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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P08564 | POLS_RUBVV | MASTTPITMEDLQKALEAQSRALRAELAAGASQSRRPRPPRQRDSSTSGDDSGRDSGGPRRRRGNRGRGQLRDWSRAPPPPEERQESRSQTPAPKPSRAPPQQPQPPRMQTGRGGSAPRPELGPPTNPFQAAVARGLRPPLHDPDTEAPTEACVTSWLWSEGEGAVFYRVDLHFTNLGTPPLDEDGRWDPALMYNPCGPEPPAHVVRAYNQPAGDVRGVWGKGERTYAEQDFRVGGTRWHRLLRMPVRGLDGDSAPLPPHTTERIETRSARHPWRIRFGAPQAFLAGLLLAAVAVGTARAGLQPRADMAAPPTLPQPPRA... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; virion attachment to host cell [GO:0019062] | host cell Golgi membrane [GO:0044178]; host cell mitochondrion [GO:0033650]; membrane [GO:0016020]; T=4 icosahedral viral capsid [GO:0039619]; viral envelope [GO:0019031]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | metal ion binding [GO:0046872]; RNA binding [GO:0003723] | PF05750;PF05748;PF05749; | 2.60.98.30;3.30.67.20;2.60.40.2650;3.10.50.50; | null | PTM: Structural polyprotein: Specific enzymatic cleavages in vivo yield mature proteins. Two signal peptidase-mediated cleavages within the polyprotein produce the structural proteins capsid, E2, and E1. The E2 signal peptide remains attached to the C-terminus of the capsid protein after cleavage by the signal peptidas... | SUBCELLULAR LOCATION: [Capsid protein]: Virion {ECO:0000250|UniProtKB:P08563}. Host cytoplasm. Host mitochondrion {ECO:0000250|UniProtKB:P08563}. Note=The capsid protein is concentrated around Golgi region (By similarity). In the virion, it is probably associated to the viral membrane (By similarity). {ECO:0000250|UniP... | null | null | null | null | null | FUNCTION: [Capsid protein]: Capsid protein interacts with genomic RNA and assembles into icosahedric core particles 65-70 nm in diameter. The resulting nucleocapsid eventually associates with the cytoplasmic domain of E2 at the cell membrane, leading to budding and formation of mature virions from host Golgi membranes.... | Rubella virus (strain TO-336) (RUBV) |
P08566 | ARO1_YEAST | MVQLAKVPILGNDIIHVGYNIHDHLVETIIKHCPSSTYVICNDTNLSKVPYYQQLVLEFKASLPEGSRLLTYVVKPGETSKSRETKAQLEDYLLVEGCTRDTVMVAIGGGVIGDMIGFVASTFMRGVRVVQVPTSLLAMVDSSIGGKTAIDTPLGKNFIGAFWQPKFVLVDIKWLETLAKREFINGMAEVIKTACIWNADEFTRLESNASLFLNVVNGAKNVKVTNQLTNEIDEISNTDIEAMLDHTYKLVLESIKVKAEVVSSDERESSLRNLLNFGHSIGHAYEAILTPQALHGECVSIGMVKEAELSRYFGILSPTQ... | 1.1.1.25; 2.5.1.19; 2.7.1.71; 4.2.1.10; 4.2.3.4 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-Rule:MF_03143}; | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737] | 3-dehydroquinate dehydratase activity [GO:0003855]; 3-dehydroquinate synthase activity [GO:0003856]; 3-phosphoshikimate 1-carboxyvinyltransferase activity [GO:0003866]; ATP binding [GO:0005524]; metal ion binding [GO:0046872]; shikimate 3-dehydrogenase (NADP+) activity [GO:0004764]; shikimate kinase activity [GO:000476... | PF01761;PF01487;PF00275;PF18317;PF01488;PF08501;PF01202; | 3.40.50.1970;3.20.20.70;1.20.1090.10;3.65.10.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Sugar phosphate cyclases superfamily, Dehydroquinate synthase family; EPSP synthase family; Shikimate kinase family; Type-I 3-dehydroquinase family; Shikimate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate; Xref=Rhea:RHEA:21968, ChEBI:CHEBI:32364, ChEBI:CHEBI:43474, ChEBI:CHEBI:58394; EC=4.2.3.4; Evidence={ECO:0000255|HAMAP-Rule:MF_03143}; CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xr... | null | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7. {ECO:0000255|HAMAP-Rule:MF_03143}.; PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: st... | null | null | FUNCTION: The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P08567 | PLEK_HUMAN | MEPKRIREGYLVKKGSVFNTWKPMWVVLLEDGIEFYKKKSDNSPKGMIPLKGSTLTSPCQDFGKRMFVFKITTTKQQDHFFQAAFLEERDAWVRDIKKAIKCIEGGQKFARKSTRRSIRLPETIDLGALYLSMKDTEKGIKELNLEKDKKIFNHCFTGNCVIDWLVSNQSVRNRQEGLMIASSLLNEGYLQPAGDMSKSAVDGTAENPFLDNPDAFYYFPDSGFFCEENSSDDDVILKEEFRGVIIKQGCLLKQGHRRKNWKVRKFILREDPAYLHYYDPAGAEDPLGAIHLRGCVVTSVESNSNGRKSEEENLFEIITA... | null | null | actin cytoskeleton organization [GO:0030036]; cell projection organization [GO:0030030]; cortical actin cytoskeleton organization [GO:0030866]; hematopoietic progenitor cell differentiation [GO:0002244]; integrin-mediated signaling pathway [GO:0007229]; negative regulation of calcium-mediated signaling [GO:0050849]; ne... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; membrane [GO:0016020]; plasma membrane [GO:0005886]; ruffle membrane [GO:0032587] | phosphatidylinositol-3,4-bisphosphate binding [GO:0043325]; protein homodimerization activity [GO:0042803]; protein kinase C binding [GO:0005080] | PF00610;PF00169; | 2.30.29.30;1.10.10.10; | null | null | null | null | null | null | null | null | FUNCTION: Major protein kinase C substrate of platelets. | Homo sapiens (Human) |
P08569 | MSP1_PLAFM | MKIIFFLCSFLFFIINTQCVTHESYQELVKKLEALEDAVLTGYSLFQKEKMVLNEGTSGTAVTTSTPGSSGSVTSGGSVASVASVASGGSGGSVASGGSGNSRRTNPSDNSSDSNTKTYADLKHRVQNYLFTIKELKYPELFDLTNHMLTLSKNVDGFKYLIDGYEEINELLYKLNFYYDLLRAKLNDACANSYCQIPFNLKIRANELDVLKKIVFGYRKPLDNIKDNVGKMEDYIKKNKTTIANINELIEGSKKTIDQNKNADNEEGKKKLYQAQYNLFIYNKQLQEAHNLISVLEKRIDTLKKNENIKKLLEDIDKIK... | null | null | null | extracellular region [GO:0005576]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]; vacuolar membrane [GO:0005774] | null | PF12946;PF07462; | 2.10.25.10; | null | PTM: The p190 precursor is cleaved by SUB1 prior to merozoite egress into 4 subunits p83, p30, p38, and p42 which remain non-covalently associated (PubMed:1474993). SUB1-mediated proteolytic cleavage occurs in an orderly manner; the first cleavage occurs at the p30/p38 site, followed by cleavage at the p83/p30 site, th... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8I0U8}; Lipid-anchor, GPI-anchor {ECO:0000255}. Secreted {ECO:0000250|UniProtKB:Q8I0U8}.; SUBCELLULAR LOCATION: [p19 subunit]: Cell membrane {ECO:0000250|UniProtKB:Q8I0U8}; Lipid-anchor, GPI-anchor {ECO:0000255}. Vacuole membrane {ECO:0000250|UniProtKB:Q8I0U8}... | null | null | null | null | null | FUNCTION: During the asexual blood stage, involved in merozoite egress from host erythrocytes possibly via its interaction with the host cytoskeleton protein spectrin resulting in the destabilization of the host cytoskeleton and thus leading to erythrocyte cell membrane rupture. Involved in the binding to host erythroc... | Plasmodium falciparum (isolate mad20 / Papua New Guinea) |
P08570 | RLA1_DROME | MSTKAELACVYASLILVDDDVAVTGEKINTILKAANVEVEPYWPGLFAKALEGINVKDLITNIGSGVGAAPAGGAAPAAAAAAPAAESKKEEKKKEEESDQSDDDMGFGLFD | null | null | cytoplasmic translation [GO:0002181]; translational elongation [GO:0006414] | cytosolic large ribosomal subunit [GO:0022625]; cytosolic ribosome [GO:0022626] | protein kinase activator activity [GO:0030295]; ribonucleoprotein complex binding [GO:0043021]; structural constituent of ribosome [GO:0003735] | PF00428; | 1.10.10.1410; | Eukaryotic ribosomal protein P1/P2 family | null | null | null | null | null | null | null | FUNCTION: Plays an important role in the elongation step of protein synthesis. | Drosophila melanogaster (Fruit fly) |
P08571 | CD14_HUMAN | MERASCLLLLLLPLVHVSATTPEPCELDDEDFRCVCNFSEPQPDWSEAFQCVSAVEVEIHAGGLNLEPFLKRVDADADPRQYADTVKALRVRRLTVGAAQVPAQLLVGALRVLAYSRLKELTLEDLKITGTMPPLPLEATGLALSSLRLRNVSWATGRSWLAELQQWLKPGLKVLSIAQAHSPAFSCEQVRAFPALTSLDLSDNPGLGERGLMAALCPHKFPAIQNLALRNTGMETPTGVCAALAAAGVQPHSLDLSHNSLRATVNPSAPRCMWSSALNSLNLSFAGLEQVPKGLPAKLRVLDLSCNRLNRAPQPDELPE... | null | null | apoptotic process [GO:0006915]; cell surface pattern recognition receptor signaling pathway [GO:0002752]; cell surface receptor signaling pathway [GO:0007166]; cellular response to diacyl bacterial lipopeptide [GO:0071726]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to lipoteichoic acid [GO... | endosome membrane [GO:0010008]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; lipopolysaccharide receptor complex [GO:0046696]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]... | lipopolysaccharide binding [GO:0001530]; lipopolysaccharide immune receptor activity [GO:0001875]; lipoteichoic acid binding [GO:0070891]; opsonin receptor activity [GO:0001847]; peptidoglycan immune receptor activity [GO:0016019] | PF13516; | 3.80.10.10; | null | PTM: N- and O- glycosylated. O-glycosylated with a core 1 or possibly core 8 glycan. {ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19838169}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1698311, ECO:0000269|PubMed:2462937, ECO:0000269|PubMed:3385210}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:1698311, ECO:0000269|PubMed:2462937, ECO:0000269|PubMed:3385210}. Secreted {ECO:0000269|PubMed:25497142, ECO:0000269|PubMed:2779588}. Membrane raft {ECO:... | null | null | null | null | null | FUNCTION: Coreceptor for bacterial lipopolysaccharide (PubMed:1698311, PubMed:23264655). In concert with LBP, binds to monomeric lipopolysaccharide and delivers it to the LY96/TLR4 complex, thereby mediating the innate immune response to bacterial lipopolysaccharide (LPS) (PubMed:20133493, PubMed:22265692, PubMed:23264... | Homo sapiens (Human) |
P08572 | CO4A2_HUMAN | MGRDQRAVAGPALRRWLLLGTVTVGFLAQSVLAGVKKFDVPCGGRDCSGGCQCYPEKGGRGQPGPVGPQGYNGPPGLQGFPGLQGRKGDKGERGAPGVTGPKGDVGARGVSGFPGADGIPGHPGQGGPRGRPGYDGCNGTQGDSGPQGPPGSEGFTGPPGPQGPKGQKGEPYALPKEERDRYRGEPGEPGLVGFQGPPGRPGHVGQMGPVGAPGRPGPPGPPGPKGQQGNRGLGFYGVKGEKGDVGQPGPNGIPSDTLHPIIAPTGVTFHPDQYKGEKGSEGEPGIRGISLKGEEGIMGFPGLRGYPGLSGEKGSPGQKG... | null | null | angiogenesis [GO:0001525]; cellular response to transforming growth factor beta stimulus [GO:0071560]; collagen-activated tyrosine kinase receptor signaling pathway [GO:0038063]; DNA-templated transcription [GO:0006351]; endodermal cell differentiation [GO:0035987]; extracellular matrix organization [GO:0030198]; glome... | basement membrane [GO:0005604]; collagen type IV trimer [GO:0005587]; collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | extracellular matrix structural constituent [GO:0005201]; extracellular matrix structural constituent conferring tensile strength [GO:0030020]; molecular adaptor activity [GO:0060090] | PF01413;PF01391; | 2.170.240.10; | Type IV collagen family | PTM: Prolines at the third position of the tripeptide repeating unit (G-X-Y) are hydroxylated in some or all of the chains.; PTM: Type IV collagens contain numerous cysteine residues which are involved in inter- and intramolecular disulfide bonding. 12 of these, located in the NC1 domain, are conserved in all known typ... | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. | null | null | null | null | null | FUNCTION: Type IV collagen is the major structural component of glomerular basement membranes (GBM), forming a 'chicken-wire' meshwork together with laminins, proteoglycans and entactin/nidogen.; FUNCTION: Canstatin, a cleavage product corresponding to the collagen alpha 2(IV) NC1 domain, possesses both anti-angiogenic... | Homo sapiens (Human) |
P08574 | CY1_HUMAN | MAAAAASLRGVVLGPRGAGLPGARARGLLCSARPGQLPLRTPQAVALSSKSGLSRGRKVMLSALGMLAAGGAGLAMALHSAVSASDLELHPPSYPWSHRGLLSSLDHTSIRRGFQVYKQVCASCHSMDFVAYRHLVGVCYTEDEAKELAAEVEVQDGPNEDGEMFMRPGKLFDYFPKPYPNSEAARAANNGALPPDLSYIVRARHGGEDYVFSLLTGYCEPPTGVSLREGLYFNPYFPGQAIAMAPPIYTDVLEFDDGTPATMSQIAKDVCTFLRWASEPEHDHRKRMGLKMLMMMALLVPLVYTIKRHKWSVLKSRKLA... | 7.1.1.8 | COFACTOR: Name=heme c; Xref=ChEBI:CHEBI:61717; Evidence={ECO:0000269|PubMed:28844695}; Note=Binds 1 heme c group covalently per subunit. {ECO:0000269|PubMed:28844695}; | cellular respiration [GO:0045333]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]; response to glucagon [GO:0033762] | membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex III [GO:0005750]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | heme binding [GO:0020037]; metal ion binding [GO:0046872]; ubiquinol-cytochrome-c reductase activity [GO:0008121] | PF02167; | 1.10.760.10;1.20.5.100; | Cytochrome c family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P07143}; Single-pass membrane protein {ECO:0000250|UniProtKB:P07143}. | CATALYTIC ACTIVITY: Reaction=a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2 Fe(II)-[cytochrome c](out) + 2 H(+)(out); Xref=Rhea:RHEA:11484, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:132124; EC=7.1.1.8; Evidence={ECO:0000... | null | null | null | null | FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrom... | Homo sapiens (Human) |
P08575 | PTPRC_HUMAN | MTMYLWLKLLAFGFAFLDTEVFVTGQSPTPSPTGLTTAKMPSVPLSSDPLPTHTTAFSPASTFERENDFSETTTSLSPDNTSTQVSPDSLDNASAFNTTGVSSVQTPHLPTHADSQTPSAGTDTQTFSGSAANAKLNPTPGSNAISDVPGERSTASTFPTDPVSPLTTTLSLAHHSSAALPARTSNTTITANTSDAYLNASETTTLSPSGSAVISTTTIATTPSKPTCDEKYANITVDYLYNKETKLFTAKLNVNENVECGNNTCTNNEVHNLTECKNASVSISHNSCTAPDKTLILDVPPGVEKFQLHDCTQVEKADTT... | 3.1.3.48 | null | alpha-beta T cell proliferation [GO:0046633]; B cell differentiation [GO:0030183]; B cell proliferation [GO:0042100]; B cell receptor signaling pathway [GO:0050853]; bone marrow development [GO:0048539]; calcium-mediated signaling using intracellular calcium source [GO:0035584]; cell cycle phase transition [GO:0044770]... | bleb [GO:0032059]; cell surface [GO:0009986]; cytoplasmic side of plasma membrane [GO:0009898]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; membrane microdomain [GO:0098857]; membrane raft [GO:0045121]; plasma membrane [GO:000588... | ankyrin binding [GO:0030506]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; protein kinase binding [GO:0019901]; protein tyrosine phosphatase activity [GO:0004725]; signaling receptor binding [GO:0005102]; spectrin binding [GO:0030507]; transmembrane receptor protein tyrosine phosphat... | PF12567;PF00041;PF12453;PF00102; | 2.60.40.10;3.90.190.10; | Protein-tyrosine phosphatase family, Receptor class 1/6 subfamily | PTM: Heavily N- and O-glycosylated. {ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:19349973}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12676959, ECO:0000269|PubMed:22174689}; Single-pass type I membrane protein {ECO:0000255}. Membrane raft {ECO:0000269|PubMed:12676959}. Synapse {ECO:0000269|PubMed:35767951}. Note=Colocalized with DPP4 in membrane rafts. {ECO:0000269|PubMed:12676959}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044}; | null | null | null | null | FUNCTION: Protein tyrosine-protein phosphatase required for T-cell activation through the antigen receptor (PubMed:35767951). Acts as a positive regulator of T-cell coactivation upon binding to DPP4. The first PTPase domain has enzymatic activity, while the second one seems to affect the substrate specificity of the fi... | Homo sapiens (Human) |
P08579 | RU2B_HUMAN | MDIRPNHTIYINNMNDKIKKEELKRSLYALFSQFGHVVDIVALKTMKMRGQAFVIFKELGSSTNALRQLQGFPFYGKPMRIQYAKTDSDIISKMRGTFADKEKKKEKKKAKTVEQTATTTNKKPGQGTPNSANTQGNSTPNPQVPDYPPNYILFLNNLPEETNEMMLSMLFNQFPGFKEVRLVPGRHDIAFVEFENDGQAGAARDALQGFKITPSHAMKITYAKK | null | null | mRNA splicing, via spliceosome [GO:0000398]; U2-type prespliceosome assembly [GO:1903241] | catalytic step 2 spliceosome [GO:0071013]; cytoplasmic ribonucleoprotein granule [GO:0036464]; fibrillar center [GO:0001650]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spliceosomal complex [GO:0005681]; U1 snRNP [GO:0005685]; U2 snRNP [GO:0005686]; U2-type catalytic step 2 spliceosome ... | U1 snRNA binding [GO:0030619] | PF00076; | 3.30.70.330; | RRM U1 A/B'' family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28076346, ECO:0000269|PubMed:28502770, ECO:0000269|PubMed:28781166}. | null | null | null | null | null | FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome (PubMed:11991638, PubMed:28076346, PubMed:28502770, PubMed:28781166, PubMed:32494006). Associated with sn-RNP U2, where it contributes to the binding of stem loop IV of U2 snRNA (PubMed:32494006, PubMed:9716128). {ECO:0000269|PubMed:11991638, ECO:0... | Homo sapiens (Human) |
P08581 | MET_HUMAN | MKAPAVLAPGILVLLFTLVQRSNGECKEALAKSEMNVNMKYQLPNFTAETPIQNVILHEHHIFLGATNYIYVLNEEDLQKVAEYKTGPVLEHPDCFPCQDCSSKANLSGGVWKDNINMALVVDTYYDDQLISCGSVNRGTCQRHVFPHNHTADIQSEVHCIFSPQIEEPSQCPDCVVSALGAKVLSSVKDRFINFFVGNTINSSYFPDHPLHSISVRRLKETKDGFMFLTDQSYIDVLPEFRDSYPIKYVHAFESNNFIYFLTVQRETLDAQTFHTRIIRFCSINSGLHSYMEMPLECILTEKRKKRSTKKEVFNILQAA... | 2.7.10.1 | null | branching morphogenesis of an epithelial tube [GO:0048754]; cell migration [GO:0016477]; cell surface receptor signaling pathway [GO:0007166]; endothelial cell morphogenesis [GO:0001886]; establishment of skin barrier [GO:0061436]; liver development [GO:0001889]; negative regulation of autophagy [GO:0010507]; negative ... | basal plasma membrane [GO:0009925]; cell surface [GO:0009986]; extracellular region [GO:0005576]; membrane [GO:0016020]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]; semaphorin receptor complex [GO:0002116] | ATP binding [GO:0005524]; hepatocyte growth factor receptor activity [GO:0005008]; identical protein binding [GO:0042802]; molecular function activator activity [GO:0140677]; protein phosphatase binding [GO:0019903]; protein tyrosine kinase activity [GO:0004713]; semaphorin receptor activity [GO:0017154] | PF07714;PF01437;PF01403;PF01833; | 2.60.40.10;1.10.510.10;2.130.10.10; | Protein kinase superfamily, Tyr protein kinase family | PTM: Autophosphorylated in response to ligand binding on Tyr-1234 and Tyr-1235 in the kinase domain leading to further phosphorylation of Tyr-1349 and Tyr-1356 in the C-terminal multifunctional docking site. Dephosphorylated by PTPRJ at Tyr-1349 and Tyr-1365. Dephosphorylated by PTPN1 and PTPN2. {ECO:0000269|PubMed:124... | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to hepatocyte growth factor/HGF ligand. Regulates many physiological processes including proliferation, scattering, morphogenesis and survival. Ligand binding at the cell surface induces autophosphoryl... | Homo sapiens (Human) |
P08582 | TRFM_HUMAN | MRGPSGALWLLLALRTVLGGMEVRWCATSDPEQHKCGNMSEAFREAGIQPSLLCVRGTSADHCVQLIAAQEADAITLDGGAIYEAGKEHGLKPVVGEVYDQEVGTSYYAVAVVRRSSHVTIDTLKGVKSCHTGINRTVGWNVPVGYLVESGRLSVMGCDVLKAVSDYFGGSCVPGAGETSYSESLCRLCRGDSSGEGVCDKSPLERYYDYSGAFRCLAEGAGDVAFVKHSTVLENTDGKTLPSWGQALLSQDFELLCRDGSRADVTEWRQCHLARVPAHAVVVRADTDGGLIFRLLNEGQRLFSHEGSSFQMFSSEAYGQ... | null | null | iron ion transport [GO:0006826]; negative regulation of substrate adhesion-dependent cell spreading [GO:1900025]; positive regulation of extracellular matrix disassembly [GO:0090091]; positive regulation of plasminogen activation [GO:0010756] | cell surface [GO:0009986]; early endosome [GO:0005769]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; side of membrane [GO:0098552] | iron ion binding [GO:0005506] | PF00405; | 3.40.190.10; | Transferrin family | null | SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Lipid-anchor, GPI-anchor. | null | null | null | null | null | FUNCTION: Involved in iron cellular uptake. Seems to be internalized and then recycled back to the cell membrane. Binds a single atom of iron per subunit. Could also bind zinc. {ECO:0000269|PubMed:7556058}. | Homo sapiens (Human) |
