECO:0000269|PubMed:1400872, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=In testis, it is synthesized by the Sertoli cells, secreted into the lumen of the seminiferous tubule and transported to the epididymis. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Functions as an androgen transport protein, but may also be involved in receptor mediated processes. Each dimer binds one molecule of steroid. Specific for 5-alpha-dihydrotestosterone, testosterone, and 17-beta-estradiol. Regulates the plasma metabolic clearance rate of steroid hormones by controlling their p... | Homo sapiens (Human) |
P04279 | SEMG1_HUMAN | MKPNIIFVLSLLLILEKQAAVMGQKGGSKGRLPSEFSQFPHGQKGQHYSGQKGKQQTESKGSFSIQYTYHVDANDHDQSRKSQQYDLNALHKTTKSQRHLGGSQQLLHNKQEGRDHDKSKGHFHRVVIHHKGGKAHRGTQNPSQDQGNSPSGKGISSQYSNTEERLWVHGLSKEQTSVSGAQKGRKQGGSQSSYVLQTEELVANKQQRETKNSHQNKGHYQNVVEVREEHSSKVQTSLCPAHQDKLQHGSKDIFSTQDELLVYNKNQHQTKNLNQDQQHGRKANKISYQSSSTEERRLHYGENGVQKDVSQSSIYSQTEE... | null | null | antibacterial humoral response [GO:0019731]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; coagulation [GO:0050817]; insemination [GO:0007320]; killing of cells of another organism [GO:0031640]; negative regulation of calcium ion import [GO:0090281]; negative regulation of flagel... | extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; nucleus [GO:0005634]; protein-containing complex [GO:0032991] | zinc ion binding [GO:0008270] | PF05474; | null | Semenogelin family | PTM: Transglutaminase substrate.; PTM: Rapidly cleaved after ejaculation by KLK3/PSA, resulting in liquefaction of the semen coagulum and the progressive release of motile spermatozoa. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Predominant protein in semen. It participates in the formation of a gel matrix entrapping the accessory gland secretions and ejaculated spermatozoa. Fragments of semenogelin and/or fragments of the related proteins may contribute to the activation of progressive sperm movements as the gel-forming proteins are... | Homo sapiens (Human) |
P04280 | PRP1_HUMAN | MLLILLSVALLALSSAQNLNEDVSQEESPSLIAGNPQGPSPQGGNKPQGPPPPPGKPQGPPPQGGNKPQGPPPPGKPQGPPPQGDKSRSPRSPPGKPQGPPPQGGNQPQGPPPPPGKPQGPPPQGGNKPQGPPPPGKPQGPPPQGDKSQSPRSPPGKPQGPPPQGGNQPQGPPPPPGKPQGPPPQGGNKPQGPPPPGKPQGPPPQGDKSQSPRSPPGKPQGPPPQGGNQPQGPPPPPGKPQGPPQQGGNRPQGPPPPGKPQGPPPQGDKSRSPQSPPGKPQGPPPQGGNQPQGPPPPPGKPQGPPPQGGNKPQGPPPPGK... | null | null | null | extracellular space [GO:0005615] | null | PF15240; | null | null | PTM: O-glycosylated. O-glycosylation on Ser-87 is prevalent in head and neck cancer patients. O-Glycosylation on Ser-330 has a 5 times prevalence in head and neck cancers. {ECO:0000269|PubMed:20879038}.; PTM: Proteolytically cleaved at the tripeptide Xaa-Pro-Gln, where Xaa in the P(3) position is mostly lysine. The end... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3521730}. | null | null | null | null | null | null | Homo sapiens (Human) |
P04289 | CEP3_HHV11 | MGLSFSGARPCCCRNNVLITDDGEVVSLTAHDFDVVDIESEEEGNFYVPPDMRGVTRAPGRQRLRSSDPPSRHTHRRTPGGACPATQFPPPMSDSE | null | null | anatomical structure morphogenesis [GO:0009653]; viral budding from Golgi membrane [GO:0046760] | host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral tegument [GO:0019033]; virion membrane [GO:0055036] | null | PF11094; | null | Herpesviridae cytoplasmic envelopment protein 3 family | PTM: Myristoylation and palmitoylation (probably on one or more of the nearby cysteines at the N-terminus) enable membrane-binding and Golgi apparatus-specific targeting and are essential for efficient packaging. {ECO:0000255|HAMAP-Rule:MF_04040, ECO:0000269|PubMed:11711612, ECO:0000269|PubMed:16928743}.; PTM: Phosphor... | SUBCELLULAR LOCATION: Virion tegument {ECO:0000255|HAMAP-Rule:MF_04040, ECO:0000269|PubMed:1312117, ECO:0000269|PubMed:18596102}. Virion membrane {ECO:0000255|HAMAP-Rule:MF_04040}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04040}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04040, ECO:0000269|PubMed:11711612}; Lipid-an... | null | null | null | null | null | FUNCTION: Plays an important role in the cytoplasmic envelopment of tegument proteins and capsids during the assembly and egress processes. Participates also in viral entry at the fusion step probably by regulating the core fusion machinery. {ECO:0000255|HAMAP-Rule:MF_04040, ECO:0000269|PubMed:1321297, ECO:0000269|PubM... | Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) |
