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 |
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P15532 | NDKA_MOUSE | MANSERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFLQASEDLLKEHYTDLKDRPFFTGLVKYMHSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGSDSVKSAEKEISLWFQPEELVEYKSCAQNWIYE | 2.7.4.6 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | cell differentiation [GO:0030154]; CTP biosynthetic process [GO:0006241]; dTMP biosynthetic process [GO:0006231]; endocytosis [GO:0006897]; GTP biosynthetic process [GO:0006183]; lactation [GO:0007595]; mammary gland development [GO:0030879]; negative regulation of gene expression [GO:0010629]; negative regulation of m... | centrosome [GO:0005813]; cytosol [GO:0005829]; early endosome [GO:0005769]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; ruffle membrane [GO:0032587] | 3'-5' exonuclease activity [GO:0008408]; ATP binding [GO:0005524]; DNA nuclease activity [GO:0004536]; enzyme binding [GO:0019899]; gamma-tubulin binding [GO:0043015]; GTP binding [GO:0005525]; identical protein binding [GO:0042802]; intermediate filament binding [GO:0019215]; magnesium ion binding [GO:0000287]; nucleo... | PF00334; | 3.30.70.141; | NDK family | null | SUBCELLULAR LOCATION: Cytoplasm. Nucleus. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640, ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316, ChEBI:CHEBI:456216; EC=2.7.4.6; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleosid... | null | null | null | null | FUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Possesses nucleoside-diphosphate kinase, serine/threonine-specific protein kinase, geranyl and fa... | Mus musculus (Mouse) |
P15533 | TR30A_MOUSE | MASSVLEMIKEEVTCPICLELLKEPVSADCNHSFCRACITLNYESNRNTDGKGNCPVCRVPYPFGNLRPNLHVANIVERLKGFKSIPEEEQKVNICAQHGEKLRLFCRKDMMVICWLCERSQEHRGHQTALIEEVDQEYKEKLQGALWKLMKKAKICDEWQDDLQLQRVDWENQIQINVENVQRQFKGLRDLLDSKENEELQKLKKEKKEVMEKLEESENELEDQTELVRDLISDVEHHLELSTLEMLQGANCVLRRSQSLSLQQPQTVPQKRKRTFQAPDLKGMLQVYQGLMDIQQYWVHMTLHARNNAVIAINKEKRQ... | null | null | innate immune response [GO:0045087]; negative regulation of interleukin-6 production [GO:0032715]; negative regulation of NLRP3 inflammasome complex assembly [GO:1900226]; negative regulation of reactive oxygen species metabolic process [GO:2000378]; negative regulation of toll-like receptor signaling pathway [GO:00341... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654] | DNA binding [GO:0003677]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270] | PF00622;PF00643;PF13445; | 2.60.120.920;3.30.160.60;3.30.40.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm. Nucleus. | null | null | null | null | null | FUNCTION: Trans-acting factor that regulates gene expression of interleukin 2 receptor alpha chain. May affect IL2R-alpha expression through cis-acting negative regulatory elements or through competition with proteins that bind to enhancer or activator sequences. Negatively regulates Toll-like receptor (TLR)-mediated a... | Mus musculus (Mouse) |
P15535 | B4GT1_MOUSE | MRFREQFLGGSAAMPGATLQRACRLLVAVCALHLGVTLVYYLSGRDLSRLPQLVGVSSTLQGGTNGAAASKQPPGEQRPRGARPPPPLGVSPKPRPGLDSSPGAASGPGLKSNLSSLPVPTTTGLLSLPACPEESPLLVGPMLIDFNIAVDLELLAKKNPEIKTGGRYSPKDCVSPHKVAIIIPFRNRQEHLKYWLYYLHPILQRQQLDYGIYVINQAGDTMFNRAKLLNIGFQEALKDYDYNCFVFSDVDLIPMDDRNAYRCFSQPRHISVAMDKFGFSLPYVQYFGGVSALSKQQFLAINGFPNNYWGWGGEDDDIFN... | 2.4.1.-; 2.4.1.22; 2.4.1.275; 2.4.1.38; 2.4.1.90 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P15291}; | acute inflammatory response [GO:0002526]; angiogenesis involved in wound healing [GO:0060055]; binding of sperm to zona pellucida [GO:0007339]; cell adhesion [GO:0007155]; cell population proliferation [GO:0008283]; development of secondary sexual characteristics [GO:0045136]; epithelial cell development [GO:0002064]; ... | basolateral plasma membrane [GO:0016323]; brush border membrane [GO:0031526]; cell surface [GO:0009986]; desmosome [GO:0030057]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; filopodium [GO:0030175]; Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]; Golgi trans cist... | beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity [GO:0003831]; cytoskeletal protein binding [GO:0008092]; galactosyltransferase activity [GO:0008378]; lactose synthase activity [GO:0004461]; manganese ion binding [GO:0030145]; N-acetyllactosamine synthase activity [GO:0003945] | PF02709;PF13733; | null | Glycosyltransferase 7 family | PTM: The soluble form derives from the membrane forms by proteolytic processing. | SUBCELLULAR LOCATION: [Isoform Long]: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:18511602}; Single-pass type II membrane protein. Cell membrane; Single-pass type II membrane protein. Cell surface. Cell projection, filopodium {ECO:0000269|PubMed:18511602}. Note=Found in trans cisternae of Golgi. B4GALT1 c... | CATALYTIC ACTIVITY: Reaction=D-glucose + UDP-alpha-D-galactose = H(+) + lactose + UDP; Xref=Rhea:RHEA:12404, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378, ChEBI:CHEBI:17716, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.22; Evidence={ECO:0000250|UniProtKB:P08037}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12405; Evi... | null | PATHWAY: Protein modification; protein glycosylation. | null | null | FUNCTION: [Beta-1,4-galactosyltransferase 1]: The Golgi complex form catalyzes the production of lactose in the lactating mammary gland and could also be responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. {ECO:0000250|UniPro... | Mus musculus (Mouse) |
P15538 | C11B1_HUMAN | MALRAKAEVCMAVPWLSLQRAQALGTRAARVPRTVLPFEAMPRRPGNRWLRLLQIWREQGYEDLHLEVHQTFQELGPIFRYDLGGAGMVCVMLPEDVEKLQQVDSLHPHRMSLEPWVAYRQHRGHKCGVFLLNGPEWRFNRLRLNPEVLSPNAVQRFLPMVDAVARDFSQALKKKVLQNARGSLTLDVQPSIFHYTIEASNLALFGERLGLVGHSPSSASLNFLHALEVMFKSTVQLMFMPRSLSRWTSPKVWKEHFEAWDCIFQYGDNCIQKIYQELAFSRPQQYTSIVAELLLNAELSPDAIKANSMELTAGSVDTTV... | 1.14.15.4 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P19099}; | aldosterone biosynthetic process [GO:0032342]; C21-steroid hormone biosynthetic process [GO:0006700]; cellular response to hormone stimulus [GO:0032870]; cellular response to peptide hormone stimulus [GO:0071375]; cellular response to potassium ion [GO:0035865]; cholesterol metabolic process [GO:0008203]; cortisol bios... | mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739] | corticosterone 18-monooxygenase activity [GO:0047783]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; steroid 11-beta-monooxygenase activity [GO:0004507] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P14137}; Peripheral membrane protein {ECO:0000250|UniProtKB:P14137}. | CATALYTIC ACTIVITY: Reaction=a steroid + 2 H(+) + O2 + 2 reduced [adrenodoxin] = an 11beta-hydroxysteroid + H2O + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:15629, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:35341, Ch... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=338.4 uM for 11-deoxycortisol {ECO:0000269|PubMed:18215163}; KM=179.5 uM for 21-hydroxyprogesterone {ECO:0000269|PubMed:18215163}; Note=kcat is 1.67 sec(-1) with 11-deoxycortisol as substrate. kcat is 0.85 sec(-1) with 21-hydroxyprogesterone as substrate. {ECO:0000... | PATHWAY: Steroid biosynthesis; glucocorticoid biosynthesis. {ECO:0000269|PubMed:18215163}.; PATHWAY: Steroid hormone biosynthesis. {ECO:0000269|PubMed:18215163}. | null | null | FUNCTION: A cytochrome P450 monooxygenase involved in the biosynthesis of adrenal corticoids (PubMed:12530636, PubMed:1518866, PubMed:1775135, PubMed:18215163, PubMed:23322723). Catalyzes a variety of reactions that are essential for many species, including detoxification, defense, and the formation of endogenous chemi... | Homo sapiens (Human) |
P15539 | C11B2_MOUSE | MALRVTADVWLARPWQCLHRTRALGTTATLAPKTLQPFEAIPQYSRNKWLKMIQILREQGQENLHLEMHQVFRELGPIFRHSVGKTQIVSVMLPEDAEKLHQVESMLPRRMHLEPWVAHRELRGLRRGVFLLNGPEWRLNRLRLNRNVLSPKAVQKFVPMVDMVARDFLETLKEKVLQNARGSLTMDVQQSLFNYTIEASNFALFGERLGLLGHDLSPGSLKFIHALHSMFKSTSQLLFLPKSLTRWTSTRVWKEHFDAWDVISEYANRCIWKVHQELRLGSSQTYSGIVAELISQGSLPLDAIKANSMELTAGSVDTTA... | 1.14.15.4; 1.14.15.5 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P19099}; | aldosterone biosynthetic process [GO:0032342]; cellular response to peptide hormone stimulus [GO:0071375]; cholesterol metabolic process [GO:0008203]; cortisol metabolic process [GO:0034650]; drinking behavior [GO:0042756]; glucocorticoid biosynthetic process [GO:0006704]; monoatomic ion homeostasis [GO:0050801]; regul... | dendrite [GO:0030425]; mitochondrial inner membrane [GO:0005743] | corticosterone 18-monooxygenase activity [GO:0047783]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; steroid 11-beta-monooxygenase activity [GO:0004507] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P14137}; Peripheral membrane protein {ECO:0000250|UniProtKB:P14137}. | CATALYTIC ACTIVITY: Reaction=a steroid + 2 H(+) + O2 + 2 reduced [adrenodoxin] = an 11beta-hydroxysteroid + H2O + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:15629, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:35341, Ch... | null | PATHWAY: Steroid biosynthesis. {ECO:0000250|UniProtKB:P19099}. | null | null | FUNCTION: A cytochrome P450 monooxygenase that catalyzes the biosynthesis of aldosterone, the main mineralocorticoid in the human body responsible for salt and water homeostasis, thus involved in blood pressure regulation, arterial hypertension, and the development of heart failure. Catalyzes three sequential oxidative... | Mus musculus (Mouse) |
P15541 | AMPN_RABIT | MAKGFYISKSLGILGILLGVAALCTIVALSVVYRQEKNKNTSQSPSMAPLNPTATSSPATTLDQNLPWNRYRLPKTLIPDSYNVVLRPYLSPNSQGLYIFTGSSTVRFTCQEATNVIIIHSKKLNYTITQGHRVVLRGVRGSQPPAIASTELVELTEYLVVHLQGQLVAGSQYEMDTQFQGELADDLAGFYRSEYMEGNVRKVVATTQMQAADARKSFPCFDEPAMKATFNITPIHPRDYTALSNMLPRSSTALPEDPNWTVTEFHTTPKMSTYLLAYIVSEFTNIEAQSPNNVQIRIWARPSAISEGHGQYALNVTGPI... | 3.4.11.2 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P15144}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P15144}; | angiogenesis [GO:0001525]; cell differentiation [GO:0030154]; peptide catabolic process [GO:0043171]; proteolysis [GO:0006508] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | metalloaminopeptidase activity [GO:0070006]; metallopeptidase activity [GO:0008237]; peptide binding [GO:0042277]; zinc ion binding [GO:0008270] | PF11838;PF01433;PF17900; | 1.25.50.20;2.60.40.1910;1.10.390.10;2.60.40.1730; | Peptidase M1 family | PTM: Sulfated. {ECO:0000250|UniProtKB:P15145}.; PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:P15144}.; PTM: May undergo proteolysis and give rise to a soluble form. {ECO:0000250|UniProtKB:P15144}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P15144}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P15144}. Note=Also found as a soluble form. {ECO:0000250|UniProtKB:P15144}. | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.; E... | null | null | null | null | FUNCTION: Broad specificity aminopeptidase which plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. Also involved in the processing of various peptides including peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines. May a... | Oryctolagus cuniculus (Rabbit) |
P15559 | NQO1_HUMAN | MVGRRALIVLAHSERTSFNYAMKEAAAAALKKKGWEVVESDLYAMNFNPIISRKDITGKLKDPANFQYPAESVLAYKEGHLSPDIVAEQKKLEAADLVIFQFPLQWFGVPAILKGWFERVFIGEFAYTYAAMYDKGPFRSKKAVLSITTGGSGSMYSLQGIHGDMNVILWPIQSGILHFCGFQVLEPQLTYSIGHTPADARIQILEGWKKRLENIWDETPLYFAPSSLFDLNFQAGFLMKKEVQDEEKNKKFGLSVGHHLGKSIPTDNQIKARK | 1.6.5.2 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:28291250}; | cell redox homeostasis [GO:0045454]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to metal ion [GO:0071248]; cellular response to oxidative stress [GO:0034599]; innate immune response [GO:0045087]; NADH oxidation [GO:0006116]; NADPH oxidation [GO:0070995]; negative regulation of apoptotic proc... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; synapse [GO:0045202] | cytochrome-b5 reductase activity, acting on NAD(P)H [GO:0004128]; identical protein binding [GO:0042802]; NAD(P)H dehydrogenase (quinone) activity [GO:0003955]; NADH dehydrogenase (quinone) activity [GO:0050136]; NADPH dehydrogenase (quinone) activity [GO:0008753]; RNA binding [GO:0003723]; superoxide dismutase activit... | PF02525; | 3.40.50.360; | NAD(P)H dehydrogenase (quinone) family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P05982}. | CATALYTIC ACTIVITY: Reaction=a quinone + H(+) + NADH = a quinol + NAD(+); Xref=Rhea:RHEA:46160, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:132124; EC=1.6.5.2; Evidence={ECO:0000269|PubMed:8999809, ECO:0000269|PubMed:9271353}; PhysiologicalDirection=left-to-right; Xref=Rhea:R... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.7 uM for menadione {ECO:0000269|PubMed:8999809}; KM=220 uM for NADH {ECO:0000269|PubMed:8999809}; KM=1370 uM for 5-(aziridin-1-yl)-2,4-dinitrobenzamide {ECO:0000269|PubMed:8999809}; Vmax=1100 umol/min/mg enzyme toward menadione {ECO:0000269|PubMed:8999809}; Vmax=... | null | null | null | FUNCTION: Flavin-containing quinone reductase that catalyzes two-electron reduction of quinones to hydroquinones using either NADH or NADPH as electron donors. In a ping-pong kinetic mechanism, the electrons are sequentially transferred from NAD(P)H to flavin cofactor and then from reduced flavin to the quinone, bypass... | Homo sapiens (Human) |
P15565 | TRM1_YEAST | MEGFFRIPLKRANLHGMLKAAISKIKANFTAYGAPRINIEDFNIVKEGKAEILFPKKETVFYNPIQQFNRDLSVTCIKAWDNLYGEECGQKRNNKKSKKKRCAETNDDSSKRQKMGNGSPKEAVGNSNRNEPYINILEALSATGLRAIRYAHEIPHVREVIANDLLPEAVESIKRNVEYNSVENIVKPNLDDANVLMYRNKATNNKFHVIDLDPYGTVTPFVDAAIQSIEEGGLMLVTCTDLSVLAGNGYPEKCFALYGGANMVSHESTHESALRLVLNLLKQTAAKYKKTVEPLLSLSIDFYVRVFVKVKTSPIEVKNV... | 2.1.1.216 | null | tRNA methylation [GO:0030488]; tRNA N2-guanine methylation [GO:0002940] | mitochondrion [GO:0005739]; nuclear envelope [GO:0005635]; nuclear inner membrane [GO:0005637]; nucleus [GO:0005634] | tRNA (guanine(10)-N2)-methyltransferase activity [GO:0160102]; tRNA (guanine(26)-N2)-dimethyltransferase activity [GO:0160104]; tRNA (guanine(26)-N2/guanine(27)-N2)-dimethyltransferase activity [GO:0160103]; tRNA binding [GO:0000049] | PF02005; | 3.30.56.70;3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, Trm1 family | PTM: Isoform 2 is N-acetylated by NatC at position 1. N-acetylation is necessary for targeting of the protein to the inner nuclear membrane. | SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion.; SUBCELLULAR LOCATION: [Isoform 2]: Mitochondrion. Nucleus inner membrane; Peripheral membrane protein; Nucleoplasmic side. Note=Predominantly targeted to the nucleus. | CATALYTIC ACTIVITY: Reaction=guanosine(26) in tRNA + 2 S-adenosyl-L-methionine = 2 H(+) + N(2)-dimethylguanosine(26) in tRNA + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:43140, Rhea:RHEA-COMP:10359, Rhea:RHEA-COMP:10360, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:74269, ChEBI:CHEBI:74513; EC=... | null | null | null | null | FUNCTION: Dimethylates a single guanine residue at position 26 of most tRNAs using S-adenosyl-L-methionine as donor of the methyl groups. Required for the modification of both mitochondrial and cytoplasmic tRNAs. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P15586 | GNS_HUMAN | MRLLPLAPGRLRRGSPRHLPSCSPALLLLVLGGCLGVFGVAAGTRRPNVVLLLTDDQDEVLGGMTPLKKTKALIGEMGMTFSSAYVPSALCCPSRASILTGKYPHNHHVVNNTLEGNCSSKSWQKIQEPNTFPAILRSMCGYQTFFAGKYLNEYGAPDAGGLEHVPLGWSYWYALEKNSKYYNYTLSINGKARKHGENYSVDYLTDVLANVSLDFLDYKSNFEPFFMMIATPAPHSPWTAAPQYQKAFQNVFAPRNKNFNIHGTNKHWLIRQAKTPMTNSSIQFLDNAFRKRWQTLLSVDDLVEKLVKRLEFTGELNNTY... | 3.1.6.14 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250}; | glycosaminoglycan catabolic process [GO:0006027]; keratan sulfate catabolic process [GO:0042340] | azurophil granule lumen [GO:0035578]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; ficolin-1-rich granule lumen [GO:1904813]; lysosomal lumen [GO:0043202] | glycosaminoglycan binding [GO:0005539]; metal ion binding [GO:0046872]; N-acetylglucosamine-6-sulfatase activity [GO:0008449]; sulfate binding [GO:0043199]; sulfuric ester hydrolase activity [GO:0008484] | PF00884; | 3.40.720.10; | Sulfatase family | PTM: The form A (78 kDa) is processed by internal peptidase cleavage to a 32 kDa N-terminal species (form B) and a 48 kDa C-terminal species.; PTM: The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical fo... | SUBCELLULAR LOCATION: Lysosome. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of the 6-sulfate groups of the N-acetyl-D-glucosamine 6-sulfate units of heparan sulfate and keratan sulfate.; EC=3.1.6.14; | null | null | null | null | null | Homo sapiens (Human) |
P15589 | STS_RAT | MLWPCLLALLLSQLNFLCAARPGPGPNFLLIMADDLGIGDLGCYGNRTLRTPHIDRLALEGVKLTQHLAAAPLCTPSRAAFLTGRYPVRSGMASHGRLGVFLFSASSGGLPPNEVTFAKLLKGQGYTTGLVGKWHLGLSCQAASDFCHHPGRHGFDRFLGTPTTNLRDCKPGGGTVFGSAQQVFVVLPMNILGAVLLAMALARWAGLARPPGWVFGVTVAAMAAVGGAYVAFLYHFRPANCFLMADFTITQQPTDYKGLTQRLASEAGDFLRRNRDTPFLLFLSFMHVHTAHFANPEFAGQSLHGAYGDAVEEMDWAVGQ... | 3.1.6.2 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P08842}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P08842}; | female pregnancy [GO:0007565]; learning or memory [GO:0007611]; positive regulation of cell population proliferation [GO:0008284]; response to estrogen [GO:0043627]; response to organic cyclic compound [GO:0014070]; response to peptide hormone [GO:0043434]; response to pH [GO:0009268]; skin development [GO:0043588]; st... | endoplasmic reticulum membrane [GO:0005789]; nuclear envelope [GO:0005635] | arylsulfatase activity [GO:0004065]; metal ion binding [GO:0046872]; steryl-sulfatase activity [GO:0004773]; sulfuric ester hydrolase activity [GO:0008484] | PF00884;PF14707; | 3.30.1120.10;3.40.720.10;1.10.287.550; | Sulfatase family | PTM: The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity. {ECO:0000250|UniProtKB:P08842}. | SUBCELLULAR LOCATION: Microsome membrane {ECO:0000250|UniProtKB:P08842}; Multi-pass membrane protein. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P08842}; Multi-pass membrane protein {ECO:0000305}. Note=The sequence shows several membrane-spanning domains that could serve to anchor the protein in the microsom... | CATALYTIC ACTIVITY: Reaction=dehydroepiandrosterone 3-sulfate + H2O = 3beta-hydroxyandrost-5-en-17-one + H(+) + sulfate; Xref=Rhea:RHEA:19873, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16189, ChEBI:CHEBI:28689, ChEBI:CHEBI:57905; EC=3.1.6.2; Evidence={ECO:0000250|UniProtKB:P08842}; CATALYTIC ACTIVITY: Reaction=... | null | null | null | null | FUNCTION: Catalyzes the conversion of sulfated steroid precursors, such as dehydroepiandrosterone sulfate (DHEA-S) and estrone sulfate to the free steroid. {ECO:0000250|UniProtKB:P08842}. | Rattus norvegicus (Rat) |
P15622 | ZN250_HUMAN | MAAARLLPVPAGPQPLSFQAKLTFEDVAVLLSQDEWDRLCPAQRGLYRNVMMETYGNVVSLGLPGSKPDIISQLERGEDPWVLDRKGAKKSQGLWSDYSDNLKYDHTTACTQQDSLSCPWECETKGESQNTDLSPKPLISEQTVILGKTPLGRIDQENNETKQSFCLSPNSVDHREVQVLSQSMPLTPHQAVPSGERPYMCVECGKCFGRSSHLLQHQRIHTGEKPYVCSVCGKAFSQSSVLSKHRRIHTGEKPYECNECGKAFRVSSDLAQHHKIHTGEKPHECLECRKAFTQLSHLIQHQRIHTGERPYVCPLCGKAF... | null | null | regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA binding [GO:1990837] | PF01352;PF00096; | 6.10.140.140;3.30.160.60; | Krueppel C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: May be involved in transcriptional regulation. | Homo sapiens (Human) |