P08587 | TGM2_CAVCU | MAEDLILERCDLQLEVNGRDHRTADLCRERLVLRRGQPFWLTLHFEGRGYEAGVDTLTFNAVTGPDPSEEAGTMARFSLSSAVEGGTWSASAVDQQDSTVSLLLSTPADAPIGLYRLSLEASTGYQGSSFVLGHFILLYNPRCPADAVYMDSDQERQEYVLTQQGFIYQGSAKFINGIPWNFGQFEDGILDICLMLLDTNPKFLKNAGQDCSRRSRPVYVGRVVSAMVNCNDDQGVLQGRWDNNYSDGVSPMSWIGSVDILRRWKDYGCQRVKYGQCWVFAAVACTVLRCLGIPTRVVTNFNSAHDQNSNLLIEYFRNES... | 2.3.1.-; 2.3.2.13; 3.4.-.-; 3.5.1.44 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P21980}; | cellular response to dopamine [GO:1903351]; cellular response to serotonin [GO:1904015]; peptide cross-linking [GO:0018149]; phospholipase C-activating G protein-coupled receptor signaling pathway [GO:0007200]; positive regulation of apoptotic process [GO:0043065]; positive regulation of GTPase activity [GO:0043547]; p... | chromatin [GO:0000785]; collagen-containing extracellular matrix [GO:0062023]; cytosol [GO:0005829]; extracellular region [GO:0005576]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | calcium ion binding [GO:0005509]; GTP binding [GO:0005525]; histone dopaminyltransferase activity [GO:0120297]; histone serotonyltransferase activity [GO:0120295]; peptidase activity [GO:0008233]; peptide dopaminyltransferase activity [GO:0120296]; peptide histaminyltransferase activity [GO:0120299]; peptide noradrenal... | PF00927;PF01841;PF00868; | 2.60.40.10;3.90.260.10; | Transglutaminase superfamily, Transglutaminase family | PTM: Disulfide bond formation inactivates the calcium-dependent acyltransferase activity. Cys-370 can form disulfide bonds with both Cys-230 and Cys-371: formation of a disulfide bond between Cys-230 and Cys-370 facilitates formation of the disulfide between Cys-370 and Cys-371, which promotes inactivation of the acylt... | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P21980}. Nucleus {ECO:0000250|UniProtKB:P21980}. Chromosome {ECO:0000250|UniProtKB:P21980}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P21980}. Cell membrane {ECO:0000250|UniProtKB:Q9WVJ6}. Mitochondrion {ECO:0000250|UniProt... | CATALYTIC ACTIVITY: Reaction=L-glutaminyl-[protein] + L-lysyl-[protein] = [protein]-L-lysyl-N(6)-5-L-glutamyl-[protein] + NH4(+); Xref=Rhea:RHEA:54816, Rhea:RHEA-COMP:9752, Rhea:RHEA-COMP:10207, Rhea:RHEA-COMP:14005, ChEBI:CHEBI:28938, ChEBI:CHEBI:29969, ChEBI:CHEBI:30011, ChEBI:CHEBI:138370; EC=2.3.2.13; Evidence={ECO... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=794.1 nM for serotonin (for protein-glutamine serotonyltransferase activity) {ECO:0000269|PubMed:22858378}; | null | null | null | FUNCTION: Calcium-dependent acyltransferase that catalyzes the formation of covalent bonds between peptide-bound glutamine and various primary amines, such as gamma-amino group of peptide-bound lysine, or mono- and polyamines, thereby producing cross-linked or aminated proteins, respectively (PubMed:14697203, PubMed:16... | Cavia cutleri (Guinea pig) |
P08588 | ADRB1_HUMAN | MGAGVLVLGASEPGNLSSAAPLPDGAATAARLLVPASPPASLLPPASESPEPLSQQWTAGMGLLMALIVLLIVAGNVLVIVAIAKTPRLQTLTNLFIMSLASADLVMGLLVVPFGATIVVWGRWEYGSFFCELWTSVDVLCVTASIETLCVIALDRYLAITSPFRYQSLLTRARARGLVCTVWAISALVSFLPILMHWWRAESDEARRCYNDPKCCDFVTNRAYAIASSVVSFYVPLCIMAFVYLRVFREAQKQVKKIDSCERRFLGGPARPPSPSPSPVPAPAPPPGPPRPAAAAATAPLANGRAGKRRPSRLVALREQ... | null | null | adenylate cyclase-activating adrenergic receptor signaling pathway [GO:0071880]; brown fat cell differentiation [GO:0050873]; diet induced thermogenesis [GO:0002024]; fear response [GO:0042596]; heat generation [GO:0031649]; negative regulation of multicellular organism growth [GO:0040015]; norepinephrine-epinephrine-m... | early endosome [GO:0005769]; neuronal dense core vesicle [GO:0098992]; plasma membrane [GO:0005886]; Schaffer collateral - CA1 synapse [GO:0098685] | alpha-2A adrenergic receptor binding [GO:0031694]; beta-adrenergic receptor activity [GO:0004939]; beta1-adrenergic receptor activity [GO:0004940]; G protein-coupled neurotransmitter receptor activity involved in regulation of postsynaptic membrane potential [GO:0099579]; PDZ domain binding [GO:0030165]; protein hetero... | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family, Adrenergic receptor subfamily, ADRB1 sub-subfamily | PTM: Homologous desensitization of the receptor is mediated by its phosphorylation by beta-adrenergic receptor kinase. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P18090}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P18090}. Early endosome. Note=Colocalizes with RAPGEF2 at the plasma membrane (By similarity). Localized at the plasma membrane. Found in the Golgi upon GOPC overexpression. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. This receptor binds epinephrine and norepinephrine with approximately equal affinity. Mediates Ras activation through G(s)-alpha- and cAMP-mediated signaling. Involved in the regulatio... | Homo sapiens (Human) |
P08590 | MYL3_HUMAN | MAPKKPEPKKDDAKAAPKAAPAPAPPPEPERPKEVEFDASKIKIEFTPEQIEEFKEAFMLFDRTPKCEMKITYGQCGDVLRALGQNPTQAEVLRVLGKPRQEELNTKMMDFETFLPMLQHISKNKDTGTYEDFVEGLRVFDKEGNGTVMGAELRHVLATLGERLTEDEVEKLMAGQEDSNGCINYEAFVKHIMSS | null | null | cardiac muscle contraction [GO:0060048]; positive regulation of ATP-dependent activity [GO:0032781]; regulation of striated muscle contraction [GO:0006942]; regulation of the force of heart contraction [GO:0002026]; ventricular cardiac muscle tissue morphogenesis [GO:0055010] | A band [GO:0031672]; cytosol [GO:0005829]; I band [GO:0031674]; muscle myosin complex [GO:0005859]; myosin II complex [GO:0016460]; sarcomere [GO:0030017] | actin monomer binding [GO:0003785]; calcium ion binding [GO:0005509]; myosin II heavy chain binding [GO:0032038]; structural constituent of muscle [GO:0008307] | null | 1.10.238.10; | null | PTM: The N-terminus is blocked.; PTM: N-terminus is methylated by METTL11A/NTM1. {ECO:0000250}. | null | null | null | null | null | null | FUNCTION: Regulatory light chain of myosin. Does not bind calcium. | Homo sapiens (Human) |
P08592 | A4_RAT | MLPSLALLLLAAWTVRALEVPTDGNAGLLAEPQIAMFCGKLNMHMNVQNGKWESDPSGTKTCIGTKEGILQYCQEVYPELQITNVVEANQPVTIQNWCKRGRKQCKTHTHIVIPYRCLVGEFVSDALLVPDKCKFLHQERMDVCETHLHWHTVAKETCSEKSTNLHDYGMLLPCGIDKFRGVEFVCCPLAEESDSIDSADAEEDDSDVWWGGADTDYADGGEDKVVEVAEEEEVADVEEEEAEDDEDVEDGDEVEEEAEEPYEEATERTTSIATTTTTTTESVEEVVREVCSEQAETGPCRAMISRWYFDVTEGKCAPFF... | null | null | adult locomotory behavior [GO:0008344]; amyloid fibril formation [GO:1990000]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; astrocyte activation [GO:0048143]; astrocyte activation involved in immune response [GO:0002265]; axo-dendritic transport [GO:0008088]; axon midline choice... | amyloid-beta complex [GO:0106003]; apical part of cell [GO:0045177]; astrocyte projection [GO:0097449]; axon [GO:0030424]; cell surface [GO:0009986]; cell-cell junction [GO:0005911]; ciliary rootlet [GO:0035253]; clathrin-coated pit [GO:0005905]; COPII-coated ER to Golgi transport vesicle [GO:0030134]; cytoplasm [GO:00... | apolipoprotein binding [GO:0034185]; DNA binding [GO:0003677]; enzyme binding [GO:0019899]; frizzled binding [GO:0005109]; growth factor receptor binding [GO:0070851]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; ion binding [GO:0043167]; low-d... | PF10515;PF12924;PF12925;PF02177;PF03494;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 | PTM: Proteolytically processed under normal cellular conditions. Cleavage either by alpha-secretase, beta-secretase or theta-secretase leads to generation and extracellular release of soluble APP peptides, S-APP-alpha and S-APP-beta, and the retention of corresponding membrane-anchored C-terminal fragments, C80, C83 an... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P05067}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P05067}. Membrane {ECO:0000250|UniProtKB:P05067}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P05067}. Perikaryon {ECO:0000269|PubMed:10341243}. Cell projection, growth cone {ECO... | null | null | null | null | null | FUNCTION: Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Interaction between APP molecules on neighboring cells promotes synaptogenesis. Involved in cell mobility and transcription regulation through pro... | Rattus norvegicus (Rat) |
P08594 | AQL1_THEAQ | MRKTYWLMALFAVLVLGGCQMASRSDPTPTLAEAFWPKEAPVYGLDDPEAIPGRYIVVFKKGKGQSLLQGGITTLQARLAPQGVVVTQAYTGALQGFAAEMAPQALEAFRQSPDVEFIEADKVVRAWATQSPAPWGLDRIDQRDLPLSNSYTYTATGRGVNVYVIDTGIRTTHREFGGRARVGYDALGGNGQDCNGHGTHVAGTIGGVTYGVAKAVNLYAVRVLDCNGSGSTSGVIAGVDWVTRNHRRPAVANMSLGGGVSTALDNAVKNSIAAGVVYAVAAGNDNANACNYSPARVAEALTVGATTSSDARASFSNYGS... | 3.4.21.111 | null | proteolysis [GO:0006508] | extracellular space [GO:0005615] | serine-type endopeptidase activity [GO:0004252] | PF05922;PF00082; | 2.60.120.380;3.30.70.80;3.40.50.200; | Peptidase S8 family | PTM: The N- and C-terminal Pro-sequences are successively removed through the proteolytic activity of PstI itself. The C-terminal Pro-sequence is required for translocation of the proteases across the outer membrane. | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Exhibits low specificity toward esters of amino acids with small hydrophobic or aromatic residues at the P1 position.; EC=3.4.21.111; | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 80 degrees Celsius for caseinolytic activity.; | FUNCTION: Aqualysin I is a thermophilic alkaline serine protease. | Thermus aquaticus |
P08603 | CFAH_HUMAN | MRLLAKIICLMLWAICVAEDCNELPPRRNTEILTGSWSDQTYPEGTQAIYKCRPGYRSLGNVIMVCRKGEWVALNPLRKCQKRPCGHPGDTPFGTFTLTGGNVFEYGVKAVYTCNEGYQLLGEINYRECDTDGWTNDIPICEVVKCLPVTAPENGKIVSSAMEPDREYHFGQAVRFVCNSGYKIEGDEEMHCSDDGFWSKEKPKCVEISCKSPDVINGSPISQKIIYKENERFQYKCNMGYEYSERGDAVCTESGWRPLPSCEEKSCDNPYIPNGDYSPLRIKHRTGDEITYQCRNGFYPATRGNTAKCTSTGWIPAPRC... | null | null | complement activation [GO:0006956]; complement activation, alternative pathway [GO:0006957]; proteolysis [GO:0006508]; regulation of complement activation [GO:0030449]; regulation of complement activation, alternative pathway [GO:0030451]; regulation of complement-dependent cytotoxicity [GO:1903659] | blood microparticle [GO:0072562]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; serine-type endopeptidase complex [GO:1905370]; symbiont cell surface [GO:0106139] | complement component C3b binding [GO:0001851]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; identical protein binding [GO:0042802] | PF00084; | 2.10.70.10; | null | PTM: Sulfated on tyrosine residues. {ECO:0000269|PubMed:25136834}.; PTM: According to a report, Asn-217 is not glycosylated (PubMed:17591618). Another study observed glycosylation at this position (PubMed:19139490). {ECO:0000305|PubMed:17591618, ECO:0000305|PubMed:19139490}. | SUBCELLULAR LOCATION: Secreted.; SUBCELLULAR LOCATION: Note=(Microbial infection) In the mosquito midgut, localizes to P.falciparum (NF54 strain) macrogamete and young zygote cell membranes. {ECO:0000269|PubMed:23332154}. | null | null | null | null | null | FUNCTION: Glycoprotein that plays an essential role in maintaining a well-balanced immune response by modulating complement activation. Acts as a soluble inhibitor of complement, where its binding to self markers such as glycan structures prevents complement activation and amplification on cell surfaces (PubMed:2128536... | Homo sapiens (Human) |
P08617 | POLG_HAVHM | MNMSRQGIFQTVGSGLDHILSLADIEEEQMIQSVDRTAVTGASYFTSVDQSSVHTAEVGSHQVEPLRTSVDKPGSKKTQGEKFFLIHSADWLTTHALFHEVAKLDVVKLLYNEQFAVQGLLRYHTYARFGIEIQVQINPTPFQQGGLICAMVPGDQSYGSIASLTVYPHGLLNCNINNVVRIKVPFIYTRGAYHFKDPQYPVWELTIRVWSELNIGTGTSAYTSLNVLARFTDLELHGLTPLSTQMMRNEFRVSTTENVVNLSNYEDARAKMSFALDQEDWKSDPSQGGGIKITHFTTWTSIPTLAAQFPFNASDSVGQQ... | 2.7.7.48; 3.4.22.28; 3.6.1.15 | null | DNA-templated transcription [GO:0006351]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of MAVS activity [GO:0039545]; viral RNA genome re... | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell mitochondrial outer membrane [GO:0044193]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; monoatomic ion channel activity [GO:0005216]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural molecule ... | PF20758;PF12944;PF00548;PF00680;PF00073;PF00910; | 1.20.960.20;2.60.120.20;3.30.70.270;2.40.10.10; | Picornaviridae polyprotein family | PTM: [Genome polyprotein]: Specific enzymatic cleavages by viral protease in vivo yield a variety of precursors and mature proteins. Polyprotein processing intermediates are produced, such as P1-2A which is a functional precursor of the structural proteins, VP0 which is a VP4-VP2 precursor, VP1-2A precursor, 3ABC precu... | SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000269|PubMed:25327248, ECO:0000269|PubMed:28074040}. Host endosome, host multivesicular body {ECO:0000269|PubMed:28490497}. Note=The egress of newly formed virions occurs through an exosome-like mechanism involving endosomal budding of viral capsids into multive... | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539, ECO:0000269|PubMed:8291234}; CATALYTIC... | null | null | null | null | FUNCTION: [Capsid protein VP1]: Capsid proteins VP1, VP2, and VP3 form a closed capsid enclosing the viral positive strand RNA genome (PubMed:25327248, PubMed:28074040). All these proteins contain a beta-sheet structure called beta-barrel jelly roll (PubMed:25327248). Together they form an icosahedral capsid (T=3) comp... | Human hepatitis A virus genotype IB (isolate HM175) (HHAV) (Human hepatitis A virus (isolate Human/Australia/HM175/1976)) |
P08619 | NIA_NEUCR | MEAPALEQRQSLHDSSERQQRFTSLILPNGVGCSSREEPQGSGGLLVPHNDNDIDNDLASTRTASPTTTDFSSSSSDDNSTTLETSVNYSHSSNTNTNTSCPPSPITSSSLKPAYPLPPPSTRLTTILPTDLKTPDHLIRDPRLIRLTGSHPFNVEPPLTALFEHGFLTPQNLHYVRNHGPIPSSVATPPATINKEEDDSLLNWEFTVEGLVEHPLKISVRELMDASKWDNVTYPVTLVCAGNRRKEQNVLRKSKGFSWGAGGLSTALWTGVGLSEILARAKPLTKKGGGARYVCFEGADQLPNGTYGTSVKLAWAMDPN... | 1.7.1.3 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; Note=Binds 1 FAD per subunit. {ECO:0000250}; COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; Note=Binds 1 heme group per subunit. The heme group is called cytochrome b-557. {ECO:0000250}; COFACTOR: Name=Mo-molybdopterin; Xref=ChEBI... | nitrate assimilation [GO:0042128]; sulfur compound metabolic process [GO:0006790] | mitochondrion [GO:0005739] | FAD binding [GO:0071949]; heme binding [GO:0020037]; molybdenum ion binding [GO:0030151]; molybdopterin cofactor binding [GO:0043546]; nitrate reductase (NADPH) activity [GO:0050464]; sulfite oxidase activity [GO:0008482] | PF00173;PF00970;PF03404;PF00175;PF00174; | 2.60.40.650;3.10.120.10;3.40.50.80;3.90.420.10;2.40.30.10; | Nitrate reductase family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + NADP(+) + nitrite = H(+) + NADPH + nitrate; Xref=Rhea:RHEA:19061, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16301, ChEBI:CHEBI:17632, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.7.1.3; | null | PATHWAY: Nitrogen metabolism; nitrate reduction (assimilation). | null | null | FUNCTION: Nitrate reductase is a key enzyme involved in the first step of nitrate assimilation in plants, fungi and bacteria. | Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
P08620 | FGF4_HUMAN | MSGPGTAAVALLPAVLLALLAPWAGRGGAAAPTAPNGTLEAELERRWESLVALSLARLPVAAQPKEAAVQSGAGDYLLGIKRLRRLYCNVGIGFHLQALPDGRIGGAHADTRDSLLELSPVERGVVSIFGVASRFFVAMSSKGKLYGSPFFTDECTFKEILLPNNYNAYESYKYPGMFIALSKNGKTKKGNRVSPTMKVTHFLPRL | null | null | animal organ morphogenesis [GO:0009887]; apoptotic process involved in morphogenesis [GO:0060561]; cartilage condensation [GO:0001502]; cell differentiation [GO:0030154]; cell-cell signaling [GO:0007267]; cellular response to leukemia inhibitory factor [GO:1990830]; chondroblast differentiation [GO:0060591]; cranial su... | cytoplasm [GO:0005737]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | fibroblast growth factor receptor binding [GO:0005104]; growth factor activity [GO:0008083]; heparin binding [GO:0008201] | 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 embryonic development, cell proliferation, and cell differentiation. Required for normal limb and cardiac valve development during embryogenesis. May play a role in embryonic molar tooth bud development via inducing the expression of MSX1, MSX2 and MSX1-mediated ex... | Homo sapiens (Human) |
P08621 | RU17_HUMAN | MTQFLPPNLLALFAPRDPIPYLPPLEKLPHEKHHNQPYCGIAPYIREFEDPRDAPPPTRAETREERMERKRREKIERRQQEVETELKMWDPHNDPNAQGDAFKTLFVARVNYDTTESKLRREFEVYGPIKRIHMVYSKRSGKPRGYAFIEYEHERDMHSAYKHADGKKIDGRRVLVDVERGRTVKGWRPRRLGGGLGGTRRGGADVNIRHSGRDDTSRYDERPGPSPLPHRDRDRDRERERRERSRERDKERERRRSRSRDRRRRSRSRDKEERRRSRERSKDKDRDRKRRSSRSRERARRERERKEELRGGGGDMAEPS... | null | null | mRNA splicing, via spliceosome [GO:0000398]; negative regulation of chaperone-mediated autophagy [GO:1904715]; negative regulation of protein refolding [GO:0061084]; positive regulation of mRNA splicing, via spliceosome [GO:0048026]; regulation of ATP-dependent activity [GO:0043462]; regulation of RNA splicing [GO:0043... | nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; precatalytic spliceosome [GO:0071011]; spliceosomal complex [GO:0005681]; U1 snRNP [GO:0005685]; U2-type prespliceosome [GO:0071004] | mRNA binding [GO:0003729]; RNA binding [GO:0003723]; U1 snRNA binding [GO:0030619] | PF00076;PF12220; | 3.30.70.330; | null | PTM: The N-terminus is blocked.; PTM: Extensively phosphorylated on serine residues in the C-terminal region. {ECO:0000269|PubMed:8332490}. | SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:17656373}. Nucleus, nucleoplasm {ECO:0000269|PubMed:17656373, ECO:0000269|PubMed:21113136}. Note=Colocalizes with SCNM1 and LUC7L2 in nuclear speckles. {ECO:0000250|UniProtKB:Q62376}. | null | null | null | null | null | FUNCTION: Component of the spliceosomal U1 snRNP, which is essential for recognition of the pre-mRNA 5' splice-site and the subsequent assembly of the spliceosome (PubMed:19325628, PubMed:25555158). SNRNP70 binds to the loop I region of U1-snRNA (PubMed:19325628, PubMed:2467746, PubMed:25555158). {ECO:0000269|PubMed:19... | Homo sapiens (Human) |