P04290 | UL13_HHV11 | MDESRRQRPAGHVAANLSPQGARQRSFKDWLASYVHSNPHGASGRPSGPSLQDAAVSRSSHGSRHRSGLRERLRAGLSRWRMSRSSHRRASPETPGTAAKLNRPPLRRSQAALTAPPSSPSHILTLTRIRKLCSPVFAINPALHYTTLEIPGARSFGGSGGYGDVQLIREHKLAVKTIKEKEWFAVELIATLLVGECVLRAGRTHNIRGFIAPLGFSLQQRQIVFPAYDMDLGKYIGQLASLRTTNPSVSTALHQCFTELARAVVFLNTTCGISHLDIKCANILVMLRSDAVSLRRAVLADFSLVTLNSNSTIARGQFCL... | 2.7.11.1 | null | phosphorylation [GO:0016310] | host cell nucleus [GO:0042025]; viral tegument [GO:0019033] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | null | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | PTM: Autophosphorylated. | SUBCELLULAR LOCATION: Virion tegument {ECO:0000269|PubMed:18596102}. Host nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Multifunctional serine/threonine kinase that plays a role in several processes including egress of virus particles from the nucleus, modulation of the actin cytoskeleton and regulation of viral and cellular gene expression. Regulates the nuclear localization of viral envelopment factors UL34 and UL31, by phos... | Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) |
P04293 | DPOL_HHV11 | MFSGGGGPLSPGGKSAARAASGFFAPAGPRGASRGPPPCLRQNFYNPYLAPVGTQQKPTGPTQRHTYYSECDEFRFIAPRVLDEDAPPEKRAGVHDGHLKRAPKVYCGGDERDVLRVGSGGFWPRRSRLWGGVDHAPAGFNPTVTVFHVYDILENVEHAYGMRAAQFHARFMDAITPTGTVITLLGLTPEGHRVAVHVYGTRQYFYMNKEEVDRHLQCRAPRDLCERMAAALRESPGASFRGISADHFEAEVVERTDVYYYETRPALFYRVYVRSGRVLSYLCDNFCPAIKKYEGGVDATTRFILDNPGFVTFGWYRLKP... | 2.7.7.7; 3.1.26.4 | null | base-excision repair, gap-filling [GO:0006287]; bidirectional double-stranded viral DNA replication [GO:0039686]; DNA replication proofreading [GO:0045004]; nucleotide-excision repair, DNA gap filling [GO:0006297]; SOS response [GO:0009432] | DNA polymerase complex [GO:0042575]; host cell nucleus [GO:0042025] | 3'-5'-DNA exonuclease activity [GO:0008296]; 5'-3' exonuclease activity [GO:0008409]; DNA binding [GO:0003677]; DNA polymerase activity [GO:0034061]; DNA-directed DNA polymerase activity [GO:0003887]; nucleotide binding [GO:0000166]; RNA-DNA hybrid ribonuclease activity [GO:0004523] | PF00136;PF03104;PF11590; | 1.10.132.60;3.30.342.10;1.10.287.690;3.90.1600.10;3.30.420.10; | DNA polymerase type-B family | null | SUBCELLULAR LOCATION: Host nucleus {ECO:0000305}. Note=The protein is present at discrete sites in nuclei, called replication compartments where viral DNA replication occurs. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; ... | null | null | null | null | FUNCTION: Replicates viral genomic DNA. The replication complex is composed of six viral proteins: the DNA polymerase, processivity factor, primase, primase-associated factor, helicase, and ssDNA-binding protein. Additionally, the polymerase contains an intrinsic ribonuclease H (RNase H) activity that specifically degr... | Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) |
P04296 | DNBI_HHV11 | METKPKTATTIKVPPGPLGYVYARACPSEGIELLALLSARSGDSDVAVAPLVVGLTVESGFEANVAVVVGSRTTGLGGTAVSLKLTPSHYSSSVYVFHGGRHLDPSTQAPNLTRLCERARRHFGFSDYTPRPGDLKHETTGEALCERLGLDPDRALLYLVVTEGFKEAVCINNTFLHLGGSDKVTIGGAEVHRIPVYPLQLFMPDFSRVIAEPFNANHRSIGEKFTYPLPFFNRPLNRLLFEAVVGPAAVALRCRNVDAVARAAAHLAFDENHEGAALPADITFTAFEASQGKTPRGGRDGGGKGAAGGFEQRLASVMAG... | null | null | bidirectional double-stranded viral DNA replication [GO:0039686]; DNA replication [GO:0006260] | host cell nucleus [GO:0042025]; nuclear viral factory [GO:0039715] | DNA binding [GO:0003677]; metal ion binding [GO:0046872]; single-stranded DNA binding [GO:0003697] | PF00747; | 1.10.150.560;1.20.190.40; | Herpesviridae major DNA-binding protein family | null | SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04007, ECO:0000269|PubMed:26676794, ECO:0000269|PubMed:9151871}. Note=In the absence of DNA replication, found in the nuclear framework-associated structures (prereplicative sites). As viral DNA replication proceeds, it migrates to globular intranuclear stru... | null | null | null | null | null | FUNCTION: Plays several crucial roles in viral infection. Participates in the opening of the viral DNA origin to initiate replication by interacting with the origin-binding protein. May disrupt loops, hairpins and other secondary structures present on ssDNA to reduce and eliminate pausing of viral DNA polymerase at spe... | Human herpesvirus 1 (strain 17) (HHV-1) (Human herpes simplex virus 1) |
P04298 | MCEL_VACCW | MDANVVSSSTIATYIDALAKNASELEQRSTAYEINNELELVFIKPPLITLTNVVNISTIQESFIRFTVTNKEGVKIRTKIPLSKVHGLDVKNVQLVDAIDNIVWEKKSLVTENRLHKECLLRLSTEERHIFLDYKKYGSSIRLELVNLIQAKTKNFTIDFKLKYFLGSGAQSKSSLLHAINHPKSRPNTSLEIEFTPRDNETVPYDELIKELTTLSRHIFMASPENVILSPPINAPIKTFMLPKQDIVGLDLENLYAVTKTDGIPITIRVTSNGLYCYFTHLGYIIRYPVKRIIDSEVVVFGEAVKDKNWTVYLIKLIEP... | 2.1.1.56; 2.7.7.50; 3.6.1.74 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305|PubMed:2164022, ECO:0000305|PubMed:24607143}; | DNA-templated transcription termination [GO:0006353] | virion component [GO:0044423] | GTP binding [GO:0005525]; inorganic triphosphate phosphatase activity [GO:0050355]; metal ion binding [GO:0046872]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; mRNA 