P15624 | SYFB_YEAST | MPTVSVNKQQLFDLLGKNYTSQEFDELCFEFGMEMDEDTTEEALKTGEEPELKLDISANRYDLLCIEGISQSLNEYLERKERPDYKLSKPTTKLIIDKSTEQIRPFATAAVLRNIKLNEKSYASFIALQDKLHANLCRNRSLVAMGTHDLDSIEGPFHYRALPPKDIKFVPLNQTQEFTGDKLIEFYKSPEQKNNIGRYVHIIEDSPVFPVIMDSKDRVCSLPPLINSEHSKISVNTRNILIDITATDKTKAEIVLNILTTMFSRYCDEPFTVEPVEIVSEHNGQSRLAPNFNDRIMDVSIKYINSCLGLDQSADEIAHC... | 6.1.1.20 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A5K464}; | phenylalanyl-tRNA aminoacylation [GO:0006432] | cytoplasm [GO:0005737]; phenylalanine-tRNA ligase complex [GO:0009328] | ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; phenylalanine-tRNA ligase activity [GO:0004826]; RNA binding [GO:0003723] | PF03483;PF03484;PF18262;PF17759; | 3.30.56.10;3.50.40.10; | Phenylalanyl-tRNA synthetase beta subunit family, Type 2 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413, Rhea:RHEA-COMP:9668, Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58095, ChEBI:CHEBI:78442, ChEBI:CHEBI:78531, ChEBI:CHEBI:456215; EC=6... | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P15625 | SYFA_YEAST | MSDFQLEILKKLDELDEIKSTLATFPQHGSQDVLSALNSLKAHNKLEFSKVDTVTYDLTKEGAQILNEGSYEIKLVKLIQELGQLQIKDVMSKLGPQVGKVGQARAFKNGWIAKNASNELELSAKLQNTDLNELTDETQSILAQIKNNSHLDSIDAKILNDLKKRKLIAQGKITDFNVTKGPEFSTDLTKLETDLTSDMVSTNAYKDLKFKPYNFNSQGVQISSGALHPLNKVREEFRQIFFSMGFTEMPSNQYVETGFWNFDALYVPQQHPARDLQDTFYIKDPLTADLPDDKTYMDNIKAVHEQGRFGSIGYRYNWKP... | 6.1.1.20 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A5K9S0}; | phenylalanyl-tRNA aminoacylation [GO:0006432] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; phenylalanine-tRNA ligase complex [GO:0009328] | aminoacyl-tRNA editing activity [GO:0002161]; ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; phenylalanine-tRNA ligase activity [GO:0004826]; tRNA binding [GO:0000049] | PF18554;PF18553;PF01409; | 1.10.10.2320;1.10.10.2330;3.30.1370.240; | Class-II aminoacyl-tRNA synthetase family, Phe-tRNA synthetase alpha subunit type 2 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=ATP + L-phenylalanine + tRNA(Phe) = AMP + diphosphate + H(+) + L-phenylalanyl-tRNA(Phe); Xref=Rhea:RHEA:19413, Rhea:RHEA-COMP:9668, Rhea:RHEA-COMP:9699, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58095, ChEBI:CHEBI:78442, ChEBI:CHEBI:78531, ChEBI:CHEBI:456215; EC=6... | null | null | null | null | null | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P15626 | GSTM2_MOUSE | MPMTLGYWDIRGLAHAIRLLLEYTDTSYEDKKYTMGDAPDYDRSQWLSEKFKLGLDFPNLPYLIDGSHKITQSNAILRYLARKHNLCGETEEERIRVDILENQAMDTRIQLAMVCYSPDFEKKKPEYLEGLPEKMKLYSEFLGKQPWFAGNKVTYVDFLVYDVLDQHRIFEPKCLDAFPNLKDFMGRFEGLKKISDYMKSSRFLSKPIFAKMAFWNPK | 2.5.1.18 | null | glutathione metabolic process [GO:0006749]; hepoxilin biosynthetic process [GO:0051122]; xenobiotic catabolic process [GO:0042178] | cytosol [GO:0005829]; protein-containing complex [GO:0032991] | glutathione binding [GO:0043295]; glutathione transferase activity [GO:0004364]; identical protein binding [GO:0042802] | PF00043;PF02798; | 1.20.1050.10;3.40.30.10; | GST superfamily, Mu family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=glutathione + RX = a halide anion + an S-substituted glutathione + H(+); Xref=Rhea:RHEA:16437, ChEBI:CHEBI:15378, ChEBI:CHEBI:16042, ChEBI:CHEBI:17792, ChEBI:CHEBI:57925, ChEBI:CHEBI:90779; EC=2.5.1.18; Evidence={ECO:0000250|UniProtKB:P28161}; PhysiologicalDirection=left-to-right; Xref=Rhea... | null | null | null | null | FUNCTION: Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles. Participates in the formation of novel hepoxilin regioisomers. {ECO:0000250|UniProtKB:P28161}. | Mus musculus (Mouse) |
P15640 | PUR2_ECOLI | MKVLVIGNGGREHALAWKAAQSPLVETVFVAPGNAGTALEPALQNVAIGVTDIPALLDFAQNEKIDLTIVGPEAPLVKGVVDTFRAAGLKIFGPTAGAAQLEGSKAFTKDFLARHKIPTAEYQNFTEVEPALAYLREKGAPIVIKADGLAAGKGVIVAMTLEEAEAAVHDMLAGNAFGDAGHRIVIEEFLDGEEASFIVMVDGEHVLPMATSQDHKRVGDKDTGPNTGGMGAYSPAPVVTDDVHQRTMERIIWPTVKGMAAEGNTYTGFLYAGLMIDKQGNPKVIEFNCRFGDPETQPIMLRMKSDLVELCLAACESKLD... | 6.3.4.13 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:2182115}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250}; | 'de novo' IMP biosynthetic process [GO:0006189]; DNA damage response [GO:0006974]; purine nucleobase biosynthetic process [GO:0009113]; purine nucleotide biosynthetic process [GO:0006164] | null | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; metal ion binding [GO:0046872]; phosphoribosylamine-glycine ligase activity [GO:0004637] | PF01071;PF02843;PF02844; | 3.40.50.20;3.30.1490.20;3.30.470.20;3.90.600.10; | GARS family | null | null | CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate; Xref=Rhea:RHEA:17453, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:58681, ChEBI:CHEBI:143788, ChEBI:CHEBI:456216; EC=6.3.4.13; Evid... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=70 uM for 5-phospho-beta-D-ribosylamine {ECO:0000269|PubMed:2182115}; KM=270 uM for glycine {ECO:0000269|PubMed:2182115}; KM=170 uM for ATP {ECO:0000269|PubMed:2182115}; KM=30 uM for N(1)-(5-phospho-beta-D-ribosyl)glycinamide {ECO:0000269|PubMed:2182115}; KM=6.4 uM... | PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/2. {ECO:0000305|PubMed:2182115}. | null | null | FUNCTION: Catalyzes the reversible conversion of phosphoribosylamine to glycinamide ribonucleotide, an enzymatic step in purine biosynthesis pathway. {ECO:0000269|PubMed:2182115}. | Escherichia coli (strain K12) |
P15646 | FBRL_YEAST | MSFRPGSRGGSRGGSRGGFGGRGGSRGGARGGSRGGFGGRGGSRGGARGGSRGGFGGRGGSRGGARGGSRGGRGGAAGGARGGAKVVIEPHRHAGVYIARGKEDLLVTKNMAPGESVYGEKRISVEEPSKEDGVPPTKVEYRVWNPFRSKLAAGIMGGLDELFIAPGKKVLYLGAASGTSVSHVSDVVGPEGVVYAVEFSHRPGRELISMAKKRPNIIPIIEDARHPQKYRMLIGMVDCVFADVAQPDQARIIALNSHMFLKDQGGVVISIKANCIDSTVDAETVFAREVQKLREERIKPLEQLTLEPYERDHCIVVGRY... | 2.1.1.- | null | box C/D RNA 3'-end processing [GO:0000494]; maturation of SSU-rRNA [GO:0030490]; regulation of transcription by RNA polymerase I [GO:0006356]; rRNA 2'-O-methylation [GO:0000451]; rRNA methylation [GO:0031167]; rRNA processing [GO:0006364]; snoRNA guided rRNA 2'-O-methylation [GO:0000452] | 90S preribosome [GO:0030686]; box C/D RNP complex [GO:0031428]; Cajal body [GO:0015030]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; small-subunit processome [GO:0032040] | histone H2AQ104 methyltransferase activity [GO:1990259]; O-methyltransferase activity [GO:0008171]; RNA binding [GO:0003723]; rRNA methyltransferase activity [GO:0008649] | PF01269; | 3.40.50.150; | Methyltransferase superfamily, Fibrillarin family | PTM: Methylated by HMT1, forming asymmetric dimethylarginines (DMA) within a domain referred to as an RGG box, made up of repeated Gly-Gly dipeptides interspersed with Arg and aromatic residues. {ECO:0000269|PubMed:12756332}. | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12756332, ECO:0000269|PubMed:2298745, ECO:0000269|PubMed:2686980}. Note=Fibrillar region of the nucleolus. | CATALYTIC ACTIVITY: Reaction=L-glutaminyl-[histone H2A] + S-adenosyl-L-methionine = H(+) + N(5)-methyl-L-glutaminyl-[histone H2A] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:50904, Rhea:RHEA-COMP:12837, Rhea:RHEA-COMP:12839, ChEBI:CHEBI:15378, ChEBI:CHEBI:30011, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61891; ... | null | null | null | null | FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that has the ability to methylate both RNAs and proteins. Involved in pre-rRNA processing by catalyzing the site-specific 2'-hydroxyl methylation of ribose moieties in pre-ribosomal RNA (PubMed:12215523, PubMed:1825809, PubMed:2686980). Site specificity is p... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P15650 | ACADL_RAT | MAARLLLRSLRVLSARSATLPPPSARCSHSGAEARLETPSAKKLTDIGIRRIFSSEHDIFRESVRKFFQEEVIPYHEEWEKAGEVSRELWEKAGKQGLLGINIAEKHGGIGGDLLSTAVTWEEQAYSNCTGPGFSLHSDIVMPYIANYGTKEQIEQFIPQMTAGKCIGAIAMTEPGAGSDLQGVRTNAKRSGSDWILNGSKVFITNGWLSDLVIVVAVTNREARSPAHGISLFLVENGMKGFIKGKKLHKMGMKAQDTAELFFEDVRLPASALLGEENKGFYYLMQELPQERLLIADLAISACEFMFEETRNYVRQRKAF... | 1.3.8.8 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:3968063}; | carnitine catabolic process [GO:0042413]; carnitine metabolic process, CoA-linked [GO:0019254]; cellular lipid catabolic process [GO:0044242]; fatty acid beta-oxidation using acyl-CoA dehydrogenase [GO:0033539]; fatty acid catabolic process [GO:0009062]; leucine catabolic process [GO:0006552]; long-chain fatty acid cat... | cytoplasm [GO:0005737]; mitochondrial matrix [GO:0005759]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739] | fatty-acyl-CoA binding [GO:0000062]; flavin adenine dinucleotide binding [GO:0050660]; identical protein binding [GO:0042802]; isovaleryl-CoA dehydrogenase activity [GO:0008470]; long-chain fatty acyl-CoA dehydrogenase activity [GO:0004466]; palmitoyl-CoA oxidase activity [GO:0016401] | PF00441;PF02770;PF02771; | 1.10.540.10;2.40.110.10;1.20.140.10; | Acyl-CoA dehydrogenase family | PTM: Acetylation at Lys-318 and Lys-322 in proximity of the cofactor-binding sites strongly reduces catalytic activity. These sites are deacetylated by SIRT3. {ECO:0000250|UniProtKB:P51174}. | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:3813556}. | CATALYTIC ACTIVITY: Reaction=a long-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = a long-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:17721, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307, C... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=123 uM for octanoyl-CoA (at 32 degrees Celsius and pH 8.0) {ECO:0000269|PubMed:3968063}; KM=24.3 uM for decanoyl-CoA (at 32 degrees Celsius and pH 8.0) {ECO:0000269|PubMed:3968063}; KM=9 uM for dodecanoyl-CoA (at 32 degrees Celsius and pH 8.0) {ECO:0000269|PubMed:3... | PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-oxidation. {ECO:0000303|PubMed:3968063}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:3968063}; | null | FUNCTION: Long-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats (PubMed:3968063). The first step of fatty acid ... | Rattus norvegicus (Rat) |
P15651 | ACADS_RAT | MAAALLARAGGSLGRALRARDWRRLHTVYQSVELPETHQMLRQTCRDFAEKELVPIAAQLDKEHLFPTSQVKKMGELGLLAMDVPEELSGAGLDYLAYSIALEEISRGCASTGVIMSVNNSLYLGPILKFGSSQQKQQWITPFTNGDKIGCFALSEPGNGSDAGAASTTAREEGDSWVLNGTKAWITNSWEASATVVFASTDRSRQNKGISAFLVPMPTPGLTLGKKEDKLGIRASSTANLIFEDCRIPKENLLGEPGMGFKIAMQTLDMGRIGIASQALGIAQASLDCAVKYAENRHAFGAPLTKLQNIQFKLADMALA... | 1.3.8.1 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:11812788, ECO:0000269|PubMed:3968063}; Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:11812788, ECO:0000269|PubMed:3968063}; | butyrate catabolic process [GO:0046359]; fatty acid beta-oxidation [GO:0006635]; fatty acid beta-oxidation using acyl-CoA dehydrogenase [GO:0033539]; response to glucocorticoid [GO:0051384]; response to starvation [GO:0042594] | mitochondrial matrix [GO:0005759]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739] | acyl-CoA dehydrogenase activity [GO:0003995]; butyryl-CoA dehydrogenase activity [GO:0004085]; fatty-acyl-CoA binding [GO:0000062]; flavin adenine dinucleotide binding [GO:0050660]; identical protein binding [GO:0042802] | PF00441;PF02770;PF02771; | 1.10.540.10;2.40.110.10;1.20.140.10; | Acyl-CoA dehydrogenase family | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:Q3ZBF6}. | CATALYTIC ACTIVITY: Reaction=a short-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = a short-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47196, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10.7 uM for butanoyl-CoA {ECO:0000269|PubMed:3968063}; KM=32.9 uM for pentanoyl-CoA {ECO:0000269|PubMed:3968063}; KM=285 uM for hexanoyl-CoA {ECO:0000269|PubMed:3968063}; | PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-oxidation. {ECO:0000305|PubMed:3968063}. | null | null | FUNCTION: Short-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats (PubMed:3968063). The first step of fatty acid... | Rattus norvegicus (Rat) |
P15655 | FGF2_MOUSE | MAASGITSLPALPEDGGAAFPPGHFKDPKRLYCKNGGFFLRIHPDGRVDGVREKSDPHVKLQLQAEERGVVSIKGVCANRYLAMKEDGRLLASKCVTEECFFFERLESNNYNTYRSRKYSSWYVALKRTGQYKLGSKTGPGQKAILFLPMSAKS | null | null | angiogenesis [GO:0001525]; angiogenesis involved in coronary vascular morphogenesis [GO:0060978]; animal organ morphogenesis [GO:0009887]; branching involved in ureteric bud morphogenesis [GO:0001658]; canonical Wnt signaling pathway [GO:0060070]; cardiac muscle cell proliferation [GO:0060038]; cell differentiation [GO... | cytoplasm [GO:0005737]; extracellular space [GO:0005615]; nucleus [GO:0005634] | chemoattractant activity [GO:0042056]; chemokine binding [GO:0019956]; cytokine activity [GO:0005125]; fibroblast growth factor receptor binding [GO:0005104]; growth factor activity [GO:0008083]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; integrin binding [GO:0005178]; nuclear receptor coacti... | PF00167; | 2.80.10.50; | Heparin-binding growth factors family | PTM: Phosphorylation at Tyr-81 regulates FGF2 unconventional secretion. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P09038}. Nucleus {ECO:0000250|UniProtKB:P09038}. Note=Exported from cells by an endoplasmic reticulum (ER)/Golgi-independent mechanism (By similarity). Unconventional secretion of FGF2 occurs by direct translocation across the plasma membrane (By similarity). Bindin... | null | null | null | null | null | FUNCTION: Acts as a ligand for FGFR1, FGFR2, FGFR3 and FGFR4 (By similarity). Also acts as an integrin ligand which is required for FGF2 signaling (By similarity). Binds to integrin ITGAV:ITGB3 (By similarity). Plays an important role in the regulation of cell survival, cell division, cell differentiation and cell migr... | Mus musculus (Mouse) |
P15656 | FGF5_MOUSE | MSLSLLFLIFCSHLIHSAWAHGEKRLTPEGQPAPPRNPGDSSGSRGRSSATFSSSSASSPVAASPGSQGSGSEHSSFQWSPSGRRTGSLYCRVGIGFHLQIYPDGKVNGSHEASVLSILEIFAVSQGIVGIRGVFSNKFLAMSKKGKLHASAKFTDDCKFRERFQENSYNTYASAIHRTEKTGREWYVALNKRGKAKRGCSPRVKPQHVSTHFLPRFKQSEQPELSFTVTVPEKKKPPVKPKVPLSQPRRSPSPVKYRLKFRFG | null | null | animal organ morphogenesis [GO:0009887]; cell differentiation [GO:0030154]; fibroblast growth factor receptor signaling pathway [GO:0008543]; glial cell differentiation [GO:0010001]; positive regulation of cell division [GO:0051781]; positive regulation of cell population proliferation [GO:0008284]; positive regulation... | cytoplasm [GO:0005737]; extracellular space [GO:0005615] | fibroblast growth factor receptor binding [GO:0005104]; growth factor activity [GO:0008083] | PF00167; | 2.80.10.50; | Heparin-binding growth factors family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | null | null | null | null | null | FUNCTION: Plays an important role in the regulation of cell proliferation and cell differentiation. Required for normal regulation of the hair growth cycle. Functions as an inhibitor of hair elongation by promoting progression from anagen, the growth phase of the hair follicle, into catagen the apoptosis-induced regres... | Mus musculus (Mouse) |
P15659 | PA_I33A0 | MEDFVRQCFNPMIVELAEKAMKEYGEDLKIETNKFAAICTHLEVCFMYSDFHFIDEQGESIVVELGDPNALLKHRFEIIEGRDRTIAWTVINSICNTTGAEKPKFLPDLYDYKKNRFIEIGVTRREVHIYYLEKANKIKSEKTHIHIFSFTGEEMATKADYTLDEESRARIKTRLFTIRQEMASRGLWDSFRQSERGEETIEERFEITGTMRKLADQSLPPNFSSLENFRAYVDGFEPNGYIEGKLSQMSKEVNARIEPFLKSTPRPLRLPDGPPCSQRSKFLLMDALKLSIEDPSHEGEGIPLYDAIKCMRTFFGWKEP... | 3.1.-.- | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_04063}; Note=Binds 2 manganese ions per subunit. {ECO:0000255|HAMAP-Rule:MF_04063}; | cap snatching [GO:0075526]; DNA-templated transcription [GO:0006351]; negative regulation of viral genome replication [GO:0045071]; negative regulation of viral transcription [GO:0032897]; negative stranded viral RNA replication [GO:0039689]; protein import into nucleus [GO:0006606]; symbiont-mediated suppression of ho... | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025] | endonuclease activity [GO:0004519]; metal ion binding [GO:0046872]; RNA binding [GO:0003723]; RNA polymerase activity [GO:0097747] | PF00603; | 3.40.91.90; | Influenza viruses PA family | PTM: Phosphorylated on serines and threonines by host kinases, including human casein kinase II. {ECO:0000250|UniProtKB:P03433, ECO:0000255|HAMAP-Rule:MF_04063}. | SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04063}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04063}. Note=PB1 and PA are transported in the host nucleus as a complex. {ECO:0000250|UniProtKB:P03433, ECO:0000255|HAMAP-Rule:MF_04063}. | null | null | null | null | null | FUNCTION: Plays an essential role in viral RNA transcription and replication by forming the heterotrimeric polymerase complex together with PB1 and PB2 subunits. The complex transcribes viral mRNAs by using a unique mechanism called cap-snatching. It consists in the hijacking and cleavage of host capped pre-mRNAs. Thes... | Influenza A virus (strain A/Wilson-Smith/1933 H1N1) (Influenza A virus (strain A/WS/1933 H1N1)) |
P15684 | AMPN_RAT | MAKGFYISKTLGILGILLGVAAVCTIIALSVVYAQEKNRNAENSAIAPTLPGSTSATTSTTNPAIDESKPWNQYRLPKTLIPDSYQVTLRPYLTPNEQGLYIFKGSSTVRFTCNETTNVIIIHSKKLNYTNKGNHRVALRALGDTPAPNIDTTELVERTEYLVVHLQGSLVKGHQYEMDSEFQGELADDLAGFYRSEYMEGGNKKVVATTQMQAADARKSFPCFDEPAMKASFNITLIHPNNLTALSNMLPKDSRTLQEDPSWNVTEFHPTPKMSTYLLAYIVSEFKYVEAVSPNRVQIRIWARPSAIDEGHGDYALQVT... | 3.4.11.2 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P15144}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:P15144}; | angiogenesis [GO:0001525]; cell differentiation [GO:0030154]; metanephric proximal tubule development [GO:0072237]; peptide catabolic process [GO:0043171]; protein processing [GO:0016485]; proteolysis [GO:0006508] | brush border membrane [GO:0031526]; cytoplasm [GO:0005737]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | aminopeptidase activity [GO:0004177]; metalloaminopeptidase activity [GO:0070006]; peptide binding [GO:0042277]; zinc ion binding [GO:0008270] | PF11838;PF01433;PF17900; | 1.25.50.20;2.60.40.1910;1.10.390.10;2.60.40.1730; | Peptidase M1 family | PTM: Sulfated. {ECO:0000250|UniProtKB:P15145}.; PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:P15144}.; PTM: May undergo proteolysis and give rise to a soluble form. {ECO:0000250|UniProtKB:P15144}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2564389}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:P15144}. Note=Also found as a soluble form. {ECO:0000250|UniProtKB:P15144}. | CATALYTIC ACTIVITY: Reaction=Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.; E... | null | null | null | null | FUNCTION: Broad specificity aminopeptidase which plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. Also involved in the processing of various peptides including peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines. May a... | Rattus norvegicus (Rat) |
P15690 | NDUS1_BOVIN | MLRIPVRKALVGLSKSSKGCVRTTATAASNLIEVFVDGQSVMVEPGTTVLQACEKVGMQIPRFCYHERLSVAGNCRMCLVEIEKAPKVVAACAMPVMKGWNILTNSEKTKKAREGVMEFLLANHPLDCPICDQGGECDLQDQSMMFGSDRSRFLEGKRAVEDKNIGPLVKTIMTRCIQCTRCIRFASEIAGVDDLGTTGRGNDMQVGTYIEKMFMSELSGNIIDICPVGALTSKPYAFTARPWETRKTESIDVMDAVGSNIVVSTRTGEVMRILPRMHEDINEEWISDKTRFAYDGLKRQRLTEPMVRNEKGLLTHTTWE... | 7.1.1.2 | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000250|UniProtKB:Q56223}; Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000250|UniProtKB:Q56223}; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250|UniProtKB:Q56223}; Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO... | apoptotic mitochondrial changes [GO:0008637]; ATP metabolic process [GO:0046034]; cellular respiration [GO:0045333]; mitochondrial electron transport, NADH to ubiquinone [GO:0006120]; mitochondrial respiratory chain complex I assembly [GO:0032981]; reactive oxygen species metabolic process [GO:0072593]; regulation of m... | mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrial respiratory chain complex I [GO:0005747]; mitochondrion [GO:0005739] | 2 iron, 2 sulfur cluster binding [GO:0051537]; 4 iron, 4 sulfur cluster binding [GO:0051539]; metal ion binding [GO:0046872]; NADH dehydrogenase (ubiquinone) activity [GO:0008137] | PF13510;PF00384;PF10588;PF09326; | 3.10.20.740;3.30.200.210;3.30.70.20;3.40.50.740; | Complex I 75 kDa subunit family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:10852722, ECO:0000269|PubMed:18721790, ECO:0000269|PubMed:25209663}; Peripheral membrane protein {ECO:0000305|PubMed:25209663}; Matrix side {ECO:0000305|PubMed:25209663}. | CATALYTIC ACTIVITY: Reaction=a ubiquinone + 5 H(+)(in) + NADH = a ubiquinol + 4 H(+)(out) + NAD(+); Xref=Rhea:RHEA:29091, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15378, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=7.1.1.2; Evidence={ECO:0000250|UniProtKB:P28331}; | null | null | null | null | FUNCTION: Core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I) which catalyzes electron transfer from NADH through the respiratory chain, using ubiquinone as an electron acceptor (PubMed:10852722, PubMed:18721790). Essential for catalysing the entry and efficient transfer of elect... | Bos taurus (Bovine) |