P08622 | DNAJ_ECOLI | MAKQDYYEILGVSKTAEEREIRKAYKRLAMKYHPDRNQGDKEAEAKFKEIKEAYEVLTDSQKRAAYDQYGHAAFEQGGMGGGGFGGGADFSDIFGDVFGDIFGGGRGRQRAARGADLRYNMELTLEEAVRGVTKEIRIPTLEECDVCHGSGAKPGTQPQTCPTCHGSGQVQMRQGFFAVQQTCPHCQGRGTLIKDPCNKCHGHGRVERSKTLSVKIPAGVDTGDRIRLAGEGEAGEHGAPAGDLYVQVQVKQHPIFEREGNNLYCEVPINFAMAALGGEIEVPTLDGRVKLKVPGETQTGKLFRMRGKGVKSVRGGAQGD... | null | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per monomer.; | chaperone cofactor-dependent protein refolding [GO:0051085]; DNA replication [GO:0006260]; protein folding [GO:0006457]; protein refolding [GO:0042026]; protein unfolding [GO:0043335]; protein-containing complex assembly [GO:0065003]; response to heat [GO:0009408]; viral process [GO:0016032] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; protein-containing complex [GO:0032991] | ATP binding [GO:0005524]; heat shock protein binding [GO:0031072]; protein disulfide isomerase activity [GO:0003756]; protein homodimerization activity [GO:0042803]; protein-disulfide reductase activity [GO:0015035]; protein-folding chaperone binding [GO:0051087]; sigma factor antagonist activity [GO:0016989]; unfolded... | PF00226;PF01556;PF00684; | 1.10.287.110;2.10.230.10;2.60.260.20; | DnaJ family | null | SUBCELLULAR LOCATION: Cytoplasm. | null | null | null | null | null | FUNCTION: Interacts with DnaK and GrpE to disassemble a protein complex at the origins of replication of phage lambda and several plasmids. Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomou... | Escherichia coli (strain K12) |
P08630 | BTKL_DROME | MMGTKHRNSHVNGSIKSSSSLRSSSKSFQAKMDLMSERLYDVVKSGSMVKRAQNKKRFTPVNYKHRWFELTKRTFSYFDVENVERRRERGRIHLKGVRLVEEATVSGEGGDPFAPDGYPFQVGYCEISASANSHQLENGNGGGSGVGIEGQQSGRAVPQYTLYVIANSEKERSEWIRAIRQVCEDSNTPKSYRYHPGLWSGKKWSCCKGLSRTTFGCRAAAHWREANNNPSNGSSPAQNSTRSISPNSSTTNSQFSLQHNSSGSLGGGVGGGLGGGGSLGLGGGGGGGGSCTPTSLQPQSSLTTFKQSPTLLNGNGTLLD... | 2.7.10.2 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:Q06187}; Note=Binds 1 zinc ion per subunit. {ECO:0000250|UniProtKB:Q06187}; | actin cytoskeleton organization [GO:0030036]; adaptive immune response [GO:0002250]; B cell receptor signaling pathway [GO:0050853]; cellularization [GO:0007349]; courtship behavior [GO:0007619]; determination of adult lifespan [GO:0008340]; DNA endoreduplication [GO:0042023]; dorsal closure [GO:0007391]; female germli... | apical part of cell [GO:0045177]; cell periphery [GO:0071944]; cytoplasm [GO:0005737]; germline ring canal [GO:0045172]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein tyrosine kinase activity [GO:0004713] | PF00779;PF00169;PF07714;PF00017;PF00018; | 2.30.29.30;3.30.505.10;2.30.30.40;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, TEC subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000250|UniProtKB:Q06187}; | null | null | null | null | FUNCTION: Required for proper ring canal development. Also required for the development of male genitalia and for adult survival. {ECO:0000269|PubMed:10330180, ECO:0000269|PubMed:9655810}. | Drosophila melanogaster (Fruit fly) |
P08631 | HCK_HUMAN | MGGRSSCEDPGCPRDEERAPRMGCMKSKFLQVGGNTFSKTETSASPHCPVYVPDPTSTIKPGPNSHNSNTPGIREAGSEDIIVVALYDYEAIHHEDLSFQKGDQMVVLEESGEWWKARSLATRKEGYIPSNYVARVDSLETEEWFFKGISRKDAERQLLAPGNMLGSFMIRDSETTKGSYSLSVRDYDPRQGDTVKHYKIRTLDNGGFYISPRSTFSTLQELVDHYKKGNDGLCQKLSVPCMSSKPQKPWEKDAWEIPRESLKLEKKLGAGQFGEVWMATYNKHTKVAVKTMKPGSMSVEAFLAEANVMKTLQHDKLVKL... | 2.7.10.2 | null | cell adhesion [GO:0007155]; cell differentiation [GO:0030154]; cytokine-mediated signaling pathway [GO:0019221]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; innate immune response-activating signaling pathway [GO:000... | caveola [GO:0005901]; cell projection [GO:0042995]; cytoplasmic side of plasma membrane [GO:0009898]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organe... | ATP binding [GO:0005524]; lipid binding [GO:0008289]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; phosphotyrosine residue binding [GO:0001784]; protein tyrosine kinase activity [GO:0004713]; signaling receptor binding [GO:0005102] | PF07714;PF00017;PF00018; | 3.30.505.10;2.30.30.40;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, SRC subfamily | PTM: Phosphorylated on several tyrosine residues. Autophosphorylated. Becomes rapidly phosphorylated upon activation of the immunoglobulin receptors FCGR1A and FCGR2A. Phosphorylation by the BCR-ABL fusion protein mediates activation of HCK. Phosphorylation at Tyr-411 increases kinase activity. Phosphorylation at Tyr-5... | SUBCELLULAR LOCATION: [Isoform 1]: Lysosome. Membrane; Lipid-anchor. Cell projection, podosome membrane; Lipid-anchor. Cytoplasm, cytosol. Note=Associated with specialized secretory lysosomes called azurophil granules. At least half of this isoform is found in the cytoplasm, some of this fraction is myristoylated.; SUB... | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Non-receptor tyrosine-protein kinase found in hematopoietic cells that transmits signals from cell surface receptors and plays an important role in the regulation of innate immune responses, including neutrophil, monocyte, macrophage and mast cell functions, phagocytosis, cell survival and proliferation, cell... | Homo sapiens (Human) |
P08635 | SAST_RAT | METAVNAKSPRNEKVLNCLYQNPDAVFKLICFPWAGGGSIHFAKWGQKINDSLEVHAVRLAGRETRLGEPFANDIYQIADEIVTALLPIIQDKAFAFFGHSFGSYIALITALLLKEKYKMEPLHIFVSGASAPHSTSRPQVPDLNELTEEQVRHHLLDFGGTPKHLIEDQDVLRMFIPLLKADAGVVKKFIFDKPSKALLSLDITGFLGSEDTIKDIEGWQDLTSGKFDVHMLPGDHFYLMKPDNENFIKNYIAKCLELSSLT | 3.1.2.14 | null | lipid biosynthetic process [GO:0008610]; medium-chain fatty acid biosynthetic process [GO:0051792] | cytosol [GO:0005829] | fatty acyl-[ACP] hydrolase activity [GO:0016297] | PF00975; | 3.40.50.1820; | Thioesterase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:3105579}. | CATALYTIC ACTIVITY: Reaction=(9Z)-octadecenoyl-[ACP] + H2O = (9Z)-octadecenoate + H(+) + holo-[ACP]; Xref=Rhea:RHEA:15057, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9924, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30823, ChEBI:CHEBI:64479, ChEBI:CHEBI:78783; EC=3.1.2.14; Evidence={ECO:0000269|PubMed:8446599}; CATALYTI... | null | null | null | null | FUNCTION: Contributes to the release of free fatty acids from fatty acid synthase (FASN). Has broad substrate specificity, giving rise to a range of free fatty acids with chain lengths between 10 and 16 carbon atoms (C10 - C16). {ECO:0000269|PubMed:8446599}. | Rattus norvegicus (Rat) |
P08637 | FCG3A_HUMAN | MWQLLLPTALLLLVSAGMRTEDLPKAVVFLEPQWYRVLEKDSVTLKCQGAYSPEDNSTQWFHNESLISSQASSYFIDAATVDDSGEYRCQTNLSTLSDPVQLEVHIGWLLLQAPRWVFKEEDPIHLRCHSWKNTALHKVTYLQNGKGRKYFHHNSDFYIPKATLKDSGSYFCRGLFGSKNVSSETVNITITQGLAVSTISSFFPPGYQVSFCLVMVLLFAVDTGLYFSVKTNIRSSTRDWKDHKFKWRKDPQDK | null | null | antibody-dependent cellular cytotoxicity [GO:0001788]; calcium-mediated signaling [GO:0019722]; cell surface receptor signaling pathway [GO:0007166]; Fc-gamma receptor signaling pathway [GO:0038094]; immune response [GO:0006955]; macrophage activation [GO:0042116]; natural killer cell activation [GO:0030101]; natural k... | external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; Fc-gamma receptor III complex [GO:0033001]; plasma membrane [GO:0005886] | IgG binding [GO:0019864]; IgG receptor activity [GO:0019770]; immune receptor activity [GO:0140375]; low-affinity IgG receptor activity [GO:0019772] | PF13895; | 2.60.40.10; | null | PTM: Glycosylated. Contains high mannose- and complex-type oligosaccharides. Glycosylation at Asn-180 is mandatory for high affinity binding to the Fc and for discrimination between fucosylated and afucosylated IgG glycoforms. {ECO:0000269|PubMed:21768335, ECO:0000269|PubMed:22023369}.; PTM: Undergoes rapid ectodomain ... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1825220, ECO:0000269|PubMed:23006327, ECO:0000269|PubMed:24337742, ECO:0000269|PubMed:2532305, ECO:0000269|PubMed:28652325, ECO:0000269|PubMed:29967280}; Single-pass type I membrane protein {ECO:0000255}. Secreted {ECO:0000269|PubMed:25816339, ECO:0000269|PubMed:2... | null | null | null | null | null | FUNCTION: Receptor for the invariable Fc fragment of immunoglobulin gamma (IgG). Optimally activated upon binding of clustered antigen-IgG complexes displayed on cell surfaces, triggers lysis of antibody-coated cells, a process known as antibody-dependent cellular cytotoxicity (ADCC). Does not bind free monomeric IgG, ... | Homo sapiens (Human) |
P08638 | LEUR_YEAST | MEGRSDFVATSQSGSEMSHSETRNRTGMNARKRKFACVECRQQKSKCDAHERAPEPCTKCAKKNVPCILKRDFRRTYKRARNEAIEKRFKELTRTLTNLTSDEILKKIEEEQEIVLDNSNFTKEKVKQLRKSAFETTEIEPRSYKTLRGEPISYSTNRRHTDSSPLTLLSSSTNFDPVHSTNVMTDDQLKCLPKSLGDVYLSSSDIAELFQEFATKYHQFLPVVDLSKGAERIYHLSPCLFWVILLIGLRRKFGATDLMTRLSVLVKSVLSEITISPIIRYTPSDKDEPVLNVASVYSVQAFLLYTFWPPLTSSLSADTS... | null | null | amino acid biosynthetic process [GO:0008652]; leucine biosynthetic process [GO:0009098]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of leucine biosynthetic process [GO:2001278]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-tem... | nucleus [GO:0005634] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; sequence-specific DNA binding [GO:0043565]; transcription cis-... | PF00172; | 4.10.240.10; | null | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Factor for control of RNA levels of a group of leucine-specific genes. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P08640 | FLO11_YEAST | MQRPFLLAYLVLSLLFNSALGFPTALVPRGSSEGTSCNSIVNGCPNLDFNWHMDQQNIMQYTLDVTSVSWVQDNTYQITIHVKGKENIDLKYLWSLKIIGVTGPKGTVQLYGYNENTYLIDNPTDFTATFEVYATQDVNSCQVWMPNFQIQFEYLQGSAAQYASSWQWGTTSFDLSTGCNNYDNQGHSQTDFPGFYWNIDCDNNCGGTKSSTTTSSTSESSTTTSSTSESSTTTSSTSESSTTTSSTSESSTSSSTTAPATPTTTSCTKEKPTPPTTTSCTKEKPTPPHHDTTPCTKKKTTTSKTCTKKTTTPVPTPSSS... | null | null | cell adhesion involved in single-species biofilm formation [GO:0043709]; cell-cell adhesion [GO:0098609]; cell-cell self recognition [GO:0097656]; filamentous growth [GO:0030447]; flocculation [GO:0000128]; homotypic cell-cell adhesion [GO:0034109]; invasive growth in response to glucose limitation [GO:0001403]; pseudo... | cellular bud neck [GO:0005935]; extracellular region [GO:0005576]; fungal-type vacuole [GO:0000324]; plasma membrane [GO:0005886]; side of membrane [GO:0098552] | identical protein binding [GO:0042802] | PF10182; | null | Flocculin family | PTM: Extensively O-mannosylated. {ECO:0000269|PubMed:17921350, ECO:0000269|PubMed:22129043}.; PTM: The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannopro... | SUBCELLULAR LOCATION: Secreted, cell wall {ECO:0000269|PubMed:10383953, ECO:0000269|PubMed:11027318, ECO:0000269|PubMed:20619652}. Membrane; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:20619652}. Note=The protein is attached to the cell wall via a GPI-anchor and is also shed liberally into extracellular fluid; increas... | null | null | null | null | null | FUNCTION: Homophilic binding protein that enables kin discrimination in heterogeneous yeast populations by mediating homotypic cell-cell interactions during flocculation, a reversible and asexual process in which cells adhere to form aggregates (flocs) (PubMed:17921350, PubMed:22129043, PubMed:25960408, PubMed:27547826... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P08641 | CADH1_CHICK | MGRRWGSPALQRFPVLVLLLLLQVCGRRCDEAAPCQPGFAAETFSFSVPQDSVAAGRELGRVSFAACSGRPWAVYVPTDTRFKVNGDGVVSTKRPLTLYGRKISFTIYAQDAMGKRHSARVTVGRHRHRRHHHNHHLQDTTPAVLTFPKHDPGFLRRQKRDWVIPPISCLENHRGPYPMRLVQIKSNKDKESKVYYSITGQGADSPPVGIFIIERETGWLEVTEQLDREKIDRYTLLSHAVSASGQPVEDPMEIIITVMDQNDNKPVFIKEVFVGYIEENAKPGTSVMTVNATDADDAVNTDNGIVSYSIVSQQPPRPHP... | null | null | adherens junction organization [GO:0034332]; calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0016339]; cell morphogenesis [GO:0000902]; cell-cell adhesion mediated by cadherin [GO:0044331]; cell-cell junction assembly [GO:0007043]; homophilic cell adhesion via plasma membrane adhesi... | adherens junction [GO:0005912]; apical junction complex [GO:0043296]; catenin complex [GO:0016342]; cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; flotillin complex [GO:0016600] | cadherin binding [GO:0045296]; calcium ion binding [GO:0005509] | PF01049;PF00028;PF08758; | 2.60.40.60;4.10.900.10; | null | null | SUBCELLULAR LOCATION: Cell junction, adherens junction {ECO:0000250|UniProtKB:P09803}. Cell membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}. Endosome {ECO:0000250|UniProtKB:P12830}. Golgi apparatus, trans-Golgi network {ECO:0000250|UniProtKB:P12830}. Cytoplasm {ECO:0000250|UniProtKB:P09803}. C... | null | null | null | null | null | FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the sorting of heterogeneous cell types. E-cadherin is a ligand for integrin alpha-E/beta-7. | Gallus gallus (Chicken) |
P08642 | RASH_CHICK | MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHQYREQIKRVKDSDDVPMVLVGNKCDLPARTVETRQAQDLARSYGIPYIETSAKTRQGVEDAFYTLVREIRQHKLRKLNPPDESGPGCMNCKCVIS | 3.6.5.2 | null | adipose tissue development [GO:0060612]; cellular response to gamma radiation [GO:0071480]; defense response to protozoan [GO:0042832]; endocytosis [GO:0006897]; fibroblast proliferation [GO:0048144]; insulin receptor signaling pathway [GO:0008286]; intrinsic apoptotic signaling pathway [GO:0097193]; myelination [GO:00... | cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; Golgi membrane [GO:0000139]; GTPase complex [GO:1905360]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886] | G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; protein-membrane adaptor activity [GO:0043495] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Ras family | PTM: Palmitoylated by the ZDHHC9-GOLGA7 complex. A continuous cycle of de- and re-palmitoylation regulates rapid exchange between plasma membrane and Golgi. {ECO:0000250|UniProtKB:P01112}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Note=Shuttles between the plasma membrane and the Golgi apparatus. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P01112}; | null | null | null | null | FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. | Gallus gallus (Chicken) |
P08644 | RASK_RAT | MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLCVFAINNTKSFEDIHHYREQIKRVKDSEDVPMVLVGNKCDLPSRTVDTKQAQELARSYGIPFIETSAKTRQRVEDAFYTLVREIRQYRLKKISKEEKTPGCVKIKKCVIM | 3.6.5.2 | null | actin cytoskeleton organization [GO:0030036]; cardiac muscle cell proliferation [GO:0060038]; cell population proliferation [GO:0008283]; cytokine-mediated signaling pathway [GO:0019221]; epithelial tube branching involved in lung morphogenesis [GO:0060441]; female pregnancy [GO:0007565]; forebrain astrocyte developmen... | cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; endomembrane system [GO:0012505]; membrane [GO:0016020]; plasma membrane [GO:0005886] | G protein activity [GO:0003925]; GDP binding [GO:0019003]; GMP binding [GO:0019002]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; LRR domain binding [GO:0030275]; protein-containing complex binding [GO:0044877]; protein-membrane adaptor activity [GO:0043495] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Ras family | PTM: Acetylation at Lys-104 prevents interaction with guanine nucleotide exchange factors (GEFs). {ECO:0000250|UniProtKB:P01116}.; PTM: Ubiquitinated by the BCR(LZTR1) E3 ubiquitin ligase complex at Lys-170 in a non-degradative manner, leading to inhibit Ras signaling by decreasing Ras association with membranes. {ECO:... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P01116}; Lipid-anchor {ECO:0000250|UniProtKB:P01116}; Cytoplasmic side {ECO:0000250|UniProtKB:P01116}. Endomembrane system {ECO:0000250|UniProtKB:P01116}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P01116}.; SUBCELLULAR LOCATION: [Isoform 2B]: Cell membrane {ECO... | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P01116}; | null | null | null | null | FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity (By similarity). Plays an important role in the regulation of cell proliferation (PubMed:3110778). Plays a role in promoting oncogenic events by inducing transcriptional silencing of tumor suppressor genes (TSGs) in colorectal cancer (CRC) cells ... | Rattus norvegicus (Rat) |
P08645 | RAP1_DROME | MREYKIVVLGSGGVGKSALTVQFVQCIFVEKYDPTIEDSYRKQVEVDGQQCMLEILDTAGTEQFTAMRDLYMKNGQGFVLVYSITAQSTFNDLQDLREQILRVKDTDDVPMVLVGNKCDLEEERVVGKELGKNLATQFNCAFMETSAKAKVNVNDIFYDLVRQINKKSPEKKQKKPKKSLCVLL | 3.6.5.2 | null | adherens junction assembly [GO:0034333]; border follicle cell migration [GO:0007298]; cellular response to cAMP [GO:0071320]; dorsal closure [GO:0007391]; germ-line stem cell population maintenance [GO:0030718]; hemocyte migration [GO:0035099]; imaginal disc-derived wing hair organization [GO:0035317]; negative regulat... | cell leading edge [GO:0031252]; cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; protein kinase binding [GO:0019901] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Ras family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P61224}; | null | null | null | null | FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity. Plays a role in photoreceptor cell determination. {ECO:0000269|PubMed:1934069}. | Drosophila melanogaster (Fruit fly) |
P08646 | RAS1_DROME | MTEYKLVVVGAGGVGKSALTIQLIQNHFVDEYDPTIEDSYRKQVVIDGETCLLDILDTAGQEEYSAMRDQYMRTGEGFLLVFAVNSAKSFEDIGTYREQIKRVKDAEEVPMVLVGNKCDLASWNVNNEQAREVAKQYGIPYIETSAKTRMGVDDAFYTLVREIRKDKDNKGRRGRKMNKPNRRFKCKML | 3.6.5.2 | null | border follicle cell migration [GO:0007298]; cell fate determination [GO:0001709]; cellular response to starvation [GO:0009267]; chorion-containing eggshell pattern formation [GO:0030381]; compound eye development [GO:0048749]; defense response to virus [GO:0051607]; determination of adult lifespan [GO:0008340]; dorsal... | membrane [GO:0016020]; plasma membrane [GO:0005886] | G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; protein kinase regulator activity [GO:0019887]; protein serine/threonine kinase activator activity [GO:0043539] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Ras family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18503409}; Lipid-anchor {ECO:0000269|PubMed:18503409}; Cytoplasmic side {ECO:0000269|PubMed:18503409}. Note=Loss of prenylation causes protein location to the cytoplasm. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P01112}; | null | null | null | null | FUNCTION: Ras proteins bind GDP/GTP and possess intrinsic GTPase activity (By similarity). Plays a role in eye development by regulating cell growth, survival of postmitotic ommatidial cells and differentiation of photoreceptor cells (PubMed:11290305). During larval development, mediates Ptth/tor signaling leading to t... | Drosophila melanogaster (Fruit fly) |