5'-phosphatase activity [GO:0140818]; mRNA guanylyltransferase activity [GO:0004484]; polynucleotide 5'-phosphatase activity [GO:000... | PF21004;PF21005;PF10640;PF03291; | 2.40.50.830;3.20.100.20;3.30.470.140;3.40.50.150; | DsDNA virus mRNA guanylyltransferase family; Class I-like SAM-binding methyltransferase superfamily, mRNA cap 0 methyltransferase family | null | SUBCELLULAR LOCATION: Virion {ECO:0000305}. Note=All the enzymes and other proteins required to synthesize early mRNAs are packaged within the virion core along with the DNA genome. | CATALYTIC ACTIVITY: Reaction=a 5'-end triphospho-ribonucleoside in mRNA + H2O = a 5'-end diphospho-ribonucleoside in mRNA + H(+) + phosphate; Xref=Rhea:RHEA:67004, Rhea:RHEA-COMP:17164, Rhea:RHEA-COMP:17165, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:167616, ChEBI:CHEBI:167618; EC=3.6.1.74; Ev... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=23 uM for GpppA {ECO:0000269|PubMed:18256245}; Note=A-570 and A-763 mutants have 3-fold and 10-fold higher Km values for GpppA.; | null | null | null | FUNCTION: Catalytic subunit of the mRNA capping enzyme which catalyzes three enzymatic reactions: the 5' triphosphate end of the pre-mRNA is hydrolyzed to a diphosphate by RNA 5' triphosphatase; the diphosphate RNA end is capped with GMP by RNA guanylyltransferase and the GpppN cap is methylated by RNA (guanine-N7) met... | Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR)) |
P04305 | PG117_VACCW | MDAAIRGNDVIFVLKTIGVPSACRQNEDPRFVEAFKCDELERYIENNPECTLFESLRDEEAYSIVRIFMDVDLDACLDEIDYLTAIQDFIIEVSNCVARFAFTECGAIHENVIKSMRSNFSLTKSTNRDKTSFHIIFLDTYTTMDTLIAMKRTLLELSRSSENPLTRSIDTAVYRRKTTLRVVGTRKNPNCDTIHVMQPPHDNIEDYLFTYVDMNNNSYYFSLQQRLEDLVPDKLWEPGFISFEDAIKRVSKIFINSIINFNDLDENNFTTVPLVIDYVTPCALCKKRSHKHPHQLSLENGAIRIYKTGNPHSCKVKIVP... | 3.6.4.- | null | DNA replication, synthesis of RNA primer [GO:0006269]; viral DNA genome replication [GO:0039693] | host cell cytoplasm [GO:0030430] | ATP binding [GO:0005524]; DNA primase activity [GO:0003896]; helicase activity [GO:0004386]; ribonucleoside triphosphate phosphatase activity [GO:0017111] | PF08706;PF03288; | 3.40.50.300; | Orthopoxvirus OPG117 family | null | SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000269|PubMed:24439902}. Note=Colocalizes with free cytoplasmic cores containing the viral DNA genome. {ECO:0000269|PubMed:24439902}. | null | null | null | null | null | FUNCTION: Multifunctional protein required for genome uncoating and replication (PubMed:17093187, PubMed:18000036, PubMed:26912611). Major viral uncoating protein that is required for the release of the viral genome from incoming viral cores containing the viral DNA genome (PubMed:24439902). Possesses an ATPase activit... | Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR)) |
P04312 | PG122_VACCW | MNFYRSSIISQIIKYNRRLAKSIICEDDSQIITLTAFVNQCLWCHKRVSVSAILLTTDNKILVCNRRDSFLYSEIIRTRNMFRKKRLFLNYSNYLNKQERSILSSFFSLDPATADNDRIDAIYPGGIPKRGENVPECLSREIKEEVNIDNSFVFIDTRFFIHGIIEDTIINKFFEVIFFVGRISLTSDQIIDTFKSNHEIKDLIFLDPNSGNGLQYEIAKYALDTAKLKCYGHRGCYYESLKKLTEDD | 3.1.3.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:19210265}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:19210265}; | null | host cell mitochondrion [GO:0033650] | metal ion binding [GO:0046872]; phosphatase activity [GO:0016791] | PF00293;PF08476; | 3.90.79.10; | Nudix hydrolase family | null | SUBCELLULAR LOCATION: Host mitochondrion {ECO:0000269|PubMed:35435699}. Note=Mitochondria localization is required to efficiently decap mRNAs. {ECO:0000269|PubMed:35435699}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.4 nM for capped RNA; | null | null | null | FUNCTION: Decapping enzyme that remove the protective 5'-cap from both host and viral mRNAs to commit transcripts for decay by the cellular exonuclease XRN1 (PubMed:24155373, PubMed:35202449). Preferentially targets spliced mRNAs and since all viral genes are intronless, it preferentially targets host over viral transc... | Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR)) |