P15691 | VEGFA_BOVIN | MNFLLSWVHWSLALLLYLHHAKWSQAAPMAEGGQKPHEVVKFMDVYQRSFCRPIETLVDIFQEYPDEIEFIFKPSCVPLMRCGGCCNDESLECVPTEEFNITMQIMRIKPHQSQHIGEMSFLQHNKCECRPKKDKARQENPCGPCSERRKHLFVQDPQTCKCSCKNTDSRCKARQLELNERTCRCDKPRR | null | null | cellular response to hypoxia [GO:0071456]; induction of positive chemotaxis [GO:0050930]; motor neuron migration [GO:0097475]; positive regulation of angiogenesis [GO:0045766]; positive regulation of cell division [GO:0051781]; positive regulation of endothelial cell migration [GO:0010595]; positive regulation of endot... | extracellular space [GO:0005615]; membrane [GO:0016020] | chemoattractant activity [GO:0042056]; cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; heparin binding [GO:0008201]; protein homodimerization activity [GO:0042803]; vascular endothelial growth factor receptor 1 binding [GO:0043183]; vascular endothelial growth factor receptor 2 binding [GO:0043184] | PF00341;PF14554; | 2.10.90.10;2.10.160.10; | PDGF/VEGF growth factor family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Secreted but remains associated to cells or to the extracellular matrix unless released by heparin. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Growth factor active in angiogenesis, vasculogenesis and endothelial cell growth. Induces endothelial cell proliferation, promotes cell migration, inhibits apoptosis and induces permeabilization of blood vessels. Binds to the FLT1/VEGFR1 and KDR/VEGFR2 receptors, heparan sulfate and heparin (By similarity). B... | Bos taurus (Bovine) |
P15692 | VEGFA_HUMAN | MTDRQTDTAPSPSYHLLPGRRRTVDAAASRGQGPEPAPGGGVEGVGARGVALKLFVQLLGCSRFGGAVVRAGEAEPSGAARSASSGREEPQPEEGEEEEEKEEERGPQWRLGARKPGSWTGEAAVCADSAPAARAPQALARASGRGGRVARRGAEESGPPHSPSRRGSASRAGPGRASETMNFLLSWVHWSLALLLYLHHAKWSQAAPMAEGGGQNHHEVVKFMDVYQRSYCHPIETLVDIFQEYPDEIEYIFKPSCVPLMRCGGCCNDEGLECVPTEESNITMQIMRIKPHQGQHIGEMSFLQHNKCECRPKKDRARQE... | null | null | angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; artery morphogenesis [GO:0048844]; basophil chemotaxis [GO:0002575]; bone trabecula formation [GO:0060346]; branching involved in blood vessel morphogenesis [GO:0001569]; camera-type eye morphogenesis [GO:0048593]; cardiac muscle cell development [GO:0055013]; ... | adherens junction [GO:0005912]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; nucleus [GO:0005634]; platelet alpha granule... | chemoattractant activity [GO:0042056]; cytokine activity [GO:0005125]; extracellular matrix binding [GO:0050840]; fibronectin binding [GO:0001968]; growth factor activity [GO:0008083]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; neuropilin binding [GO:0038191]; platelet-derived growth factor r... | PF00341;PF14554; | 2.10.90.10;2.10.160.10; | PDGF/VEGF growth factor family | PTM: [Vascular endothelial growth factor A, long form]: Produced by use of an alternative upstream CUG codon and post-translationally processed into the N-terminal N-VEGF form and the C-terminal secreted VEGFA form. {ECO:0000269|PubMed:11731620}. | SUBCELLULAR LOCATION: [N-VEGF]: Cytoplasm {ECO:0000269|PubMed:15896327}. Nucleus {ECO:0000269|PubMed:15896327, ECO:0000269|PubMed:35455969}. Note=Cytoplasmic in normoxic conditions and localizes to the nucleus under hypoxic conditions. {ECO:0000269|PubMed:15896327, ECO:0000269|PubMed:35455969}.; SUBCELLULAR LOCATION: [... | null | null | null | null | null | FUNCTION: [N-VEGF]: Participates in the induction of key genes involved in the response to hypoxia and in the induction of angiogenesis such as HIF1A (PubMed:35455969). Involved in protecting cells from hypoxia-mediated cell death (By similarity). {ECO:0000250|UniProtKB:Q00731, ECO:0000269|PubMed:35455969}.; FUNCTION: ... | Homo sapiens (Human) |
P15693 | PPBI1_RAT | MQGDWVLLLLLGLRIHLSFGVIPVEEENPVFWNQKAKEALDVAKKLQPIQTSAKNLILFLGDGMGVPTVTATRILKGQLGGHLGPETPLAMDHFPFTALSKTYNVDRQVPDSAGTATAYLCGVKANYKTIGVSAAARFNQCNSTFGNEVFSVMHRAKKAGKSVGVVTTTRVQHASPAGTYAHTVNRDWYSDADMPSSALQEGCKDIATQLISNMDIDVILGGGRKFMFPKGTPDPEYPGDSDQSGVRLDSRNLVEEWLAKYQGTRYVWNREQLMQASQDPAVTRLMGLFEPTEMKYDVNRNASADPSLAEMTEVAVRLLS... | 3.1.3.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:24076154}; Note=Binds 1 Mg(2+) ion. {ECO:0000269|PubMed:24076154}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:24076154}; Note=Binds 2 Zn(2+) ions. {ECO:0000269|PubMed:24076154}; COFACTOR: Name=Ca(2+); Xref=ChEBI... | cellular response to BMP stimulus [GO:0071773]; dephosphorylation [GO:0016311] | external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886] | alkaline phosphatase activity [GO:0004035]; magnesium ion binding [GO:0000287]; protease binding [GO:0002020]; protein homodimerization activity [GO:0042803]; zinc ion binding [GO:0008270] | PF00245; | 3.40.720.10; | Alkaline phosphatase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2155025}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:2155025}. | CATALYTIC ACTIVITY: Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10042, ECO:0000269|PubMed:2155025, ECO:0000269|PubMed:24076154}; | null | null | null | null | FUNCTION: Alkaline phosphatase that can hydrolyze various phosphate compounds. {ECO:0000269|PubMed:2155025, ECO:0000269|PubMed:24076154}. | Rattus norvegicus (Rat) |
P15696 | IFNT1_BOVIN | MAFVLSLLMALVLVSYGPGRSLGCYLSEDHMLGARENLRLLARMNRLSPHPCLQDRKDFGLPQEMVEGNQLQKDQAISVLHEMLQQCFNLFYTEHSSAAWNTTLLEQLCTGLQQQLEDLDACLGPVMGEKDSDMGRMGPILTVKKYFQGIHVYLKEKEYSDCAWEIIRVEMMRALSSSTTLQKRLRKMGGDLNSL | null | null | adaptive immune response [GO:0002250]; B cell differentiation [GO:0030183]; B cell proliferation [GO:0042100]; cytokine-mediated signaling pathway [GO:0019221]; defense response to virus [GO:0051607]; female pregnancy [GO:0007565]; humoral immune response [GO:0006959]; natural killer cell activation involved in immune ... | extracellular space [GO:0005615] | cytokine activity [GO:0005125]; hormone activity [GO:0005179]; type I interferon receptor binding [GO:0005132] | PF00143; | 1.20.1250.10; | Alpha/beta interferon family, IFN-alphaII subfamily | null | SUBCELLULAR LOCATION: Secreted. Note=Secreted into the uterine lumen. | null | null | null | null | null | FUNCTION: Paracrine hormone primarily responsible for maternal recognition of pregnancy. Interacts with endometrial receptors, probably type I interferon receptors, and blocks estrogen receptor expression, preventing the estrogen-induced increase in oxytocin receptor expression in the endometrium. This results in the s... | Bos taurus (Bovine) |
P15700 | KCY_YEAST | MTAATTSQPAFSPDQVSVIFVLGGPGAGKGTQCEKLVKDYSFVHLSAGDLLRAEQGRAGSQYGELIKNCIKEGQIVPQEITLALLRNAISDNVKANKHKFLIDGFPRKMDQAISFERDIVESKFILFFDCPEDIMLERLLERGKTSGRSDDNIESIKKRFNTFKETSMPVIEYFETKSKVVRVRCDRSVEDVYKDVQDAIRDSL | 2.7.4.14 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_03172, ECO:0000269|PubMed:16240436, ECO:0000269|PubMed:8391780}; Note=Binds 1 Mg(2+) ion per monomer. {ECO:0000255|HAMAP-Rule:MF_03172, ECO:0000269|PubMed:16240436, ECO:0000269|PubMed:8391780}; | 'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; CDP biosynthetic process [GO:0046705]; nucleobase-containing compound metabolic process [GO:0006139]; phosphorylation [GO:0016310]; UDP biosynthetic process [GO:0006225] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | adenylate kinase activity [GO:0004017]; ATP binding [GO:0005524]; cytidylate kinase activity [GO:0004127]; nucleoside diphosphate kinase activity [GO:0004550]; UMP kinase activity [GO:0033862]; UMP/dUMP kinase activity [GO:0009041] | PF00406; | 3.40.50.300; | Adenylate kinase family, UMP-CMP kinase subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03172, ECO:0000269|PubMed:1333436, ECO:0000269|PubMed:8391780}. Nucleus {ECO:0000255|HAMAP-Rule:MF_03172, ECO:0000269|PubMed:1333436, ECO:0000269|PubMed:8391780}. Note=Predominantly cytoplasmic. {ECO:0000255|HAMAP-Rule:MF_03172, ECO:0000269|PubMed:8391780}. | CATALYTIC ACTIVITY: Reaction=ATP + UMP = ADP + UDP; Xref=Rhea:RHEA:24400, ChEBI:CHEBI:30616, ChEBI:CHEBI:57865, ChEBI:CHEBI:58223, ChEBI:CHEBI:456216; EC=2.7.4.14; Evidence={ECO:0000255|HAMAP-Rule:MF_03172, ECO:0000269|PubMed:1333436, ECO:0000269|PubMed:16240436, ECO:0000269|PubMed:1655742, ECO:0000269|PubMed:2172245, ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.15 mM for UMP {ECO:0000269|PubMed:2172245}; KM=1 mM for dUMP {ECO:0000269|PubMed:2172245}; KM=1.8 mM for dTMP {ECO:0000269|PubMed:2172245}; KM=0.11 mM for ATP {ECO:0000269|PubMed:16240436}; KM=0.53 mM for dCMP {ECO:0000269|PubMed:16240436}; Vmax=120 umol/min/mg e... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6-9.5. {ECO:0000269|PubMed:8391780}; | null | FUNCTION: Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and dUMP as phosphate acceptors, but can also use CMP, dCMP, AMP, GMP, dGMP and dTMP. ATP and dATP are the best phosphate d... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P15702 | LEUK_MOUSE | MALHLLLLFGACWVQVASPDSLQRTTMLPSTPHITAPSTSEAQNASPSVSVGSGTVDSKETISPWGQTTIPVSLTPLETTELSSLETSAGASMSTPVPEPTASQEVSSKTSALLPEPSNVASDPPVTAANPVTDGPAANPVTDGTAASTSISKGTSAPPTTVTTSSNETSGPSVATTVSSKTSGPPVTTATGSLGPSSEMHGLPATTATSSVESSSVARGTSVSSRKTSTTSTQDPITTRSPSQESSGMLLVPMLIALVVVLALVALLLLWRQRQKRRTGALTLSGGGKRNGVVDAWAGPARVPDEEATTTSGAGGNKGS... | null | null | apoptotic signaling pathway [GO:0097190]; cell surface receptor signaling pathway [GO:0007166]; defense response to bacterium [GO:0042742]; leukocyte tethering or rolling [GO:0050901]; negative regulation of cell adhesion [GO:0007162]; negative regulation of T cell activation [GO:0050868]; negative regulation of T cell... | basement membrane [GO:0005604]; cell surface [GO:0009986]; cleavage furrow [GO:0032154]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; microvillus [GO:0005902]; plasma membrane [GO:0005886]; PML body [GO:0016605]; uropod [GO:0001931] | heat shock protein binding [GO:0031072]; Hsp70 protein binding [GO:0030544]; protein domain specific binding [GO:0019904]; transmembrane signaling receptor activity [GO:0004888] | null | null | null | PTM: Phosphorylation at Ser-347 is regulated by chemokines, requires its association with ERM proteins (EZR, RDX and MSN) and is essential for its function in the regulation of T-cell trafficking to lymph nodes. {ECO:0000269|PubMed:17638845, ECO:0000269|PubMed:21289089}.; PTM: Has a high content of sialic acid and O-li... | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, microvillus {ECO:0000250|UniProtKB:P13838}. Cell projection, uropodium {ECO:0000269|PubMed:21289089}. Note=Localizes to the uropodium and microvilli via its interaction with ERM proteins (EZR, RDX and MSN).... | null | null | null | null | null | FUNCTION: Predominant cell surface sialoprotein of leukocytes which regulates multiple T-cell functions, including T-cell activation, proliferation, differentiation, trafficking and migration. Positively regulates T-cell trafficking to lymph-nodes via its association with ERM proteins (EZR, RDX and MSN) (PubMed:1172833... | Mus musculus (Mouse) |
P15703 | BGL2_YEAST | MRFSTTLATAATALFFTASQVSAIGELAFNLGVKNNDGTCKSTSDYETELQALKSYTSTVKVYAASDCNTLQNLGPAAEAEGFTIFVGVWPTDDSHYAAEKAALQTYLPKIKESTVAGFLVGSEALYRNDLTASQLSDKINDVRSVVADISDSDGKSYSGKQVGTVDSWNVLVAGYNSAVIEASDFVMANAFSYWQGQTMQNASYSFFDDIMQALQVIQSTKGSTDITFWVGETGWPTDGTNFESSYPSVDNAKQFWKEGICSMRAWGVNVIVFEAFDEDWKPNTSGTSDVEKHWGVFTSSDNLKYSLDCDFS | 3.2.1.58 | null | carbohydrate metabolic process [GO:0005975]; cell wall organization [GO:0071555]; fungal-type cell wall organization [GO:0031505] | cell surface [GO:0009986]; extracellular region [GO:0005576]; fungal-type cell wall [GO:0009277]; fungal-type vacuole [GO:0000324] | chitin binding [GO:0008061]; glucan endo-1,3-beta-D-glucosidase activity [GO:0042973]; glucan exo-1,3-beta-glucosidase activity [GO:0004338] | PF00332; | 3.20.20.80; | Glycosyl hydrolase 17 family | null | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:9748433}. Note=Tightly bound to cell wall. | CATALYTIC ACTIVITY: Reaction=Successive hydrolysis of beta-D-glucose units from the non-reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose.; EC=3.2.1.58; | null | null | null | null | FUNCTION: Glucanases possibly play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme may be involved in beta-glucan degradation and also function biosynthetically as a transglycosylase. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P15705 | STI1_YEAST | MSLTADEYKQQGNAAFTAKDYDKAIELFTKAIEVSETPNHVLYSNRSACYTSLKKFSDALNDANECVKINPSWSKGYNRLGAAHLGLGDLDEAESNYKKALELDASNKAAKEGLDQVHRTQQARQAQPDLGLTQLFADPNLIENLKKNPKTSEMMKDPQLVAKLIGYKQNPQAIGQDLFTDPRLMTIMATLMGVDLNMDDINQSNSMPKEPETSKSTEQKKDAEPQSDSTTSKENSSKAPQKEESKESEPMEVDEDDSKIEADKEKAEGNKFYKARQFDEAIEHYNKAWELHKDITYLNNRAAAEYEKGEYETAISTLND... | null | null | protein folding [GO:0006457]; protein localization [GO:0008104]; protein targeting to mitochondrion [GO:0006626] | cytoplasm [GO:0005737] | ATPase inhibitor activity [GO:0042030]; Hsp70 protein binding [GO:0030544]; Hsp90 protein binding [GO:0051879]; mRNA binding [GO:0003729] | PF17830;PF00515;PF13432;PF13181; | 1.10.260.100;1.25.40.10; | null | PTM: N-glycosylated. {ECO:0000269|PubMed:19756047}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. | null | null | null | null | null | FUNCTION: May play a role in mediating the heat shock response of some HSP70 genes. It is required for optimal growth of yeast cells at both low and high temperature. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P15709 | ST2A1_RAT | MPDYTWFEGIPFHAFGISKETLQNVCNKFVVKDEDLILLAYPKSGTNWLIEIVCLIQTKGDPKWIQSVTIWDRSPWIETDLGYDMLIKKKGPRLITSHLPMHLFSKSLFSSKAKVIYLVRNPRDVLVSGYYFWGNSTLAKKPDSLGTYVEWFLKGNVLYGSWFEHIRAWLSMREWDNFLLLYYEDMKKDTMGTIKKICDFLGKKLEPDELDLVLKYSSFQVMKENDMSNYSLLMKKSIFTGIGLMRKGTVGDWKNHFTVSQAEAFDKVFQEKMAGFPPGMFPWE | 2.8.2.14; 2.8.2.2 | null | 3'-phosphoadenosine 5'-phosphosulfate metabolic process [GO:0050427]; cellular response to vitamin D [GO:0071305]; cholesterol metabolic process [GO:0008203]; ethanol catabolic process [GO:0006068]; response to activity [GO:0014823]; response to insecticide [GO:0017085]; response to nutrient levels [GO:0031667]; steroi... | cytoplasm [GO:0005737] | 3'-phosphoadenosine 5'-phosphosulfate binding [GO:0050656]; alcohol sulfotransferase activity [GO:0004027]; bile-salt sulfotransferase activity [GO:0047704]; steroid sulfotransferase activity [GO:0050294]; sulfotransferase activity [GO:0008146]; transferase activity [GO:0016740] | PF00685; | 3.40.50.300; | Sulfotransferase 1 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:2590219}. | CATALYTIC ACTIVITY: Reaction=3'-phosphoadenylyl sulfate + an alcohol = adenosine 3',5'-bisphosphate + an alkyl sulfate + H(+); Xref=Rhea:RHEA:22552, ChEBI:CHEBI:15378, ChEBI:CHEBI:30879, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343, ChEBI:CHEBI:83414; EC=2.8.2.2; Evidence={ECO:0000250|UniProtKB:Q06520}; PhysiologicalDirection=... | null | null | null | null | FUNCTION: Sulfotransferase that utilizes 3'-phospho-5'-adenylyl sulfate (PAPS) as sulfonate donor to catalyze the sulfonation of steroids and bile acids in the liver and adrenal glands (By similarity). Mediates the sulfation of a wide range of steroids and sterols, including pregnenolone, androsterone, DHEA, bile acids... | Rattus norvegicus (Rat) |
P15719 | MDHP_MAIZE | MGLSTVYSPAGPRLVPAPLGRCRSAQPRRPRRAPLATVRCSVDATKQAQDGVATAVATEAPASRKECFGVFCTTYDLKAEDKTKSWRKLVNVAVSGAAGMISNHLLFKLASGEVFGQDQPIALKLLGSERSFQALEGVAMELEDSLYPLLREVSIGIDPYVVFQDVDWALLIGAKPRGPGMERAALLDINGQIFADQGKALNAVASRNDEVLVVGNPCNTNALICLKNAPNIPAKNFHALTRLDENRAKCQLALKAGVFYDKVSNVTIWGNHSTTQVPDFLNAKIDGRPVKEVIKDTKWLEEEFTLTVQKRGGVLIQKWG... | 1.1.1.82 | null | malate metabolic process [GO:0006108]; NADH metabolic process [GO:0006734]; oxaloacetate metabolic process [GO:0006107]; tricarboxylic acid cycle [GO:0006099] | chloroplast [GO:0009507] | L-malate dehydrogenase activity [GO:0030060]; malate dehydrogenase (NADP+) activity [GO:0046554] | PF02866;PF00056; | 3.90.110.10;3.40.50.720; | LDH/MDH superfamily, MDH type 2 family | null | SUBCELLULAR LOCATION: Plastid, chloroplast. | CATALYTIC ACTIVITY: Reaction=(S)-malate + NADP(+) = H(+) + NADPH + oxaloacetate; Xref=Rhea:RHEA:10824, ChEBI:CHEBI:15378, ChEBI:CHEBI:15589, ChEBI:CHEBI:16452, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.82; | null | null | null | null | FUNCTION: The chloroplastic, NADP-dependent form is essential for the photosynthesis C4 cycle, which allows plants to circumvent the problem of photorespiration. In C4 plants, NADP-MDH activity acts to convert oxaloacetate to malate in chloroplasts of mesophyll cells for transport to the bundle sheath cells. | Zea mays (Maize) |
P15723 | DGTP_ECOLI | MAQIDFRKKINWHRRYRSPQGVKTEHEILRIFESDRGRIINSPAIRRLQQKTQVFPLERNAAVRTRLTHSMEVQQVGRYIAKEILSRLKELKLLEAYGLDELTGPFESIVEMSCLMHDIGNPPFGHFGEAAINDWFRQRLHPEDAESQPLTDDRCSVAALRLRDGEEPLNELRRKIRQDLCHFEGNAQGIRLVHTLMRMNLTWAQVGGILKYTRPAWWRGETPETHHYLMKKPGYYLSEEAYIARLRKELNLALYSRFPLTWIMEAADDISYCVADLEDAVEKRIFTVEQLYHHLHEAWGQHEKGSLFSLVVENAWEKSR... | 3.1.5.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00030, ECO:0000269|PubMed:2826481}; | dGTP catabolic process [GO:0006203]; nucleobase-containing small molecule interconversion [GO:0015949] | null | cobalt ion binding [GO:0050897]; dGTPase activity [GO:0008832]; GTPase activity [GO:0003924]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; manganese ion binding [GO:0030145]; single-stranded DNA binding [GO:0003697] | PF01966; | 1.10.3210.10;1.10.3410.10; | DGTPase family, Type 1 subfamily | null | null | CATALYTIC ACTIVITY: Reaction=dGTP + H2O = 2'-deoxyguanosine + H(+) + triphosphate; Xref=Rhea:RHEA:15193, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17172, ChEBI:CHEBI:18036, ChEBI:CHEBI:61429; EC=3.1.5.1; Evidence={ECO:0000255|HAMAP-Rule:MF_00030, ECO:0000269|PubMed:2826481}; | null | null | null | null | FUNCTION: dGTPase preferentially hydrolyzes dGTP over the other canonical NTPs. {ECO:0000255|HAMAP-Rule:MF_00030, ECO:0000269|PubMed:2826481}. | Escherichia coli (strain K12) |
P15725 | TNR4_RAT | MYVWVQQPTAFLLLGLSLGVTVKLNCVKDTYPSGHKCCRECQPGHGMVSRCDHTRDTVCHPCEPGFYNEAVNYDTCKQCTQCNHRSGSELKQNCTPTEDTVCQCRPGTQPRQDSSHKLGVDCVPCPPGHFSPGSNQACKPWTNCTLSGKQIRHPASNSLDTVCEDRSLLATLLWETQRTTFRPTTVPSTTVWPRTSQLPSTPTLVAPEGPAFAVILGLGLGLLAPLTVLLALYLLRKAWRSPNTPKPCWGNSFRTPIQEEQTDTHFTLAKI | null | null | cellular defense response [GO:0006968]; inflammatory response [GO:0006954]; negative regulation of activation-induced cell death of T cells [GO:0070236]; negative regulation of cytokine production [GO:0001818]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of extrinsic apoptotic s... | cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886] | tumor necrosis factor receptor activity [GO:0005031] | PF00020; | 2.10.50.10; | null | null | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Receptor for TNFSF4/OX40L/GP34. Is a costimulatory molecule implicated in long-term T-cell immunity (By similarity). {ECO:0000250}. | Rattus norvegicus (Rat) |