P08647 | RAS_SCHPO | MRSTYLREYKLVVVGDGGVGKSALTIQLIQSHFVDEYDPTIEDSYRKKCEIDGEGALLDVLDTAGQEEYSAMREQYMRTGEGFLLVYNITSRSSFDEISTFYQQILRVKDKDTFPVVLVANKCDLEAERVVSRAEGEQLAKSMHCLYVETSAKLRLNVEEAFYSLVRTIRRYNKSEEKGFQNKQAVQTAQVPASTAKRASAVNNSKTEDEVSTKCCVIC | 3.6.5.2 | null | conjugation with cellular fusion [GO:0000747]; establishment of cell polarity [GO:0030010]; establishment or maintenance of cell polarity [GO:0007163]; positive regulation of conjugation with cellular fusion [GO:0031139]; positive regulation of mating projection assembly [GO:1902917]; positive regulation of pheromone r... | Cdc42 GTPase complex [GO:0071521]; cell cortex of cell tip [GO:0051285]; cell division site [GO:0032153]; cortical dynamic polarity patch [GO:0090726]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; division septum [GO:0000935]; mating projection actin fusion focus [GO:1990819]; nucleus [GO:0005634]; plasma membrane [GO... | CTP binding [GO:0002135]; G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; protein serine/threonine kinase activator activity [GO:0043539]; UTP binding [GO:0002134] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Ras family | PTM: Palmitoylated by the erf2-erf4 complex. {ECO:0000269|PubMed:23843742}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}; Cytoplasmic side {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P01112}; | null | null | null | null | FUNCTION: Participates in the process of sexual differentiation and the determination of cell shape. Essential for mating and for recognition of the mating pheromone, but not for vegetative growth. Does not regulate the intracellular cAMP level. Regulates two downstream pathways, namely the byr2/byr1/spk1 mitogen-activ... | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
P08648 | ITA5_HUMAN | MGSRTPESPLHAVQLRWGPRRRPPLLPLLLLLLPPPPRVGGFNLDAEAPAVLSGPPGSFFGFSVEFYRPGTDGVSVLVGAPKANTSQPGVLQGGAVYLCPWGASPTQCTPIEFDSKGSRLLESSLSSSEGEEPVEYKSLQWFGATVRAHGSSILACAPLYSWRTEKEPLSDPVGTCYLSTDNFTRILEYAPCRSDFSWAAGQGYCQGGFSAEFTKTGRVVLGGPGSYFWQGQILSATQEQIAESYYPEYLINLVQGQLQTRQASSIYDDSYLGYSVAVGEFSGDDTEDFVAGVPKGNLTYGYVTILNGSDIRSLYNFSGE... | null | null | angiogenesis [GO:0001525]; CD40 signaling pathway [GO:0023035]; cell adhesion [GO:0007155]; cell adhesion mediated by integrin [GO:0033627]; cell-cell adhesion [GO:0098609]; cell-cell adhesion mediated by integrin [GO:0033631]; cell-matrix adhesion [GO:0007160]; cell-substrate adhesion [GO:0031589]; cell-substrate junc... | alphav-beta3 integrin-vitronectin complex [GO:0071062]; cell surface [GO:0009986]; cytoplasmic vesicle [GO:0031410]; endoplasmic reticulum [GO:0005783]; external side of plasma membrane [GO:0009897]; focal adhesion [GO:0005925]; glutamatergic synapse [GO:0098978]; Golgi apparatus [GO:0005794]; integrin alpha5-beta1 com... | calcium ion binding [GO:0005509]; epidermal growth factor receptor binding [GO:0005154]; integrin binding [GO:0005178]; platelet-derived growth factor receptor binding [GO:0005161]; vascular endothelial growth factor receptor 2 binding [GO:0043184]; virus receptor activity [GO:0001618] | PF01839;PF08441;PF20805;PF20806; | 1.20.5.930;2.130.10.130;2.60.40.1460;2.60.40.1510;2.60.40.1530; | Integrin alpha chain family | PTM: Proteolytic cleavage by PCSK5 mediates activation of the precursor. {ECO:0000269|PubMed:22740495}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17158881}; Single-pass type I membrane protein {ECO:0000255}. Cell junction, focal adhesion {ECO:0000269|PubMed:17158881}. | null | null | null | null | null | FUNCTION: Integrin alpha-5/beta-1 (ITGA5:ITGB1) is a receptor for fibronectin and fibrinogen. It recognizes the sequence R-G-D in its ligands. ITGA5:ITGB1 binds to PLA2G2A via a site (site 2) which is distinct from the classical ligand-binding site (site 1) and this induces integrin conformational changes and enhanced ... | Homo sapiens (Human) |
P08649 | CO4_RAT | MRLLWGLAWAFSFFASSLQKPRLLLFSPSVVNLGTPLSVGVQLLDAPAGQEVKGSVYLRNPTSGPCSPKKDFKLSSGNDFVLLRLEVPLKDVRSCGLFGLRRAPHIQLVAHSPWLKNTASKATETQGVNLLFSSRRGHIFVQTDQPIYNPGQRVRYRVFALDQKMRPSTDTLTVTVENSHGLRVRKKEVFAPTSIFQDDFIIPDISEPGTWKISARFSDGLESNRSTHFEVKKYVLPNFEVKLTPWKPYILTVPSYREEIQLDVQARYVYGKPVQGVAYTRFALMDEQGKKSFLRGLETQTKLVEGQTHISISRDQFQAA... | null | null | complement activation [GO:0006956]; complement activation, classical pathway [GO:0006958]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; positive regulation of apoptotic cell clearance [GO:2000427] | axon [GO:0030424]; dendrite [GO:0030425]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; neuronal cell body [GO:0043025]; synapse [GO:0045202] | complement component C1q complex binding [GO:0001849]; endopeptidase inhibitor activity [GO:0004866] | PF00207;PF07703;PF07677;PF01821;PF21145;PF01835;PF17791;PF17789;PF01759;PF07678; | 1.50.10.20;2.20.130.20;2.40.50.120;2.60.120.1540;2.60.40.1930;2.60.40.1940;6.20.50.160;2.60.40.690;1.20.91.20;2.60.40.10; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P0C0L4}. Synapse {ECO:0000250|UniProtKB:P0C0L4}. Cell projection, axon {ECO:0000250|UniProtKB:P0C0L4}. Cell projection, dendrite {ECO:0000250|UniProtKB:P0C0L4}. | null | null | null | null | null | FUNCTION: Non-enzymatic component of C3 and C5 convertases and thus essential for the propagation of the classical complement pathway. Covalently binds to immunoglobulins and immune complexes and enhances the solubilization of immune aggregates and the clearance of IC through CR1 on erythrocytes (By similarity). {ECO:0... | Rattus norvegicus (Rat) |
P08650 | CO5_RAT | MGLWGLLCLLIFLDKTWGQEQTYVISAPKIFRVGSSENVVIQAHGYTEAFDATISLKSYPDKKVTYSSGYVNLSPENKFQNSALLTLPPKQFPRDENPVSHVYLEVVSMHFSKSKKIPITYDNGFLFIHTDKPVYTPDQSVKIRVYSLSDDLKPAKRETVLTFVDPEGTEVDIVEENDYTGIISFPDFKIPSNPKYGVWTIKAKYKKDFTTTGTAYFEVKEYVLPRFSVSIEPESNFIGYKNFKNFEITVKARYFYNKMVPDAEVYIFFGLREDIKEDEKQMMHKAMQAATLMDGAAQTCWLAETEVREINYNMFEDRNN... | null | null | chemotaxis [GO:0006935]; complement activation, alternative pathway [GO:0006957]; complement activation, classical pathway [GO:0006958]; glomerulus development [GO:0032835]; in utero embryonic development [GO:0001701]; inflammatory response to wounding [GO:0090594]; intracellular calcium ion homeostasis [GO:0006874]; k... | extracellular space [GO:0005615]; membrane attack complex [GO:0005579] | C5a anaphylatoxin chemotactic receptor binding [GO:0031714]; endopeptidase inhibitor activity [GO:0004866] | PF00207;PF07703;PF07677;PF01821;PF21309;PF17790;PF01835;PF17791;PF17789;PF01759;PF07678; | 1.50.10.20;2.20.130.20;2.40.50.120;2.60.120.1540;2.60.40.1930;2.60.40.1940;6.20.50.160;2.60.40.690;1.20.91.20;2.60.40.10; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7987212}. | null | null | null | null | null | FUNCTION: Activation of C5 by a C5 convertase initiates the spontaneous assembly of the late complement components, C5-C9, into the membrane attack complex. C5b has a transient binding site for C6. The C5b-C6 complex is the foundation upon which the lytic complex is assembled.; FUNCTION: [C5a anaphylatoxin]: Derived fr... | Rattus norvegicus (Rat) |
P08651 | NFIC_HUMAN | MYSSPLCLTQDEFHPFIEALLPHVRAFAYTWFNLQARKRKYFKKHEKRMSKDEERAVKDELLGEKPEVKQKWASRLLAKLRKDIRPECREDFVLSITGKKAPGCVLSNPDQKGKMRRIDCLRQADKVWRLDLVMVILFKGIPLESTDGERLVKAAQCGHPVLCVQPHHIGVAVKELDLYLAYFVRERDAEQSGSPRTGMGSDQEDSKPITLDTTDFQESFVTSGVFSVTELIQVSRTPVVTGTGPNFSLGELQGHLAYDLNPASTGLRRTLPSTSSSGSKRHKSGSMEEDVDTSPGGDYYTSPSSPTSSSRNWTEDMEGG... | null | null | DNA replication [GO:0006260]; 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]; transcription by RNA polymerase II [GO:0006366] | chromatin [GO:0000785]; fibrillar center [GO:0001650]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-... | PF00859;PF03165;PF10524; | null | CTF/NF-I family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Recognizes and binds the palindromic sequence 5'-TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in the origin of replication of adenovirus type 2. These proteins are individually capable of activating transcription and replication. | Homo sapiens (Human) |
P08660 | AK3_ECOLI | MSEIVVSKFGGTSVADFDAMNRSADIVLSDANVRLVVLSASAGITNLLVALAEGLEPGERFEKLDAIRNIQFAILERLRYPNVIREEIERLLENITVLAEAAALATSPALTDELVSHGELMSTLLFVEILRERDVQAQWFDVRKVMRTNDRFGRAEPDIAALAELAALQLLPRLNEGLVITQGFIGSENKGRTTTLGRGGSDYTAALLAEALHASRVDIWTDVPGIYTTDPRVVSAAKRIDEIAFAEAAEMATFGAKVLHPATLLPAVRSDIPVFVGSSKDPRAGGTLVCNKTENPPLFRALALRRNQTLLTLHSLNMLH... | 2.7.2.4 | null | homoserine biosynthetic process [GO:0009090]; lysine biosynthetic process via diaminopimelate [GO:0009089]; phosphorylation [GO:0016310] | cytosol [GO:0005829] | aspartate kinase activity [GO:0004072]; ATP binding [GO:0005524]; protein homodimerization activity [GO:0042803] | PF00696; | 3.30.70.260;3.40.1160.10;1.20.120.1320; | Aspartokinase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-aspartate = 4-phospho-L-aspartate + ADP; Xref=Rhea:RHEA:23776, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:57535, ChEBI:CHEBI:456216; EC=2.7.2.4; Evidence={ECO:0000269|PubMed:14623187}; | null | PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4. | null | null | null | Escherichia coli (strain K12) |
P08661 | MBL2_RAT | MSLFTSFLLLCVLTAVYAETLTEGAQSSCPVIACSSPGLNGFPGKDGHDGAKGEKGEPGQGLRGLQGPPGKVGPAGPPGNPGSKGATGPKGDRGESVEFDTTNIDLEIAALRSELRAMRKWVLLSMSENVGKKYFMSSVRRMPLNRAKALCSELQGTVATPRNAEENRAIQNVAKDVAFLGITDQRTENVFEDLTGNRVRYTNWNEGEPNNVGSGENCVVLLTNGKWNDVPCSDSFLVVCEFSD | null | null | antiviral innate immune response [GO:0140374]; cell surface pattern recognition receptor signaling pathway [GO:0002752]; complement activation, classical pathway [GO:0006958]; complement activation, lectin pathway [GO:0001867]; defense response to Gram-positive bacterium [GO:0050830]; innate immune response [GO:0045087... | collagen trimer [GO:0005581]; extracellular space [GO:0005615]; multivesicular body [GO:0005771]; protein-containing complex [GO:0032991]; serine-type endopeptidase complex [GO:1905370] | calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; galactose binding [GO:0005534]; identical protein binding [GO:0042802]; mannose binding [GO:0005537]; phosphatidylinositol-4-phosphate binding [GO:0070273]; protease binding [GO:0002020]; protein self-association [GO:0043621]; signaling r... | PF01391;PF00059; | 3.10.100.10; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | null | null | null | null | null | FUNCTION: Calcium-dependent lectin involved in innate immune defense. Binds mannose, fucose and N-acetylglucosamine on different microorganisms and activates the lectin complement pathway. Binds to late apoptotic cells, as well as to apoptotic blebs and to necrotic cells, but not to early apoptotic cells, facilitating ... | Rattus norvegicus (Rat) |
P08668 | GP_HANTV | MGIWKWLVMASLVWPVLTLRNVYDMKIECPHTVSFGENSVIGYVELPPVPLADTAQMVPESSCNMDNHQSLNTITKYTQVSWRGKADQSQSSQNSFETVSTEVDLKGTCVLKHKMVEESYRSRKSVTCYDLSCNSTYCKPTLYMIVPIHACNMMKSCLIALGPYRVQVVYERSYCMTGVLIEGKCFVPDQSVVSIIKHGIFDIASVHIVCFFVAVKGNTYKIFEQVKKSFESTCNDTENKVQGYYICIVGGNSAPIYVPTLDDFRSMEAFTGIFRSPHGEDHDLAGEEIASYSIVGPANAKVPHSASSDTLSLIAYSGIP... | null | null | endocytosis involved in viral entry into host cell [GO:0075509]; fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; signal transduction [GO:0007165]; suppression by virus of host autophagy [GO:0039521]; symbiont-mediated suppression of host cytoplasmic ... | host cell endoplasmic reticulum membrane [GO:0044167]; host cell Golgi membrane [GO:0044178]; host cell mitochondrion [GO:0033650]; host cell surface [GO:0044228]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | metal ion binding [GO:0046872] | PF20682;PF01561;PF20679;PF01567;PF10538; | 1.10.8.1320; | Hantavirus envelope glycoprotein family | PTM: [Envelopment polyprotein]: Specific enzymatic cleavage in vivo yield the mature proteins Glycoprotein N and Glycoprotein C. {ECO:0000269|PubMed:11689045}. | SUBCELLULAR LOCATION: [Glycoprotein N]: Virion membrane {ECO:0000269|PubMed:21068243}; Multi-pass membrane protein {ECO:0000305}. Host cell surface {ECO:0000269|PubMed:15367644}. Host Golgi apparatus membrane {ECO:0000269|PubMed:24070985}; Multi-pass membrane protein {ECO:0000305}. Host endoplasmic reticulum membrane {... | null | null | null | null | null | FUNCTION: [Glycoprotein N]: Forms homotetramers with glycoprotein C at the surface of the virion. Attaches the virion to host cell receptors including integrin ITGAV/ITGB3 (PubMed:15657120, PubMed:16310165, PubMed:31054291). This attachment induces virion internalization predominantly through clathrin-dependent endocyt... | Hantaan virus (strain 76-118) (Korean hemorrhagic fever virus) |
P08669 | GLYC_LASSJ | MGQIVTFFQEVPHVIEEVMNIVLIALSVLAVLKGLYNFATCGLVGLVTFLLLCGRSCTTSLYKGVYELQTLELNMETLNMTMPLSCTKNNSHHYIMVGNETGLELTLTNTSIINHKFCNLSDAHKKNLYDHALMSIISTFHLSIPNFNQYEAMSCDFNGGKISVQYNLSHSYAGDAANHCGTVANGVLQTFMRMAWGGSYIALDSGRGNWDCIMTSYQYLIIQNTTWEDHCQFSRPSPIGYLGLLSQRTRDIYISRRLLGTFTWTLSDSEGKDTPGGYCLTRWMLIEAELKCFGNTAVAKCNEKHDEEFCDMLRLFDFNK... | null | null | fusion of virus membrane with host endosome membrane [GO:0039654]; receptor-mediated endocytosis of virus by host cell [GO:0019065]; virion attachment to host cell [GO:0019062] | host cell endoplasmic reticulum membrane [GO:0044167]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | metal ion binding [GO:0046872] | PF00798; | 6.10.140.1590;2.20.28.180; | Arenaviridae GPC protein family | PTM: [Pre-glycoprotein polyprotein GP complex]: Specific enzymatic cleavages in vivo yield mature proteins (PubMed:11606739, PubMed:14555961). GP-C polyprotein is cleaved in the endoplasmic reticulum by the host protease MBTPS1 (PubMed:11606739). Only cleaved glycoprotein is incorporated into virions. The SSP remains s... | SUBCELLULAR LOCATION: [Stable signal peptide]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host Go... | null | null | null | null | null | FUNCTION: [Stable signal peptide]: Functions as a cleaved signal peptide that is retained as the third component of the GP complex (GP-C) (PubMed:35173332). Helps to stabilize the spike complex in its native conformation (PubMed:35173332). The SSP is required for efficient glycoprotein expression, post-translational ma... | Lassa virus (strain Mouse/Sierra Leone/Josiah/1976) (LASV) |
P08670 | VIME_HUMAN | MSTRSVSSSSYRRMFGGPGTASRPSSSRSYVTTSTRTYSLGSALRPSTSRSLYASSPGGVYATRSSAVRLRSSVPGVRLLQDSVDFSLADAINTEFKNTRTNEKVELQELNDRFANYIDKVRFLEQQNKILLAELEQLKGQGKSRLGDLYEEEMRELRRQVDQLTNDKARVEVERDNLAEDIMRLREKLQEEMLQREEAENTLQSFRQDVDNASLARLDLERKVESLQEEIAFLKKLHEEEIQELQAQIQEQHVQIDVDVSKPDLTAALRDVRQQYESVAAKNLQEAEEWYKSKFADLSEAANRNNDALRQAKQESTEYR... | null | null | astrocyte development [GO:0014002]; Bergmann glial cell differentiation [GO:0060020]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to muramyl dipeptide [GO:0071225]; cellular response to type II interferon [GO:0071346]; intermediate filament organization [GO:0045109]; lens fiber cell developm... | axon [GO:0030424]; cell leading edge [GO:0031252]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; intermediate filament [GO:0005882]; intermediate filament cytoskeleton [GO:0045111]; microtubule organizing center [GO:0005815]; nu... | double-stranded RNA binding [GO:0003725]; identical protein binding [GO:0042802]; keratin filament binding [GO:1990254]; molecular adaptor activity [GO:0060090]; protein domain specific binding [GO:0019904]; scaffold protein binding [GO:0097110]; structural constituent of cytoskeleton [GO:0005200]; structural constitue... | PF00038;PF04732; | 1.20.5.170;1.20.5.500;1.20.5.1160; | Intermediate filament family | PTM: Filament disassembly during mitosis is promoted by phosphorylation at Ser-55 as well as by nestin (By similarity). One of the most prominent phosphoproteins in various cells of mesenchymal origin. Phosphorylation is enhanced during cell division, at which time vimentin filaments are significantly reorganized. Phos... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21465480, ECO:0000269|PubMed:29496907}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:18408015, ECO:0000269|PubMed:29496907}. Nucleus matrix {ECO:0000250|UniProtKB:P31000}. Cell membrane {ECO:0000250|UniProtKB:P20152}. | null | null | null | null | null | FUNCTION: Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally. {ECO:0000250|UniProtKB:P31000}.; FUNCTION: Involved with LARP6 in the stabilization ... | Homo sapiens (Human) |