P04324 | NEF_HV112 | MGGKWSKSSVVGWPAVRERMRRAEPAADGVGAASRDLEKHGAITSSNTAANNAACAWLEAQEEEKVGFPVTPQVPLRPMTYKAAVDLSHFLKEKGGLEGLIHSQRRQDILDLWIYHTQGYFPDWQNYTPGPGIRYPLTFGWCYKLVPVEPEKLEEANKGENTSLLHPVSLHGMDDPEREVLEWRFDSRLAFHHVARELHPEYFKNC | null | null | negative regulation of CD4 production [GO:0045225]; perturbation by virus of host immune response [GO:0075528]; regulation of calcium-mediated signaling [GO:0050848]; suppression by virus of host autophagy [GO:0039521]; symbiont-mediated suppression of host antigen processing and presentation of peptide antigen via MHC... | extracellular region [GO:0005576]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion component [GO:0044423] | ATPase binding [GO:0051117]; CD4 receptor binding [GO:0042609]; GTP binding [GO:0005525]; MHC class I protein binding [GO:0042288]; protein kinase binding [GO:0019901]; SH3 domain binding [GO:0017124]; signaling receptor binding [GO:0005102]; thioesterase binding [GO:0031996] | PF00469; | 4.10.890.10;3.30.62.10; | Lentivirus primate group Nef protein family | PTM: The virion-associated Nef proteins are cleaved by the viral protease to release the soluble C-terminal core protein. Nef is probably cleaved concomitantly with viral structural proteins on maturation of virus particles. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04078}.; PTM... | SUBCELLULAR LOCATION: Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04078}; Lipid-anchor {ECO:0000255|HAMAP-Rule:MF_04078}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04078}. Virion {ECO:0000255|HAMAP-Rule:MF_04078}. Secreted {ECO:0000255|HAMAP-Rule:MF_04078}. Host Golgi apparatus membrane {ECO:0000255|HAMAP-Rule:MF_0... | null | null | null | null | null | FUNCTION: Factor of infectivity and pathogenicity, required for optimal virus replication. Alters numerous pathways of T-lymphocyte function and down-regulates immunity surface molecules in order to evade host defense and increase viral infectivity. Alters the functionality of other immunity cells, like dendritic cells... | Human immunodeficiency virus type 1 group M subtype B (isolate PCV12) (HIV-1) |
P04326 | TAT_HV112 | MEPVDPRLEPWKHPGSQPKTACTNCYCKKCCFHCQVCFITKALGISYGRKKRRQRRRAPQGSQTHQVSLSKQPTSQSRGDPTGPKE | null | null | DNA-templated transcription [GO:0006351]; modulation by virus of host chromatin organization [GO:0039525]; negative regulation of peptidyl-threonine phosphorylation [GO:0010801]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of viral transcription [GO:0050434]; s... | extracellular region [GO:0005576]; host cell cytoplasm [GO:0030430]; host cell nucleolus [GO:0044196] | actinin binding [GO:0042805]; cyclin binding [GO:0030332]; metal ion binding [GO:0046872]; protein domain specific binding [GO:0019904]; protein serine/threonine phosphatase inhibitor activity [GO:0004865]; RNA-binding transcription regulator activity [GO:0001070]; trans-activation response element binding [GO:1990970] | PF00539; | 4.10.20.10; | Lentiviruses Tat family | PTM: Asymmetrical arginine methylation by host PRMT6 seems to diminish the transactivation capacity of Tat and affects the interaction with host CCNT1. {ECO:0000255|HAMAP-Rule:MF_04079}.; PTM: Acetylation by EP300, CREBBP, GCN5L2/GCN5 and PCAF regulates the transactivation activity of Tat. EP300-mediated acetylation of... | SUBCELLULAR LOCATION: Host nucleus, host nucleolus {ECO:0000255|HAMAP-Rule:MF_04079}. Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04079}. Secreted {ECO:0000255|HAMAP-Rule:MF_04079}. Note=Probably localizes to both nuclear and nucleolar compartments. Nuclear localization is mediated through the interaction of the nuclear ... | null | null | null | null | null | FUNCTION: Transcriptional activator that increases RNA Pol II processivity, thereby increasing the level of full-length viral transcripts. Recognizes a hairpin structure at the 5'-LTR of the nascent viral mRNAs referred to as the transactivation responsive RNA element (TAR) and recruits the cyclin T1-CDK9 complex (P-TE... | Human immunodeficiency virus type 1 group M subtype B (isolate PCV12) (HIV-1) |
P04347 | GLYG5_SOYBN | MGKPFFTLSLSSLCLLLLSSACFAITSSKFNECQLNNLNALEPDHRVESEGGLIETWNSQHPELQCAGVTVSKRTLNRNGSHLPSYLPYPQMIIVVQGKGAIGFAFPGCPETFEKPQQQSSRRGSRSQQQLQDSHQKIRHFNEGDVLVIPLGVPYWTYNTGDEPVVAISPLDTSNFNNQLDQNPRVFYLAGNPDIEHPETMQQQQQQKSHGGRKQGQHRQQEEEGGSVLSGFSKHFLAQSFNTNEDTAEKLRSPDDERKQIVTVEGGLSVISPKWQEQEDEDEDEDEEYGRTPSYPPRRPSHGKHEDDEDEDEEEDQPRP... | null | null | null | aleurone grain [GO:0033095]; endoplasmic reticulum [GO:0005783]; protein storage vacuole [GO:0000326] | nutrient reservoir activity [GO:0045735] | PF00190; | 2.60.120.10; | 11S seed storage protein (globulins) family | PTM: During soybean germination, seed storage proteins are hydrolyzed by protease/26S proteasome. {ECO:0000269|PubMed:29037738}. | SUBCELLULAR LOCATION: Vacuole, aleurone grain. Endoplasmic reticulum {ECO:0000269|PubMed:29348620}. Protein storage vacuole {ECO:0000269|PubMed:29348620}. Note=Hexamers are assembled in the endoplasmic reticulum and later sorted to the protein storage vacuoles (PubMed:29348620). Cotyledonary membrane-bound vacuolar pro... | null | null | null | null | null | FUNCTION: Glycinin is the major seed storage protein of soybean (PubMed:2485233). Glycinin basic peptides (GBPs), and, to a lower extent, glycinin exhibit antibacterial activity against Gram-negative and Gram-positive bacteria (e.g. L.monocytogenes, B.subtilis, E.coli and S.enteritidis) by forming pores and aggregating... | Glycine max (Soybean) (Glycine hispida) |