P15731 | UBC4_YEAST | MSSSKRIAKELSDLERDPPTSCSAGPVGDDLYHWQASIMGPADSPYAGGVFFLSIHFPTDYPFKPPKISFTTKIYHPNINANGNICLDILKDQWSPALTLSKVLLSICSLLTDANPDDPLVPEIAHIYKTDRPKYEATAREWTKKYAV | 2.3.2.23 | null | cytoplasm protein quality control by the ubiquitin-proteasome system [GO:0071629]; mitochondria-associated ubiquitin-dependent protein catabolic process [GO:0072671]; protein K48-linked ubiquitination [GO:0070936]; protein monoubiquitination [GO:0006513]; protein polyubiquitination [GO:0000209]; protein ubiquitination ... | cytoplasm [GO:0005737]; nucleus [GO:0005634]; ubiquitin ligase complex [GO:0000151] | ATP binding [GO:0005524]; proteasome binding [GO:0070628]; protein-macromolecule adaptor activity [GO:0030674]; ubiquitin binding [GO:0043130]; ubiquitin conjugating enzyme activity [GO:0061631]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-protein transferase activity [GO:0004842] | PF00179; | 3.10.110.10; | Ubiquitin-conjugating enzyme family | PTM: The N-terminus is blocked. | null | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.; EC=2.3.2.23; Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROS... | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000255|PROSITE-ProRule:PRU00388}. | null | null | FUNCTION: Catalyzes the covalent attachment of ubiquitin to other proteins (PubMed:17550898). Mediates the selective degradation of short-lived and abnormal proteins (PubMed:17550898). Mediates ubiquitination of PEX5 (PubMed:17550898). {ECO:0000269|PubMed:17550898}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P15732 | UBC5_YEAST | MSSSKRIAKELSDLGRDPPASCSAGPVGDDLYHWQASIMGPSDSPYAGGVFFLSIHFPTDYPFKPPKVNFTTKIYHPNINSSGNICLDILKDQWSPALTLSKVLLSICSLLTDANPDDPLVPEIAQIYKTDKAKYEATAKEWTKKYAV | 2.3.2.23 | null | protein K48-linked ubiquitination [GO:0070936]; protein polyubiquitination [GO:0000209]; ubiquitin-dependent protein catabolic process [GO:0006511] | nucleus [GO:0005634]; ubiquitin ligase complex [GO:0000151] | ATP binding [GO:0005524]; proteasome binding [GO:0070628]; ubiquitin conjugating enzyme activity [GO:0061631]; ubiquitin protein ligase binding [GO:0031625]; ubiquitin-protein transferase activity [GO:0004842] | PF00179; | 3.10.110.10; | Ubiquitin-conjugating enzyme family | PTM: The N-terminus is blocked. | null | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.; EC=2.3.2.23; Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROS... | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000255|PROSITE-ProRule:PRU00388}. | null | null | FUNCTION: Catalyzes the covalent attachment of ubiquitin to other proteins (PubMed:19920177, PubMed:2154373). Mediates the selective degradation of short-lived and abnormal proteins (PubMed:2154373). The RSP5-UBA1-UBC5 ubiquitin ligase complex ubiquitinates RPO21 forming 'Lys-63'-linked polyubiquitin chains (PubMed:199... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P15735 | PHKG2_HUMAN | MTLDVGPEDELPDWAAAKEFYQKYDPKDVIGRGVSSVVRRCVHRATGHEFAVKIMEVTAERLSPEQLEEVREATRRETHILRQVAGHPHIITLIDSYESSSFMFLVFDLMRKGELFDYLTEKVALSEKETRSIMRSLLEAVSFLHANNIVHRDLKPENILLDDNMQIRLSDFGFSCHLEPGEKLRELCGTPGYLAPEILKCSMDETHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQILMLRMIMEGQYQFSSPEWDDRSSTVKDLISRLLQVDPEARLTAEQALQHPFFERCEGSQPWNLTPRQRFRVAVWTVLAAGR... | 2.7.11.19 | null | generation of precursor metabolites and energy [GO:0006091]; glycogen biosynthetic process [GO:0005978]; glycogen catabolic process [GO:0005980]; glycogen metabolic process [GO:0005977]; positive regulation of glycogen catabolic process [GO:0045819]; protein phosphorylation [GO:0006468] | cytosol [GO:0005829]; phosphorylase kinase complex [GO:0005964] | ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; enzyme binding [GO:0019899]; phosphorylase kinase activity [GO:0004689]; protein serine/threonine kinase activity [GO:0004674]; tau-protein kinase activity [GO:0050321] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family | null | null | CATALYTIC ACTIVITY: Reaction=2 ATP + phosphorylase b = 2 ADP + phosphorylase a.; EC=2.7.11.19; | null | null | null | null | FUNCTION: Catalytic subunit of the phosphorylase b kinase (PHK), which mediates the neural and hormonal regulation of glycogen breakdown (glycogenolysis) by phosphorylating and thereby activating glycogen phosphorylase. May regulate glycogeneolysis in the testis. In vitro, phosphorylates PYGM (By similarity). {ECO:0000... | Homo sapiens (Human) |
P15770 | AROE_ECOLI | METYAVFGNPIAHSKSPFIHQQFAQQLNIEHPYGRVLAPINDFINTLNAFFSAGGKGANVTVPFKEEAFARADELTERAALAGAVNTLMRLEDGRLLGDNTDGVGLLSDLERLSFIRPGLRILLIGAGGASRGVLLPLLSLDCAVTITNRTVSRAEELAKLFAHTGSIQALSMDELEGHEFDLIINATSSGISGDIPAIPSSLIHPGIYCYDMFYQKGKTPFLAWCEQRGSKRNADGLGMLVAQAAHAFLLWHGVLPDVEPVIKQLQEELSA | 1.1.1.25 | null | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; shikimate metabolic process [GO:0019632] | cytosol [GO:0005829] | NADP binding [GO:0050661]; nucleotide binding [GO:0000166]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764] | PF18317;PF01488;PF08501; | 3.40.50.10860;3.40.50.720; | Shikimate dehydrogenase family | null | null | CATALYTIC ACTIVITY: Reaction=NADP(+) + shikimate = 3-dehydroshikimate + H(+) + NADPH; Xref=Rhea:RHEA:17737, ChEBI:CHEBI:15378, ChEBI:CHEBI:16630, ChEBI:CHEBI:36208, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.25; Evidence={ECO:0000255|HAMAP-Rule:MF_00222, ECO:0000269|PubMed:12637497}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=56 uM for NADP {ECO:0000269|PubMed:12637497}; KM=65 uM for shikimate {ECO:0000269|PubMed:12637497}; Note=kcat is 14.2 min(-1) for dehydrogenase activity with NADP or shikimate. {ECO:0000269|PubMed:12637497}; | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_00222}. | null | null | FUNCTION: Involved in the biosynthesis of the chorismate, which leads to the biosynthesis of aromatic amino acids. Catalyzes the reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to yield shikimate (SA). It displays no activity in the presence of NAD. {ECO:0000255|HAMAP-Rule:MF_00222, ECO:0000269|PubMed:12... | Escherichia coli (strain K12) |
P15776 | HEMA_CVBM | MFLLLRFVLVSCIIGSLGFDNPPTNVVSHLNGDWFLFGDSRSDCNHVVNTNPRNYSYMDLNPALCDSGKISSKAGNSIFRSFHFTDFYNYTGEGQQIIFYEGVNFTPYHAFKCTTSGSNDIWMQNKGLFYTQVYKNMAVYRSLTFVNVPYVYNGSAQSTALCKSGSLVLNNPAYIAREANFGDYYYKVEADFYLSGCDEYIVPLCIFNGKFLSNTKYYDDSQYYFNKDTGVIYGLNSTETITTGFDFNCHYLVLPSGNYLAISNELLLTVPTKAICLNKRKDFTPVQVVDSRWNNARQSDNMTAVACQPPYCYFRNSTTN... | 3.1.1.53 | null | fusion of virus membrane with host plasma membrane [GO:0019064]; negative regulation of immune system process [GO:0002683]; receptor-mediated virion attachment to host cell [GO:0046813] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | host cell surface receptor binding [GO:0046789]; identical protein binding [GO:0042802]; protein homodimerization activity [GO:0042803]; sialate 4-O-acetylesterase activity [GO:0106331]; sialate 9-O-acetylesterase activity [GO:0106330]; sialate O-acetylesterase activity [GO:0001681]; signaling receptor binding [GO:0005... | PF03996;PF02710; | null | Influenza type C/coronaviruses hemagglutinin-esterase family | PTM: N-glycosylated in the host RER. {ECO:0000255|HAMAP-Rule:MF_04207, ECO:0000269|PubMed:18550812}. | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04207}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04207}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04207}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04207}. Note=In infected cells becomes incorporated into th... | CATALYTIC ACTIVITY: Reaction=H2O + N-acetyl-9-O-acetylneuraminate = acetate + H(+) + N-acetylneuraminate; Xref=Rhea:RHEA:22600, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28999, ChEBI:CHEBI:30089, ChEBI:CHEBI:35418; EC=3.1.1.53; Evidence={ECO:0000255|HAMAP-Rule:MF_04207, ECO:0000269|PubMed:18550812}; CATALYTIC A... | null | null | null | null | FUNCTION: Structural protein that makes short spikes at the surface of the virus. Contains receptor binding and receptor-destroying activities. Mediates de-O-acetylation of N-acetyl-4-O-acetylneuraminic acid, which is probably the receptor determinant recognized by the virus on the surface of erythrocytes and susceptib... | Bovine coronavirus (strain Mebus) (BCoV) (BCV) |
P15777 | SPIKE_CVBM | MFLILLISLPMAFAVIGDLKCTTVSINDVDTGAPSISTDIVDVTNGLGTYYVLDRVYLNTTLLLNGYYPTSGSTYRNMALKGTLLLSRLWFKPPFLSDFINGIFAKVKNTKVIKKGVMYSEFPAITIGSTFVNTSYSVVVQPHTTNLDNKLQGLLEISVCQYTMCEYPHTICHPNLGNKRVELWHWDTGVVSCLYKRNFTYDVNADYLYFHFYQEGGTFYAYFTDTGVVTKFLFNVYLGTVLSHYYVLPLTCSSAMTLEYWVTPLTSKQYLLAFNQDGVIFNAVDCKSDFMSEIKCKTLSIAPSTGVYELNGYTVQPIAD... | null | null | endocytosis involved in viral entry into host cell [GO:0075509]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; receptor-mediated virion attachment to host cell [GO:0046813] | host cell endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0044173]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF16451;PF09408;PF19209;PF01601;PF19214; | 1.20.5.300;3.30.70.1840;2.60.120.960; | Betacoronaviruses spike protein family | PTM: Specific enzymatic cleavages in vivo yield mature proteins. The precursor is processed into S1 and S2 by host cell furin or another cellular protease to yield the mature S1 and S2 proteins. Additionally, a second cleavage leads to the release of a fusion peptide after viral attachment to host cell receptor. {ECO:0... | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099}. Host endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000255|HAMAP-Rule:MF_04099}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04099}. Hos... | null | null | null | null | null | FUNCTION: [Spike protein S1]: Attaches the virion to the cell membrane by interacting with host receptor, initiating the infection. {ECO:0000255|HAMAP-Rule:MF_04099}.; FUNCTION: [Spike protein S2]: Mediates fusion of the virion and cellular membranes by acting as a class I viral fusion protein. Under the current model,... | Bovine coronavirus (strain Mebus) (BCoV) (BCV) |
P15790 | CSK21_YEAST | MKCRVWSEARVYTNINKQRTEEYWDYENTVIDWSTNTKDYEIENKVGRGKYSEVFQGVKLDSKVKIVIKMLKPVKKKKIKREIKILTDLSNEKVPPTTLPFQKDQYYTNQKEDVLKFIRPYIFDQPHNGHANIIHLFDIIKDPISKTPALVFEYVDNVDFRILYPKLTDLEIRFYMFELLKALDYCHSMGIMHRDVKPHNVMIDHKNKKLRLIDWGLAEFYHVNMEYNVRVASRFFKGPELLVDYRMYDYSLDLWSFGTMLASMIFKREPFFHGTSNTDQLVKIVKVLGTSDFEKYLLKYEITLPREFYDMDQYIRKPWH... | 2.7.11.1 | null | DNA damage response [GO:0006974]; donor selection [GO:0007535]; maturation of SSU-rRNA [GO:0030490]; nucleolar large rRNA transcription by RNA polymerase I [GO:0042790]; phosphorylation [GO:0016310]; regulation of cell cycle [GO:0051726]; regulation of ribosomal protein gene transcription by RNA polymerase II [GO:00609... | CURI complex [GO:0032545]; cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein kinase CK2 complex [GO:0005956]; small-subunit processome [GO:0032040]; UTP-C complex [GO:0034456] | ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, CK2 subfamily | null | null | 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; Evidence={ECO:0000250|UniProtKB:P68400}; CATALYTI... | null | null | null | null | FUNCTION: Catalytic subunit of a constitutively active serine/threonine-protein kinase complex that phosphorylates a large number of substrates containing acidic residues C-terminal to the phosphorylated serine or threonine (By similarity). Phosphorylates YTA7 during S-phase to promote transcription of histones (PubMed... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P15791 | KCC2D_RAT | MASTTTCTRFTDEYQLFEELGKGAFSVVRRCMKIPTGQEYAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFDLVTGGELFEDIVAREYYSEADASHCIQQILESVNHCHLNGIVHRDLKPENLLLASKSKGAAVKLADFGLAIEVQGDQQAWFGFAGTPGYLSPEVLRKDPYGKPVDMWACGVILYILLVGYPPFWDEDQHRLYQQIKAGAYDFPSPEWDTVTPEAKDLINKMLTINPAKRITASEALKHPWICQRSTVASMMHRQETVDCLKKFNARRKLKGAILTTMLATRNFSAAKSL... | 2.7.11.17 | null | calcium ion transport [GO:0006816]; cardiac muscle cell contraction [GO:0086003]; cardiac muscle contraction [GO:0060048]; cell growth involved in cardiac muscle cell development [GO:0061049]; endoplasmic reticulum calcium ion homeostasis [GO:0032469]; G1/S transition of mitotic cell cycle [GO:0000082]; intracellular p... | axon initial segment [GO:0043194]; calcium- and calmodulin-dependent protein kinase complex [GO:0005954]; cytoplasm [GO:0005737]; intercalated disc [GO:0014704]; neuromuscular junction [GO:0031594]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; perinuclear region of cytoplasm [G... | ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]; identical protein binding [GO:0042802]; nitric-oxide synthase binding [GO:0050998]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; protein serine kinase activity [... | PF08332;PF00069; | 3.10.450.50;6.10.140.620;1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family, CaMK subfamily | PTM: Autophosphorylation of Thr-287 following activation by Ca(2+)/calmodulin. Phosphorylation of Thr-287 locks the kinase into an activated state (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane, sarcolemma {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Sarcoplasmic reticulum membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform Delta 1]: Nucleus. | 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=2.7.11.17; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: Calcium/calmodulin-dependent protein kinase involved in the regulation of Ca(2+) homeostatis and excitation-contraction coupling (ECC) in heart by targeting ion channels, transporters and accessory proteins involved in Ca(2+) influx into the myocyte, Ca(2+) release from the sarcoplasmic reticulum (SR), SR Ca(... | Rattus norvegicus (Rat) |
P15797 | E13B_TOBAC | MSTSSHKHNTPQMAAITLLGLLLVASSIDIAGAQSIGVCYGMLGNNLPNHWEVIQLYKSRNIGRLRLYDPNHGALQALKGSNIEVMLGLPNSDVKHIASGMEHARWWVQKNVKDFWPDVKIKYIAVGNEISPVTGTSYLTSFLTPAMVNIYKAIGEAGLGNNIKVSTSVDMTLIGNSYPPSQGSFRNDARWFTDPIVGFLRDTRAPLLVNIYPYFSYSGNPGQISLPYSLFTAPNVVVQDGSRQYRNLFDAMLDSVYAALERSGGASVGIVVSESGWPSAGAFGATYDNAATYLRNLIQHAKEGSPRKPGPIETYIFAMF... | 3.2.1.39 | null | carbohydrate metabolic process [GO:0005975]; defense response [GO:0006952] | vacuole [GO:0005773] | glucan endo-1,3-beta-D-glucosidase activity [GO:0042973] | PF00332; | 3.20.20.80; | Glycosyl hydrolase 17 family | null | SUBCELLULAR LOCATION: Vacuole. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans.; EC=3.2.1.39; | null | null | null | null | FUNCTION: Implicated in the defense of plants against pathogens. | Nicotiana tabacum (Common tobacco) |
P15800 | LAMB2_RAT | MEWASGKPGRGRQGQPVPWELRLGLLLSVLAATLAQVPSLDVPGCSRGSCYPATGDLLVGRADRLTASSTCGLHSPQPYCIVSHLQDEKKCFLCDSRRPFSARDNPNSHRIQNVVTSFAPQRRTAWWQSENGVPMVTIQLDLEAEFHFTHLIMTFKTFRPAAMLVERSADFGRTWRVYRYFSYDCGADFPGIPLAPPRRWDDVVCESRYSEIEPSTEGEVIYRVLDPAIPIPDPYSSRIQNLLKITNLRVNLTRLHTLGDNLLDPRREIREKYYYALYELVIRGNCFCYGHASQCAPAPGAPAHAEGMVHGACICKHNTR... | null | null | animal organ morphogenesis [GO:0009887]; astrocyte development [GO:0014002]; axon extension involved in regeneration [GO:0048677]; axon guidance [GO:0007411]; basement membrane assembly [GO:0070831]; cell migration [GO:0016477]; cell morphogenesis [GO:0000902]; metanephric glomerular basement membrane development [GO:0... | basement membrane [GO:0005604]; laminin complex [GO:0043256]; laminin-3 complex [GO:0005608]; neuromuscular junction [GO:0031594]; synapse [GO:0045202]; synaptic cleft [GO:0043083] | integrin binding [GO:0005178]; structural constituent of synapse-associated extracellular matrix [GO:0150043] | PF00053;PF21199;PF00055; | 2.60.120.260;2.10.25.10;2.170.300.10; | null | null | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. | null | null | null | null | null | FUNCTION: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. | Rattus norvegicus (Rat) |
P15801 | DPOG_YEAST | MTKLMVRSECMLRMVRRRPLRVQFCARWFSTKKNTAEAPRINPVGIQYLGESLQRQVFGSCGGKDEVEQSDKLMELSKKSLKDHGLWGKKTLITDPISFPLPPLQGRSLDEHFQKIGRFNSEPYKSFCEDKFTEMVARPAEWLRKPGWVKYVPGMAPVEVAYPDEELVVFDVETLYNVSDYPTLATALSSTAWYLWCSPFICGGDDPAALIPLNTLNKEQVIIGHNVAYDRARVLEEYNFRDSKAFFLDTQSLHIASFGLCSRQRPMFMKNNKKKEAEVESEVHPEISIEDYDDPWLNVSALNSLKDVAKFHCKIDLDKT... | 2.7.7.7 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; | mitochondrial DNA catabolic process [GO:0032043]; mitochondrial DNA replication [GO:0006264]; mitochondrial genome maintenance [GO:0000002] | gamma DNA polymerase complex [GO:0005760]; mitochondrion [GO:0005739] | 3'-5' exonuclease activity [GO:0008408]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887] | PF00476;PF18136; | 3.30.420.390;3.30.70.370;1.10.150.20; | DNA polymerase type-A family | null | SUBCELLULAR LOCATION: Mitochondrion. | 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; | null | null | null | null | FUNCTION: Involved in the replication of mitochondrial DNA. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P15802 | AATA_PENCH | MLHILCQGTPFEIGYEHGSAAKAVIARSIDFAVDLIRGKTKKTDEELKQVLSQLGRVIEERWPKYYEEIRGIAKGAERDVSEIVMLNTRTEFAYGLKAARDGCTTAYCQLPNGALQGQNWDFFSATKENLIRLTIRQAGLPTIKFITEAGIIGKVGFNSAGVAVNYNALHLQGLRPTGVPSHIALRIALESTSPSQAYDRIVEQGGMAASAFIMVGNGHEAFGLEFSPTSIRKQVLDANGRMVHTNHCLLQHGKNEKELDPLPDSWNRHQRMEFLLDGFDGTKQAFAQLWADEDNYPFSICRAYEEGKSRGATLFNIIYD... | 2.3.1.164 | null | penicillin biosynthetic process [GO:0042318] | peroxisomal matrix [GO:0005782] | acyl coenzyme A: isopenicillin N acyltransferase activity [GO:0102920]; isopenicillin-N N-acyltransferase activity [GO:0050640] | PF03417; | 1.10.10.2120; | Peptidase C45 family | PTM: The pre-AAT protein is synthesized as 40 kDa precursor which is then self-processed into an 11 kDa (protein A) and a 29 kDa (protein B). The B protein carries AAT activity. {ECO:0000269|PubMed:18439860, ECO:0000269|PubMed:20223213, ECO:0000269|PubMed:2120195, ECO:0000269|PubMed:8396910}. | SUBCELLULAR LOCATION: Peroxisome matrix {ECO:0000269|PubMed:18439860}. Note=The unprocessed preprotein is translocated inside peroxisomes and regulates its self-processing. {ECO:0000269|PubMed:18439860}. | CATALYTIC ACTIVITY: Reaction=H2O + isopenicillin N + phenylacetyl-CoA = CoA + H(+) + L-2-aminoadipate + penicillin G; Xref=Rhea:RHEA:20720, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:51354, ChEBI:CHEBI:57287, ChEBI:CHEBI:57390, ChEBI:CHEBI:58399, ChEBI:CHEBI:58672; EC=2.3.1.164; Evidence={ECO:0000269|PubMed:1368... | null | PATHWAY: Antibiotic biosynthesis; penicillin G biosynthesis; penicillin G from L-alpha-aminoadipate and L-cysteine and L-valine: step 3/3. {ECO:0000269|PubMed:1368505, ECO:0000269|PubMed:2110531, ECO:0000269|PubMed:2120195}. | null | null | FUNCTION: Isopenicillin-N N-acyltransferase; part of the gene cluster that mediates the biosynthesis of penicillin, the world's most important antibiotic (PubMed:1368505, PubMed:2110531, PubMed:2120195). AatA catalyzes the exchange of the alpha-aminoadipyl side chain of isopenicillin N for phenylacetic acid to yield pe... | Penicillium chrysogenum (Penicillium notatum) |
P15804 | CAPP3_SORBI | MASERHHSIDAQLRALAPGKVSEELIQYDALLVDRFLDILQDLHGPSLREFVQECYEVSADYEGKKDTSKLGELGAKLTGLAPADAILVASSILHMLNLANLAEEVELAHRRRNSKLKHGDFSDEGSATTESDIEETLKRLVSLGKTPAEVFEALKNQSVDLVFTAHPTQSARRSLLQKNARIRNCLTQLSAKDVTVEDKKELDEALHREIQAAFRTDEIRRAQPTPQDEMRYGMSYIHETVWNGVPKFLRRVDTALKNIGINERLPYDVPLIKFCSWMGGDRDGNPRVTPEVTRDVCLLSRMMAANLYINQVEDLMFEL... | 4.1.1.31 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | carbon fixation [GO:0015977]; leaf development [GO:0048366]; photosynthesis [GO:0015979]; tricarboxylic acid cycle [GO:0006099] | apoplast [GO:0048046]; chloroplast [GO:0009507]; cytosol [GO:0005829] | phosphoenolpyruvate carboxylase activity [GO:0008964] | PF00311; | 1.20.1440.90; | PEPCase type 1 family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=oxaloacetate + phosphate = hydrogencarbonate + phosphoenolpyruvate; Xref=Rhea:RHEA:28370, ChEBI:CHEBI:16452, ChEBI:CHEBI:17544, ChEBI:CHEBI:43474, ChEBI:CHEBI:58702; EC=4.1.1.31; | null | PATHWAY: Photosynthesis; C4 acid pathway. | null | null | FUNCTION: Through the carboxylation of phosphoenolpyruvate (PEP) it forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle. | Sorghum bicolor (Sorghum) (Sorghum vulgare) |