P08678 | CYAA_YEAST | MSSKPDTGSEISGPQRQEEQEQQIEQSSPTEANDRSIHDEVPKVKKRHEQNSGHKSRRNSAYSYYSPRSLSMTKSRESITPNGMDDVSISNVEHPRPTEPKIKRGPYLLKKTLSSLSMTSANSTHDDNKDHGYALNSSKTHNYTSTHNHHDGHHDHHHVQFFPNRKPSLAETLFKRFSGSNSHDGNKSGKESKVANLSLSTVNPAPANRKPSKDSTLSNHLADNVPSTLRRKVSSLVRGSSVHDINNGIADKQIRPKAVAQSENTLHSSDVPNSKRSHRKSFLLGSTSSSSSRRGSNVSSMTNSDSASMATSGSHVLQHN... | 4.6.1.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; | adenylate cyclase-modulating G protein-coupled receptor signaling pathway [GO:0007188]; cAMP biosynthetic process [GO:0006171]; positive regulation of Ras protein signal transduction [GO:0046579]; Ras protein signal transduction [GO:0007265] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886] | adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]; magnesium ion binding [GO:0000287] | PF08509;PF21187;PF00211;PF13855;PF00481; | 3.30.70.1230;3.60.40.10;3.80.10.10; | Adenylyl cyclase class-3 family | null | null | CATALYTIC ACTIVITY: Reaction=ATP = 3',5'-cyclic AMP + diphosphate; Xref=Rhea:RHEA:15389, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:58165; EC=4.6.1.1; Evidence={ECO:0000269|PubMed:2934138}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15390; Evidence={ECO:0000269|PubMed:2934138}; | null | null | null | null | FUNCTION: Plays essential roles in regulation of cellular metabolism by catalyzing the synthesis of a second messenger, cAMP. {ECO:0000269|PubMed:2934138}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P08679 | CISY2_YEAST | MTVPYLNSNRNVASYLQSNSSQEKTLKERFSEIYPIHAQDVRQFVKEHGKTKISDVLLEQVYGGMRGIPGSVWEGSVLDPEDGIRFRGRTIADIQKDLPKAKGSSQPLPEALFWLLLTGEVPTQAQVENLSADLMSRSELPSHVVQLLDNLPKDLHPMAQFSIAVTALESESKFAKAYAQGISKQDYWSYTFEDSLDLLGKLPVIAAKIYRNVFKDGKMGEVDPNADYAKNLVNLIGSKDEDFVDLMRLYLTIHSDHEGGNVSAHTSHLVGSALSSPYLSLASGLNGLAGPLHGRANQEVLEWLFALKEEVNDDYSKDTI... | 2.3.3.16 | null | carbohydrate metabolic process [GO:0005975]; citrate metabolic process [GO:0006101]; tricarboxylic acid cycle [GO:0006099] | cytoplasm [GO:0005737]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; peroxisome [GO:0005777] | citrate (Si)-synthase activity [GO:0004108]; identical protein binding [GO:0042802] | PF00285; | 1.10.580.10;1.10.230.10; | Citrate synthase family | PTM: Ubiquitinated by the E3 ubiquitin-protein ligase complex SCF(UCC1), which leads to its degradation by the proteasome (PubMed:25982115). Ubiquitination is prevented by oxaloacetate, suggesting the existence of an oxaloacetate-dependent positive feedback loop that stabilizes CIT2 (PubMed:25982115). {ECO:0000269|PubM... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25982115}. Peroxisome {ECO:0000269|PubMed:2181273, ECO:0000269|PubMed:25982115}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + H2O + oxaloacetate = citrate + CoA + H(+); Xref=Rhea:RHEA:16845, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16452, ChEBI:CHEBI:16947, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.3.16; Evidence={ECO:0000255|PROSITE-ProRule:PRU10117, ECO:0000269|PubMed:3023912}; | null | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 1/2. {ECO:0000269|PubMed:3023912}. | null | null | FUNCTION: Peroxisomal citrate synthase involved in the citrate homeostasis (PubMed:25982115, PubMed:3023912). Catalyzes the condensation of acetyl coenzyme A and oxaloacetate to form citrate (PubMed:25982115, PubMed:3023912). Citrate synthase is the rate-limiting enzyme of the tricarboxylic acid (TCA) cycle (Probable).... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P08680 | HEM0_MOUSE | MVAAAMLLRSCPVLSQGPTGLLGKVAKTYQFLFSIGRCPILATQGPTCSQIHLKATKAGGDSPSWAKSHCPFMLSELQDRKSKIVQRAAPEVQEDVKTFKTDLLSTMDSTTRSHSFPSFQEPEQTEGAVPHLIQNNMTGSQAFGYDQFFRDKIMEKKQDHTYRVFKTVNRWANAYPFAQHFSEASMASKDVSVWCSNDYLGISRHPRVLQAIEETLKNHGAGAGGTRNISGTSKFHVELEQELAELHQKDSALLFSSCFVANDSTLFTLAKLLPGCEIYSDAGNHASMIQGIRNSGAAKFVFRHNDPGHLKKLLEKSDPK... | 2.3.1.37 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:P22557}; | erythrocyte development [GO:0048821]; erythrocyte differentiation [GO:0030218]; heme biosynthetic process [GO:0006783]; hemoglobin biosynthetic process [GO:0042541]; intracellular iron ion homeostasis [GO:0006879]; protoporphyrinogen IX biosynthetic process [GO:0006782]; response to hypoxia [GO:0001666] | mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | 5-aminolevulinate synthase activity [GO:0003870]; coenzyme A binding [GO:0120225]; pyridoxal phosphate binding [GO:0030170] | PF00155;PF09029; | 4.10.92.10;3.90.1150.10;3.40.640.10; | Class-II pyridoxal-phosphate-dependent aminotransferase family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P22557}; Peripheral membrane protein {ECO:0000250|UniProtKB:P22557}. Mitochondrion {ECO:0000269|PubMed:3557128}. Note=Localizes to the matrix side of the mitochondrion inner membrane. {ECO:0000250|UniProtKB:P22557}. | CATALYTIC ACTIVITY: Reaction=glycine + H(+) + succinyl-CoA = 5-aminolevulinate + CO2 + CoA; Xref=Rhea:RHEA:12921, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:57305, ChEBI:CHEBI:356416; EC=2.3.1.37; Evidence={ECO:0000269|PubMed:3557128, ECO:0000269|PubMed:8268805}; Physiologic... | null | PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from glycine: step 1/1. {ECO:0000250|UniProtKB:P22557}. | null | null | FUNCTION: Catalyzes the pyridoxal 5'-phosphate (PLP)-dependent condensation of succinyl-CoA and glycine to form aminolevulinic acid (ALA), with CoA and CO2 as by-products (PubMed:3557128, PubMed:8268805). Contributes significantly to heme formation during erythropoiesis (By similarity). {ECO:0000250|UniProtKB:P22557, E... | Mus musculus (Mouse) |
P08682 | CP2E1_RABIT | MAVLGITVALLGWMVILLFISVWKQIHSSWNLPPGPFPLPIIGNLLQLDLKDIPKSFGRLAERFGPVFTVYLGSRRVVVLHGYKAVREMLLNHKNEFSGRGEIPAFREFKDKGIIFNNGPTWKDTRRFSLTTLRDYGMGKQGNEDRIQKEAHFLLEELRKTQGQPFDPTFVIGCTPFNVIAKILFNDRFDYKDKQALRLMSLFNENFYLLSTPWLQVYNNFSNYLQYMPGSHRKVIKNVSEIKEYTLARVKEHHKSLDPSCPRDFIDSLLIEMEKDKHSTEPLYTLENIAVTVADMFFAGTETTSTTLRYGLLILLKHPE... | 1.14.13.n7; 1.14.14.1 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; | epoxygenase P450 pathway [GO:0019373]; xenobiotic metabolic process [GO:0006805] | endoplasmic reticulum membrane [GO:0005789]; mitochondrial inner membrane [GO:0005743] | arachidonic acid epoxygenase activity [GO:0008392]; aromatase activity [GO:0070330]; heme binding [GO:0020037]; Hsp70 protein binding [GO:0030544]; Hsp90 protein binding [GO:0051879]; iron ion binding [GO:0005506] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P05182}; Peripheral membrane protein {ECO:0000250|UniProtKB:P05182}. Microsome membrane {ECO:0000250|UniProtKB:P05182}; Peripheral membrane protein {ECO:0000250|UniProtKB:P05182}. Mitochondrion inner membrane {ECO:0000250|UniProtKB:P05182}; Per... | CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57... | null | PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000250|UniProtKB:P05181}. | null | null | FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of fatty acids. Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via cytochrome P450 reductase (NADPH--hemoprotein reductase). Cataly... | Oryctolagus cuniculus (Rabbit) |
P08683 | CP2CB_RAT | MDPVLVLVLTLSSLLLLSLWRQSFGRGKLPPGPTPLPIIGNTLQIYMKDIGQSIKKFSKVYGPIFTLYLGMKPFVVLHGYEAVKEALVDLGEEFSGRGSFPVSERVNKGLGVIFSNGMQWKEIRRFSIMTLRTFGMGKRTIEDRIQEEAQCLVEELRKSKGAPFDPTFILGCAPCNVICSIIFQNRFDYKDPTFLNLMHRFNENFRLFSSPWLQVCNTFPAIIDYFPGSHNQVLKNFFYIKNYVLEKVKEHQESLDKDNPRDFIDCFLNKMEQEKHNPQSEFTLESLVATVTDMFGAGTETTSTTLRYGLLLLLKHVDVT... | 1.14.14.1 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P33261}; | amide metabolic process [GO:0043603]; epoxygenase P450 pathway [GO:0019373]; estrogen metabolic process [GO:0008210]; icosanoid biosynthetic process [GO:0046456]; monocarboxylic acid metabolic process [GO:0032787]; monoterpenoid metabolic process [GO:0016098]; oxidative demethylation [GO:0070989]; steroid metabolic pro... | cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231] | arachidonic acid 11,12-epoxygenase activity [GO:0008405]; arachidonic acid 14,15-epoxygenase activity [GO:0008404]; arachidonic acid epoxygenase activity [GO:0008392]; aromatase activity [GO:0070330]; caffeine oxidase activity [GO:0034875]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activit... | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:2434473}; Peripheral membrane protein. Microsome membrane {ECO:0000269|PubMed:2434473}; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=4.5 uM for (5Z,8Z,11Z,14Z)-eicosatetraenoate (total epoxygenase activity) {ECO:0000269|PubMed:15766564}; KM=9.5 uM for (5Z,8Z,11Z,14Z,17Z)-eicosapentaenoate (total epoxygenase activity) {ECO:0000269|PubMed:15766564}; Vmax=5.8 nmol/min/nmol enzyme toward (5Z,8Z,11Z,... | PATHWAY: Lipid metabolism; arachidonate metabolism. {ECO:0000305|PubMed:10491410}.; PATHWAY: Steroid metabolism. {ECO:0000305|PubMed:2434473}. | null | null | FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of steroid hormones and fatty acids. Catalyzes the hydroxylation of carbon-hydrogen bonds. Metabolizes testosterone to 2alpha- and 16alpha-hydroxytestosterone (PubMed:2434473). Catalyzes the epoxidation of double bonds of polyunsaturated fatty acids (... | Rattus norvegicus (Rat) |
P08684 | CP3A4_HUMAN | MALIPDLAMETWLLLAVSLVLLYLYGTHSHGLFKKLGIPGPTPLPFLGNILSYHKGFCMFDMECHKKYGKVWGFYDGQQPVLAITDPDMIKTVLVKECYSVFTNRRPFGPVGFMKSAISIAEDEEWKRLRSLLSPTFTSGKLKEMVPIIAQYGDVLVRNLRREAETGKPVTLKDVFGAYSMDVITSTSFGVNIDSLNNPQDPFVENTKKLLRFDFLDPFFLSITVFPFLIPILEVLNICVFPREVTNFLRKSVKRMKESRLEDTQKHRVDFLQLMIDSQNSKETESHKALSDLELVAQSIIFIFAGYETTSSVLSFIMYE... | 1.14.14.1; 1.14.14.55; 1.14.14.56; 1.14.14.73 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000269|PubMed:15256616, ECO:0000269|PubMed:15258162}; | aflatoxin metabolic process [GO:0046222]; alkaloid catabolic process [GO:0009822]; androgen metabolic process [GO:0008209]; cholesterol metabolic process [GO:0008203]; estrogen metabolic process [GO:0008210]; heterocycle metabolic process [GO:0046483]; lipid hydroxylation [GO:0002933]; lipid metabolic process [GO:00066... | cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231] | 1,8-cineole 2-exo-monooxygenase activity [GO:0102320]; 1-alpha,25-dihydroxyvitamin D3 23-hydroxylase activity [GO:0062181]; anandamide 11,12 epoxidase activity [GO:0062188]; anandamide 14,15 epoxidase activity [GO:0062189]; anandamide 8,9 epoxidase activity [GO:0062187]; aromatase activity [GO:0070330]; caffeine oxidas... | PF00067; | 1.10.630.10; | Cytochrome P450 family | PTM: Polyubiquitinated in the presence of AMFR and UBE2G1 and also STUB1/CHIP and UBE2D1 (in vitro). {ECO:0000269|PubMed:19103148}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass membrane protein. Microsome membrane {ECO:0000269|PubMed:21576599}; Single-pass membrane protein. | CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=52.16 uM for 17beta-estradiol (2-hydroxylation) {ECO:0000269|PubMed:12865317}; KM=53.88 uM for 17beta-estradiol (4-hydroxylation) {ECO:0000269|PubMed:12865317}; KM=7.69 uM for estrone (2-hydroxylation) {ECO:0000269|PubMed:12865317}; KM=7.18 uM for estrone (4-hydrox... | PATHWAY: Steroid hormone biosynthesis. {ECO:0000269|PubMed:11555828, ECO:0000269|PubMed:12865317}.; PATHWAY: Cofactor metabolism; retinol metabolism. {ECO:0000269|PubMed:10681376}.; PATHWAY: Steroid metabolism; cholesterol metabolism. {ECO:0000269|PubMed:21576599}.; PATHWAY: Lipid metabolism; fatty acid metabolism. {EC... | null | null | FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of sterols, steroid hormones, retinoids and fatty acids (PubMed:10681376, PubMed:11093772, PubMed:11555828, PubMed:12865317, PubMed:14559847, PubMed:15373842, PubMed:15764715, PubMed:19965576, PubMed:20702771, PubMed:21490593, PubMed:21576599). Mechan... | Homo sapiens (Human) |
P08686 | CP21A_HUMAN | MLLLGLLLLLPLLAGARLLWNWWKLRSLHLPPLAPGFLHLLQPDLPIYLLGLTQKFGPIYRLHLGLQDVVVLNSKRTIEEAMVKKWADFAGRPEPLTYKLVSRNYPDLSLGDYSLLWKAHKKLTRSALLLGIRDSMEPVVEQLTQEFCERMRAQPGTPVAIEEEFSLLTCSIICYLTFGDKIKDDNLMPAYYKCIQEVLKTWSHWSIQIVDVIPFLRFFPNPGLRRLKQAIEKRDHIVEMQLRQHKESLVAGQWRDMMDYMLQGVAQPSMEEGSGQLLEGHVHMAAVDLLIGGTETTANTLSWAVVFLLHHPEIQQRLQE... | 1.14.14.16 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:25855791}; | glucocorticoid biosynthetic process [GO:0006704]; mineralocorticoid biosynthetic process [GO:0006705]; progesterone metabolic process [GO:0042448]; steroid biosynthetic process [GO:0006694]; steroid metabolic process [GO:0008202]; sterol metabolic process [GO:0016125] | endoplasmic reticulum membrane [GO:0005789] | 17-alpha-hydroxyprogesterone aldolase activity [GO:0047442]; 17-hydroxyprogesterone 21-hydroxylase activity [GO:0103069]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; progesterone 21-hydroxylase activity [GO:0106309]; steroid 17-alpha-monooxygenase activity [GO:0004508]; steroid 21-monooxygenase activity [... | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein {ECO:0000269|PubMed:10198222}. Microsome membrane {ECO:0000269|PubMed:10198222}; Peripheral membrane protein {ECO:0000269|PubMed:10198222}. | CATALYTIC ACTIVITY: Reaction=O2 + progesterone + reduced [NADPH--hemoprotein reductase] = 21-hydroxyprogesterone + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:50304, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16973, ChEBI:CHE... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.59 uM for 17alpha-hydroxyprogesterone {ECO:0000269|PubMed:22014889}; KM=12.5 uM for 17alpha-hydroxyprogesterone (at 37 degrees Celsius) {ECO:0000269|PubMed:27721825}; KM=1.5 uM for 17alpha-hydroxyprogesterone {ECO:0000269|PubMed:25855791}; KM=1.05 uM for progeste... | null | null | null | FUNCTION: A cytochrome P450 monooxygenase that plays a major role in adrenal steroidogenesis. Catalyzes the hydroxylation at C-21 of progesterone and 17alpha-hydroxyprogesterone to respectively form 11-deoxycorticosterone and 11-deoxycortisol, intermediate metabolites in the biosynthetic pathway of mineralocorticoids a... | Homo sapiens (Human) |
P08692 | ARSC1_ECOLX | MSNITIYHNPACGTSRNTLEMIRNSGTEPTIILYLENPPSRDELVKLIADMGISVRALLRKNVEPYEQLGLAEDKFTDDQLIDFMLQHPILINRPIVVTPLGTRLCRPSEVVLDILQDAQKGAFTKEDGEKVVDEAGKRLK | 1.20.4.1 | null | response to arsenic-containing substance [GO:0046685] | null | arsenate reductase (glutaredoxin) activity [GO:0008794] | PF03960; | 3.40.30.10; | ArsC family | null | null | CATALYTIC ACTIVITY: Reaction=[glutaredoxin]-dithiol + arsenate + glutathione + H(+) = arsenite + glutathionyl-S-S-[glutaredoxin] + H2O; Xref=Rhea:RHEA:22016, Rhea:RHEA-COMP:10729, Rhea:RHEA-COMP:17668, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29242, ChEBI:CHEBI:29950, ChEBI:CHEBI:48597, ChEBI:CHEBI:57925, ChEB... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8 mM for arsenate {ECO:0000269|PubMed:8003492}; KM=15.2 mM for arsenate {ECO:0000269|PubMed:14592722}; KM=32.9 nM for glutaredoxin Grx2 {ECO:0000269|PubMed:14592722}; Note=kcat is 0.53 sec(-1) with arsenate as substrate. kcat is 0.218 sec(-1) with Grx2 as substrate... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.3-6.8. {ECO:0000269|PubMed:8003492}; | null | FUNCTION: Involved in resistance to arsenate (PubMed:3021763, PubMed:7577935, PubMed:8003492). Catalyzes the reduction of arsenate [As(V)] to arsenite [As(III)] (PubMed:14592722, PubMed:7577935, PubMed:8003492). The resulting arsenite is then extruded from the cell via the ArsAB transport system (Probable). {ECO:000026... | Escherichia coli |
P08697 | A2AP_HUMAN | MALLWGLLVLSWSCLQGPCSVFSPVSAMEPLGRQLTSGPNQEQVSPLTLLKLGNQEPGGQTALKSPPGVCSRDPTPEQTHRLARAMMAFTADLFSLVAQTSTCPNLILSPLSVALALSHLALGAQNHTLQRLQQVLHAGSGPCLPHLLSRLCQDLGPGAFRLAARMYLQKGFPIKEDFLEQSEQLFGAKPVSLTGKQEDDLANINQWVKEATEGKIQEFLSGLPEDTVLLLLNAIHFQGFWRNKFDPSLTQRDSFHLDEQFTVPVEMMQARTYPLRWFLLEQPEIQVAHFPFKNNMSFVVLVPTHFEWNVSQVLANLSWD... | null | null | acute-phase response [GO:0006953]; blood vessel morphogenesis [GO:0048514]; collagen fibril organization [GO:0030199]; fibrinolysis [GO:0042730]; maintenance of blood vessel diameter homeostasis by renin-angiotensin [GO:0002034]; negative regulation of fibrinolysis [GO:0051918]; negative regulation of plasminogen activ... | blood microparticle [GO:0072562]; cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; fibrinogen complex [GO:0005577]; platelet alpha granule lumen [GO:0031093] | endopeptidase inhibitor activity [GO:0004866]; protease binding [GO:0002020]; protein homodimerization activity [GO:0042803]; serine-type endopeptidase inhibitor activity [GO:0004867] | PF00079; | 2.30.39.10;3.30.497.10; | Serpin family | PTM: Proteolytically cleaved at Pro-39 by both the prolyl endopeptidase FAP form and antiplasmin-cleaving enzyme FAP soluble form to generate mature alpha-2-antiplasmin. {ECO:0000269|PubMed:14751930, ECO:0000269|PubMed:16223769}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Serine protease inhibitor. The major targets of this inhibitor are plasmin and trypsin, but it also inactivates matriptase-3/TMPRSS7 and chymotrypsin. {ECO:0000269|PubMed:15853774}. | Homo sapiens (Human) |
P08699 | LEG3_RAT | MADGFSLNDALAGSGNPNPQGWPGAWGNQPGAGGYPGASYPGAYPGQAPPGGYPGQAPPSAYPGPTGPSAYPGPTAPGAYPGPTAPGAFPGQPGGPGAYPSAPGAYPSAPGAYPATGPFGAPTGPLTVPYDMPLPGGVMPRMLITIIGTVKPNANSITLNFKKGNDIAFHFNPRFNENNRRVIVCNTKQDNNWGREERQSAFPFESGKPFKIQVLVEADHFKVAVNDVHLLQYNHRMKNLREISQLGIIGDITLTSASHAMI | null | null | eosinophil chemotaxis [GO:0048245]; epithelial cell differentiation [GO:0030855]; extracellular matrix organization [GO:0030198]; innate immune response [GO:0045087]; macrophage chemotaxis [GO:0048246]; monocyte chemotaxis [GO:0002548]; mononuclear cell migration [GO:0071674]; mRNA processing [GO:0006397]; negative reg... | cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; external side of plasma membrane [GO:0009897]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; glial cell projection [GO:0097386]; immunological synapse [GO:000... | advanced glycation end-product receptor activity [GO:0050785]; carbohydrate binding [GO:0030246]; chemoattractant activity [GO:0042056]; disaccharide binding [GO:0048030]; Fc-gamma receptor I complex binding [GO:0034988]; IgE binding [GO:0019863]; laminin binding [GO:0043236]; molecular condensate scaffold activity [GO... | PF00337; | 2.60.120.200; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P17931}. Nucleus {ECO:0000250|UniProtKB:P17931}. Secreted {ECO:0000250|UniProtKB:P17931}. Note=Secreted by a non-classical secretory pathway and associates with the cell surface. Can be secreted; the secretion is dependent on protein unfolding and facilitated by th... | null | null | null | null | null | FUNCTION: Galactose-specific lectin which binds IgE. May mediate with the alpha-3, beta-1 integrin the stimulation by CSPG4 of endothelial cells migration. In the nucleus: acts as a pre-mRNA splicing factor. Involved in acute inflammatory responses including neutrophil activation and adhesion, chemoattraction of monocy... | Rattus norvegicus (Rat) |
P08700 | IL3_HUMAN | MSRLPVLLLLQLLVRPGLQAPMTQTTPLKTSWVNCSNMIDEIITHLKQPPLPLLDFNNLNGEDQDILMENNLRRPNLEAFNRAVKSLQNASAIESILKNLLPCLPLATAAPTRHPIHIKDGDWNEFRRKLTFYLKTLENAQAQQTTLSLAIF | null | null | cell-cell signaling [GO:0007267]; embryonic hemopoiesis [GO:0035162]; immune response [GO:0006955]; interleukin-3-mediated signaling pathway [GO:0038156]; nervous system development [GO:0007399]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of peptidyl-tyrosine phosphorylation ... | extracellular region [GO:0005576]; extracellular space [GO:0005615] | cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; interleukin-3 receptor binding [GO:0005135] | PF02059; | 1.20.1250.10; | IL-3 family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Cytokine secreted predominantly by activated T-lymphocytes as well as mast cells and osteoblastic cells that controls the production and differentiation of hematopoietic progenitor cells into lineage-restricted cells (PubMed:2556442). Stimulates also mature basophils, eosinophils, and monocytes to become func... | Homo sapiens (Human) |
P08708 | RS17_HUMAN | MGRVRTKTVKKAARVIIEKYYTRLGNDFHTNKRVCEEIAIIPSKKLRNKIAGYVTHLMKRIQRGPVRGISIKLQEEERERRDNYVPEVSALDQEIIEVDPDTKEMLKLLDFGSLSNLQVTQPTVGMNFKTPRGPV | null | null | cytoplasmic translation [GO:0002181]; erythrocyte homeostasis [GO:0034101]; ribosomal small subunit biogenesis [GO:0042274]; rRNA processing [GO:0006364]; translation [GO:0006412]; translational initiation [GO:0006413] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic ribosome [GO:0022626]; cytosolic small ribosomal subunit [GO:0022627]; focal adhesion [GO:0005925]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; ribosome [GO:0005840]; small-subunit processome [GO:0032040]; synapse [GO:0045202] | RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735] | PF00833; | 1.10.60.20; | Eukaryotic ribosomal protein eS17 family | PTM: Ubiquitinated at Lys-103 by RNF14 and RNF25 in response to ribosome collisions (ribosome stalling). {ECO:0000269|PubMed:36638793}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399}. Nucleus, nucleolus {ECO:0000269|PubMed:34516797}. | null | null | null | null | null | FUNCTION: Component of the small ribosomal subunit (PubMed:23636399). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of t... | Homo sapiens (Human) |