P04350 | TBB4A_HUMAN | MREIVHLQAGQCGNQIGAKFWEVISDEHGIDPTGTYHGDSDLQLERINVYYNEATGGNYVPRAVLVDLEPGTMDSVRSGPFGQIFRPDNFVFGQSGAGNNWAKGHYTEGAELVDAVLDVVRKEAESCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEFPDRIMNTFSVVPSPKVSDTVVEPYNATLSVHQLVENTDETYCIDNEALYDICFRTLKLTTPTYGDLNHLVSATMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMMAACDPRHGRYLTVAAVFRGR... | null | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363}; | microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278]; negative regulation of microtubule polymerization [GO:0031115] | axoneme [GO:0005930]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; intercellular bridge [GO:0045171]; internode region of axon [GO:0033269]; microtubule [GO:0005874]; microtubule cytoskeleton [GO:0015630]; mitotic spindle [GO:0072686]; myelin sheath [GO:0043209]; neuronal cell body ... | calcium ion binding [GO:0005509]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; structural constituent of cytoskeleton [GO:0005200] | PF00091;PF03953; | 1.10.287.600;3.30.1330.20;3.40.50.1440; | Tubulin family | PTM: Some glutamate residues at the C-terminus are polyglutamylated, resulting in polyglutamate chains on the gamma-carboxyl group (PubMed:26875866). Polyglutamylation plays a key role in microtubule severing by spastin (SPAST). SPAST preferentially recognizes and acts on microtubules decorated with short polyglutamate... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. | null | null | null | null | null | FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers a... | Homo sapiens (Human) |
P04351 | IL2_MOUSE | MYSMQLASCVTLTLVLLVNSAPTSSSTSSSTAEAQQQQQQQQQQQQHLEQLLMDLQELLSRMENYRNLKLPRMLTFKFYLPKQATELKDLQCLEDELGPLRHVLDLTQSKSFQLEDAENFISNIRVTVVKLKGSDNTFECQFDDESATVVDFLRRWIAFCQSIISTSPQ | null | null | activated T cell proliferation [GO:0050798]; adaptive immune response [GO:0002250]; extrinsic apoptotic signaling pathway in absence of ligand [GO:0097192]; G protein-coupled receptor signaling pathway [GO:0007186]; gene expression [GO:0010467]; interleukin-2-mediated signaling pathway [GO:0038110]; leukocyte activatio... | extracellular space [GO:0005615] | carbohydrate binding [GO:0030246]; cytokine activity [GO:0005125]; glycosphingolipid binding [GO:0043208]; growth factor activity [GO:0008083]; interleukin-2 receptor binding [GO:0005134]; kappa-type opioid receptor binding [GO:0031851] | PF00715; | 1.20.1250.10; | IL-2 family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Cytokine produced by activated CD4-positive helper T-cells and to a lesser extend activated CD8-positive T-cells and natural killer (NK) cells that plays pivotal roles in the immune response and tolerance (PubMed:14614860, PubMed:9814585). Binds to a receptor complex composed of either the high-affinity trime... | Mus musculus (Mouse) |
P04354 | CALB1_CHICK | MTAETHLQGVEISAAQFFEIWHHYDSDGNGYMDGKELQNFIQELQQARKKAGLDLTPEMKAFVDQYGKATDGKIGIVELAQVLPTEENFLLFFRCQQLKSSEDFMQTWRKYDSDHSGFIDSEELKSFLKDLLQKANKQIEDSKLTEYTEIMLRMFDANNDGKLELTELARLLPVQENFLIKFQGVKMCAKEFNKAFEMYDQDGNGYIDENELDALLKDLCEKNKKELDINNLATYKKSIMALSDGGKLYRAELALILCAEEN | null | null | calcium ion transport [GO:0006816]; intracellular calcium ion homeostasis [GO:0006874]; regulation of long-term synaptic potentiation [GO:1900271]; regulation of presynaptic cytosolic calcium ion concentration [GO:0099509]; sensory perception of pain [GO:0019233] | cytosol [GO:0005829]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; nucleus [GO:0005634]; postsynaptic membrane [GO:0045211]; synapse [GO:0045202]; terminal bouton [GO:0043195]; vesicle membrane [GO:0012506] | calcium ion binding [GO:0005509]; vitamin D binding [GO:0005499] | PF00036;PF13499; | 1.10.238.10; | Calbindin family | null | null | null | null | null | null | null | FUNCTION: Buffers cytosolic calcium. May stimulate a membrane Ca(2+)-ATPase and a 3',5'-cyclic nucleotide phosphodiesterase. | Gallus gallus (Chicken) |
P04361 | PA2HB_AGKPI | SVLELGKMILQETGKNAITSYGSYGCNCGWGHRGQPKDATDRCCFVHKCCYKKLTDCNHKTDRYSYSWKNKAIICEEKNPCLKEMCECDKAVAICLRENLDTYNKKYKAYFKLKCKKPDTC | null | null | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, K49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:28633930, ECO:0000269|PubMed:3082870}. | null | null | null | null | null | FUNCTION: Snake venom phospholipase A2 (PLA2) that lacks enzymatic activity (PubMed:1429612, PubMed:28633930). Displays edema-inducing activities (PubMed:1429612). Is myotoxic (By similarity). A model of myotoxic mechanism has been proposed: an apo Lys49-PLA2 is activated by the entrance of a hydrophobic molecule (e.g.... | Agkistrodon piscivorus piscivorus (Eastern cottonmouth) |