P15806 | TFE2_MOUSE | MMNQSQRMAPVGSDKELSDLLDFSMMFPLPVANGKSRPASLGGTQFAGSGLEDRPSSGSWGSSDQNSSSFDPSRTYSEGAHFSDSHSSLPPSTFLGAGLGGKGSERNAYATFGRDTSVGTLSQAGFLPGELSLSSPGPLSPSGIKSSSQYYPSFPSNPRRRAADGGLDTQPKKVRKVPPGLPSSVYPPSSGDSYSRDAAAYPSAKTPSSAYPSPFYVADGSLHPSAELWSTPSQVGFGPMLGDGSSPLPLAPGSSSVGSGTFGGLQQQDRMGYQLHGSEVNGSLPAVSSFSAAPGTYSGTSGHTPPVSGAAAESLLGTRG... | null | null | B cell lineage commitment [GO:0002326]; cell development [GO:0048468]; chromatin remodeling [GO:0006338]; erythrocyte differentiation [GO:0030218]; gastrulation [GO:0007369]; gene expression [GO:0010467]; immunoglobulin V(D)J recombination [GO:0033152]; lymphocyte differentiation [GO:0030098]; natural killer cell diffe... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleosome [GO:0000786]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; RNA polymerase II transcription regulator complex [GO:0090575]; transcription regulator complex [GO:0005667] | bHLH transcription factor binding [GO:0043425]; chromatin binding [GO:0003682]; cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-b... | PF00010; | 4.10.280.10; | null | PTM: Phosphorylated following NGF stimulation. {ECO:0000250}.; PTM: Undergoes Notch-induced ubiquitination and subsequent proteasomal degradation which is mediated by ASB1 or ASB2, the substrate-recognition components of probable ECS E3 ubiquitin-protein ligase complexes. {ECO:0000250|UniProtKB:P15923}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12200424}. | null | null | null | null | null | FUNCTION: Transcriptional regulator involved in the initiation of neuronal differentiation and mesenchymal to epithelial transition (PubMed:15226298, PubMed:18214987). Heterodimers between TCF3 and tissue-specific basic helix-loop-helix (bHLH) proteins play major roles in determining tissue-specific cell fate during em... | Mus musculus (Mouse) |
P15807 | MET8_YEAST | MVKSLQLAHQLKDKKILLIGGGEVGLTRLYKLIPTGCKLTLVSPDLHKSIIPKFGKFIQNEDQPDYREDAKRFINPNWDPTKNEIYEYIRSDFKDEYLDLEDENDAWYIIMTCIPDHPESARIYHLCKERFGKQQLVNVADKPDLCDFYFGANLEIGDRLQILISTNGLSPRFGALVRDEIRNLFTQMGDLALEDAVVKLGELRRGIRLLAPDDKDVKYRMDWARRCTDLFGIQHCHNIDVKRLLDLFKVMFQEQNCSLQFPPRERLLSEYCSS | 1.3.1.76; 4.99.1.4 | null | siroheme biosynthetic process [GO:0019354]; sulfate assimilation [GO:0000103] | null | ferrochelatase activity [GO:0004325]; precorrin-2 dehydrogenase activity [GO:0043115]; sirohydrochlorin ferrochelatase activity [GO:0051266] | PF13241;PF14823;PF14824; | 3.40.50.720; | Precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family, MET8 subfamily | null | null | CATALYTIC ACTIVITY: Reaction=NAD(+) + precorrin-2 = 2 H(+) + NADH + sirohydrochlorin; Xref=Rhea:RHEA:15613, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:58351, ChEBI:CHEBI:58827; EC=1.3.1.76; Evidence={ECO:0000269|PubMed:11980703}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15614; Evid... | null | PATHWAY: Porphyrin-containing compound metabolism; siroheme biosynthesis; siroheme from sirohydrochlorin: step 1/1.; PATHWAY: Porphyrin-containing compound metabolism; siroheme biosynthesis; sirohydrochlorin from precorrin-2: step 1/1. | null | null | FUNCTION: Catalyzes the conversion of precorrin-2 into siroheme. This reaction consist of the NAD-dependent oxidation of precorrin-2 into sirohydrochlorin and its subsequent ferrochelation into siroheme. {ECO:0000269|PubMed:10051442}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P15812 | CD1E_HUMAN | MLLLFLLFEGLCCPGENTAAPQALQSYHLAAEEQLSFRMLQTSSFANHSWAHSEGSGWLGDLQTHGWDTVLGTIRFLKPWSHGNFSKQELKNLQSLFQLYFHSFIQIVQASAGQFQLEYPFEIQILAGCRMNAPQIFLNMAYQGSDFLSFQGISWEPSPGAGIRAQNICKVLNRYLDIKEILQSLLGHTCPRFLAGLMEAGESELKRKVKPEAWLSCGPSPGPGRLQLVCHVSGFYPKPVWVMWMRGEQEQRGTQRGDVLPNADETWYLRATLDVAAGEAAGLSCRVKHSSLGGHDLIIHWGGYSIFLILICLTVIVTLV... | null | null | adaptive immune response [GO:0002250]; antigen processing and presentation, endogenous lipid antigen via MHC class Ib [GO:0048006]; antigen processing and presentation, exogenous lipid antigen via MHC class Ib [GO:0048007]; immune response [GO:0006955]; positive regulation of T cell mediated cytotoxicity [GO:0001916] | early endosome [GO:0005769]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; late endosome [GO:0005770]; lysosomal lumen [GO:0043202]; nucleolus [GO:0005730]; plasma membrane [GO:0005886] | endogenous lipid antigen binding [GO:0030883]; exogenous lipid antigen binding [GO:0030884]; lipopeptide binding [GO:0071723] | PF07654;PF16497; | 2.60.40.10;3.30.500.10; | null | PTM: Mono-ubiquitinated. {ECO:0000269|PubMed:18208508}.; PTM: Proteolytically cleaved in late endosomes to yield a soluble form. {ECO:0000269|PubMed:10948205, ECO:0000269|PubMed:18208508, ECO:0000269|PubMed:19196239}. | SUBCELLULAR LOCATION: [T-cell surface glycoprotein CD1e, membrane-associated]: Golgi apparatus membrane; Single-pass type I membrane protein. Early endosome. Late endosome. Note=Predominantly localized in the trans-Golgi network in immature dendritic cells, and as a cleaved, soluble protein in the lysosome lumen of mat... | null | null | null | null | null | FUNCTION: T-cell surface glycoprotein CD1e, soluble binds diacetylated lipids, including phosphatidyl inositides and diacylated sulfoglycolipids, and is required for the presentation of glycolipid antigens on the cell surface. The membrane-associated form is not active. {ECO:0000269|PubMed:10948205, ECO:0000269|PubMed:... | Homo sapiens (Human) |
P15813 | CD1D_HUMAN | MGCLLFLLLWALLQAWGSAEVPQRLFPLRCLQISSFANSSWTRTDGLAWLGELQTHSWSNDSDTVRSLKPWSQGTFSDQQWETLQHIFRVYRSSFTRDVKEFAKMLRLSYPLELQVSAGCEVHPGNASNNFFHVAFQGKDILSFQGTSWEPTQEAPLWVNLAIQVLNQDKWTRETVQWLLNGTCPQFVSGLLESGKSELKKQVKPKAWLSRGPSPGPGRLLLVCHVSGFYPKPVWVKWMRGEQEQQGTQPGDILPNADETWYLRATLDVVAGEAAGLSCRVKHSSLEGQDIVLYWGGSYTSMGLIALAVLACLLFLLIVG... | null | null | antigen processing and presentation, endogenous lipid antigen via MHC class Ib [GO:0048006]; antigen processing and presentation, exogenous lipid antigen via MHC class Ib [GO:0048007]; detection of bacterium [GO:0016045]; heterotypic cell-cell adhesion [GO:0034113]; immune response [GO:0006955]; innate immune response ... | basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; endosome membrane [GO:0010008]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lysosomal membrane [GO:0005765]; ... | beta-2-microglobulin binding [GO:0030881]; cell adhesion molecule binding [GO:0050839]; endogenous lipid antigen binding [GO:0030883]; exogenous lipid antigen binding [GO:0030884]; histone binding [GO:0042393]; lipid antigen binding [GO:0030882]; lipopeptide binding [GO:0071723] | PF07654;PF16497; | 2.60.40.10;3.30.500.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11927549, ECO:0000269|PubMed:17475845, ECO:0000269|PubMed:9973405}; Single-pass type I membrane protein {ECO:0000305|PubMed:9973405}. Basolateral cell membrane {ECO:0000269|PubMed:9973405}; Single-pass type I membrane protein {ECO:0000305|PubMed:9973405}. Endosome... | null | null | null | null | null | FUNCTION: Antigen-presenting protein that binds self and non-self glycolipids and presents them to T-cell receptors on natural killer T-cells. {ECO:0000269|PubMed:17475845}. | Homo sapiens (Human) |
P15814 | IGLL1_HUMAN | MRPGTGQGGLEAPGEPGPNLRQRWPLLLLGLAVVTHGLLRPTAASQSRALGPGAPGGSSRSSLRSRWGRFLLQRGSWTGPRCWPRGFQSKHNSVTHVFGSGTQLTVLSQPKATPSVTLFPPSSEELQANKATLVCLMNDFYPGILTVTWKADGTPITQGVEMTTPSKQSNNKYAASSYLSLTPEQWRSRRSYSCQVMHEGSTVEKTVAPAECS | null | null | immune response [GO:0006955]; immunoglobulin mediated immune response [GO:0016064] | endoplasmic reticulum [GO:0005783]; extracellular region [GO:0005576]; IgG immunoglobulin complex [GO:0071735]; membrane [GO:0016020] | antigen binding [GO:0003823] | PF07654; | 2.60.40.10; | null | null | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:P20764}. Secreted {ECO:0000269|PubMed:9419212}. Note=In pre-B cells, localizes predominantly to the endoplasmic reticulum. {ECO:0000250|UniProtKB:P20764}. | null | null | null | null | null | FUNCTION: Critical for B-cell development. {ECO:0000269|PubMed:9419212}. | Homo sapiens (Human) |
P15822 | ZEP1_HUMAN | MPRTKQIHPRNLRDKIEEAQKELNGAEVSKKEILQAGVKGTSESLKGVKRKKIVAENHLKKIPKSPLRNPLQAKHKQNTEESSFAVLHSASESHKKQNYIPVKNGKQFTKQNGETPGIIAEASKSEESVSPKKPLFLQQPSELRRWRSEGADPAKFSDLDEQCDSSSLSSKTRTDNSECISSHCGTTSPSYTNTAFDVLLKAMEPELSTLSQKGSPCAIKTEKLRPNKTARSPPKLKNSSMDAPNQTSQELVAESQSSCTSYTVHMSAAQKNEQGAMQSASHLYHQHEHFVPKSNQHNQQLPGCSGFTGSLTNLQNQENA... | null | null | BMP signaling pathway [GO:0030509]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357] | cytosol [GO:0005829]; mitochondrion [GO:0005739]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded... | PF00096; | 3.30.160.60; | null | null | SUBCELLULAR LOCATION: [Isoform 1]: Nucleus.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Nucleus.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm {ECO:0000269|Ref.2}. Nucleus {ECO:0000269|Ref.2}. | null | null | null | null | null | FUNCTION: This protein specifically binds to the DNA sequence 5'-GGGACTTTCC-3' which is found in the enhancer elements of numerous viral promoters such as those of SV40, CMV, or HIV-1. In addition, related sequences are found in the enhancer elements of a number of cellular promoters, including those of the class I MHC... | Homo sapiens (Human) |
P15823 | ADA1B_RAT | MNPDLDTGHNTSAPAHWGELKDDNFTGPNQTSSNSTLPQLDVTRAISVGLVLGAFILFAIVGNILVILSVACNRHLRTPTNYFIVNLAIADLLLSFTVLPFSATLEVLGYWVLGRIFCDIWAAVDVLCCTASILSLCAISIDRYIGVRYSLQYPTLVTRRKAILALLSVWVLSTVISIGPLLGWKEPAPNDDKECGVTEEPFYALFSSLGSFYIPLAVILVMYCRVYIVAKRTTKNLEAGVMKEMSNSKELTLRIHSKNFHEDTLSSTKAKGHNPRSSIAVKLFKFSREKKAAKTLGIVVGMFILCWLPFFIALPLGSLF... | null | null | adenylate cyclase-activating adrenergic receptor signaling pathway [GO:0071880]; adult heart development [GO:0007512]; behavioral response to cocaine [GO:0048148]; blood vessel remodeling [GO:0001974]; cell growth involved in cardiac muscle cell development [GO:0061049]; cell-cell signaling [GO:0007267]; glucose homeos... | caveola [GO:0005901]; cytoplasm [GO:0005737]; intercalated disc [GO:0014704]; membrane [GO:0016020]; nuclear membrane [GO:0031965]; nucleus [GO:0005634]; T-tubule [GO:0030315] | alpha1-adrenergic receptor activity [GO:0004937]; protein heterodimerization activity [GO:0046982] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family, Adrenergic receptor subfamily, ADRA1B sub-subfamily | null | SUBCELLULAR LOCATION: Nucleus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Cell membrane {ECO:0000250|UniProtKB:P35368}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P35368}. Membrane, caveola {ECO:0000250|UniProtKB:P35368}. Note=Location at the nuclear membrane faci... | null | null | null | null | null | FUNCTION: This alpha-adrenergic receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Its effect is mediated by G(q) and G(11) proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate phenylephrine (PE)-stimulated ERK signaling in cardiac myocy... | Rattus norvegicus (Rat) |
P15831 | ENV_HV2D2 | MAYFSSRLPIALLLIGISGFVCKQYVTVFYGIPAWRNATVPLICATTNRDTWGTVQCLPDNGDYTEIRLNITEAFDAWDNTVTQQAVDDVWRLFETSIKPCVKLTPLCVAMNCSKTETNPGNASSTTTTKPTTTSRGLKTINETDPCIKNDSCTGLGEEEIMQCNFSMTGLRRDELKQYKDTWYSEDLECNNTRKYTSRCYIRTCNTTIIQESCDKHYWDSLRFRYCAPPGFFLLRCNDTNYSGFMPNCSKVVASSCTRMMETQSSTWFGFNGTRAENRTYIYWHEKDNRTIISLNTYYNLSIHCKRPGNKTVVPIRTVS... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; suppression by virus of host tetherin activity [GO:0039587]; virion attachment to host cell [GO:0019062] | host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | structural molecule activity [GO:0005198] | PF00516;PF00517; | 1.10.287.210;2.170.40.20; | null | PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is heavily N-glycosylated and processed likely by host cell furin in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [... | SUBCELLULAR LOCATION: [Transmembrane protein gp41]: Virion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host endosome membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=It is p... | null | null | null | null | null | FUNCTION: The surface protein gp120 (SU) attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CXCR4 and/or CCR5. This peculiar 2 stage receptor-interaction strategy a... | Human immunodeficiency virus type 2 subtype B (isolate D205) (HIV-2) |
P15832 | GAG_HV2D2 | MGARGSVLSGKKTDELEKVRLRPGGKKKYMLKHVVWAVNELDRFGLAESLLESKEGCQKILKVLAPLVPTGSENLKSLFNIVCVIFCLHAEEKVKDTEEAKKIAQRHLAADTEKMPATNKPTAPPSGGNYPVQQLAGNYVHLPLSPRTLNAWVKLVEEKKFGAEVVPGFQALSEGCTPYDINQMLNCVGEHQAAMQIIREIINEEAADWDQQHPSPGPMPAGQLRDPRGSDIAGTTSTVEEQIQWMYRAQNPVPVGNIYRRWIQLGLQKCVRMYNPTNILDIKQGPKEPFQSYVDRFYKSLRAEQTDPAVKNWMTQTLLI... | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF00540;PF00607;PF19317;PF00098; | 1.10.1200.30;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10; | Primate lentivirus group gag polyprotein family | PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the viral protease yield mature proteins. {ECO:0000250|UniProtKB:P12493}.; PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association. {ECO:0000250|Uni... | SUBCELLULAR LOCATION: [Gag polyprotein]: Host cell membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P12493}. Note=These locations are probably linked to virus assembly sites. The main location is the cell membrane, but u... | null | null | null | null | null | FUNCTION: [Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 2 subtype B (isolate D205) (HIV-2) |
P15833 | POL_HV2D2 | MGARGSVLSGKKTDELEKVRLRPGGKKKYMLKHVVWAVNELDRFGLAESLLESKEGCQKILKVLAPLVPTGSENLKSLFNIVCVIFCLHAEEKVKDTEEAKKIAQRHLAADTEKMPATNKPTAPPSGGNYPVQQLAGNYVHLPLSPRTLNAWVKLVEEKKFGAEVVPGFQALSEGCTPYDINQMLNCVGEHQAAMQIIREIINEEAADWDQQHPSPGPMPAGQLRDPRGSDIAGTTSTVEEQIQWMYRAQNPVPVGNIYRRWIQLGLQKCVRMYNPTNILDIKQGPKEPFQSYVDRFYKSLRAEQTDPAVKNWMTQTLLI... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.13.2; 3.1.26.13; 3.4.23.47 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for reverse transcriptase polymerase activity. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is ... | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral genome integration into host DNA [GO:0044826]; viral pe... | host cell [GO:0043657]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; exoribonuclease H activity [GO:0004533]; lipid binding [GO:0008289]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity... | PF00540;PF00607;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06815;PF06817;PF00098; | 1.10.10.200;1.10.1200.30;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;1.10.150.90;2.30.30.10;3.30.420.10;1.20.5.760;4.10.60.10; | null | PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT ... | SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane; Lipid-anchor. Host endosome, host multivesicular body. Note=These locations are linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion asse... | CATALYTIC ACTIVITY: Reaction=Endopeptidase for which the P1 residue is preferably hydrophobic.; EC=3.4.23.47; Evidence={ECO:0000255|PROSITE-ProRule:PRU00275}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immun... | null | null | null | null | FUNCTION: [Gag-Pol polyprotein]: Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 2 subtype B (isolate D205) (HIV-2) |
P15848 | ARSB_HUMAN | MGPRGAASLPRGPGPRRLLLPVVLPLLLLLLLAPPGSGAGASRPPHLVFLLADDLGWNDVGFHGSRIRTPHLDALAAGGVLLDNYYTQPLCTPSRSQLLTGRYQIRTGLQHQIIWPCQPSCVPLDEKLLPQLLKEAGYTTHMVGKWHLGMYRKECLPTRRGFDTYFGYLLGSEDYYSHERCTLIDALNVTRCALDFRDGEEVATGYKNMYSTNIFTKRAIALITNHPPEKPLFLYLALQSVHEPLQVPEEYLKPYDFIQDKNRHHYAGMVSLMDEAVGNVTAALKSSGLWNNTVFIFSTDNGGQTLAGGNNWPLRGRKWS... | 3.1.6.12 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 1 Ca(2+) ion per subunit.; | autophagy [GO:0006914]; colon epithelial cell migration [GO:0061580]; lysosomal transport [GO:0007041]; lysosome organization [GO:0007040]; positive regulation of neuron projection development [GO:0010976]; regulation of epithelial cell migration [GO:0010632]; response to estrogen [GO:0043627]; response to methylmercur... | azurophil granule lumen [GO:0035578]; cell surface [GO:0009986]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; ficolin-1-rich granule lumen [GO:1904813]; lysosomal lumen [GO:0043202]; lysosome [GO:0005764] | arylsulfatase activity [GO:0004065]; metal ion binding [GO:0046872]; N-acetylgalactosamine-4-sulfatase activity [GO:0003943] | PF00884; | 3.30.1120.10;3.40.720.10; | Sulfatase family | PTM: The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity. This post-translational modification is severely defective in multiple sulfatase deficiency (MSD). {ECO:0000269|PubMed:76... | SUBCELLULAR LOCATION: Lysosome {ECO:0000250|UniProtKB:P50429}. Cell surface {ECO:0000250|UniProtKB:P50429}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of the 4-sulfate groups of the N-acetyl-D-galactosamine 4-sulfate units of chondroitin sulfate and dermatan sulfate.; EC=3.1.6.12; | null | null | null | null | FUNCTION: Removes sulfate groups from chondroitin-4-sulfate (C4S) and regulates its degradation (PubMed:19306108). Involved in the regulation of cell adhesion, cell migration and invasion in colonic epithelium (PubMed:19306108). In the central nervous system, is a regulator of neurite outgrowth and neuronal plasticity,... | Homo sapiens (Human) |
P15863 | PAX1_HUMAN | MKFTLGLGSRAWRVSWEGAAAAAAGPGAGGSALRCRAQRVSSPRLGRRGSRLSGALPLCLSRGGGGAQALPDCAGPSPGHPGHPGARQLAGPLAMEQTYGEVNQLGGVFVNGRPLPNAIRLRIVELAQLGIRPCDISRQLRVSHGCVSKILARYNETGSILPGAIGGSKPRVTTPNVVKHIRDYKQGDPGIFAWEIRDRLLADGVCDKYNVPSVSSISRILRNKIGSLAQPGPYEASKQPPSQPTLPYNHIYQYPYPSPVSPTGAKMGSHPGVPGTAGHVSIPRSWPSAHSVSNILGIRTFMEQTGALAGSEGTAYSPKM... | null | null | regulation of transcription by RNA polymerase II [GO:0006357]; skeletal system development [GO:0001501]; transcription by RNA polymerase II [GO:0006366] | chromatin [GO:0000785]; nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA binding [GO:1990837] | PF00292; | 1.10.10.10; | null | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: This protein is a transcriptional activator. It may play a role in the formation of segmented structures of the embryo. May play an important role in the normal development of the vertebral column (By similarity). {ECO:0000250}. | Homo sapiens (Human) |
P15864 | H12_MOUSE | MSEAAPAAPAAAPPAEKAPAKKKAAKKPAGVRRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGILVQTKGTGASGSFKLNKKAASGEAKPQAKKAGAAKAKKPAGAAKKPKKATGAATPKKAAKKTPKKAKKPAAAAVTKKVAKSPKKAKVTKPKKVKSASKAVKPKAAKPKVAKAKKVAAKKK | null | null | chromatin organization [GO:0006325]; chromosome condensation [GO:0030261]; negative regulation of DNA recombination [GO:0045910]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nucleosome assembly [GO:0006334]; regulation of transcription by RNA polymerase II [GO:0006357] | euchromatin [GO:0000791]; nucleosome [GO:0000786]; nucleus [GO:0005634] | DNA binding [GO:0003677]; double-stranded DNA binding [GO:0003690]; nucleosomal DNA binding [GO:0031492]; structural constituent of chromatin [GO:0030527] | PF00538; | 1.10.10.10; | Histone H1/H5 family | PTM: H1 histones are progressively phosphorylated during the cell cycle, becoming maximally phosphorylated during late G2 phase and M phase, and being dephosphorylated sharply thereafter. {ECO:0000250}.; PTM: Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic ... | SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Mainly localizes in euchromatin. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin rem... | Mus musculus (Mouse) |
P15865 | H14_RAT | MSETAPAAPAAPAPAEKTPIKKKARKAAGGAKRKASGPPVSELITKAVAASKERSGVSLAALKKALAAAGYDVEKNNSRIKLGLKSLVSKGTLVQTKGTGASGSFKLNKKAASGEAKPKAKKAGAAKAKKPAGAAKKPKKATGTATPKKSTKKTPKKAKKPAAAAGAKKAKSPKKAKATKAKKAPKSPAKARAVKPKAAKPKTSKPKAAKPKKTAAKKK | null | null | chromatin organization [GO:0006325]; chromosome condensation [GO:0030261]; negative regulation of DNA recombination [GO:0045910]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nucleosome assembly [GO:0006334]; regulation of transcription by RNA polymerase II [GO:0006357] | chromatin [GO:0000785]; heterochromatin [GO:0000792]; nucleosome [GO:0000786]; nucleus [GO:0005634] | ADP binding [GO:0043531]; AMP binding [GO:0016208]; ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; chromatin DNA binding [GO:0031490]; dATP binding [GO:0032564]; DNA binding [GO:0003677]; double-stranded DNA binding [GO:0003690]; GTP binding [GO:0005525]; histone deacetylase binding [GO:0042826]; nucleosom... | PF00538; | 1.10.10.10; | Histone H1/H5 family | PTM: H1 histones are progressively phosphorylated during the cell cycle, becoming maximally phosphorylated during late G2 phase and M phase, and being dephosphorylated sharply thereafter. {ECO:0000250|UniProtKB:P43275}.; PTM: Acetylated at Lys-26. Deacetylated at Lys-26 by SIRT1. {ECO:0000250|UniProtKB:P10412}.; PTM: C... | SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Mainly localizes in euchromatin. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin rem... | Rattus norvegicus (Rat) |