P08709 | FA7_HUMAN | MVSQALRLLCLLLGLQGCLAAGGVAKASGGETRDMPWKPGPHRVFVTQEEAHGVLHRRRRANAFLEELRPGSLERECKEEQCSFEEAREIFKDAERTKLFWISYSDGDQCASSPCQNGGSCKDQLQSYICFCLPAFEGRNCETHKDDQLICVNENGGCEQYCSDHTGTKRSCRCHEGYSLLADGVSCTPTVEYPCGKIPILEKRNASKPQGRIVGGKVCPKGECPWQVLLLVNGAQLCGGTLINTIWVVSAAHCFDKIKNWRNLIAVLGEHDLSEHDGDEQSRRVAQVIIPSTYVPGTTNHDIALLRLHQPVVLTDHVVP... | 3.4.21.21 | null | animal organ regeneration [GO:0031100]; blood coagulation [GO:0007596]; circadian rhythm [GO:0007623]; positive regulation of blood coagulation [GO:0030194]; positive regulation of cell migration [GO:0030335]; positive regulation of leukocyte chemotaxis [GO:0002690]; positive regulation of platelet-derived growth facto... | collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum lumen [GO:0005788]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796]; plasma membrane [GO:0005886]; serine-type peptidase complex [GO:1905286]; vesicle [GO:0031982] | calcium ion binding [GO:0005509]; serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236]; signaling receptor binding [GO:0005102] | PF00008;PF14670;PF00594;PF00089; | 4.10.740.10;2.10.25.10;2.40.10.10; | Peptidase S1 family | PTM: The vitamin K-dependent, enzymatic carboxylation of some glutamate residues allows the modified protein to bind calcium.; PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000269|PubMed:3264725}.; PTM: O- and N-glycosylated. N-gly... | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa.; EC=3.4.21.21; | null | null | null | null | FUNCTION: Initiates the extrinsic pathway of blood coagulation. Serine protease that circulates in the blood in a zymogen form. Factor VII is converted to factor VIIa by factor Xa, factor XIIa, factor IXa, or thrombin by minor proteolysis. In the presence of tissue factor and calcium ions, factor VIIa then converts fac... | Homo sapiens (Human) |
P08721 | OSTP_RAT | MRLAVVCFCLFGLASCLPVKVAEFGSSEEKAHYSKHSDAVATWLKPDPSQKQNLLAPQNSVSSEETDDFKQETLPSNSNESHDHMDDDDDDDDDGDHAESEDSVNSDESDESHHSDESDESFTASTQADVLTPIAPTVDVPDGRGDSLAYGLRSKSRSFPVSDEQYPDATDEDLTSRMKSQESDEAIKVIPVAQRLSVPSDQDSNGKTSHESSQLDEPSVETHSLEQSKEYKQRASHESTEQSDAIDSAEKPDAIDSAERSDAIDSQASSKASLEHQSHEFHSHEDKLVLDPKSKEDDRYLKFRISHELESSSSEVN | null | null | androgen catabolic process [GO:0006710]; bone mineralization [GO:0030282]; calcium ion homeostasis [GO:0055074]; cell adhesion [GO:0007155]; cell differentiation [GO:0030154]; cellular response to fluid shear stress [GO:0071498]; cellular response to leukemia inhibitory factor [GO:1990830]; cellular response to testost... | apical part of cell [GO:0045177]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; perinuclear region of cytoplasm [GO:0048471]; vesicle [GO:0031982] | cytokine activity [GO:0005125]; extracellular matrix binding [GO:0050840]; integrin binding [GO:0005178]; ion binding [GO:0043167]; small molecule binding [GO:0036094] | PF00865; | null | Osteopontin family | PTM: Extensively phosphorylated by FAM20C in the extracellular medium at multiple sites within the S-x-E/pS motif (By similarity). The phosphorylated form inhibits hydroxyapatite crystallization. Dephosphorylation via a mechanism involving ALPL/TNAP promotes hydroxyapatite crystallization (By similarity). {ECO:0000250|... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P10451}. | null | null | null | null | null | FUNCTION: Major non-collagenous bone protein that binds tightly to hydroxyapatite. Appears to form an integral part of the mineralized matrix. Probably important to cell-matrix interaction. {ECO:0000250|UniProtKB:P31096}.; FUNCTION: Acts as a cytokine involved in enhancing production of interferon-gamma and interleukin... | Rattus norvegicus (Rat) |
P08727 | K1C19_HUMAN | MTSYSYRQSSATSSFGGLGGGSVRFGPGVAFRAPSIHGGSGGRGVSVSSARFVSSSSSGAYGGGYGGVLTASDGLLAGNEKLTMQNLNDRLASYLDKVRALEAANGELEVKIRDWYQKQGPGPSRDYSHYYTTIQDLRDKILGATIENSRIVLQIDNARLAADDFRTKFETEQALRMSVEADINGLRRVLDELTLARTDLEMQIEGLKEELAYLKKNHEEEISTLRGQVGGQVSVEVDSAPGTDLAKILSDMRSQYEVMAEQNRKDAEAWFTSRTEELNREVAGHTEQLQMSRSEVTDLRRTLQGLEIELQSQLSMKAAL... | null | null | cell differentiation involved in embryonic placenta development [GO:0060706]; epithelial cell differentiation [GO:0030855]; intermediate filament organization [GO:0045109]; Notch signaling pathway [GO:0007219]; response to estrogen [GO:0043627]; sarcomere organization [GO:0045214] | apicolateral plasma membrane [GO:0016327]; cell periphery [GO:0071944]; costamere [GO:0043034]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; intermediate filament [GO:0005882]; plasma membrane [GO:0005886]; sarcolemma [GO:0042383]; terminal web [GO:1990357]; Z disc [GO:0030018] | structural constituent of cytoskeleton [GO:0005200]; structural constituent of muscle [GO:0008307] | PF00038; | 1.20.5.170;1.20.5.500;1.20.5.1160; | Intermediate filament family | null | null | null | null | null | null | null | FUNCTION: Involved in the organization of myofibers. Together with KRT8, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle. {ECO:0000269|PubMed:16000376}. | Homo sapiens (Human) |
P08729 | K2C7_HUMAN | MSIHFSSPVFTSRSAAFSGRGAQVRLSSARPGGLGSSSLYGLGASRPRVAVRSAYGGPVGAGIREVTINQSLLAPLRLDADPSLQRVRQEESEQIKTLNNKFASFIDKVRFLEQQNKLLETKWTLLQEQKSAKSSRLPDIFEAQIAGLRGQLEALQVDGGRLEAELRSMQDVVEDFKNKYEDEINHRTAAENEFVVLKKDVDAAYMSKVELEAKVDALNDEINFLRTLNETELTELQSQISDTSVVLSMDNSRSLDLDGIIAEVKAQYEEMAKCSRAEAEAWYQTKFETLQAQAGKHGDDLRNTRNEISEMNRAIQRLQA... | null | null | intermediate filament organization [GO:0045109]; keratinization [GO:0031424] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; intermediate filament [GO:0005882]; intermediate filament cytoskeleton [GO:0045111]; keratin filament [GO:0045095]; nucleus [GO:0005634] | structural constituent of skin epidermis [GO:0030280] | PF00038;PF16208; | 1.20.5.170;1.20.5.500;1.20.5.1160; | Intermediate filament family | PTM: Arg-20 is dimethylated, probably to asymmetric dimethylarginine. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:2459129}. | null | null | null | null | null | FUNCTION: Blocks interferon-dependent interphase and stimulates DNA synthesis in cells. Involved in the translational regulation of the human papillomavirus type 16 E7 mRNA (HPV16 E7). {ECO:0000269|PubMed:10492017, ECO:0000269|PubMed:12072504}. | Homo sapiens (Human) |
P08730 | K1C13_MOUSE | MSCRFQSSSMSYGGGFGAGSCQLGGGRNISSCSSRFVTGGSAGGYGGGMSCGFGGGAGGGFGGGFGGGFGGSYGGGFGGGFGDFGGVDGGLLSGNEKITMQNLNDRLASYLDKVRALEAANADLEVKIRDWHLKQSPASPERDYSAYYKTIEELRIKILEATTDNNRIILEIDNARLAADDFRLKYENELTLRQSVEADINGLRRVLDELTLAKTDLEMQIESLNEELAYLKKNHEEEMKEFSNQVVGQVNVEMDATPGIDLTRVLAEMREQYEALAEKNRRDAEEWFQTKSAELNKEVSSNAEMIQTSKTEITELRRTL... | null | null | cellular response to retinoic acid [GO:0071300]; epithelial cell differentiation [GO:0030855]; intermediate filament organization [GO:0045109]; regulation of translation in response to stress [GO:0043555]; tongue morphogenesis [GO:0043587] | cytoskeleton [GO:0005856]; keratin filament [GO:0045095] | structural molecule activity [GO:0005198] | PF00038; | 1.20.5.170;1.20.5.500;1.20.5.1160; | Intermediate filament family | PTM: O-glycosylated; glycans consist of single N-acetylglucosamine residues. {ECO:0000250|UniProtKB:P13646}. | null | null | null | null | null | null | FUNCTION: Type 1 keratin (Probable). Maintains postnatal tongue mucosal cell homeostasis and tissue organization in response to mechanical stress, potentially via regulation of the G1/S phase cyclins CCNE1 and CCNE2 (PubMed:32758484). {ECO:0000269|PubMed:32758484, ECO:0000305}. | Mus musculus (Mouse) |
P08733 | MLRV_RAT | MSPKKAKKRLEGGSSNVFSMFEQTQIQEFKEAFTIMDQNRDGFIDKNDLRDTFAALGRVNVKNEEIDEMIKEAPGPINFTVFLTMFGEKLKGADPEETILNAFKVFDPEGKGSLKADYVREMLTTQAERFSKEEIDQMFAAFPPDVTGNLDYKNLVHIITHGEEKD | null | null | cardiac muscle contraction [GO:0060048]; cardiac myofibril assembly [GO:0055003]; cell growth involved in cardiac muscle cell development [GO:0061049]; heart contraction [GO:0060047]; heart development [GO:0007507]; heart morphogenesis [GO:0003007]; muscle cell development [GO:0055001]; muscle cell fate specification [... | A band [GO:0031672]; cardiac myofibril [GO:0097512]; contractile fiber [GO:0043292]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; myofibril [GO:0030016]; myosin complex [GO:0016459] | actin monomer binding [GO:0003785]; calcium ion binding [GO:0005509]; structural constituent of muscle [GO:0008307] | PF13499; | 1.10.238.10; | null | PTM: N-terminus is methylated by METTL11A/NTM1. {ECO:0000250|UniProtKB:P51667}.; PTM: Phosphorylated by MYLK3 and MYLK2; promotes cardiac muscle contraction and function (By similarity) (PubMed:17885681). Dephosphorylated by PPP1CB complexed to PPP1R12B (PubMed:16431080). The phosphorylated form in adult is expressed a... | SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, A band {ECO:0000269|PubMed:17885681}. | null | null | null | null | null | FUNCTION: Contractile protein that plays a role in heart development and function (By similarity). Following phosphorylation, plays a role in cross-bridge cycling kinetics and cardiac muscle contraction by increasing myosin lever arm stiffness and promoting myosin head diffusion; as a consequence of the increase in max... | Rattus norvegicus (Rat) |
P08750 | DACA_BACSU | MNIKKCKQLLMSLVVLTLAVTCLAPMSKAKAASDPIDINASAAIMIEASSGKILYSKNADKRLPIASMTKMMTEYLLLEAIDQGKVKWDQTYTPDDYVYEISQDNSLSNVPLRKDGKYTVKELYQATAIYSANAAAIAIAEIVAGSETKFVEKMNAKAKELGLTDYKFVNATGLENKDLHGHQPEGTSVNEESEVSAKDMAVLADHLITDYPEILETSSIAKTKFREGTDDEMDMPNWNFMLKGLVSEYKKATVDGLKTGSTDSAGSCFTGTAERNGMRVITVVLNAKGNLHTGRFDETKKMFDYAFDNFSMKEIYAEGD... | 3.4.16.4 | null | cell wall organization [GO:0071555]; peptidoglycan biosynthetic process [GO:0009252]; proteolysis [GO:0006508]; regulation of cell shape [GO:0008360] | extracellular region [GO:0005576]; membrane raft [GO:0045121]; plasma membrane [GO:0005886] | serine-type D-Ala-D-Ala carboxypeptidase activity [GO:0009002] | PF07943;PF00768; | 2.60.410.10;3.40.710.10; | Peptidase S11 family | null | SUBCELLULAR LOCATION: Secreted, cell wall. Cell membrane {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22882210}. Membrane raft {ECO:0000269|PubMed:20713508, ECO:0000269|PubMed:22882210, ECO:0000269|PubMed:23651456}. Note=Present in detergent-resistant membrane (DRM) fractions that may be equivalent to eukaryotic me... | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.; EC=3.4.16.4; | null | PATHWAY: Cell wall biogenesis; peptidoglycan biosynthesis. | null | null | FUNCTION: Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors. | Bacillus subtilis (strain 168) |
P08752 | GNAI2_MOUSE | MGCTVSAEDKAAAERSKMIDKNLREDGEKAAREVKLLLLGAGESGKSTIVKQMKIIHEDGYSEEECRQYRAVVYSNTIQSIMAIVKAMGNLQIDFADPQRADDARQLFALSCAAEEQGMLPEDLSGVIRRLWADHGVQACFGRSREYQLNDSAAYYLNDLERIAQSDYIPTQQDVLRTRVKTTGIVETHFTFKDLHFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSAYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKITQSSLTICFPEYTGANKYDEAASYIQSKFEDLNKRKDTKEI... | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway [GO:0007193]; cell cycle [GO:0007049]; cell division [GO:0051301]; cell population proliferation [GO:0008283]; G protein-coupled acetylcholine receptor signal... | cell body [GO:0044297]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; heterotrimeric G-protein complex [GO:0005834]; midbody [GO:0030496]; neuronal dense core vesicle [GO:0098992]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; synapse [GO:0045202] | G protein-coupled receptor binding [GO:0001664]; G-protein beta/gamma-subunit complex binding [GO:0031683]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872] | PF00503; | 1.10.400.10;3.40.50.300; | G-alpha family, G(i/o/t/z) subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cell membrane {ECO:0000250}. Membrane {ECO:0000250|UniProtKB:P04899}; Lipid-anchor {ECO:0000250|UniProtKB:P04899}. Note=Localizes in the centrosomes of interphase and mitotic cells. Detected ... | null | null | null | null | null | FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(i) proteins are involved in hormonal regulation of adenylate cyclase: they inhibit the cyclase in response to beta-adrenergic stimuli. May play a role in cell division. | Mus musculus (Mouse) |
P08753 | GNAI3_RAT | MGCTLSAEDKAAVERSKMIDRNLREDGEKAAKEVKLLLLGAGESGKSTIVKQMKIIHEDGYSEDECKQYKVVVYSNTIQSIIAIIRAMGRLKIDFGEAARADDARQLFVLAGSAEEGVMTSELAGVIKRLWRDGGVQACFSRSREYQLNDSASYYLNDLDRISQTNYIPTQQDVLRTRVKTTGIVETHFTFKELYFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTDTSIILFLNKKDLFEEKIKRSPLTICYPEYTGSNTYEEAAAYIQCQFEDLNRRKDTKEVY... | null | null | adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway [GO:0007193]; adenylate cyclase-modulating G protein-coupled receptor signaling pathway [GO:0007188]; cell cycle [GO:0007049]; cell division [GO:0051301]; dopamine receptor signaling pathway [GO:0007212]; GTP metabolic process [GO:0046039]; negat... | centrosome [GO:0005813]; cytoplasm [GO:0005737]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; heterotrimeric G-protein complex [GO:0005834]; midbody [GO:0030496]; plasma membrane [GO:0005886]; zymogen granule [GO:0042588] | G protein-coupled receptor binding [GO:0001664]; G protein-coupled serotonin receptor binding [GO:0031821]; G-protein beta/gamma-subunit complex binding [GO:0031683]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activating protein binding [GO:0032794]; GTPase activity [GO:0003924]; metal ion binding [GO:0... | PF00503; | 1.10.400.10;3.40.50.300; | G-alpha family, G(i/o/t/z) subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P08754}. Cell membrane {ECO:0000250|UniProtKB:P08754}; Lipid-anchor {ECO:0000305}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P08754}. Note=Localizes in the centrosomes of interphase and mitotic cells. Detected at the ... | null | null | null | null | null | FUNCTION: Heterotrimeric guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades. The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound st... | Rattus norvegicus (Rat) |
P08754 | GNAI3_HUMAN | MGCTLSAEDKAAVERSKMIDRNLREDGEKAAKEVKLLLLGAGESGKSTIVKQMKIIHEDGYSEDECKQYKVVVYSNTIQSIIAIIRAMGRLKIDFGEAARADDARQLFVLAGSAEEGVMTPELAGVIKRLWRDGGVQACFSRSREYQLNDSASYYLNDLDRISQSNYIPTQQDVLRTRVKTTGIVETHFTFKDLYFKMFDVGGQRSERKKWIHCFEGVTAIIFCVALSDYDLVLAEDEEMNRMHESMKLFDSICNNKWFTETSIILFLNKKDLFEEKIKRSPLTICYPEYTGSNTYEEAAAYIQCQFEDLNRRKDTKEIY... | null | null | adenylate cyclase-inhibiting G protein-coupled receptor signaling pathway [GO:0007193]; adenylate cyclase-modulating G protein-coupled receptor signaling pathway [GO:0007188]; cell cycle [GO:0007049]; cell division [GO:0051301]; dopamine receptor signaling pathway [GO:0007212]; GTP metabolic process [GO:0046039]; negat... | centrosome [GO:0005813]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; heterotrimeric G-protein complex [GO:0005834]; lysosomal membrane [GO:0005765]; membrane [GO:0016020]; midbody [GO:0030496]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886] | G protein-coupled receptor binding [GO:0001664]; G-protein beta/gamma-subunit complex binding [GO:0031683]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872] | PF00503; | 1.10.400.10;3.40.50.300; | G-alpha family, G(i/o/t/z) subfamily | PTM: (Microbial infection) Deamidated at Gln-204 by Photorhabdus asymbiotica toxin PAU_02230, blocking GTP hydrolysis of heterotrimeric GNAQ or GNA11 and G-alphai (GNAI1, GNAI2 or GNAI3) proteins, thereby activating RhoA. {ECO:0000269|PubMed:24141704}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17635935}. Cell membrane {ECO:0000269|PubMed:17635935, ECO:0000269|PubMed:27864364}; Lipid-anchor {ECO:0000305}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17635935}. Note=Localizes in the centrosomes of interphase and mitot... | null | null | null | null | null | FUNCTION: Heterotrimeric guanine nucleotide-binding proteins (G proteins) function as transducers downstream of G protein-coupled receptors (GPCRs) in numerous signaling cascades. The alpha chain contains the guanine nucleotide binding site and alternates between an active, GTP-bound state and an inactive, GDP-bound st... | Homo sapiens (Human) |
P08758 | ANXA5_HUMAN | MAQVLRGTVTDFPGFDERADAETLRKAMKGLGTDEESILTLLTSRSNAQRQEISAAFKTLFGRDLLDDLKSELTGKFEKLIVALMKPSRLYDAYELKHALKGAGTNEKVLTEIIASRTPEELRAIKQVYEEEYGSSLEDDVVGDTSGYYQRMLVVLLQANRDPDAGIDEAQVEQDAQALFQAGELKWGTDEEKFITIFGTRSVSHLRKVFDKYMTISGFQIEETIDRETSGNLEQLLLAVVKSIRSIPAYLAETLYYAMKGAGTDDHTLIRVMVSRSEIDLFNIRKEFRKNFATSLYSMIKGDTSGDYKKALLLLCGEDD | null | null | blood coagulation [GO:0007596]; negative regulation of apoptotic process [GO:0043066]; negative regulation of coagulation [GO:0050819]; response to organic substance [GO:0010033]; signal transduction [GO:0007165] | collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endothelial microparticle [GO:0072563]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; focal adhesion [GO:0005925]; membrane [GO:0016020]; sarcolemm... | calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; phosphatidylserine binding [GO:0001786]; phospholipase inhibitor activity [GO:0004859]; phospholipid binding [GO:0005543] | PF00191; | 1.10.220.10; | Annexin family | PTM: S-nitrosylation is induced by interferon-gamma and oxidatively-modified low-densitity lipoprotein (LDL(ox)) possibly implicating the iNOS-S100A8/9 transnitrosylase complex. {ECO:0000305|PubMed:25417112}. | null | null | null | null | null | null | FUNCTION: This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade. | Homo sapiens (Human) |
P08760 | KAD3_BOVIN | MGASARLLRAAIMGAPGSGKGTVSSRITKHFELKHLSSGDLLRDNMLRGTEIGVLAKTFIDQGKLIPDDVMTRLVLHELKNLTQYNWLLDGFPRTLPQAEALDRAYQIDTVINLNVPFEVIKQRLTARWIHPGSGRVYNIEFNPPKTMGIDDLTGEPLVQREDDRPETVVKRLKAYEAQTEPVLEYYRKKGVLETFSGTETNKIWPHVYAFLQTKLPQRSQETSVTP | 2.7.4.10 | null | ADP biosynthetic process [GO:0006172]; AMP metabolic process [GO:0046033]; GTP metabolic process [GO:0046039]; ITP metabolic process [GO:0046041]; nucleoside triphosphate biosynthetic process [GO:0009142]; phosphorylation [GO:0016310]; UTP metabolic process [GO:0046051] | cytoplasm [GO:0005737]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | adenylate kinase activity [GO:0004017]; ATP binding [GO:0005524]; GTP binding [GO:0005525]; nucleoside triphosphate adenylate kinase activity [GO:0046899] | PF00406;PF05191; | 3.40.50.300; | Adenylate kinase family, AK3 subfamily | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000255|HAMAP-Rule:MF_03169, ECO:0000269|PubMed:6088234}. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + AMP = a ribonucleoside 5'-diphosphate + ADP; Xref=Rhea:RHEA:13749, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.10; Evidence={ECO:0000255|HAMAP-Rule:MF_03169}; | null | null | null | null | FUNCTION: Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Has GTP:AMP phosphotransferase and ITP:AMP phosphotransferase activities. {ECO:0000255|HAMAP-Rule:MF_03169}. | Bos taurus (Bovine) |