P04366 | AMBP_PIG | AVSASPVLTLPNDIQVQENFDLSRIYGKWFHVAVGSTCPWLKRFKDKMTMGTLMLGEGATEREISVTKTHRRKGICEVISGAYEKTSTDGKFLYHKSKWNITMESYVVHTNYDEYAIFLTKKFSRRHGPTLTAKLYGREPQLRESLLEEFREVALGVGIPEDSIFTMPDRGECVPGEQEPEPTLLSRARRAVLPQEEEGSGAGQPVADFSKKEDSCQLGYSQGPCLGMIKRYFYNGSSMACETFHYGGCMGNGNNFVSEKECLQTCRTVEACSLPIVSGPCRGFFQLWAFDAVQGKCVLFNYGGCQGNGNQFYSEKECKE... | 1.6.2.- | null | null | cell surface [GO:0009986]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; mitochondrial inner membrane [GO:0005743]; nuclear membrane [GO:0031965]; plasma membrane [GO:0005886] | heme binding [GO:0020037]; IgA binding [GO:0019862]; oxidoreductase activity [GO:0016491]; protein homodimerization activity [GO:0042803]; serine-type endopeptidase inhibitor activity [GO:0004867] | PF00014;PF00061; | 2.40.128.20;4.10.410.10; | Calycin superfamily, Lipocalin family | PTM: The precursor is proteolytically processed into separately functioning proteins. {ECO:0000250|UniProtKB:P02760}.; PTM: [Alpha-1-microglobulin]: Proteolytically cleaved in the presence of oxyhemoglobin or MPO. {ECO:0000250|UniProtKB:P02760}.; PTM: [Alpha-1-microglobulin]: 3-hydroxykynurenine, an oxidized tryptophan... | SUBCELLULAR LOCATION: [Alpha-1-microglobulin]: Secreted {ECO:0000250|UniProtKB:P02760}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P02760}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P02760}. Cell membrane {ECO:0000250|UniProtKB:P02760}; Peripheral membrane protein {ECO:0000250|UniProtKB:P02760}. Nucleus membrane {ECO... | null | null | null | null | null | FUNCTION: [Alpha-1-microglobulin]: Antioxidant and tissue repair protein with reductase, heme-binding and radical-scavenging activities. Removes and protects against harmful oxidants and repairs macromolecules in intravascular and extravascular spaces and in intracellular compartments. Intravascularly, plays a regulato... | Sus scrofa (Pig) |
P04370 | MBP_MOUSE | MGNHSGKRELSAEKASKDGEIHRGEAGKKRSVGKLSQTASEDSDVFGEADAIQNNGTSAEDTAVTDSKHTADPKNNWQGAHPADPGNRPHLIRLFSRDAPGREDNTFKDRPSESDELQTIQEDPTAASGGLDVMASQKRPSQRSKYLATASTMDHARHGFLPRHRDTGILDSIGRFFSGDRGAPKRGSGKDSHTRTTHYGSLPQKSQHGRTQDENPVVHFFKNIVTPRTPPPSQGKGGRDSRSGSPMARR | null | null | maintenance of blood-brain barrier [GO:0035633]; MAPK cascade [GO:0000165]; membrane organization [GO:0061024]; myelination [GO:0042552]; negative regulation of axonogenesis [GO:0050771]; negative regulation of heterotypic cell-cell adhesion [GO:0034115]; positive regulation of chemokine (C-X-C motif) ligand 2 producti... | cell periphery [GO:0071944]; cell projection [GO:0042995]; cell surface [GO:0009986]; compact myelin [GO:0043218]; cytoplasm [GO:0005737]; internode region of axon [GO:0033269]; myelin sheath [GO:0043209]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-containing complex [G... | calmodulin binding [GO:0005516]; protease binding [GO:0002020]; structural constituent of myelin sheath [GO:0019911] | PF01669; | null | Myelin basic protein family | PTM: As in other animals, several charge isomers may be produced as a result of optional post-translational modifications, such as phosphorylation of serine or threonine residues, deamidation of glutamine or asparagine residues, citrullination and methylation of arginine residues.; PTM: Methylated on arginine residues;... | SUBCELLULAR LOCATION: [Isoform 13]: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.; SUBCELLULAR LOCATION: [Isoform 12]: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.; SUBCELLULAR LOCATION: [Isoform 11]: Myelin membrane; Peripheral membrane protein; Cytoplasmic side.; SUBCELLULAR LOCAT... | null | null | null | null | null | FUNCTION: The classic group of MBP isoforms (isoform 4-isoform 13) are with PLP the most abundant protein components of the myelin membrane in the CNS. They have a role in both its formation and stabilization. The non-classic group of MBP isoforms (isoform 1-isoform 3/Golli-MBPs) may preferentially have a role in the e... | Mus musculus (Mouse) |
P04385 | GAL1_YEAST | MTKSHSEEVIVPEFNSSAKELPRPLAEKCPSIIKKFISAYDAKPDFVARSPGRVNLIGEHIDYCDFSVLPLAIDFDMLCAVKVLNEKNPSITLINADPKFAQRKFDLPLDGSYVTIDPSVSDWSNYFKCGLHVAHSFLKKLAPERFASAPLAGLQVFCEGDVPTGSGLSSSAAFICAVALAVVKANMGPGYHMSKQNLMRITVVAEHYVGVNNGGMDQAASVCGEEDHALYVEFKPQLKATPFKFPQLKNHEISFVIANTLVVSNKFETAPTNYNLRVVEVTTAANVLAATYGVVLLSGKEGSSTNKGNLRDFMNVYYAR... | 2.7.1.6 | null | carbohydrate phosphorylation [GO:0046835]; galactose catabolic process via UDP-galactose [GO:0033499]; galactose metabolic process [GO:0006012]; positive regulation of transcription by galactose [GO:0000411]; positive regulation of transcription from RNA polymerase II promoter by galactose [GO:0000435] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | ATP binding [GO:0005524]; galactokinase activity [GO:0004335] | PF10509;PF08544;PF00288; | 1.20.1440.340;3.30.230.10; | GHMP kinase family, GalK subfamily | null | null | CATALYTIC ACTIVITY: Reaction=alpha-D-galactose + ATP = ADP + alpha-D-galactose 1-phosphate + H(+); Xref=Rhea:RHEA:13553, ChEBI:CHEBI:15378, ChEBI:CHEBI:28061, ChEBI:CHEBI:30616, ChEBI:CHEBI:58336, ChEBI:CHEBI:456216; EC=2.7.1.6; Evidence={ECO:0000269|PubMed:12106903, ECO:0000269|PubMed:13495476, ECO:0000269|PubMed:1414... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1200 uM for alpha-D-galactose {ECO:0000269|PubMed:12106903, ECO:0000269|PubMed:14144}; KM=32 uM for ATP {ECO:0000269|PubMed:12106903}; Note=kcat is 11.7 sec(-1) for alpha-D-galactose and 8.7 sec(-1) for ATP utilization. {ECO:0000269|PubMed:12106903}; | PATHWAY: Carbohydrate metabolism; galactose metabolism. {ECO:0000269|PubMed:12106903, ECO:0000269|PubMed:13495476, ECO:0000269|PubMed:14144}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0-9.0. {ECO:0000269|PubMed:14144}; | null | FUNCTION: Galactokinase is a key enzyme in the galactose metabolism where it catalyzes the conversion of alpha-D-galactose to galactose 1-phosphate (PubMed:12106903, PubMed:13495476, PubMed:14144). Can also induce the transcription of the yeast GAL genes in response to the organism being challenged with galactose as th... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P04386 | GAL4_YEAST | MKLLSSIEQACDICRLKKLKCSKEKPKCAKCLKNNWECRYSPKTKRSPLTRAHLTEVESRLERLEQLFLLIFPREDLDMILKMDSLQDIKALLTGLFVQDNVNKDAVTDRLASVETDMPLTLRQHRISATSSSEESSNKGQRQLTVSIDSAAHHDNSTIPLDFMPRDALHGFDWSEEDDMSDGLPFLKTDPNNNGFFGDGSLLCILRSIGFKPENYTNSNVNRLPTMITDRYTLASRSTTSRLLQSYLNNFHPYCPIVHSPTLMMLYNNQIEIASKDQWQILFNCILAIGAWCIEGESTDIDVFYYQNAKSHLTSKVFES... | null | null | DNA-templated transcription [GO:0006351]; galactose metabolic process [GO:0006012]; positive regulation of transcription from RNA polymerase II promoter by galactose [GO:0000435]; regulation of transcription from RNA polymerase II promoter by galactose [GO:0000431] | nucleus [GO:0005634]; transcription repressor complex [GO:0017053] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; identical protein binding [GO:0042802]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II-specifi... | PF04082;PF03902;PF00172; | 1.20.5.170;4.10.240.10; | null | PTM: Association between GAL11 and GAL4 may serve to expedite phosphorylation of GAL4. | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: This protein is a positive regulator for the gene expression of the galactose-induced genes such as GAL1, GAL2, GAL7, GAL10, and MEL1 which code for the enzymes used to convert galactose to glucose. It recognizes a 17 base pair sequence in (5'-CGGRNNRCYNYNCNCCG-3') the upstream activating sequence (UAS-G) of ... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P04387 | GAL80_YEAST | MDYNKRSSVSTVPNAAPIRVGFVGLNAAKGWAIKTHYPAILQLSSQFQITALYSPKIETSIATIQRLKLSNATAFPTLESFASSSTIDMIVIAIQVASHYEVVMPLLEFSKNNPNLKYLFVEWALACSLDQAESIYKAAAERGVQTIISLQGRKSPYILRAKELISQGYIGDINSIEIAGNGGWYGYERPVKSPKYIYEIGNGVDLVTTTFGHTIDILQYMTSSYFSRINAMVFNNIPEQELIDERGNRLGQRVPKTVPDHLLFQGTLLNGNVPVSCSFKGGKPTKKFTKNLVIDIHGTKGDLKLEGDAGFAEISNLVLY... | null | null | galactose metabolic process [GO:0006012]; negative regulation of phosphorylation [GO:0042326]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription from RNA polymerase II promoter by galactose [GO:0000435]; regulation of transcription from RNA polymerase II promot... | cytoplasm [GO:0005737]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667]; transcription repressor complex [GO:0017053] | DNA binding [GO:0003677]; identical protein binding [GO:0042802]; kinase inhibitor activity [GO:0019210]; nucleotide binding [GO:0000166]; RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629] | PF01408; | 3.40.50.720; | null | null | null | null | null | null | null | null | FUNCTION: This protein is a negative regulator for the gene expression of the lactose/galactose metabolic genes. It binds to GAL4 and so blocks transcriptional activation by it, in the absence of an inducing sugar. {ECO:0000269|PubMed:1985957}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P04388 | RAS2_DROME | MQMQTYKLVVVGGGGVGKSAITIQFIQSYFVTDYDPTIEDSYTKQCNIDDVPAKLDILDTAGQEEFSAMREQYMRSGEGFLLVFALNDHSSFDEIPKFQRQILRVKDRDEFPMLMVGNKCDLKHQQQVSLEEAQNTSRNLMIPYIECSAKLRVNVDQAFHELVRIVRKFQIAERPFIEQDYKKKGKRKCCLM | 3.6.5.2 | null | Ras protein signal transduction [GO:0007265] | plasma membrane [GO:0005886] | G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Ras family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P01112}; | null | null | null | null | FUNCTION: May be involved in endocytic processes and/or other transport pathways mediated by vesicle trafficking. May interact functionally with ROP protein. Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. | Drosophila melanogaster (Fruit fly) |