P15873 | PCNA_YEAST | MLEAKFEEASLFKRIIDGFKDCVQLVNFQCKEDGIIAQAVDDSRVLLVSLEIGVEAFQEYRCDHPVTLGMDLTSLSKILRCGNNTDTLTLIADNTPDSIILLFEDTKKDRIAEYSLKLMDIDADFLKIEELQYDSTLSLPSSEFSKIVRDLSQLSDSINIMITKETIKFVADGDIGSGSVIIKPFVDMEHPETSIKLEMDQPVDLTFGAKYLLDIIKGSSLSDRVGIRLSSEAPALFQFDLKSGFLQFFLAPKFNDEE | null | null | error-free translesion synthesis [GO:0070987]; establishment of mitotic sister chromatid cohesion [GO:0034087]; lagging strand elongation [GO:0006273]; leading strand elongation [GO:0006272]; maintenance of DNA trinucleotide repeats [GO:0035753]; meiotic mismatch repair [GO:0000710]; mismatch repair [GO:0006298]; mitot... | chromosome, telomeric region [GO:0000781]; nucleus [GO:0005634]; PCNA complex [GO:0043626]; replication fork [GO:0005657] | DNA binding [GO:0003677]; DNA polymerase processivity factor activity [GO:0030337]; identical protein binding [GO:0042802] | PF02747;PF00705; | 3.10.150.10; | PCNA family | PTM: Sumoylated on Lys-164, and to a lesser extent on Lys-127 by the UBC9/SIZ1 complex during S-phase; which impairs ubiquitination and function in DNA repair. {ECO:0000269|PubMed:12226657, ECO:0000269|PubMed:15166219, ECO:0000269|PubMed:15542864}.; PTM: Monoubiquitinated on Lys-164 by the UBC2/RAD18 complex upon DNA d... | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: This protein is an auxiliary protein of DNA polymerase delta and is involved in the control of eukaryotic DNA replication by increasing the polymerase's processibility during elongation of the leading strand. Involved in DNA repair. {ECO:0000269|PubMed:11545742, ECO:0000269|PubMed:12226657}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P15875 | LEU1_SALTY | MSQQVIIFDTTLRDGEQALQASLSAKEKLQIALALERMGVDVMEVGFPVSSPGDFESVQTIARTIKNSRVCALARCVEKDIDVAAQALKVADAFRIHTFIATSPMHIATKLRSTLDEVIERAVYMVKRARNYTDDVEFSCEDAGRTPVDDLARVVEAAINAGARTINIPDTVGYTMPFEFAGIISGLYERVPNIDKAIISVHTHDDLGIAVGNSLAAVHAGARQVEGAMNGIGERAGNCALEEVIMAIKVRKDIMNVHTNINHHEIWRTSQTVSQICNMPIPANKAIVGSGAFAHSSGIHQDGVLKNRENYEIMTPESIG... | 2.3.3.13 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_01025}; | amino acid biosynthetic process [GO:0008652]; coenzyme B biosynthetic process [GO:0019298]; leucine biosynthetic process [GO:0009098] | cytosol [GO:0005829] | 2-isopropylmalate synthase activity [GO:0003852]; acetyl-CoA C-acetyltransferase activity [GO:0003985]; manganese ion binding [GO:0030145] | PF00682;PF08502; | 1.10.238.260;3.30.160.270;3.20.20.70; | Alpha-IPM synthase/homocitrate synthase family, LeuA type 1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01025}. | CATALYTIC ACTIVITY: Reaction=3-methyl-2-oxobutanoate + acetyl-CoA + H2O = (2S)-2-isopropylmalate + CoA + H(+); Xref=Rhea:RHEA:21524, ChEBI:CHEBI:1178, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.13; Evidence={ECO:0000255|HAMAP-Rule:MF_01025, ECO:0000269|PubMed... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.06 mM for 3-methyl-2-oxobutanoate {ECO:0000269|PubMed:4976555}; KM=1.1 mM for 2-oxobutanoate {ECO:0000269|PubMed:4976555}; KM=10 mM for pyruvate {ECO:0000269|PubMed:4976555}; KM=0.2 mM for acetyl-CoA {ECO:0000269|PubMed:4976555}; | PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 1/4. {ECO:0000255|HAMAP-Rule:MF_01025}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:4976555}; | null | FUNCTION: Catalyzes the condensation of the acetyl group of acetyl-CoA with 3-methyl-2-oxobutanoate (2-ketoisovalerate) to form 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate). {ECO:0000255|HAMAP-Rule:MF_01025, ECO:0000269|PubMed:4976555, ECO:0000269|PubMed:6195343}. | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
P15877 | DHG_ECOLI | MAINNTGSRRLLVTLTALFAALCGLYLLIGGGWLVAIGGSWYYPIAGLVMLGVAWMLWRSKRAALWLYAALLLGTMIWGVWEVGFDFWALTPRSDILVFFGIWLILPFVWRRLVIPASGAVAALVVALLISGGILTWAGFNDPQEINGTLSADATPAEAISPVADQDWPAYGRNQEGQRFSPLKQINADNVHNLKEAWVFRTGDVKQPNDPGEITNEVTPIKVGDTLYLCTAHQRLFALDAASGKEKWHYDPELKTNESFQHVTCRGVSYHEAKAETASPEVMADCPRRIILPVNDGRLIAINAENGKLCETFANKGVLN... | 1.1.5.2 | COFACTOR: Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442; | null | membrane [GO:0016020]; outer membrane-bounded periplasmic space [GO:0030288]; plasma membrane [GO:0005886] | magnesium ion binding [GO:0000287]; pyrroloquinoline quinone binding [GO:0070968]; quinoprotein glucose dehydrogenase activity [GO:0008876]; ubiquinone binding [GO:0048039] | PF01011; | 2.140.10.10; | Bacterial PQQ dehydrogenase family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:16079137}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:16079137}; Periplasmic side {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:16079137}. | CATALYTIC ACTIVITY: Reaction=a ubiquinone + D-glucose = a ubiquinol + D-glucono-1,5-lactone; Xref=Rhea:RHEA:22152, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:4167, ChEBI:CHEBI:16217, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976; EC=1.1.5.2; Evidence={ECO:0000269|PubMed:8509415}; PhysiologicalDirection=left-to-right;... | null | null | null | null | FUNCTION: GDH is probably involved in energy conservation rather than in sugar metabolism. {ECO:0000305|PubMed:8509415}. | Escherichia coli (strain K12) |
P15879 | ARC3_CBDP | MKGLRKSILCLVLSAGVIAPVTSGMIQSPQKCYAYSINQKAYSNTYQEFTNIDQAKAWGNAQYKKYGLSKSEKEAIVSYTKSASEINGKLRQNKGVINGFPSNLIKQVELLDKSFNKMKTPENIMLFRGDDPAYLGTEFQNTLLNSNGTINKTAFEKAKAKFLNKDRLEYGYISTSLMNVSQFAGRPIITKFKVAKGSKAGYIDPISAFAGQLEMLLPRHSTYHIDDMRLSSDGKQIIITATMMGTAINPK | 2.4.2.- | null | null | extracellular region [GO:0005576] | NAD+-protein ADP-ribosyltransferase activity [GO:1990404]; nucleotidyltransferase activity [GO:0016779] | PF03496; | null | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2108433}. | CATALYTIC ACTIVITY: Reaction=L-asparaginyl-[protein] + NAD(+) = H(+) + N(4)-(ADP-D-ribosyl)-L-asparaginyl-[protein] + nicotinamide; Xref=Rhea:RHEA:58228, Rhea:RHEA-COMP:12804, Rhea:RHEA-COMP:15090, ChEBI:CHEBI:15378, ChEBI:CHEBI:17154, ChEBI:CHEBI:50347, ChEBI:CHEBI:57540, ChEBI:CHEBI:142555; Evidence={ECO:0000269|PubM... | null | null | null | null | FUNCTION: ADP-ribosylates eukaryotic Rho and Rac proteins on an asparagine residue. {ECO:0000269|PubMed:11114250, ECO:0000269|PubMed:12029083, ECO:0000269|PubMed:15272191, ECO:0000269|PubMed:16177825}. | Clostridium botulinum D phage (Clostridium botulinum D bacteriophage) |
P15880 | RS2_HUMAN | MADDAGAAGGPGGPGGPGMGNRGGFRGGFGSGIRGRGRGRGRGRGRGRGARGGKAEDKEWMPVTKLGRLVKDMKIKSLEEIYLFSLPIKESEIIDFFLGASLKDEVLKIMPVQKQTRAGQRTRFKAFVAIGDYNGHVGLGVKCSKEVATAIRGAIILAKLSIVPVRRGYWGNKIGKPHTVPCKVTGRCGSVLVRLIPAPRGTGIVSAPVPKKLLMMAGIDDCYTSARGCTATLGNFAKATFDAISKTYSYLTPDLWKETVFTKSPYQEFTDHLVKTHTRVSVQRTQAPAVATT | null | null | cytoplasmic translation [GO:0002181]; positive regulation of ubiquitin-protein transferase activity [GO:0051443]; translation [GO:0006412] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic ribosome [GO:0022626]; cytosolic small ribosomal subunit [GO:0022627]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | cadherin binding [GO:0045296]; enzyme binding [GO:0019899]; fibroblast growth factor binding [GO:0017134]; mRNA binding [GO:0003729]; RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735] | PF00333;PF03719; | 3.30.160.20;3.30.230.10; | Universal ribosomal protein uS5 family | PTM: Citrullinated by PADI4 in the Arg/Gly-rich region. {ECO:0000269|PubMed:21584310}.; PTM: Asymmetric arginine dimethylation by PRMT3 occurs at multiple sites in the Arg/Gly-rich region. {ECO:0000269|PubMed:15473865}.; PTM: Monoubiquitinated at Lys-54 and Lys-58 by RNF10 when a ribosome has stalled during translation... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399, ECO:0000269|PubMed:30530495}. Nucleus, nucleolus {ECO:0000269|PubMed:30530495}. Note=Probably localized to nucleolus and cytoplasm in complex with ZNF277. {ECO:0000269|PubMed:30530495}. | null | null | null | null | null | FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399). The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules (PubMed:23636399)... | Homo sapiens (Human) |
P15882 | CHIN_HUMAN | MALTLFDTDEYRPPVWKSYLYQLQQEAPHPRRITCTCEVENRPKYYGREFHGMISREAADQLLIVAEGSYLIRESQRQPGTYTLALRFGSQTRNFRLYYDGKHFVGEKRFESIHDLVTDGLITLYIETKAAEYIAKMTINPIYEHVGYTTLNREPAYKKHMPVLKETHDERDSTGQDGVSEKRLTSLVRRATLKENEQIPKYEKIHNFKVHTFRGPHWCEYCANFMWGLIAQGVKCADCGLNVHKQCSKMVPNDCKPDLKHVKKVYSCDLTTLVKAHTTKRPMVVDMCIREIESRGLNSEGLYRVSGFSDLIEDVKMAFD... | null | null | ephrin receptor signaling pathway [GO:0048013]; motor neuron axon guidance [GO:0008045]; regulation of axonogenesis [GO:0050770]; regulation of small GTPase mediated signal transduction [GO:0051056] | cytosol [GO:0005829] | ephrin receptor binding [GO:0046875]; GTPase activator activity [GO:0005096]; metal ion binding [GO:0046872] | PF00130;PF00620;PF00017; | 3.30.60.20;1.10.555.10;3.30.505.10; | null | PTM: Phosphorylated. Phosphorylation is EPHA4 kinase activity-dependent (By similarity). {ECO:0000250}. | null | null | null | null | null | null | FUNCTION: GTPase-activating protein for p21-rac and a phorbol ester receptor. Involved in the assembly of neuronal locomotor circuits as a direct effector of EPHA4 in axon guidance. | Homo sapiens (Human) |
P15884 | ITF2_HUMAN | MHHQQRMAALGTDKELSDLLDFSAMFSPPVSSGKNGPTSLASGHFTGSNVEDRSSSGSWGNGGHPSPSRNYGDGTPYDHMTSRDLGSHDNLSPPFVNSRIQSKTERGSYSSYGRESNLQGCHQQSLLGGDMDMGNPGTLSPTKPGSQYYQYSSNNPRRRPLHSSAMEVQTKKVRKVPPGLPSSVYAPSASTADYNRDSPGYPSSKPATSTFPSSFFMQDGHHSSDPWSSSSGMNQPGYAGMLGNSSHIPQSSSYCSLHPHERLSYPSHSSADINSSLPPMSTFHRSGTNHYSTSSCTPPANGTDSIMANRGSGAAGSSQT... | null | null | cell differentiation [GO:0030154]; nervous system development [GO:0007399]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of neuron differentiation [GO:0045666]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein-DNA complex assembly [GO:0065004]; regu... | beta-catenin-TCF complex [GO:1990907]; beta-catenin-TCF7L2 complex [GO:0070369]; chromatin [GO:0000785]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | beta-catenin binding [GO:0008013]; 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]; E-box binding [GO:0070888]; iden... | PF00010; | 4.10.280.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:22777675}. | null | null | null | null | null | FUNCTION: Transcription factor that binds to the immunoglobulin enhancer Mu-E5/KE5-motif. Involved in the initiation of neuronal differentiation. Activates transcription by binding to the E box (5'-CANNTG-3'). Binds to the E-box present in the somatostatin receptor 2 initiator element (SSTR2-INR) to activate transcript... | Homo sapiens (Human) |
P15891 | ABP1_YEAST | MALEPIDYTTHSREIDAEYLKIVRGSDPDTTWLIISPNAKKEYEPESTGSSFHDFLQLFDETKVQYGLARVSPPGSDVEKIIIIGWCPDSAPLKTRASFAANFAAVANNLFKGYHVQVTARDEDDLDENELLMKISNAAGARYSIQTSSKQQGKASTPPVKKSFTPSKSPAPVSKKEPVKTPSPAPAAKISSRVNDNNDDDDWNEPELKERDFDQAPLKPNQSSYKPIGKIDLQKVIAEEKAKEDPRLVQKPTAAGSKIDPSSDIANLKNESKLKRDSEFNSFLGTTKPPSMTESSLKNDDDKVIKGFRNEKSPAQLWAE... | null | null | actin cortical patch assembly [GO:0000147]; barbed-end actin filament capping [GO:0051016]; positive regulation of Arp2/3 complex-mediated actin nucleation [GO:2000601]; positive regulation of axon extension [GO:0045773]; postsynaptic actin cytoskeleton organization [GO:0098974]; protein localization to actin cortical ... | actin cortical patch [GO:0030479]; actin filament [GO:0005884]; cell cortex [GO:0005938]; cortical actin cytoskeleton [GO:0030864]; cytoplasm [GO:0005737]; lamellipodium [GO:0030027]; mating projection tip [GO:0043332]; site of polarized growth [GO:0030427] | actin filament binding [GO:0051015] | PF00241;PF00018; | 3.40.20.10;2.30.30.40; | ABP1 family | PTM: The actin depolymerizing factor homology (ADF) domain mediates actin filament binding. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch {ECO:0000269|PubMed:11950888, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:15872087}. Note=Cortical actin patches. | null | null | null | null | null | FUNCTION: Regulates ARP2/3 complex-mediated actin assembly. Recruits ARP2/3 complex to sides of preexisting actin filaments, which may promote nucleation or stabilization of filament branches. Binds to actin filaments, but not actin monomers. Actin binding is required for ARP2/3 complex activation. May also have a role... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P15907 | SIAT1_HUMAN | MIHTNLKKKFSCCVLVFLLFAVICVWKEKKKGSYYDSFKLQTKEFQVLKSLGKLAMGSDSQSVSSSSTQDPHRGRQTLGSLRGLAKAKPEASFQVWNKDSSSKNLIPRLQKIWKNYLSMNKYKVSYKGPGPGIKFSAEALRCHLRDHVNVSMVEVTDFPFNTSEWEGYLPKESIRTKAGPWGRCAVVSSAGSLKSSQLGREIDDHDAVLRFNGAPTANFQQDVGTKTTIRLMNSQLVTTEKRFLKDSLYNEGILIVWDPSVYHSDIPKWYQNPDYNFFNNYKTYRKLHPNQPFYILKPQMPWELWDILQEISPEEIQPNP... | 2.4.3.1 | null | humoral immune response [GO:0006959]; N-acetylneuraminate metabolic process [GO:0006054]; negative regulation of chemotaxis [GO:0050922]; negative regulation of macrophage apoptotic process [GO:2000110]; O-glycan processing [GO:0016266]; positive regulation of mononuclear cell proliferation [GO:0032946]; protein N-link... | extracellular region [GO:0005576]; Golgi apparatus [GO:0005794]; Golgi cisterna membrane [GO:0032580]; Golgi medial cisterna [GO:0005797]; Golgi membrane [GO:0000139]; Golgi trans cisterna [GO:0000138] | beta-galactoside alpha-2,6-sialyltransferase activity [GO:0003835]; protein homodimerization activity [GO:0042803]; sialyltransferase activity [GO:0008373] | PF00777; | 3.90.1480.20; | Glycosyltransferase 29 family | PTM: The soluble form derives from the membrane form by proteolytic processing. {ECO:0000250|UniProtKB:P13721}.; PTM: The HB-6, CDW75, and CD76 differentiation antigens are cell-surface carbohydrate determinants generated by this enzyme.; PTM: N-glycosylated. {ECO:0000269|PubMed:23999306}. | SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:20378551}; Single-pass type II membrane protein {ECO:0000305}. Secreted. Note=Membrane-bound form in trans cisternae of Golgi. Secreted into the body fluid. | CATALYTIC ACTIVITY: Reaction=a beta-D-galactoside + CMP-N-acetyl-beta-neuraminate = an N-acetyl-alpha-neuraminyl-(2->6)-beta-D-galactosyl derivative + CMP + H(+); Xref=Rhea:RHEA:52104, ChEBI:CHEBI:15378, ChEBI:CHEBI:28034, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:136398; EC=2.4.3.1; Evidence={ECO:0000269|PubMe... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=530 uM for CMP-NeuAc {ECO:0000269|PubMed:21081508}; Vmax=1.074 pmol/min/ug enzyme {ECO:0000269|PubMed:21081508}; | PATHWAY: Protein modification; protein glycosylation. | null | null | FUNCTION: Transfers sialic acid from CMP-sialic acid to galactose-containing acceptor substrates. {ECO:0000269|PubMed:21081508, ECO:0000269|PubMed:23999306}. | Homo sapiens (Human) |
P15917 | LEF_BACAN | MNIKKEFIKVISMSCLVTAITLSGPVFIPLVQGAGGHGDVGMHVKEKEKNKDENKRKDEERNKTQEEHLKEIMKHIVKIEVKGEEAVKKEAAEKLLEKVPSDVLEMYKAIGGKIYIVDGDITKHISLEALSEDKKKIKDIYGKDALLHEHYVYAKEGYEPVLVIQSSEDYVENTEKALNVYYEIGKILSRDILSKINQPYQKFLDVLNTIKNASDSDGQDLLFTNQLKEHPTDFSVEFLEQNSNEVQEVFAKAFAYYIEPQHRDVLQLYAPEAFNYMDKFNEQEINLSLEELKDQRMLARYEKWEKIKQHYQHWSDSLSE... | 3.4.24.83 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|PROSITE-ProRule:PRU01339, ECO:0000269|PubMed:11700563, ECO:0000269|PubMed:14718924, ECO:0000269|PubMed:14718925, ECO:0000269|PubMed:15911756, ECO:0000269|PubMed:22342144, ECO:0000269|PubMed:25372673, ECO:0000269|PubMed:26492514, ECO:0000269|PubMed:265... | proteolysis [GO:0006508] | extracellular region [GO:0005576]; host cell cytosol [GO:0044164] | metalloendopeptidase activity [GO:0004222]; metallopeptidase activity [GO:0008237]; toxin activity [GO:0090729]; zinc ion binding [GO:0008270] | PF09156;PF07737; | 3.40.390.10; | Peptidase M34 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2509294}. Host cytoplasm, host cytosol {ECO:0000269|PubMed:1512256}. Note=Translocation into host cytosol is mediated via interaction with the cleaved form of protective antigen (PA-63): following secretion, LF binds via its N-terminal region to the upper rim of the ri... | CATALYTIC ACTIVITY: Reaction=Preferred amino acids around the cleavage site can be denoted BBBBxHx-|-H, in which B denotes Arg or Lys, H denotes a hydrophobic amino acid, and x is any amino acid. The only known protein substrates are mitogen-activated protein (MAP) kinase kinases.; EC=3.4.24.83; Evidence={ECO:0000269|P... | null | null | null | null | FUNCTION: Lethal factor (LF), which constitutes one of the three proteins composing the anthrax toxin, is able to trigger rapid cell death in macrophages (PubMed:10475971, PubMed:11104681, PubMed:3711080, PubMed:8380282, PubMed:9563949, PubMed:9703991). Acts as a protease that cleaves the N-terminal of most dual specif... | Bacillus anthracis |
P15918 | RAG1_HUMAN | MAASFPPTLGLSSAPDEIQHPHIKFSEWKFKLFRVRSFEKTPEEAQKEKKDSFEGKPSLEQSPAVLDKADGQKPVPTQPLLKAHPKFSKKFHDNEKARGKAIHQANLRHLCRICGNSFRADEHNRRYPVHGPVDGKTLGLLRKKEKRATSWPDLIAKVFRIDVKADVDSIHPTEFCHNCWSIMHRKFSSAPCEVYFPRNVTMEWHPHTPSCDICNTARRGLKRKSLQPNLQLSKKLKTVLDQARQARQHKRRAQARISSKDVMKKIANCSKIHLSTKLLAVDFPEHFVKSISCQICEHILADPVETNCKHVFCRVCILRC... | 2.3.2.27; 3.1.-.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 1 divalent metal cation per subunit. Mg(2+) or Mn(2+). {ECO:0000250}; | adaptive immune response [GO:0002250]; B cell differentiation [GO:0030183]; chromatin organization [GO:0006325]; DNA recombination [GO:0006310]; immune response [GO:0006955]; negative regulation of thymocyte apoptotic process [GO:0070244]; positive regulation of T cell differentiation [GO:0045582]; pre-B cell allelic e... | DNA recombinase complex [GO:0097519]; endodeoxyribonuclease complex [GO:1905347]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA binding [GO:0003677]; double-stranded DNA endonuclease activity [GO:1990238]; endonuclease activity [GO:0004519]; histone binding [GO:0042393]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; sequence-specific DNA binding [GO:0043565]; ubiquitin protein ligase activity [GO:0061630]; ... | PF12940;PF12560;PF00097;PF10426; | 6.10.140.510;3.30.160.60;3.30.40.10; | RAG1 family | PTM: Autoubiquitinated in the presence of CDC34/UBCH3. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00820}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; | null | null | null | null | FUNCTION: Catalytic component of the RAG complex, a multiprotein complex that mediates the DNA cleavage phase during V(D)J recombination. V(D)J recombination assembles a diverse repertoire of immunoglobulin and T-cell receptor genes in developing B and T-lymphocytes through rearrangement of different V (variable), in s... | Homo sapiens (Human) |