P08761 | MSRA_DROME | MSLTITSSVTHPELKDLSTVRNEQKELNISPVHDVNVTKATATFGMGCFWGAESLYGATRGVLRTTVGYAGGSSDLPTYRKMGDHTEVLEIDYDPTVISFKELLDLFWNNHEYGLTTPIKRQYASLILYHDEEQKQVAHASKLEEQERRAPEIITTEIASKENFYPAEAYHQKYRLQGHKDLASSLNLSPKLLQTSYVATKLNGYLAGVGGIEQFKAEAETMGLTPTQRQYCYYHVEQNEGQGLYC | 1.8.4.11 | null | cellular response to oxidative stress [GO:0034599]; determination of adult lifespan [GO:0008340]; response to oxidative stress [GO:0006979]; sulfur amino acid metabolic process [GO:0000096] | cytoplasm [GO:0005737] | L-methionine-(S)-S-oxide reductase activity [GO:0036456]; peptide-methionine (S)-S-oxide reductase activity [GO:0008113] | PF01625; | 3.30.1060.10; | MsrA Met sulfoxide reductase family | PTM: Conjugated to URM1, a ubiquitin-like protein. {ECO:0000269|PubMed:28953965}. | null | CATALYTIC ACTIVITY: Reaction=[thioredoxin]-disulfide + H2O + L-methionyl-[protein] = [thioredoxin]-dithiol + L-methionyl-(S)-S-oxide-[protein]; Xref=Rhea:RHEA:14217, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700, Rhea:RHEA-COMP:12313, Rhea:RHEA-COMP:12315, ChEBI:CHEBI:15377, ChEBI:CHEBI:16044, ChEBI:CHEBI:29950, ChEBI:CHE... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.6 mM for L-methionine sulfoxide {ECO:0000269|PubMed:30529269}; Vmax=0.15 umol/min/mg enzyme towards L-methionine sulfoxide (at 25 degrees Celsius) {ECO:0000269|PubMed:30529269}; | null | null | null | FUNCTION: Has an important function as a repair enzyme for proteins that have been inactivated by oxidation. Catalyzes the reduction of methionine sulfoxide in proteins to methionine (PubMed:12145281, PubMed:30529269). Does not catalyze the reverse reaction involving the oxidation of methionine residues (PubMed:3052926... | Drosophila melanogaster (Fruit fly) |
P08768 | POLS_EEEV | MFPYPTLNYPPMAPINPMAYRDPNPPRQVAPFRPPLAAQIEDLRRSIANLTLKQRAPNPPAGPPAKRKKPAPSLSLETKKKRPPPPAKKQKRKPKPGKRQRMCMKLESDKTFPIMLNGQVNGYACVVGGRVFKPLHVEGRIDNEQLAAIKLKKASIYDLEYGDVPQCMKSDTLQYTSDKPPGFYNWHHGAVQYENNRFTVPRGVGGKGDSGRPILDNKGRVVAIVQGGVNEGSRTALSVVTWNQKGVTVKDTPEGSEPWSLATVMCVLANITFPCDQPPCMPCCYEKNPHETLTMLEQNYDSRAYDQLLDAAVKCNARRT... | 3.4.21.90 | null | fusion of virus membrane with host endosome membrane [GO:0039654]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host gene expression [GO:0039657]; symbiont-mediated suppression of host toll-like receptor signaling pathway [GO:0039722]; virion attachment to host ... | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; T=4 icosahedral viral capsid [GO:0039619]; virion membrane [GO:0055036] | RNA binding [GO:0003723]; serine-type endopeptidase activity [GO:0004252]; structural molecule activity [GO:0005198] | PF01589;PF00943;PF01563;PF00944; | 1.10.287.2230;2.60.40.350;2.60.40.3200;2.60.40.4310;2.60.40.2400;2.60.98.10;2.40.10.10; | null | PTM: Structural polyprotein: Specific enzymatic cleavages in vivo yield mature proteins. Capsid protein is auto-cleaved during polyprotein translation, unmasking a signal peptide at the N-terminus of the precursor of E3/E2. The remaining polyprotein is then targeted to the host endoplasmic reticulum, where host signal ... | SUBCELLULAR LOCATION: [Capsid protein]: Virion {ECO:0000250|UniProtKB:P03316}. Host cytoplasm {ECO:0000250|UniProtKB:P09592}. Host cell membrane {ECO:0000250|UniProtKB:P03316}. Host nucleus {ECO:0000250|UniProtKB:P09592}.; SUBCELLULAR LOCATION: [Spike glycoprotein E2]: Virion membrane {ECO:0000250|UniProtKB:Q8JUX5}; Si... | CATALYTIC ACTIVITY: Reaction=Autocatalytic release of the core protein from the N-terminus of the togavirus structural polyprotein by hydrolysis of a -Trp-|-Ser- bond.; EC=3.4.21.90; Evidence={ECO:0000250|UniProtKB:P03316}; | null | null | null | null | FUNCTION: [Capsid protein]: Forms an icosahedral capsid with a T=4 symmetry composed of 240 copies of the capsid protein surrounded by a lipid membrane through which penetrate 80 spikes composed of trimers of E1-E2 heterodimers (By similarity). The capsid protein binds to the viral RNA genome at a site adjacent to a ri... | Eastern equine encephalitis virus (EEEV) (Eastern equine encephalomyelitis virus) |
P08775 | RPB1_MOUSE | MHGGGPPSGDSACPLRTIKRVQFGVLSPDELKRMSVTEGGIKYPETTEGGRPKLGGLMDPRQGVIERTGRCQTCAGNMTECPGHFGHIELAKPVFHVGFLVKTMKVLRCVCFFCSKLLVDSNNPKIKDILAKSKGQPKKRLTHVYDLCKGKNICEGGEEMDNKFGVEQPEGDEDLTKEKGHGGCGRYQPRIRRSGLELYAEWKHVNEDSQEKKILLSPERVHEIFKRISDEECFVLGMEPRYARPEWMIVTVLPVPPLSVRPAVVMQGSARNQDDLTHKLADIVKINNQLRRNEQNGAAAHVIAEDVKLLQFHVATMVDN... | 2.7.7.48; 2.7.7.6; 3.1.13.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P24928}; Note=Two Mg(2+) ions are coordinated by both the catalytic residues and the nucleic acid substrate to enhance substrate recognition and catalytic efficiency. {ECO:0000250|UniProtKB:P24928}; | cellular response to oxygen levels [GO:0071453]; DNA-templated transcription termination [GO:0006353]; positive regulation of RNA splicing [GO:0033120]; response to organic cyclic compound [GO:0014070]; transcription by RNA polymerase II [GO:0006366] | cytoplasm [GO:0005737]; euchromatin [GO:0000791]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II, core complex [GO:0005665] | core promoter sequence-specific DNA binding [GO:0001046]; DNA binding [GO:0003677]; DNA-directed 5'-3' RNA polymerase activity [GO:0003899]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; promoter-specific chromatin binding [GO:1990841]; RNA polymerase II activity [GO:0001055] | PF04997;PF00623;PF04983;PF05000;PF04998;PF04992;PF04990;PF05001; | 1.10.132.30;1.10.150.390;2.40.40.20;3.30.1360.140;6.10.250.2940;6.20.50.80;3.30.1490.180;4.10.860.120;1.10.274.100; | RNA polymerase beta' chain family | PTM: The tandem heptapeptide repeats in the C-terminal domain (CTD) can be highly phosphorylated. The phosphorylation activates Pol II. Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5' of the heptapeptide repeat and is mediated, at least, by CDK7 and CDK9. CDK7 phosphorylation of POLR2A associated with DNA... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:24207025, ECO:0000269|PubMed:26687004}. Cytoplasm {ECO:0000250|UniProtKB:P24928}. Chromosome {ECO:0000250|UniProtKB:P24928}. Note=Hypophosphorylated form is mainly found in the cytoplasm, while the hyperphosphorylated and active form is nuclear. Co-localizes with kinase... | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.6; Evidence={ECO:0000250|UniProtKB:P24928}; PhysiologicalDirection=left-to-right; Xref=Rhe... | null | null | null | null | FUNCTION: Catalytic core component of RNA polymerase II (Pol II), a DNA-dependent RNA polymerase which synthesizes mRNA precursors and many functional non-coding RNAs using the four ribonucleoside triphosphates as substrates (By similarity). Pol II-mediated transcription cycle proceeds through transcription initiation,... | Mus musculus (Mouse) |
P08779 | K1C16_HUMAN | MTTCSRQFTSSSSMKGSCGIGGGIGGGSSRISSVLAGGSCRAPSTYGGGLSVSSRFSSGGACGLGGGYGGGFSSSSSFGSGFGGGYGGGLGAGFGGGLGAGFGGGFAGGDGLLVGSEKVTMQNLNDRLASYLDKVRALEEANADLEVKIRDWYQRQRPSEIKDYSPYFKTIEDLRNKIIAATIENAQPILQIDNARLAADDFRTKYEHELALRQTVEADVNGLRRVLDELTLARTDLEMQIEGLKEELAYLRKNHEEEMLALRGQTGGDVNVEMDAAPGVDLSRILNEMRDQYEQMAEKNRRDAETWFLSKTEELNKEVA... | null | null | cytoskeleton organization [GO:0007010]; epithelial cell differentiation [GO:0030855]; establishment of skin barrier [GO:0061436]; hair cycle [GO:0042633]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; intermediate filament organization [GO:0045109]; keratinization [GO:0031424]; keratinocyte d... | cornified envelope [GO:0001533]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; intermediate filament [GO:0005882]; keratin filament [GO:0045095]; nucleus [GO:0005634] | structural constituent of cytoskeleton [GO:0005200] | PF00038; | 1.20.5.170;1.20.5.500;1.20.5.1160; | Intermediate filament family | null | null | null | null | null | null | null | FUNCTION: Epidermis-specific type I keratin that plays a key role in skin. Acts as a regulator of innate immunity in response to skin barrier breach: required for some inflammatory checkpoint for the skin barrier maintenance. {ECO:0000250|UniProtKB:Q9Z2K1}. | Homo sapiens (Human) |
P08796 | CSA_DICDI | MKFLLVLIILYNILNSAHSAPTITAVSNGKFGVPTYITITGTGFTGTPVVTIGGQTCDPVIVANTASLQCQFSAQLAPGNSNFDVIVKVGGVPSTGGNGLFKYTPPTLSTIFPNNGRIGMILVDGPSNISGYKLNVNDSINSAMLSVTADSVSPTIYFLVPNTIAGGLLNLELIQPFGFSTIVTSKSVFSPTITSITPLAFDLTPTNVTVTGKYFGTTASVTMGSHIYTGLTVQDDGTNCHVIFTTRSVYESSNTITAKASTGVDMIYLDNQGNQQPITFTYNPPTITSTKQVNDSVEISTTNTGTDFTQISLTMGTSSP... | null | null | aggregation involved in sorocarp development [GO:0031152]; calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules [GO:0016338]; cell-cell adhesion [GO:0098609]; cell-cell adhesion via plasma-membrane adhesion molecules [GO:0098742]; cortical actin cytoskeleton organization [GO:0030866]; homo... | cell surface [GO:0009986]; cell-cell junction [GO:0005911]; external side of plasma membrane [GO:0009897]; filopodium [GO:0030175]; membrane raft [GO:0045121]; plasma membrane [GO:0005886] | cell-cell adhesion mediator activity [GO:0098632]; identical protein binding [GO:0042802] | null | 2.60.40.10; | null | PTM: Phosphorylated on serine and N-glycosylated with two types of oligosaccharide chains.; PTM: The GPI-like-anchor contains a phosphoceramide group, rather than a phosphatidyl group. | SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. Note=Attached to the membrane by a GPI-anchor that contains a phosphoceramide moiety. Such anchor mediates a fast and long persistence cell adhesion of the protein. | null | null | null | null | null | FUNCTION: This cell-surface glycoprotein mediates cell-cell binding via homophilic interaction. | Dictyostelium discoideum (Social amoeba) |
P08799 | MYS2_DICDI | MNPIHDRTSDYHKYLKVKQGDSDLFKLTVSDKRYIWYNPDPKERDSYECGEIVSETSDSFTFKTVDGQDRQVKKDDANQRNPIKFDGVEDMSELSYLNEPAVFHNLRVRYNQDLIYTYSGLFLVAVNPFKRIPIYTQEMVDIFKGRRRNEVAPHIFAISDVAYRSMLDDRQNQSLLITGESGAGKTENTKKVIQYLASVAGRNQANGSGVLEQQILQANPILEAFGNAKTTRNNNSSRFGKFIEIQFNSAGFISGASIQSYLLEKSRVVFQSETERNYHIFYQLLAGATAEEKKALHLAGPESFNYLNQSGCVDIKGVSD... | null | null | actin-myosin filament sliding [GO:0033275]; aggregation involved in sorocarp development [GO:0031152]; bleb assembly [GO:0032060]; cell motility [GO:0048870]; chemotaxis [GO:0006935]; contractile actin filament bundle assembly [GO:0030038]; contractile vacuole organization [GO:0033298]; cortical actin cytoskeleton orga... | actomyosin [GO:0042641]; actomyosin contractile ring [GO:0005826]; apical cortex [GO:0045179]; cell cortex [GO:0005938]; cell trailing edge [GO:0031254]; cleavage furrow [GO:0032154]; cortical actin cytoskeleton [GO:0030864]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; cytoskeleton [GO:0005856]; cytosol [... | 14-3-3 protein binding [GO:0071889]; actin filament binding [GO:0051015]; adenyl nucleotide binding [GO:0030554]; ATP binding [GO:0005524]; calcium-dependent ATPase activity [GO:0030899]; calmodulin binding [GO:0005516]; cytoskeletal motor activity [GO:0003774]; identical protein binding [GO:0042802]; microfilament mot... | PF00063;PF02736;PF01576; | 1.10.10.820;1.20.5.340;1.20.58.530;3.30.70.1590;3.40.850.10;2.30.30.360;1.20.120.720;4.10.270.10; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | PTM: Phosphorylation inhibits thick filament formation and reduces the actin-activated ATPase activity. {ECO:0000269|PubMed:2387408, ECO:0000269|PubMed:2828113}. | SUBCELLULAR LOCATION: Cytoplasm, cell cortex. Note=Highest concentration in the posterior cell cortex. | null | null | null | null | null | FUNCTION: Myosin is a protein that binds to actin and has ATPase activity that is activated by actin. | Dictyostelium discoideum (Social amoeba) |
P08810 | ENV_SIVM2 | MGCLGNQLLIAILLLSVYGIYCTQYVTVFYGVPAWRNATIPLFCATKNRDTWGTTQCLPDNGDYSELALNVTESFDAWENTVTEQAIEDVWQLFETSIKPCVKLSPLCITMRCNKSETDRWGLTKSSTTITTAAPTSAPVSEKIDMVNETSSCIAQNNCTGLEQEQMISCKFTMTGLKRDKTKEYNETWYSTDLVCEQGNSTDNESRCYMNHCNTSVIQESCDKHYWDTIRFRYCAPPGYALLRCNDTNYSGFMPKCSKVVVSSCTRMMETQTSTWFGFNGTRAENRTYIYWHGRDNRTIISLNKYYNLTMKCRRPGNKT... | null | null | membrane fusion involved in viral entry into host cell [GO:0039663]; symbiont entry into host cell [GO:0046718]; 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 CCR5. This peculiar 2 stage receptor-interaction strategy allows gp120 t... | Simian immunodeficiency virus (isolate Mm251) (SIV-mac) (Simian immunodeficiency virus rhesus monkey) |
P08818 | CBP2_HORVU | MRTTTRRLPPAPAAAAVLLAALTCLLLRPAAVAAAGGHAADRIVRLPGQPEVDFDMYSGYITVDEAAGRSLFYLLQEAPEEAQPAPLVLWLNGGPGCSSVAYGASEELGAFRVMPRGAGLVLNEYRWNKVANVLFLDSPAGVGFSYTNTSSDIYTSGDNRTAHDSYAFLAAWFERFPHYKYREFYVAGESYAGHYVPELSQLVHRSGNPVINLKGFMVGNGLIDDYHDYVGTFEFWWNHGIVSDDTYRRLKDACLHDSFIHPSPACDAATDVATAEQGNIDMYSLYTPVCNISSSSSSSSLSRRRTRGRYPWLTGSYDPC... | 3.4.16.6 | null | proteolysis [GO:0006508] | extracellular region [GO:0005576] | serine-type carboxypeptidase activity [GO:0004185] | PF00450; | 3.40.50.11320;6.10.250.940;3.40.50.1820; | Peptidase S10 family | null | SUBCELLULAR LOCATION: Secreted. Note=Secreted into the endosperm. | CATALYTIC ACTIVITY: Reaction=Preferential release of a C-terminal arginine or lysine residue.; EC=3.4.16.6; | null | null | null | null | FUNCTION: May be involved in the degradation of small peptides (2-5 residues) or in the degradation of storage proteins in the embryo. | Hordeum vulgare (Barley) |
P08819 | CBP2_WHEAT | VEPSGHAADRIARLPGQPAVDFDMYSGYITVDEGAGRSLFYLLQEAPEDAQPAPLVLWLNGGPGCSSVAYGASEELGAFRVKPRGAGLVLNEYRWNKVANVLFLDSPAGVGFSYTNTSSDIYTSGDNRTAHDSYAFLAKWFERFPHYKYRDFYIAGESYAGHYVPELSQLVHRSKNPVINLKGFMVGNGLIDDYHDYVGTFEFWWNHGIVSDDTYRRLKEACLHDSFIHPSPACDAATDVATAEQGNIDMYSLYTPVCNITSSSSSSSSSLSQQRRSRGRYPWLTGSYDPCTERYSTAYYNRRDVQMALHANVTGAMNYT... | 3.4.16.6 | null | proteolysis [GO:0006508] | null | serine-type carboxypeptidase activity [GO:0004185] | PF00450; | 3.40.50.11320;6.10.250.940;3.40.50.1820; | Peptidase S10 family | PTM: N-glycosylated. | null | CATALYTIC ACTIVITY: Reaction=Preferential release of a C-terminal arginine or lysine residue.; EC=3.4.16.6; | null | null | null | null | null | Triticum aestivum (Wheat) |
P08821 | DBH1_BACSU | MNKTELINAVAEASELSKKDATKAVDSVFDTILDALKNGDKIQLIGFGNFEVRERSARKGRNPQTGEEIEIPASKVPAFKPGKALKDAVAGK | null | null | chromosome condensation [GO:0030261] | cytosol [GO:0005829]; nucleoid [GO:0009295] | DNA binding [GO:0003677]; structural constituent of chromatin [GO:0030527] | PF00216; | 4.10.520.10; | Bacterial histone-like protein family | null | SUBCELLULAR LOCATION: Cytoplasm, nucleoid {ECO:0000269|PubMed:21085634, ECO:0000269|PubMed:8439548}. Note=Evenly distributed along the nucleoid (PubMed:21085634). {ECO:0000269|PubMed:21085634}. | null | null | null | null | null | FUNCTION: Histone-like DNA-binding protein which introduces negative supercoils in relaxed plasmid DNA in the presence of topoisomerase I. There are at least 20,000 monomers/cell (PubMed:8439548). Capable of wrapping DNA to stabilize it, and thus to prevent its denaturation under extreme environmental conditions. Binds... | Bacillus subtilis (strain 168) |
P08833 | IBP1_HUMAN | MSEVPVARVWLVLLLLTVQVGVTAGAPWQCAPCSAEKLALCPPVSASCSEVTRSAGCGCCPMCALPLGAACGVATARCARGLSCRALPGEQQPLHALTRGQGACVQESDASAPHAAEAGSPESPESTEITEEELLDNFHLMAPSEEDHSILWDAISTYDGSKALHVTNIKKWKEPCRIELYRVVESLAKAQETSGEEISKFYLPNCNKNGFYHSRQCETSMDGEAGLCWCVYPWNGKRIPGSPEIRGDPNCQIYFNVQN | null | null | insulin receptor signaling pathway [GO:0008286]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; positive regulation of cell growth [GO:0030307]; regulation of insulin-like growth factor receptor signaling pathway [GO:0043567]; response to organic cyclic compound [GO:0014070]; signal transduction [... | endoplasmic reticulum lumen [GO:0005788]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794] | insulin-like growth factor binding [GO:0005520]; insulin-like growth factor I binding [GO:0031994]; insulin-like growth factor II binding [GO:0031995]; signaling receptor binding [GO:0005102] | PF00219;PF00086; | 4.10.40.20;4.10.800.10; | null | PTM: Phosphorylated; probably by casein kinase II. Phosphorylation alters the affinity of the protein for IGFs. In amniotic fluid, the unmodified protein is the most abundant form, while mono-, bi-, tri- and tetraphosphorylated forms are present in decreasing amounts. The phosphorylation state may influence the propens... | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. Promotes cell migration. {ECO:0000269|PubMed:15972819}. | Homo sapiens (Human) |
P08835 | ALBU_PIG | MKWVTFISLLFLFSSAYSRGVFRRDTYKSEIAHRFKDLGEQYFKGLVLIAFSQHLQQCPYEEHVKLVREVTEFAKTCVADESAENCDKSIHTLFGDKLCAIPSLREHYGDLADCCEKEEPERNECFLQHKNDNPDIPKLKPDPVALCADFQEDEQKFWGKYLYEIARRHPYFYAPELLYYAIIYKDVFSECCQAADKAACLLPKIEHLREKVLTSAAKQRLKCASIQKFGERAFKAWSLARLSQRFPKADFTEISKIVTDLAKVHKECCHGDLLECADDRADLAKYICENQDTISTKLKECCDKPLLEKSHCIAEAKRDE... | null | null | cellular response to calcium ion starvation [GO:0072732]; cellular response to starvation [GO:0009267]; negative regulation of mitochondrial depolarization [GO:0051902] | blood microparticle [GO:0072562]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; protein-containing complex [GO:0032991] | DNA binding [GO:0003677]; enterobactin binding [GO:1903981]; fatty acid binding [GO:0005504]; metal ion binding [GO:0046872]; pyridoxal phosphate binding [GO:0030170]; small molecule binding [GO:0036094]; toxic substance binding [GO:0015643] | PF00273; | 1.10.246.10; | ALB/AFP/VDB family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Binds water, Ca(2+), Na(+), K(+), fatty acids, hormones, bilirubin and drugs. Its main function is the regulation of the colloidal osmotic pressure of blood. Major zinc transporter in plasma, typically binds about 80% of all plasma zinc (By similarity). Major calcium and magnesium transporter in plasma, binds... | Sus scrofa (Pig) |