P04390 | T2E5_ECOLX | MSLRSDLINALYDENQKYDVCGIISAEGKIYPLGSDTKVLSTIFELFSRPIINKIAEKHGYIVEEPKQQNHYPDFTLYKPSEPNKKIAIDIKTTYTNKENEKIKFTLGGYTSFIRNNTKNIVYPFDQYIAHWIIGYVYTRVATRKSSLKTYNINELNEIPKPYKGVKVFLQDKWVIAGDLAGSGNTTNIGSIHAHYKDFVEGKGIFDSEDEFLDYWRNYERTSQLRNDKYNNISEYRNWIYRGRK | 3.1.21.4 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 2 magnesium ions per subunit.; | DNA restriction-modification system [GO:0009307] | null | DNA binding [GO:0003677]; metal ion binding [GO:0046872]; type II site-specific deoxyribonuclease activity [GO:0009036] | PF09233; | 3.40.600.10; | null | null | null | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage of DNA to give specific double-stranded fragments with terminal 5'-phosphates.; EC=3.1.21.4; Evidence={ECO:0000269|PubMed:1647200, ECO:0000269|Ref.2}; | null | null | null | null | FUNCTION: A P subtype restriction enzyme that recognizes the double-stranded sequence 5'-GATATC-3' and cleaves after T-3. {ECO:0000269|PubMed:1647200, ECO:0000269|PubMed:6328432, ECO:0000269|Ref.2, ECO:0000303|PubMed:12654995}. | Escherichia coli |
P04391 | OTC1_ECOLI | MSGFYHKHFLKLLDFTPAELNSLLQLAAKLKADKKSGKEEAKLTGKNIALIFEKDSTRTRCSFEVAAYDQGARVTYLGPSGSQIGHKESIKDTARVLGRMYDGIQYRGYGQEIVETLAEYASVPVWNGLTNEFHPTQLLADLLTMQEHLPGKAFNEMTLVYAGDARNNMGNSMLEAAALTGLDLRLVAPQACWPEAALVTECRALAQQNGGNITLTEDVAKGVEGADFIYTDVWVSMGEAKEKWAERIALLREYQVNSKMMQLTGNPEVKFLHCLPAFHDDQTTLGKKMAEEFGLHGGMEVTDEVFESAASIVFDQAENR... | 2.1.3.3 | null | arginine biosynthetic process via ornithine [GO:0042450]; citrulline biosynthetic process [GO:0019240] | cytoplasm [GO:0005737] | amino acid binding [GO:0016597]; metal ion binding [GO:0046872]; ornithine carbamoyltransferase activity [GO:0004585] | PF00185;PF02729; | 3.40.50.1370; | Aspartate/ornithine carbamoyltransferase superfamily, OTCase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=carbamoyl phosphate + L-ornithine = H(+) + L-citrulline + phosphate; Xref=Rhea:RHEA:19513, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:46911, ChEBI:CHEBI:57743, ChEBI:CHEBI:58228; EC=2.1.3.3; Evidence={ECO:0000305|PubMed:3072022}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10 uM for carbamoyl phosphate {ECO:0000269|PubMed:789338}; KM=50 uM for carbamoyl phosphate {ECO:0000269|PubMed:3072022}; KM=0.18 mM for L-ornithine {ECO:0000269|PubMed:8845761}; KM=0.32 mM for L-ornithine {ECO:0000269|PubMed:3072022}; KM=5 mM for L-ornithine {ECO:... | PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 1/3. {ECO:0000305}. | null | null | FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine (ORN) to produce L-citrulline, which is a substrate for argininosuccinate synthetase, the enzyme involved in the final step in arginine biosynthesis. {ECO:0000269|PubMed:3072022, ECO:0000... | Escherichia coli (strain K12) |
P04392 | DMA_BPT4 | MLGAIAYTGNKQSLLPELKSHFPKYNRFVDLFCGGLSVSLNVNGPVLANDIQEPIIEMYKRLINVSWDDVLKVIKQYKLSKTSKEEFLKLREDYNKTRDPLLLYVLHFHGFSNMIRINDKGNFTTPFGKRTINKNSEKQYNHFKQNCDKIIFSSLHFKDVKILDGDFVYVDPPYLITVADYNKFWSEDEEKDLLNLLDSLNDRGIKFGQSNVLEHHGKENTLLKEWSKKYNVKHLNKKYVFNIYHSKEKNGTDEVYIFN | 2.1.1.72 | null | DNA replication [GO:0006260]; evasion of host restriction-modification system [GO:0099018]; methylation [GO:0032259]; mismatch repair [GO:0006298]; virus-mediated perturbation of host defense response [GO:0019049] | null | DNA-methyltransferase activity [GO:0009008]; S-adenosyl-L-methionine binding [GO:1904047]; sequence-specific DNA binding [GO:0043565]; site-specific DNA-methyltransferase (adenine-specific) activity [GO:0009007] | PF02086; | 1.10.1020.10;3.40.50.150; | N(4)/N(6)-methyltransferase family | null | null | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyadenosine in DNA + S-adenosyl-L-methionine = an N(6)-methyl-2'-deoxyadenosine in DNA + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:15197, Rhea:RHEA-COMP:12418, Rhea:RHEA-COMP:12419, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:90615, ChEBI:CHEBI:90616;... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.1 uM for S-adenosylmethionine {ECO:0000269|PubMed:7782299}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0-8.5. {ECO:0000269|PubMed:7782299}; | null | FUNCTION: An alpha subtype methylase, recognizes the double-stranded sequence 5'-GATC-3' and methylates A-2. Also acts on 5-hydroxymethylcytosine (hmC)-containing DNA, the normal base in this virus (PubMed:12654995, PubMed:2510127). May prevent degradation of viral DNA by the host restriction-modification antiviral def... | Enterobacteria phage T4 (Bacteriophage T4) |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.