P15919 | RAG1_MOUSE | MAASLPSTLSFSSAPDEIQHPQIKFSEWKFKLFRVRSFEKAPEEAQKEKDSSEGKPYLEQSPVVPEKPGGQNSILTQRALKLHPKFSKKFHADGKSSDKAVHQARLRHFCRICGNRFKSDGHSRRYPVHGPVDAKTQSLFRKKEKRVTSWPDLIARIFRIDVKADVDSIHPTEFCHDCWSIMHRKFSSSHSQVYFPRKVTVEWHPHTPSCDICFTAHRGLKRKRHQPNVQLSKKLKTVLNHARRDRRKRTQARVSSKEVLKKISNCSKIHLSTKLLAVDFPAHFVKSISCQICEHILADPVETSCKHLFCRICILRCLKV... | 2.3.2.27; 3.1.-.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10601032}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:10601032}; Note=Binds 1 divalent metal cation per subunit. Mg(2+) or Mn(2+). {ECO:0000269|PubMed:10601032}; | adaptive immune response [GO:0002250]; B cell differentiation [GO:0030183]; chromatin organization [GO:0006325]; DNA recombination [GO:0006310]; negative regulation of T cell apoptotic process [GO:0070233]; negative regulation of thymocyte apoptotic process [GO:0070244]; positive regulation of T cell differentiation [G... | DNA recombinase complex [GO:0097519]; endodeoxyribonuclease complex [GO:1905347]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | double-stranded DNA endonuclease activity [GO:1990238]; endonuclease activity [GO:0004519]; histone binding [GO:0042393]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; sequence-specific DNA binding [GO:0043565]; ubiquitin protein ligase activity ... | PF12940;PF12560;PF00097;PF10426; | 6.10.140.510;3.30.160.60;3.30.40.10; | RAG1 family | PTM: Autoubiquitinated in the presence of CDC34/UBCH3. {ECO:0000269|PubMed:14671314, ECO:0000269|PubMed:19118899}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00820, ECO:0000269|PubMed:8284210}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; | null | null | null | null | FUNCTION: Catalytic component of the RAG complex, a multiprotein complex that mediates the DNA cleavage phase during V(D)J recombination. V(D)J recombination assembles a diverse repertoire of immunoglobulin and T-cell receptor genes in developing B and T-lymphocytes through rearrangement of different V (variable), in s... | Mus musculus (Mouse) |
P15920 | VPP2_MOUSE | MGSLFRSESMCLAQLFLQSGTAYECLSALGEKGLVQFRDLNQNVSSFQRKFVGEVKRCEELERILVYLVQEITRADIPLPEGEASPPAPPLKHVLEMQEQLQKLEVELREVTKNKEKLRKNLLELVEYTHMLRVTKTFLKRNVEFEPTYEEFPALENDSLLDYSCMQRLGAKLGFVSGLIQQGRVEAFERMLWRACKGYTIVTYAELDECLEDPETGEVIKWYVFLISFWGEQIGHKVKKICDCYHCHIYPYPNTAEERREIQEGLNTRIQDLYTVLHKTEDYLRQVLCKAAESVCSRVVQVRKMKAIYHMLNMCSFDVT... | null | null | cellular response to increased oxygen levels [GO:0036295]; intracellular iron ion homeostasis [GO:0006879]; vacuolar acidification [GO:0007035] | acrosomal vesicle [GO:0001669]; endosome membrane [GO:0010008]; focal adhesion [GO:0005925]; intracellular organelle [GO:0043229]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; proton-transporting V-type ATPase complex [GO:0033176]; proton-transporting V-type ATPase, V0 domain [GO:0033179]... | ATPase binding [GO:0051117]; proton-transporting ATPase activity, rotational mechanism [GO:0046961] | PF01496; | null | V-ATPase 116 kDa subunit family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16415858}; Multi-pass membrane protein {ECO:0000269|PubMed:16415858}. Endosome membrane {ECO:0000269|PubMed:16415858}. Note=In kidney proximal tubules, detected in subapical early endosomes. | null | null | null | null | null | FUNCTION: Subunit of the V0 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (By similarity). V-ATPase is responsible for acidifying and maintaining the pH of intracellular compartmen... | Mus musculus (Mouse) |
P15923 | TFE2_HUMAN | MNQPQRMAPVGTDKELSDLLDFSMMFPLPVTNGKGRPASLAGAQFGGSGLEDRPSSGSWGSGDQSSSSFDPSRTFSEGTHFTESHSSLSSSTFLGPGLGGKSGERGAYASFGRDAGVGGLTQAGFLSGELALNSPGPLSPSGMKGTSQYYPSYSGSSRRRAADGSLDTQPKKVRKVPPGLPSSVYPPSSGEDYGRDATAYPSAKTPSSTYPAPFYVADGSLHPSAELWSPPGQAGFGPMLGGGSSPLPLPPGSGPVGSSGSSSTFGGLHQHERMGYQLHGAEVNGGLPSASSFSSAPGATYGGVSSHTPPVSGADSLLGS... | null | null | B cell differentiation [GO:0030183]; B cell lineage commitment [GO:0002326]; immunoglobulin V(D)J recombination [GO:0033152]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nervous system development [GO:0007399]; positive regulation of B cell proliferation [GO:0030890]; positive regulation of ... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; euchromatin [GO:0000791]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; RNA polymerase II transcription regulator complex [GO:0090575]; transcription regulator complex [GO:0005667] | bHLH transcription factor binding [GO:0043425]; cis-regulatory region sequence-specific DNA binding [GO:0000987]; 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 acti... | PF00010; | 4.10.280.10; | null | PTM: Phosphorylated following NGF stimulation. {ECO:0000250}.; PTM: Undergoes Notch-induced ubiquitination and subsequent proteasomal degradation which is mediated by ASB1 or ASB2, the substrate-recognition components of probable ECS E3 ubiquitin-protein ligase complexes. {ECO:0000269|PubMed:21119685}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:31696227}. | null | null | null | null | null | FUNCTION: Transcriptional regulator involved in the initiation of neuronal differentiation and mesenchymal to epithelial transition (By similarity). Heterodimers between TCF3 and tissue-specific basic helix-loop-helix (bHLH) proteins play major roles in determining tissue-specific cell fate during embryogenesis, like m... | Homo sapiens (Human) |
P15924 | DESP_HUMAN | MSCNGGSHPRINTLGRMIRAESGPDLRYEVTSGGGGTSRMYYSRRGVITDQNSDGYCQTGTMSRHQNQNTIQELLQNCSDCLMRAELIVQPELKYGDGIQLTRSRELDECFAQANDQMEILDSLIREMRQMGQPCDAYQKRLLQLQEQMRALYKAISVPRVRRASSKGGGGYTCQSGSGWDEFTKHVTSECLGWMRQQRAEMDMVAWGVDLASVEQHINSHRGIHNSIGDYRWQLDKIKADLREKSAIYQLEEEYENLLKASFERMDHLRQLQNIIQATSREIMWINDCEEEELLYDWSDKNTNIAQKQEAFSIRMSQLE... | null | null | adherens junction organization [GO:0034332]; bundle of His cell-Purkinje myocyte adhesion involved in cell communication [GO:0086073]; cell-cell adhesion [GO:0098609]; desmosome organization [GO:0002934]; epidermis development [GO:0008544]; epithelial cell-cell adhesion [GO:0090136]; intermediate filament cytoskeleton ... | adherens junction [GO:0005912]; basolateral plasma membrane [GO:0016323]; cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; desmosome [GO:0030057]; extracellular exosome [GO:0070062]; fascia adherens [GO:0005916]; ficolin-1-rich granule membrane [GO:0101003]; intercalated disc [GO:0014704]; intermediate filament... | cell adhesive protein binding involved in bundle of His cell-Purkinje myocyte communication [GO:0086083]; protein kinase C binding [GO:0005080]; RNA binding [GO:0003723]; scaffold protein binding [GO:0097110]; structural constituent of cytoskeleton [GO:0005200]; structural molecule activity [GO:0005198] | PF00681;PF17902;PF18373;PF21019; | 1.20.58.1060;1.20.58.60;3.30.160.780;3.90.1290.10;2.30.30.40; | Plakin or cytolinker family | null | SUBCELLULAR LOCATION: Cell junction, desmosome {ECO:0000250|UniProtKB:E9Q557}. Cell membrane {ECO:0000250|UniProtKB:E9Q557}. Note=Localizes at the intercalated disk in cardiomyocytes. {ECO:0000250|UniProtKB:E9Q557}. | null | null | null | null | null | FUNCTION: Major high molecular weight protein of desmosomes. Regulates profibrotic gene expression in cardiomyocytes via activation of the MAPK14/p38 MAPK signaling cascade and increase in TGFB1 protein abundance (By similarity). {ECO:0000250|UniProtKB:F1LMV6}. | Homo sapiens (Human) |
P15925 | FPGS_LACCA | MNYTETVAYIHSFPRLAKTGDHRRILTLLHALGNPQQQGRYIHVTGTNGKGSAANAIAHVLEASGLTVGLYTSPFIMRFNERIMIDHEPIPDAALVNAVAFVRAALERLQQQQADFNVTEFEFITALGYWYFRQRQVDVAVIEVGIGGDTDSTNVITPVVSVLTEVALDHQKLLGHTITAIAKHKAGIIKRGIPVVTGNLVPDAAAVVAAKVATTGSQWLRFDRDFSVPKAKLHGWGQRFTYEDQDGRISDLEVPLVGDYQQRNMAIAIQTAKVYAKQTEWPLTPQNIRQGLAASHWPARLEKISDTPLIVIDGAHNPDG... | 6.3.2.17 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:6138353}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000269|PubMed:11501996}; | one-carbon metabolic process [GO:0006730] | cytosol [GO:0005829] | ATP binding [GO:0005524]; dihydrofolate synthase activity [GO:0008841]; metal ion binding [GO:0046872]; tetrahydrofolylpolyglutamate synthase activity [GO:0004326] | PF02875;PF08245; | 3.90.190.20;3.40.1190.10; | Folylpolyglutamate synthase family | null | null | CATALYTIC ACTIVITY: Reaction=(6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n) + ATP + L-glutamate = (6S)-5,6,7,8-tetrahydrofolyl-(gamma-L-Glu)(n+1) + ADP + H(+) + phosphate; Xref=Rhea:RHEA:10580, Rhea:RHEA-COMP:14738, Rhea:RHEA-COMP:14740, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:C... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.3 uM for (6R)-5,10-methylenetetrahydropteroyldiglutamate {ECO:0000269|PubMed:6138353}; KM=5.6 mM for ATP {ECO:0000269|PubMed:6138353}; KM=423 uM for glutamate {ECO:0000269|PubMed:6138353}; KM=32 uM for (6RS)-5,10-methylenetetrahydrofolate {ECO:0000269|PubMed:1823... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is about 10. {ECO:0000269|PubMed:6138353}; | null | FUNCTION: Involved in the conversion of folates to polyglutamate derivatives, and likely functions in the retention of cellular folate pools. Catalyzes successive MgATP-dependent additions of glutamate to a pteroylmonoglutamate substrate, with a high preference for 5,10-methylenetetrahydrofolate (mTHF). Thus, metaboliz... | Lacticaseibacillus casei (Lactobacillus casei) |
P15926 | C5AP_STRPY | MRKKQKLPFDKLAIALMSTSILLNAQSDIKANTVTEDTPVTEQAVETPQPTAVSEEVPSSKETKTPQTPDDAEETIADDANDLAPQAPAKTADTPATSKATIRDLNDPSQVKTLQEKAGKGAGTVVAVIDAGFDKNHEAWRLTDKTKARYQSKEDLEKAKKEHGITYGEWVNDKVAYYHDYSKDGKTAVDQEHGTHVSGILSGNAPSETKEPYRLEGAMPEAQLLLMRVEIVNGLADYARNYAQAIRDAVNLGAKVINMSFGNAALAYANLPDETKKAFDYAKSKGVSIVTSAGNDSSFGGKTRLPLADHPDYGVVGTPA... | 3.4.21.110 | null | proteolysis [GO:0006508]; symbiont-mediated suppression of host innate immune response [GO:0052170] | extracellular region [GO:0005576]; membrane [GO:0016020] | serine-type endopeptidase activity [GO:0004252]; toxin activity [GO:0090729] | PF13585;PF06280;PF02225;PF00082; | 2.60.40.4070;3.50.30.30;2.60.40.10;3.40.50.200;2.60.40.1710; | Peptidase S8 family | PTM: Cleaved by SpeB protease; leading to its degradation. Degradation by SpeB is probably strictly regulated to preserve integrity of C5a peptidase. {ECO:0000250|UniProtKB:P58099}. | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000255|PROSITE-ProRule:PRU00477}; Peptidoglycan-anchor {ECO:0000255|PROSITE-ProRule:PRU00477}. | CATALYTIC ACTIVITY: Reaction=The primary cleavage site is at 67-His-|-Lys-68 in human C5a with a minor secondary cleavage site at 58-Ala-|-Ser-59.; EC=3.4.21.110; Evidence={ECO:0000269|PubMed:3906656}; | null | null | null | null | FUNCTION: This virulence factor of S.pyogenes specifically cleaves the human serum chemotaxin C5a at '68-Lys-|-Asp-69' bond near its C-terminus, destroying its ability to serve as a chemoattractant. {ECO:0000269|PubMed:2406246, ECO:0000269|PubMed:3906656}. | Streptococcus pyogenes |
P15927 | RFA2_HUMAN | MWNSGFESYGSSSYGGAGGYTQSPGGFGSPAPSQAEKKSRARAQHIVPCTISQLLSATLVDEVFRIGNVEISQVTIVGIIRHAEKAPTNIVYKIDDMTAAPMDVRQWVDTDDTSSENTVVPPETYVKVAGHLRSFQNKKSLVAFKIMPLEDMNEFTTHILEVINAHMVLSKANSQPSAGRAPISNPGMSEAGNFGGNSFMPANGLTVAQNQVLNLIKACPRPEGLNFQDLKNQLKHMSVSSIKQAVDFLSNEGHIYSTVDDDHFKSTDAE | null | null | base-excision repair [GO:0006284]; DNA replication [GO:0006260]; double-strand break repair via homologous recombination [GO:0000724]; mismatch repair [GO:0006298]; mitotic G1 DNA damage checkpoint signaling [GO:0031571]; nucleotide-excision repair [GO:0006289]; protein localization to chromosome [GO:0034502]; regulati... | chromatin [GO:0000785]; chromosome, telomeric region [GO:0000781]; DNA replication factor A complex [GO:0005662]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; PML body [GO:0016605]; site of double-strand break [GO:0035861] | damaged DNA binding [GO:0003684]; enzyme binding [GO:0019899]; G-rich strand telomeric DNA binding [GO:0098505]; protein phosphatase binding [GO:0019903]; single-stranded DNA binding [GO:0003697]; telomeric DNA binding [GO:0042162]; ubiquitin protein ligase binding [GO:0031625] | PF08784; | 2.40.50.140;1.10.10.10; | Replication factor A protein 2 family | PTM: Differentially phosphorylated throughout the cell cycle, becoming phosphorylated at the G1-S transition and dephosphorylated in late mitosis. Mainly phosphorylated at Ser-23 and Ser-29, by cyclin A-CDK2 and cyclin B-CDK1, respectively during DNA replication and mitosis. Dephosphorylation may require the serine/thr... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10982866, ECO:0000269|PubMed:12814551, ECO:0000269|PubMed:20154705, ECO:0000269|PubMed:21504906}. Nucleus, PML body {ECO:0000269|PubMed:12814551}. Note=Redistributes to discrete nuclear foci upon DNA damage in an ATR-dependent manner. {ECO:0000269|PubMed:12814551}. | null | null | null | null | null | FUNCTION: As part of the heterotrimeric replication protein A complex (RPA/RP-A), binds and stabilizes single-stranded DNA intermediates, that form during DNA replication or upon DNA stress. It prevents their reannealing and in parallel, recruits and activates different proteins and complexes involved in DNA metabolism... | Homo sapiens (Human) |
P15938 | PRP16_YEAST | MGHSGREERIKDIFKELTSKELTPGLLLTLQKLAQKPNTNLEQFIASCKALTKLSSNNPIIFNELLELLKNKSEEDSTGPKKIAPSINKRKKFKIQLDLDDNEDELDSPVQKKPAPTRTLFKRIDKLKAKQLRQYSPTVKDPSPNSEQQTQNGHAETKDYEPTRSEVVEEDREWYDNDDDYGNLVPEPLSELPEEAKLLPVIRNIDNDDALRNTVQLYPIPLKQRMEWIPPFLSKFALENKVPTSIIIGSISETSSQVSALSMVNPFRNPDSEFSANAKRGSKLVALRRINMEHIQQSRDNTTVLNTAMGEVLGLENNNK... | 3.6.4.13 | null | generation of catalytic spliceosome for second transesterification step [GO:0000350]; mRNA splicing, via spliceosome [GO:0000398]; RNA exon ligation [GO:0000378]; snRNA metabolic process [GO:0016073]; snRNA modification [GO:0040031] | spliceosomal complex [GO:0005681]; U2-type catalytic step 2 spliceosome [GO:0071007] | 3'-5' RNA helicase activity [GO:0034458]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent activity, acting on RNA [GO:0008186]; RNA binding [GO:0003723] | PF00270;PF21010;PF04408;PF00271;PF07717; | 1.20.120.1080;3.40.50.300; | DEAD box helicase family, DEAH subfamily, PRP16 sub-subfamily | null | SUBCELLULAR LOCATION: Nucleus. Note=Binds to the spliceosome. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; | null | null | null | null | FUNCTION: Influences the fidelity of branchpoint recognition in yeast splicing. This is RNA-dependent ATPase which is essential for viability. It may mediate one of the many ATP-requiring steps of spliceosome assembly and that accuracy of branchpoint recognition may be coupled to ATP binding and/or hydrolysis. {ECO:000... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P15941 | MUC1_HUMAN | MTPGTQSPFFLLLLLTVLTVVTGSGHASSTPGGEKETSATQRSSVPSSTEKNAVSMTSSVLSSHSPGSGSSTTQGQDVTLAPATEPASGSAATWGQDVTSVPVTRPALGSTTPPAHDVTSAPDNKPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTSAPDTRPAPGSTAPPAHGVTS... | null | null | DNA damage response, signal transduction by p53 class mediator [GO:0030330]; DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest [GO:0006977]; localization [GO:0051179]; negative regulation of cell adhesion mediated by integrin [GO:0033629]; negative regulation of intrinsic apo... | apical plasma membrane [GO:0016324]; chromatin [GO:0000785]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; vesicle [GO:0031982] | p53 binding [GO:0002039]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; transcription coregulator activity [GO:0003712] | PF01390; | 6.10.140.600; | null | PTM: Highly glycosylated (N- and O-linked carbohydrates and sialic acid). O-glycosylated to a varying degree on serine and threonine residues within each tandem repeat, ranging from mono- to penta-glycosylation. The average density ranges from about 50% in human milk to over 90% in T47D breast cancer cells. Further sia... | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:11118479, ECO:0000269|PubMed:12832415, ECO:0000269|PubMed:12939402, ECO:0000269|PubMed:15471854, ECO:0000269|PubMed:15972891, ECO:0000269|PubMed:16507569, ECO:0000269|PubMed:17524503, ECO:0000269|PubMed:17545600}; Single-pass type I membrane protein {ECO:00... | null | null | null | null | null | FUNCTION: The alpha subunit has cell adhesive properties. Can act both as an adhesion and an anti-adhesion protein. May provide a protective layer on epithelial cells against bacterial and enzyme attack.; FUNCTION: The beta subunit contains a C-terminal domain which is involved in cell signaling, through phosphorylatio... | Homo sapiens (Human) |
P15943 | APLP2_RAT | MAATGTAAAAATGKLLVLLLLGLTAPAAALAGYIEALAANAGTGFAVAEPQIAMFCGKLNMHVNIQTGKWEPDPTGTKSCLGTKEEVLQYCQEIYPELQITNVMEANQPVNIDSWCRRDKKQCRSHIVIPFKCLVGEFVSDVLLVPENCQFFHQERMEVCEKHQRWHTVVKEACLTEGMTLYSYGMLLPCGVDQFHGTEYVCCPQTKVVDSDSTMSKEEEEEEEEDEEEDYALDKSEFPTEADLEDFTEAAADEDEDEEEEEEEEGEEVVEDRDYYYDSFKGDDYNEENPTEPSSDGTISDKEIAHDVKAVCSQEAMTGP... | null | null | axonogenesis [GO:0007409]; central nervous system development [GO:0007417]; cholesterol metabolic process [GO:0008203]; extracellular matrix organization [GO:0030198]; forebrain development [GO:0030900]; intracellular copper ion homeostasis [GO:0006878]; locomotory behavior [GO:0007626]; mating behavior [GO:0007617]; m... | membrane [GO:0016020]; nucleus [GO:0005634]; spine apparatus [GO:0097444] | heparin binding [GO:0008201]; identical protein binding [GO:0042802]; serine-type endopeptidase inhibitor activity [GO:0004867]; transition metal ion binding [GO:0046914] | PF10515;PF12924;PF12925;PF02177;PF00014; | 6.10.250.1670;1.20.120.770;3.30.1490.140;3.90.570.10;4.10.410.10;2.30.29.30; | APP family | null | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: May play a role in the regulation of hemostasis. The soluble form may have inhibitory properties towards coagulation factors. May interact with cellular G-protein signaling pathways. May bind to the DNA 5'-GTCACATG-3'(CDEI box). Inhibits trypsin, chymotrypsin, plasmin, factor XIA and plasma and glandular kall... | Rattus norvegicus (Rat) |
P15945 | K1KB5_MOUSE | MWFLILFLALSLGGIDAAPPVQSRIFGGFNCEKNSQPWQVAVYRFTKYQCGGVLLNANWVLTAAHCHNDKYQVWLGKNNFFEDEPSAQHRLVSKAIPHPDFNMSLLNEHTPQPEDDYSNDLMLLRLKKPADITDVVKPIDLPTEEPKLGSTCLASGWGSITPVIYEPADDLQCVNFKLLPNEDCVKAHIEKVTDVMLCAGDMDGGKDTCMGDSGGPLICDGVLHGITSWGPSPCGKPNVPGIYTKLIKFNSWIKDTIAKNA | 3.4.21.35 | null | proteolysis [GO:0006508]; regulation of systemic arterial blood pressure [GO:0003073]; zymogen activation [GO:0031638] | acrosomal vesicle [GO:0001669]; apical part of cell [GO:0045177]; secretory granule [GO:0030141] | endopeptidase activity [GO:0004175]; serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236] | PF00089; | 2.40.10.10; | Peptidase S1 family, Kallikrein subfamily | null | null | CATALYTIC ACTIVITY: Reaction=Preferential cleavage of Arg-|-Xaa bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|-Xaa.; EC=3.4.21.35; | null | null | null | null | FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin. | Mus musculus (Mouse) |
P15946 | K1B11_MOUSE | MWFLILFLALSLGGIDAAPPVQSRIVGGFNCEKNSQPWHVAVYRYNKYICGGVLLDRNWVLTAAHCHVSQYNVWLGKTKLFQREPSAQHRMVSKSFPHPDYNMSLLIIHNPEPEDDESNDLMLLRLSEPADITDAVKPIALPTEEPKLGSTCLVSGWGSITPTKFQTPDDLQCVSIKLLPNEVCVKNHNQKVTDVMLCAGEMGGGKDTCKGDSGGPLICDGVLHGITAWGPIPCGKPNTPGVYTKLIKFTNWIKDTMAKNP | 3.4.21.35 | null | regulation of systemic arterial blood pressure [GO:0003073]; zymogen activation [GO:0031638] | acrosomal vesicle [GO:0001669]; apical part of cell [GO:0045177]; secretory granule [GO:0030141] | endopeptidase activity [GO:0004175]; serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236] | PF00089; | 2.40.10.10; | Peptidase S1 family, Kallikrein subfamily | null | null | CATALYTIC ACTIVITY: Reaction=Preferential cleavage of Arg-|-Xaa bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|-Xaa.; EC=3.4.21.35; | null | null | null | null | FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin. | Mus musculus (Mouse) |
P15947 | KLK1_MOUSE | MRFLILFLALSLGGIDAAPPVQSRIVGGFNCEKNSQPWQVAVYRFTKYQCGGILLNANWVLTAAHCHNDKYQVWLGKNNFLEDEPSAQHRLVSKAIPHPDFNMSLLNEHTPQPEDDYSNDLMLLRLKKPADITDVVKPIDLPTEEPKLGSTCLASGWGSITPVKYEYPDELQCVNLKLLPNEDCAKAHIEKVTDDMLCAGDMDGGKDTCAGDSGGPLICDGVLQGITSWGPSPCGKPNVPGIYTRVLNFNTWIRETMAEND | 3.4.21.35 | null | regulation of systemic arterial blood pressure [GO:0003073]; zymogen activation [GO:0031638] | acrosomal vesicle [GO:0001669]; apical part of cell [GO:0045177]; secretory granule [GO:0030141] | endopeptidase activity [GO:0004175]; serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236] | PF00089; | 2.40.10.10; | Peptidase S1 family, Kallikrein subfamily | null | null | CATALYTIC ACTIVITY: Reaction=Preferential cleavage of Arg-|-Xaa bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|-Xaa.; EC=3.4.21.35; | null | null | null | null | FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin. | Mus musculus (Mouse) |
P15948 | K1B22_MOUSE | MRFLILFLTLSLGGIDAAPPVQSRILGGFKCEKNSQPWQVAVYYLDEYLCGGVLLDRNWVLTAAHCYEDKYNIWLGKNKLFQDEPSAQHRLVSKSFPHPDFNMSLLQSVPTGADLSNDLMLLRLSKPADITDVVKPIDLPTTEPKLGSTCLASGWGSINQLIYQNPNDLQCVSIKLHPNEVCVKAHILKVTDVMLCAGEMNGGKDTCKGDSGGPLICDGVLQGITSWGSTPCGEPNAPAIYTKLIKFTSWIKDTMAKNP | 3.4.21.35 | null | regulation of systemic arterial blood pressure [GO:0003073]; zymogen activation [GO:0031638] | acrosomal vesicle [GO:0001669]; apical part of cell [GO:0045177]; secretory granule [GO:0030141] | endopeptidase activity [GO:0004175]; peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236] | PF00089; | 2.40.10.10; | Peptidase S1 family, Kallikrein subfamily | null | null | CATALYTIC ACTIVITY: Reaction=Preferential cleavage of Arg-|-Xaa bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|-Xaa.; EC=3.4.21.35; | null | null | null | null | FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin. | Mus musculus (Mouse) |
P15949 | K1KB9_MOUSE | MRFLILFLALSLGGIDAAPPVHSRIVGGFKCEKNSQPWHVAVYRYNEYICGGVLLDANWVLTAAHCYYEENKVSLGKNNLYEEEPSAQHRLVSKSFLHPGYNRSLHRNHIRHPEYDYSNDLMLLRLSKPADITDVVKPIALPTEEPKLGSTCLASGWGSTTPFKFQNAKDLQCVNLKLLPNEDCGKAHIEKVTDVMLCAGETDGGKDTCKGDSGGPLICDGVLQGITSWGFTPCGEPKKPGVYTKLIKFTSWIKDTMAKNL | 3.4.21.35 | null | regulation of systemic arterial blood pressure [GO:0003073]; zymogen activation [GO:0031638] | acrosomal vesicle [GO:0001669]; apical part of cell [GO:0045177]; secretory granule [GO:0030141] | endopeptidase activity [GO:0004175]; peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236] | PF00089; | 2.40.10.10; | Peptidase S1 family, Kallikrein subfamily | null | null | CATALYTIC ACTIVITY: Reaction=Preferential cleavage of Arg-|-Xaa bonds in small molecule substrates. Highly selective action to release kallidin (lysyl-bradykinin) from kininogen involves hydrolysis of Met-|-Xaa or Leu-|-Xaa.; EC=3.4.21.35; | null | null | null | null | FUNCTION: Glandular kallikreins cleave Met-Lys and Arg-Ser bonds in kininogen to release Lys-bradykinin. | Mus musculus (Mouse) |
P15954 | COX7C_HUMAN | MLGQSIRRFTTSVVRRSHYEEGPGKNLPFSVENKWSLLAKMCLYFGSAFATPFLVVRHQLLKT | null | null | cellular respiration [GO:0045333]; generation of precursor metabolites and energy [GO:0006091]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123] | mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966]; mitochondrial respiratory chain complex IV [GO:0005751]; mitochondrion [GO:0005739] | null | PF02935; | 4.10.49.10; | Cytochrome c oxidase VIIc family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:30030519}; Single-pass membrane protein {ECO:0000269|PubMed:30030519}. | null | null | PATHWAY: Energy metabolism; oxidative phosphorylation. {ECO:0000250|UniProtKB:P04039}. | null | null | FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple... | Homo sapiens (Human) |
P15975 | UBP53_MOUSE | MAWVKFLRKPSGNLGKAYQAGSLLSLAPTVGLLNEPGQNSCFLNSAVQVLWQLDIFRRSLRALTGHICQGDACIFCALKTIFAQFQHSREKALPSDNIRHALAESFKDEQRFQLGLMDDAAECFENILARIHFHLVPNRDADMCTSKSCVTHQKFAMTLYEQCVCRSCGASSDPLPFTELVRYISTTALCNEVERMMERHERVKPEMFAELLQAANTADDYRKCPSNCGQKIKIRRVLMNCPEIVTIGLVWDSEHSDLTEDVVRSLATHLYLPGLFYRVTDENATDSELHLVGMICYTSRHYCAFAFHTKSSKWVFFDDA... | null | null | action potential [GO:0001508]; epithelial cell apoptotic process [GO:1904019]; neuron apoptotic process [GO:0051402]; outer hair cell apoptotic process [GO:1905584]; response to auditory stimulus [GO:0010996]; sensory perception of sound [GO:0007605] | bicellular tight junction [GO:0005923]; cell-cell junction [GO:0005911] | null | PF00443; | 3.90.70.10; | Peptidase C19 family | null | SUBCELLULAR LOCATION: Cell junction, tight junction {ECO:0000269|PubMed:26609154}. | null | null | null | null | null | FUNCTION: Tight junction-associated protein that is involved in the survival of auditory hair cells and hearing. Maybe by modulating the barrier properties and mechanical stability of tight junctions (PubMed:26609154). Has no peptidase activity (PubMed:26609154). {ECO:0000269|PubMed:26609154}. | Mus musculus (Mouse) |
P15976 | GATA1_HUMAN | MEFPGLGSLGTSEPLPQFVDPALVSSTPESGVFFPSGPEGLDAAASSTAPSTATAAAAALAYYRDAEAYRHSPVFQVYPLLNCMEGIPGGSPYAGWAYGKTGLYPASTVCPTREDSPPQAVEDLDGKGSTSFLETLKTERLSPDLLTLGPALPSSLPVPNSAYGGPDFSSTFFSPTGSPLNSAAYSSPKLRGTLPLPPCEARECVNCGATATPLWRRDRTGHYLCNACGLYHKMNGQNRPLIRPKKRLIVSKRAGTQCTNCQTTTTTLWRRNASGDPVCNACGLYYKLHQVNRPLTMRKDGIQTRNRKASGKGKKKRGSS... | null | null | animal organ regeneration [GO:0031100]; basophil differentiation [GO:0030221]; bone mineralization [GO:0030282]; cell fate commitment [GO:0045165]; cell-cell signaling [GO:0007267]; cellular response to cAMP [GO:0071320]; cellular response to follicle-stimulating hormone stimulus [GO:0071372]; cellular response to lipo... | chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-DNA complex [GO:0032993]; transcription regulator complex [GO:0005667]; transcription repressor complex [GO:0017053] | C2H2 zinc finger domain binding [GO:0070742]; chromatin DNA binding [GO:0031490]; 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... | PF00320; | 3.30.50.10; | null | PTM: Highly phosphorylated on serine residues. Phosphorylation on Ser-310 is enhanced on erythroid differentiation. Phosphorylation on Ser-142 promotes sumoylation on Lys-137 (By similarity). {ECO:0000250}.; PTM: Sumoylation on Lys-137 is enhanced by phosphorylation on Ser-142 and by interaction with PIAS4. Sumoylation... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:35030251}. | null | null | null | null | null | FUNCTION: Transcriptional activator or repressor which serves as a general switch factor for erythroid development (PubMed:35030251). It binds to DNA sites with the consensus sequence 5'-[AT]GATA[AG]-3' within regulatory regions of globin genes and of other genes expressed in erythroid cells. Activates the transcriptio... | Homo sapiens (Human) |
P15978 | HA11_RAT | MGAMAPRTLLLLLAAVLAPTQTWAGSHSLRYFHTAVSRPGLGEPRFISVGYVDDTQFVRYDSDAENPRYEPRARWMEREGPEYWEEQTLVAKGQELDYRVSLRNLLSYYNQSEGGSHTIQRMYGCDVGSDGSLLRGYEQHAYDGRDYIALNEDLKTWAVADFAAWITRSKWQRNGAAERSRAYLEGTCVEWLLRYLERGKETLLRSDPPEAHVTLHPRPEGDVTLRCWALGFYPADITLTWQLNGEDLTQDMELVETRPAGDGTFQKWASVVVPLGKEQNYTCRVEHEGLPEPLSQRWEPSPSTDSNLLLLFLELWQFL | null | null | 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 via MHC class Ib [GO:0002476]; immune response [GO:0006955]; positive regulation of T cell mediated cytotoxicity [GO:0001916] | 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] | peptide antigen binding [GO:0042605]; signaling receptor binding [GO:0005102] | PF07654;PF00129; | 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. | Rattus norvegicus (Rat) |
P15979 | HA1F_CHICK | MGPCGALGLGLLLAAVCGAAAPELHTLRYIQTAMTDPGPGQPWFVTVGYVDGELFVHYNSTARRYVPRTEWIAAKADQQYWDGQTQIGQGNEQIDRENLGILQRRYNQTGGSHTVQWMYGCDILEGGPIRGYYQMAYDGRDFTAFDKGTMTFTAAVPEAVPTKRKWEEESEPERWKNYLEETCVEWLRRYVEYGKAELGRRERPEVRVWGKEADGILTLSCRAHGFYPRPIVVSWLKDGAVRGQDAHSGGIVPNGDGTYHTWVTIDAQPGDGDKYQCRVEHASLPQPGLYSWEPPQPNLVPIVAGVAVAIVAIAIMVGVG... | null | null | 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 via MHC class Ib [GO:0002476]; immune response [GO:0006955]; positive regulation of T cell mediated cytotoxicity [GO:0001916] | 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] | peptide antigen binding [GO:0042605]; signaling receptor binding [GO:0005102] | PF07654;PF00129; | 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. | Gallus gallus (Chicken) |
P15992 | HSP26_YEAST | MSFNSPFFDFFDNINNEVDAFNRLLGEGGLRGYAPRRQLANTPAKDSTGKEVARPNNYAGALYDPRDETLDDWFDNDLSLFPSGFGFPRSVAVPVDILDHDNNYELKVVVPGVKSKKDIDIEYHQNKNQILVSGEIPSTLNEESKDKVKVKESSSGKFKRVITLPDYPGVDADNIKADYANGVLTLTVPKLKPQKDGKNHVKKIEVSSQESWGN | null | null | cellular response to heat [GO:0034605]; protein complex oligomerization [GO:0051259]; protein folding [GO:0006457]; response to hydrogen peroxide [GO:0042542]; response to salt stress [GO:0009651] | cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | identical protein binding [GO:0042802]; mRNA binding [GO:0003729]; protein self-association [GO:0043621]; unfolded protein binding [GO:0051082] | PF00011; | 2.60.40.790; | Small heat shock protein (HSP20) family | null | null | null | null | null | null | null | FUNCTION: Not known. One of the major polypeptides produced on heat shock. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P15993 | AROP_ECOLI | MMEGQQHGEQLKRGLKNRHIQLIALGGAIGTGLFLGSASVIQSAGPGIILGYAIAGFIAFLIMRQLGEMVVEEPVAGSFSHFAYKYWGSFAGFASGWNYWVLYVLVAMAELTAVGKYIQFWYPEIPTWVSAAVFFVVINAINLTNVKVFGEMEFWFAIIKVIAVVAMIIFGGWLLFSGNGGPQATVSNLWDQGGFLPHGFTGLVMMMAIIMFSFGGLELVGITAAEADNPEQSIPKATNQVIYRILIFYIGSLAVLLSLMPWTRVTADTSPFVLIFHELGDTFVANALNIVVLTAALSVYNSCVYCNSRMLFGLAQQGNA... | null | null | phenylalanine transport [GO:0015823]; tryptophan transport [GO:0015827]; tyrosine transport [GO:0015828] | plasma membrane [GO:0005886] | L-phenylalanine transmembrane transporter activity [GO:0015192]; L-tryptophan transmembrane transporter activity [GO:0015196]; L-tyrosine transmembrane transporter activity [GO:0005302] | PF00324; | 1.20.1740.10; | Amino acid-polyamine-organocation (APC) superfamily, Amino acid transporter (AAT) (TC 2.A.3.1) family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:3015892, ECO:0000269|PubMed:9150230}; Multi-pass membrane protein {ECO:0000269|PubMed:9150230}. | CATALYTIC ACTIVITY: Reaction=H(+)(in) + L-phenylalanine(in) = H(+)(out) + L-phenylalanine(out); Xref=Rhea:RHEA:28923, ChEBI:CHEBI:15378, ChEBI:CHEBI:58095; Evidence={ECO:0000305|PubMed:10735864, ECO:0000305|PubMed:4919744, ECO:0000305|PubMed:9150230}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28925; Evidence... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.47 uM for phenylalanine {ECO:0000269|PubMed:4919744}; KM=0.4 uM for tryptophan {ECO:0000269|PubMed:4919744}; KM=0.57 uM for tyrosine {ECO:0000269|PubMed:4919744}; | null | null | null | FUNCTION: Permease that is involved in the active transport across the cytoplasmic membrane of all three aromatic amino acids, phenylalanine, tyrosine and tryptophan. {ECO:0000269|PubMed:10735864, ECO:0000269|PubMed:4919744, ECO:0000269|PubMed:9150230}. | Escherichia coli (strain K12) |
P15999 | ATPA_RAT | MLSVRIAAAVARALPRRAGLVSKNALGSSFVGTRNLHASNTRLQKTGTAEMSSILEERILGADTSVDLEETGRVLSIGDGIARVHGLRNVQAEEMVEFSSGLKGMSLNLEPDNVGVVVFGNDKLIKEGDIVKRTGAIVDVPVGDELLGRVVDALGNAIDGKGPVGSKIRRRVGLKAPGIIPRISVREPMQTGIKAVDSLVPIGRGQRELIIGDRQTGKTSIAIDTIINQKRFNDGTDEKKKLYCIYVAIGQKRSTVAQLVKRLTDADAMKYTIVVSATASDAAPLQYLAPYSGCSMGEYFRDNGKHALIIYDDLSKQAVA... | null | null | ATP biosynthetic process [GO:0006754]; cellular response to dexamethasone stimulus [GO:0071549]; cellular response to nitric oxide [GO:0071732]; lipid metabolic process [GO:0006629]; negative regulation of endothelial cell proliferation [GO:0001937]; positive regulation of blood vessel endothelial cell migration [GO:00... | cell surface [GO:0009986]; COP9 signalosome [GO:0008180]; membrane [GO:0016020]; membrane raft [GO:0045121]; mitochondrial inner membrane [GO:0005743]; mitochondrial proton-transporting ATP synthase complex [GO:0005753]; mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1) [GO:0000275]; mitocho... | ADP binding [GO:0043531]; angiostatin binding [GO:0043532]; ATP binding [GO:0005524]; MHC class I protein binding [GO:0042288]; protease binding [GO:0002020]; proton-transporting ATP synthase activity, rotational mechanism [GO:0046933] | PF00006;PF00306;PF02874; | 2.40.30.20;1.20.150.20;3.40.50.300; | ATPase alpha/beta chains family | PTM: Acetylated on lysine residues. BLOC1S1 is required for acetylation. {ECO:0000250|UniProtKB:P25705}. | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:17575325}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P19483}; Peripheral membrane protein {ECO:0000250|UniProtKB:P19483}; Matrix side {ECO:0000250|UniProtKB:P19483}. Cell membrane {ECO:0000250|UniProtKB:P25705}; Peripheral membrane protein {ECO:0000250|U... | null | null | null | null | null | FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramemb... | Rattus norvegicus (Rat) |
P16009 | NEEDL_BPT4 | MEMISNNLNWFVGVVEDRMDPLKLGRVRVRVVGLHPPQRAQGDVMGIPTEKLPWMSVIQPITSAAMSGIGGSVTGPVEGTRVYGHFLDKWKTNGIVLGTYGGIVREKPNRLEGFSDPTGQYPRRLGNDTNVLNQGGEVGYDSSSNVIQDSNLDTAINPDDRPLSEIPTDDNPNMSMAEMLRRDEGLRLKVYWDTEGYPTIGIGHLIMKQPVRDMAQINKVLSKQVGREITGNPGSITMEEATTLFERDLADMQRDIKSHSKVGPVWQAVNRSRQMALENMAFQMGVGGVAKFNTMLTAMLAGDWEKAYKAGRDSLWYQQT... | 3.2.1.17 | null | cell wall macromolecule catabolic process [GO:0016998]; defense response to bacterium [GO:0042742]; killing of cells of another organism [GO:0031640]; peptidoglycan catabolic process [GO:0009253]; symbiont entry into host [GO:0044409]; symbiont entry into host cell [GO:0046718]; symbiont entry into host cell via disrup... | virus tail [GO:0098015]; virus tail, baseplate [GO:0098025] | identical protein binding [GO:0042802]; lysozyme activity [GO:0003796] | PF06715;PF06714;PF00959; | 1.10.530.40;3.10.450.190;2.40.50.260; | Glycosyl hydrolase 24 family | PTM: [Pre-baseplate central spike protein Gp5]: In the fully assembled virus, gp5 precursor is cleaved to form the mature tail lysozyme gp5*, and a C-terminus fragment, gp5C (PubMed:10217762, PubMed:15342608, PubMed:15701513). The two fragments remain associated with the virion (PubMed:10217762, PubMed:15342608). The e... | SUBCELLULAR LOCATION: [Baseplate central spike protein Gp5*]: Virion {ECO:0000255|HAMAP-Rule:MF_04151, ECO:0000269|PubMed:10217762, ECO:0000269|PubMed:15342608, ECO:0000269|PubMed:2403438, ECO:0000269|PubMed:27193680}. Note=Present in 3 copies in the baseplate. {ECO:0000255|HAMAP-Rule:MF_04151, ECO:0000269|PubMed:27193... | CATALYTIC ACTIVITY: [Baseplate central spike protein Gp5*]: Reaction=Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins.; EC=3.2.1.17; Evidence={ECO:0000255|HAMAP-Rule:MF_04151, ECO:0000269|P... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.8. {ECO:0000269|PubMed:3157805}; | null | FUNCTION: [Baseplate central spike protein Gp5*]: Baseplate central spike complex-associated lysozyme that is essential for the localized hydrolysis of bacterial cell wall, so that the tail tube, through which the phage DNA is ejected, can penetrate to the host inner membrane (PubMed:16956798, PubMed:21129200, PubMed:2... | Enterobacteria phage T4 (Bacteriophage T4) |
P16015 | CAH3_MOUSE | MAKEWGYASHNGPDHWHELYPIAKGDNQSPIELHTKDIKHDPSLQPWSASYDPGSAKTILNNGKTCRVVFDDTYDRSMLRGGPLSGPYRLRQFHLHWGSSDDHGSEHTVDGVKYAAELHLVHWNPKYNTFGEALKQPDGIAVVGIFLKIGREKGEFQILLDALDKIKTKGKEAPFTHFDPSCLFPACRDYWTYHGSFTTPPCEECIVWLLLKEPMTVSSDQMAKLRSLFSSAENEPPVPLVGNWRPPQPVKGRVVRASFK | 4.2.1.1 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P07451}; | one-carbon metabolic process [GO:0006730]; response to bacterium [GO:0009617]; response to oxidative stress [GO:0006979] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | carbonate dehydratase activity [GO:0004089]; nickel cation binding [GO:0016151]; phosphatase activity [GO:0016791]; zinc ion binding [GO:0008270] | PF00194; | 3.10.200.10; | Alpha-carbonic anhydrase family | PTM: S-thiolated both by thiol-disulfide exchange with glutathione disulfide and by oxyradical-initiated S-thiolation with reduced glutathione. {ECO:0000250|UniProtKB:P14141}.; PTM: S-glutathionylated in hepatocytes under oxidative stress. {ECO:0000250|UniProtKB:P14141}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P07451}. | CATALYTIC ACTIVITY: Reaction=H(+) + hydrogencarbonate = CO2 + H2O; Xref=Rhea:RHEA:10748, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:17544; EC=4.2.1.1; Evidence={ECO:0000250|UniProtKB:P07451}; | null | null | null | null | FUNCTION: Reversible hydration of carbon dioxide. {ECO:0000250|UniProtKB:P07451}. | Mus musculus (Mouse) |
P16027 | DHM1_METEA | MSRFVTSVSALAMLALAPAALSSGAYANDKLVELSKSDDNWVMPGKNYDSNNFSDLKQINKGNVKQLRPAWTFSTGLLNGHEGAPLVVDGKMYIHTSFPNNTFALGLDDPGTILWQDKPKQNPAARAVACCDLVNRGLAYWPGDGKTPALILKTQLDGNVAALNAETGETVWKVENSDIKVGSTLTIAPYVVKDKVIIGSSGAELGVRGYLTAYDVKTGEQVWRAYATGPDKDLLLASDFNIKNPHYGQKGLGTGTWEGDAWKIGGGTNWGWYAYDPGTNLIYFGTGNPAPWNETMRPGDNKWTMTIFGRDADTGEAKFG... | 1.1.2.7 | COFACTOR: Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442; Note=Binds 1 PQQ group per subunit. PQQ is inserted between disulfide Cys-130-Cys-131 and the indole ring of Trp-270.; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 1 Ca(2+) ion per subunit.; | methanol metabolic process [GO:0015945] | outer membrane-bounded periplasmic space [GO:0030288]; plasma membrane [GO:0005886] | alcohol dehydrogenase (cytochrome c(L)) activity [GO:0052933]; calcium ion binding [GO:0005509] | PF01011;PF13360; | 2.140.10.10; | Bacterial PQQ dehydrogenase family | null | SUBCELLULAR LOCATION: Cell inner membrane; Peripheral membrane protein; Periplasmic side. Note=Periplasmic, but associated with inner membrane. | CATALYTIC ACTIVITY: Reaction=a primary alcohol + 2 Fe(III)-[cytochrome cL] = an aldehyde + 2 Fe(II)-[cytochrome cL] + 2 H(+); Xref=Rhea:RHEA:51004, Rhea:RHEA-COMP:12863, Rhea:RHEA-COMP:12864, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734, ChEBI:CHEBI:17478, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.1.2.7; Evidence={ECO:0000269... | null | null | null | null | FUNCTION: Catalyzes the oxidation of primary alcohols including methanol. | Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1) (Methylobacterium extorquens) |
P16033 | PSBA2_SYNY3 | MTTTLQQRESASLWEQFCQWVTSTNNRIYVGWFGTLMIPTLLTATTCFIIAFIAAPPVDIDGIREPVAGSLLYGNNIISGAVVPSSNAIGLHFYPIWEAASLDEWLYNGGPYQLVVFHFLIGIFCYMGRQWELSYRLGMRPWICVAYSAPVSAATAVFLIYPIGQGSFSDGMPLGISGTFNFMIVFQAEHNILMHPFHMLGVAGVFGGSLFSAMHGSLVTSSLVRETTEVESQNYGYKFGQEEETYNIVAAHGYFGRLIFQYASFNNSRSLHFFLGAWPVIGIWFTAMGVSTMAFNLNGFNFNQSILDSQGRVIGTWADV... | 1.10.3.9 | COFACTOR: Note=The D1/D2 heterodimer binds P680, chlorophylls that are the primary electron donor of PSII, and subsequent electron acceptors. It shares a non-heme iron and each subunit binds pheophytin, quinone, additional chlorophylls, carotenoids and lipids. D1 provides most of the ligands for the Mn4-Ca-O5 cluster o... | photosynthetic electron transport in photosystem II [GO:0009772]; response to herbicide [GO:0009635] | plasma membrane-derived thylakoid membrane [GO:0031676]; plasma membrane-derived thylakoid photosystem II [GO:0030096] | chlorophyll binding [GO:0016168]; electron transporter, transferring electrons within the cyclic electron transport pathway of photosynthesis activity [GO:0045156]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on diphenols and related substances as donors, oxygen as acceptor [GO:0016682]; oxygen evolv... | PF00124; | 1.20.85.10; | Reaction center PufL/M/PsbA/D family | PTM: C-terminally processed by CtpA; processing is essential to allow assembly of the oxygen-evolving complex and photosynthetic growth. {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000269|PubMed:34937700, ECO:0000305|PubMed:8034700}.; PTM: Tyr-161 forms a radical intermediate that is referred to as redox-active TyrZ, YZ or ... | SUBCELLULAR LOCATION: Cellular thylakoid membrane {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000269|PubMed:12069591, ECO:0000269|PubMed:34937700, ECO:0000305|PubMed:9512353}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01379, ECO:0000269|PubMed:34937700, ECO:0000305|PubMed:9512353}. | CATALYTIC ACTIVITY: Reaction=2 a plastoquinone + 2 H2O + 4 hnu = 2 a plastoquinol + O2; Xref=Rhea:RHEA:36359, Rhea:RHEA-COMP:9561, Rhea:RHEA-COMP:9562, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:17757, ChEBI:CHEBI:30212, ChEBI:CHEBI:62192; EC=1.10.3.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01379}; | null | null | null | null | FUNCTION: Photosystem II (PSII) is a light-driven water:plastoquinone oxidoreductase that uses light energy to abstract electrons from H(2)O, generating O(2) and a proton gradient subsequently used for ATP formation. It consists of a core antenna complex that captures photons, and an electron transfer chain that conver... | Synechocystis sp. (strain PCC 6803 / Kazusa) |
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