P08836 | FPPS_CHICK | MHKFTGVNAKFQQPALRNLSPVVVEREREEFVGFFPQIVRDLTEDGIGHPEVGDAVARLKEVLQYNAPGGKCNRGLTVVAAYRELSGPGQKDAESLRCALAVGWCIELFQAFFLVADDIMDQSLTRRGQLCWYKKEGVGLDAINDSFLLESSVYRVLKKYCRQRPYYVHLLELFLQTAYQTELGQMLDLITAPVSKVDLSHFSEERYKAIVKYKTAFYSFYLPVAAAMYMVGIDSKEEHENAKAILLEMGEYFQIQDDYLDCFGDPALTGKVGTDIQDNKCSWLVVQCLQRVTPEQRQLLEDNYGRKEPEKVAKVKELYE... | 2.5.1.1; 2.5.1.10 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305|PubMed:8086404}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000305|PubMed:8086404}; | cholesterol biosynthetic process [GO:0006695]; farnesyl diphosphate biosynthetic process [GO:0045337]; geranyl diphosphate biosynthetic process [GO:0033384] | cytoplasm [GO:0005737] | dimethylallyltranstransferase activity [GO:0004161]; geranyltranstransferase activity [GO:0004337]; metal ion binding [GO:0046872] | PF00348; | 1.10.600.10; | FPP/GGPP synthase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=dimethylallyl diphosphate + isopentenyl diphosphate = (2E)-geranyl diphosphate + diphosphate; Xref=Rhea:RHEA:22408, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769; EC=2.5.1.1; CATALYTIC ACTIVITY: Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,... | null | PATHWAY: Isoprenoid biosynthesis; farnesyl diphosphate biosynthesis; farnesyl diphosphate from geranyl diphosphate and isopentenyl diphosphate: step 1/1.; PATHWAY: Isoprenoid biosynthesis; geranyl diphosphate biosynthesis; geranyl diphosphate from dimethylallyl diphosphate and isopentenyl diphosphate: step 1/1. | null | null | FUNCTION: Catalyzes the sequential condensation of isopentenyl pyrophosphate with the allylic pyrophosphates, dimethylallyl pyrophosphate, and then with the resultant geranylpyrophosphate to the ultimate product farnesyl pyrophosphate. | Gallus gallus (Chicken) |
P08839 | PT1_ECOLI | MISGILASPGIAFGKALLLKEDEIVIDRKKISADQVDQEVERFLSGRAKASAQLETIKTKAGETFGEEKEAIFEGHIMLLEDEELEQEIIALIKDKHMTADAAAHEVIEGQASALEELDDEYLKERAADVRDIGKRLLRNILGLKIIDLSAIQDEVILVAADLTPSETAQLNLKKVLGFITDAGGRTSHTSIMARSLELPAIVGTGSVTSQVKNDDYLILDAVNNQVYVNPTNEVIDKMRAVQEQVASEKAELAKLKDLPAITLDGHQVEVCANIGTVRDVEGAERNGAEGVGLYRTEFLFMDRDALPTEEEQFAAYKAV... | 2.7.3.9 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:17053069}; | phosphoenolpyruvate-dependent sugar phosphotransferase system [GO:0009401]; phosphorylation [GO:0016310] | cytosol [GO:0005829] | identical protein binding [GO:0042802]; kinase activity [GO:0016301]; metal ion binding [GO:0046872]; phosphoenolpyruvate-protein phosphotransferase activity [GO:0008965] | PF05524;PF00391;PF02896; | 3.20.20.60;3.50.30.10;1.10.274.10; | PEP-utilizing enzyme family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=L-histidyl-[protein] + phosphoenolpyruvate = N(pros)-phospho-L-histidyl-[protein] + pyruvate; Xref=Rhea:RHEA:23880, Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746, ChEBI:CHEBI:15361, ChEBI:CHEBI:29979, ChEBI:CHEBI:58702, ChEBI:CHEBI:64837; EC=2.7.3.9; Evidence={ECO:0000269|PubMed:12705838}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.11 mM for ZFPEP {ECO:0000269|PubMed:12705838}; KM=0.12 mM for EClPEP {ECO:0000269|PubMed:12705838}; KM=0.14 mM for PEP {ECO:0000269|PubMed:12705838}; KM=0.25 mM for ZClPEP {ECO:0000269|PubMed:12705838}; KM=0.43 mM for ZMePEP {ECO:0000269|PubMed:12705838}; Note=kc... | null | null | null | FUNCTION: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. Enzyme I transfer... | Escherichia coli (strain K12) |
P08841 | TBB3_DROME | MREIVNLQAGQCGNQIGAKFWEIISEEHGIDSNGIYVGDSDLQLERVSVYYNEASAVTRSSGGKYVPRAILLDLEPGTMESVRSGPYGQLFRPDNFVYGQSGAGNNWAKGHYTEGAELVDNVLDVVRKECENCDCLQGFQLTHSLGGGTGSGMGTLLISKIREEYPDRIMNTYSVVPSPKVSDTVVEPYNATLSIHQLVENTDETYCIDNEALYDICFRTLKVSNPSYGDLNHLVSLTMSGVTTCLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTSRGSQQYRALTVPELTQQMFDAKNMMAACDPRHGRYLTVA... | null | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363}; | axon guidance [GO:0007411]; axonogenesis [GO:0007409]; larval behavior [GO:0030537]; microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278]; response to light stimulus [GO:0009416] | cytoplasm [GO:0005737]; microtubule [GO:0005874] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872]; structural constituent of cytoskeleton [GO:0005200] | PF00091;PF03953; | 1.10.287.600;3.30.1330.20;3.40.50.1440; | Tubulin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. | null | null | null | null | null | FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers a... | Drosophila melanogaster (Fruit fly) |
P08842 | STS_HUMAN | MPLRKMKIPFLLLFFLWEAESHAASRPNIILVMADDLGIGDPGCYGNKTIRTPNIDRLASGGVKLTQHLAASPLCTPSRAAFMTGRYPVRSGMASWSRTGVFLFTASSGGLPTDEITFAKLLKDQGYSTALIGKWHLGMSCHSKTDFCHHPLHHGFNYFYGISLTNLRDCKPGEGSVFTTGFKRLVFLPLQIVGVTLLTLAALNCLGLLHVPLGVFFSLLFLAALILTLFLGFLHYFRPLNCFMMRNYEIIQQPMSYDNLTQRLTVEAAQFIQRNTETPFLLVLSYLHVHTALFSSKDFAGKSQHGVYGDAVEEMDWSVG... | 3.1.6.2 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:12657638}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:12657638}; | epidermis development [GO:0008544]; female pregnancy [GO:0007565]; steroid catabolic process [GO:0006706] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]; endosome [GO:0005768]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; lysosome [GO:0005764]; membrane [GO:0016020]; plasma membrane [GO:0005886] | 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:0000269|PubMed:12657638}. | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, microneme membrane {ECO:0000269|PubMed:2668275}; Multi-pass membrane protein. Endoplasmic reticulum membrane {ECO:0000269|PubMed:2668275}; Multi-pass membrane protein. | 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:0000269|PubMed:10844566, ECO:0000269|PubMed:23466819}; C... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=24.8 uM for 3beta-sulfooxy-androst-5-en-17-one (DHEA-S) {ECO:0000269|PubMed:23466819}; Vmax=354.4 umol/min/mg enzyme with 3beta-sulfooxy-androst-5-en-17-one (DHEA-S) {ECO:0000269|PubMed:23466819}; | 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:0000269|PubMed:10844566, ECO:0000269|PubMed:23466819, ECO:0000269|PubMed:9252398}. | Homo sapiens (Human) |
P08844 | H2A_EMENI | MTGGKSGGKASGSKNAQSRSSKAGLAFPVGRVHRLLRKGNYAQRVGAGAPVYLAAVLEYLAAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGHVTIAQGGVLPNIHQNLLPKKTPKAGKGSQEL | null | null | DNA repair [GO:0006281]; heterochromatin organization [GO:0070828] | nucleosome [GO:0000786]; nucleus [GO:0005634] | nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125;PF16211; | 1.10.20.10; | Histone H2A family | PTM: Phosphorylated to form H2AS128ph (gamma-H2A) in response to DNA double-strand breaks (DSBs) generated by exogenous genotoxic agents and by stalled replication forks. Phosphorylation is dependent on the DNA damage checkpoint kinases mec1/ATR and tel1/ATM, spreads on either side of a detected DSB site and may mark t... | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Core component of nucleosome which plays a central role in DNA double strand break (DSB) repair. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair... | Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
P08861 | CEL3B_HUMAN | MMLRLLSSLLLVAVASGYGPPSSRPSSRVVNGEDAVPYSWPWQVSLQYEKSGSFYHTCGGSLIAPDWVVTAGHCISSSRTYQVVLGEYDRAVKEGPEQVIPINSGDLFVHPLWNRSCVACGNDIALIKLSRSAQLGDAVQLASLPPAGDILPNETPCYITGWGRLYTNGPLPDKLQEALLPVVDYEHCSRWNWWGSSVKKTMVCAGGDIRSGCNGDSGGPLNCPTEDGGWQVHGVTSFVSAFGCNTRRKPTVFTRVSAFIDWIEETIASH | 3.4.21.70 | null | proteolysis [GO:0006508] | extracellular space [GO:0005615] | peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252] | PF00089; | 2.40.10.10; | Peptidase S1 family, Elastase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Ala-|-Xaa. Does not hydrolyze elastin.; EC=3.4.21.70; | null | null | null | null | FUNCTION: Efficient protease with alanine specificity but only little elastolytic activity. | Homo sapiens (Human) |
P08865 | RSSA_HUMAN | MSGALDVLQMKEEDVLKFLAAGTHLGGTNLDFQMEQYIYKRKSDGIYIINLKRTWEKLLLAARAIVAIENPADVSVISSRNTGQRAVLKFAAATGATPIAGRFTPGTFTNQIQAAFREPRLLVVTDPRADHQPLTEASYVNLPTIALCNTDSPLRYVDIAIPCNNKGAHSVGLMWWMLAREVLRMRGTISREHPWEVMPDLYFYRDPEEIEKEEQAAAEKAVTKEEFQGEWTAPAPEFTATQPEVADWSEGVQVPSVPIQQFPTEDWSAQPATEDWSAAPTAQATEWVGATTDWS | null | null | cytoplasmic translation [GO:0002181]; ribosomal small subunit assembly [GO:0000028]; translation [GO:0006412] | 90S preribosome [GO:0030686]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic ribosome [GO:0022626]; cytosolic small ribosomal subunit [GO:0022627]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | laminin binding [GO:0043236]; laminin receptor activity [GO:0005055]; ribosome binding [GO:0043022]; RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735]; virus receptor activity [GO:0001618] | PF16122;PF00318; | null | Universal ribosomal protein uS2 family | PTM: Acylated. Acylation may be a prerequisite for conversion of the monomeric 37 kDa laminin receptor precursor (37LRP) to the mature dimeric 67 kDa laminin receptor (67LR), and may provide a mechanism for membrane association (PubMed:9581863). {ECO:0000255|HAMAP-Rule:MF_03016, ECO:0000269|PubMed:9581863}.; PTM: Cleav... | SUBCELLULAR LOCATION: Cell membrane. Cytoplasm. Nucleus {ECO:0000255|HAMAP-Rule:MF_03016}. Note=67LR is found at the surface of the plasma membrane, with its C-terminal laminin-binding domain accessible to extracellular ligands. 37LRP is found at the cell surface, in the cytoplasm and in the nucleus (By similarity). Co... | null | null | null | null | null | FUNCTION: Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Also functions as a cell surface receptor for laminin. Plays a role in cell adhesion to the basement mem... | Homo sapiens (Human) |
P08870 | PYRE_SALTY | MKPYQRQFIEFALNKQVLKFGEFTLKSGRKSPYFFNAGLFNTGRDLALLGRFYAEALVDSGIEFDLLFGPAYKGIPIATTTAVALAEHHDKDLPYCFNRKEAKDHGEGGSLVGSALQGRVMLVDDVITAGTAIRESMEIIQAHGATLAGVLISLDRQERGRGEISAIQEVERDYGCKVISIITLKDLIAYLEEKPDMAEHLAAVRAYREEFGV | 2.4.2.10 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:7685580}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:7685580}; Note=Mg(2+). Mn(2+) can replace Mg(2+) as the divalent metal. The role of the metal is to bind 5-phosphoribose 1-diphosphate and form a Mg-5-phosphoribose 1-d... | 'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; 'de novo' UMP biosynthetic process [GO:0044205]; pyrimidine nucleotide biosynthetic process [GO:0006221]; pyrimidine ribonucleoside biosynthetic process [GO:0046132] | cytoplasm [GO:0005737] | magnesium ion binding [GO:0000287]; orotate phosphoribosyltransferase activity [GO:0004588] | PF00156; | 3.40.50.2020; | Purine/pyrimidine phosphoribosyltransferase family, PyrE subfamily | null | null | CATALYTIC ACTIVITY: Reaction=diphosphate + orotidine 5'-phosphate = 5-phospho-alpha-D-ribose 1-diphosphate + orotate; Xref=Rhea:RHEA:10380, ChEBI:CHEBI:30839, ChEBI:CHEBI:33019, ChEBI:CHEBI:57538, ChEBI:CHEBI:58017; EC=2.4.2.10; Evidence={ECO:0000255|HAMAP-Rule:MF_01208}; | null | PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_01208}. | null | null | FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP). {ECO:0000255|HAMAP-Rule:MF_01208, ECO:0000269|PubMed:2271660}. | Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) |
P08877 | PTHP_BACSU | MAQKTFKVTADSGIHARPATVLVQTASKYDADVNLEYNGKTVNLKSIMGVMSLGIAKGAEITISASGADENDALNALEETMKSEGLGE | null | null | phosphoenolpyruvate-dependent sugar phosphotransferase system [GO:0009401]; regulation of carbohydrate utilization [GO:0043610] | cytoplasm [GO:0005737] | null | PF00381; | 3.30.1340.10; | HPr family | PTM: Phosphorylated during sporulation. {ECO:0000269|PubMed:1556067}. | SUBCELLULAR LOCATION: Cytoplasm. | null | null | null | null | null | FUNCTION: General (non sugar-specific) component of the phosphoenolpyruvate-dependent sugar phosphotransferase system (sugar PTS). This major carbohydrate active-transport system catalyzes the phosphorylation of incoming sugar substrates concomitantly with their translocation across the cell membrane. The phosphoryl gr... | Bacillus subtilis (strain 168) |
P08878 | PA2H_CRODU | MRALWIVAVLLVGVEGSLVEFETLMMKIAGRSGISYYSSYGCYCGAGGQGWPQDASDRCCFEHDCCYAKLTGCDPTTDVYTYRQEDGEIVCGEDDPCGTQICECDKAAAICFRNSMDTYDYKYLQFSPENCQGESQPC | null | null | arachidonic acid secretion [GO:0050482]; lipid catabolic process [GO:0016042]; negative regulation of T cell proliferation [GO:0042130]; phospholipid metabolic process [GO:0006644] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; toxin activity [GO:0090729] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group II subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.05 uM for 1-palmitoyl-2-(10-pyrenyldecanoyl)-sn-glycero-3-monomethyl phosphatidic acid (class 2 heterodimer CA2-CBa2) {ECO:0000269|PubMed:8513799}; KM=0.05 uM for 1-palmitoyl-2-(10-pyrenyldecanoyl)-sn-glycero-3-monomethyl phosphatidic acid (class 2 heterodimer CA... | null | null | null | FUNCTION: CAalpha-CAbeta-CAgamma: The acidic subunit of crotoxin (CA) is a heterotrimer of three disulfide-linked chains generated by post-translational maturation of a PLA2-like precursor. CA has no PLA2 activity and is not neurotoxic by itself, but plays several important functions in the crotoxin complex by increasi... | Crotalus durissus terrificus (South American rattlesnake) |
P08879 | NDKA_DROME | MAANKERTFIMVKPDGVQRGLVGKIIERFEQKGFKLVALKFTWASKELLEKHYADLSARPFFPGLVNYMNSGPVVPMVWEGLNVVKTGRQMLGATNPADSLPGTIRGDFCIQVGRNIIHGSDAVESAEKEIALWFNEKELVTWTPAAKDWIYE | 2.7.4.6 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:7669763}; | adherens junction organization [GO:0034332]; CTP biosynthetic process [GO:0006241]; epithelial cell migration, open tracheal system [GO:0007427]; establishment or maintenance of polarity of follicular epithelium [GO:0016334]; GTP biosynthetic process [GO:0006183]; microtubule-based process [GO:0007017]; mitotic cell cy... | cytoplasm [GO:0005737]; microtubule [GO:0005874]; nuclear microtubule [GO:0005880]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; GTP binding [GO:0005525]; kinase activity [GO:0016301]; magnesium ion binding [GO:0000287]; microtubule binding [GO:0008017]; nucleoside diphosphate kinase activity [GO:0004550] | PF00334; | 3.30.70.141; | NDK family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:2175255}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:2175255}. Note=Microtubule-associated. | 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; Evidence={ECO:0000269|PubMed:1320004}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside... | 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. {ECO:0000269|PubMed:2175255, ECO:0000269|PubMed:2849580, ECO:0000269|PubMed:7559441}. | Drosophila melanogaster (Fruit fly) |
P08883 | GRAF_MOUSE | MPPILILLTLLLPLRAGAEEIIGGHEVKPHSRPYMARVRFVKDNGKRHSCGGFLVQDYFVLTAAHCTGSSMRVILGAHNIRAKEETQQIIPVAKAIPHPAYDDKDNTSDIMLLKLESKAKRTKAVRPLKLPRPNARVKPGHVCSVAGWGRTSINATQRSSCLREAQLIIQKDKECKKYFYKYFKTMQICAGDPKKIQSTYSGDSGGPLVCNNKAYGVLTYGLNRTIGPGVFTKVVHYLPWISRNMKLL | 3.4.21.- | null | killing of cells of another organism [GO:0031640]; proteolysis [GO:0006508] | cytolytic granule [GO:0044194]; cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231] | serine-type endopeptidase activity [GO:0004252] | PF00089; | 2.40.10.10; | Peptidase S1 family, Granzyme subfamily | null | SUBCELLULAR LOCATION: Cytolytic granule. | null | null | null | null | null | FUNCTION: This enzyme is probably necessary for target cell lysis in cell-mediated immune responses. | Mus musculus (Mouse) |
P08884 | GRAE_MOUSE | MPPVLILLTLLLPLGAGAEEIIGGHVVKPHSRPYMAFVKSVDIEGNRRYCGGFLVQDDFVLTAAHCRNRTMTVTLGAHNIKAKEETQQIIPVAKAIPHPDYNATAFFSDIMLLKLESKAKRTKAVRPLKLPRPNARVKPGDVCSVAGWGSRSINDTKASARLREAQLVIQEDEECKKRFRHYTETTEICAGDLKKIKTPFKGDSGGPLVCDNKAYGLLAYAKNRTISSGVFTKIVHFLPWISRNMKLL | 3.4.21.- | null | killing of cells of another organism [GO:0031640]; proteolysis [GO:0006508] | cytolytic granule [GO:0044194]; cytoplasm [GO:0005737]; intracellular membrane-bounded organelle [GO:0043231] | serine-type endopeptidase activity [GO:0004252] | PF00089; | 2.40.10.10; | Peptidase S1 family, Granzyme subfamily | null | SUBCELLULAR LOCATION: Cytolytic granule. | null | null | null | null | null | FUNCTION: This enzyme is probably necessary for target cell lysis in cell-mediated immune responses. | Mus musculus (Mouse) |
P08887 | IL6RA_HUMAN | MLAVGCALLAALLAAPGAALAPRRCPAQEVARGVLTSLPGDSVTLTCPGVEPEDNATVHWVLRKPAAGSHPSRWAGMGRRLLLRSVQLHDSGNYSCYRAGRPAGTVHLLVDVPPEEPQLSCFRKSPLSNVVCEWGPRSTPSLTTKAVLLVRKFQNSPAEDFQEPCQYSQESQKFSCQLAVPEGDSSFYIVSMCVASSVGSKFSKTQTFQGCGILQPDPPANITVTAVARNPRWLSVTWQDPHSWNSSFYRLRFELRYRAERSKTFTTWMVKDLQHHCVIHDAWSGLRHVVQLRAQEEFGQGEWSEWSPEAMGTPWTESRS... | null | null | acute-phase response [GO:0006953]; ciliary neurotrophic factor-mediated signaling pathway [GO:0070120]; cytokine-mediated signaling pathway [GO:0019221]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; endocrine pancreas development [GO:0031018]; extri... | apical plasma membrane [GO:0016324]; ciliary neurotrophic factor receptor complex [GO:0070110]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; interleukin-6 receptor complex [GO:0005896]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | ciliary neurotrophic factor binding [GO:0070119]; cytokine receptor activity [GO:0004896]; enzyme binding [GO:0019899]; interleukin-11 binding [GO:0019970]; interleukin-11 receptor activity [GO:0004921]; interleukin-6 binding [GO:0019981]; interleukin-6 receptor activity [GO:0004915]; protein homodimerization activity ... | PF00047;PF09240; | 2.60.40.10; | Type I cytokine receptor family, Type 3 subfamily | PTM: A short soluble form is released from the membrane by proteolysis (PubMed:26876177). The sIL6R is formed mostly by limited proteolysis of membrane-bound receptors, a process referred to as ectodomain shedding, but is also directly secreted from the cells after alternative mRNA splicing (PubMed:26876177, PubMed:280... | SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane {ECO:0000250|UniProtKB:P22272}; Single-pass type I membrane protein {ECO:0000255}.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted {ECO:0000269|PubMed:28060820}.; SUBCELLULAR LOCATION: [Soluble interleukin-6 receptor subunit alpha]: Secreted {ECO:0000269|PubMed:28060820}. | null | null | null | null | null | FUNCTION: Part of the receptor for interleukin 6. Binds to IL6 with low affinity, but does not transduce a signal (PubMed:28265003). Signal activation necessitate an association with IL6ST. Activation leads to the regulation of the immune response, acute-phase reactions and hematopoiesis (PubMed:30995492, PubMed:312355... | Homo sapiens (Human) |
P08897 | COGS_HYPLI | MKFLLVFALALATTSAFQHPASIFELREGRIINGYEAYTGLFPYQAGLDITLQDQRRVWCGGSLIDNKWILTAAHCVHDAVSVVVYLGSAVQYEGEAVVNSERIISHSMFNPDTYLNDVALIKIPHVEYTDNIQPIRLPSGEELNNKFENIWATVSGWGQSNTDTVILQYTYNLVIDNDRCAQEYPPGIIVESTICGDTCDGKSPCFGDSGGPFVLSDKNLLIGVVSFVSGAGCESGKPVGFSRVTSYMDWIQQNTGIIF | 3.4.21.49 | null | collagen catabolic process [GO:0030574]; proteolysis [GO:0006508] | extracellular region [GO:0005576] | serine-type endopeptidase activity [GO:0004252] | PF00089; | 2.40.10.10; | Peptidase S1 family | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins including native collagen at Xaa-|-Ala bond leaving an N-terminal (75%) and a C-terminal (25%) fragment.; EC=3.4.21.49; Evidence={ECO:0000269|PubMed:230030, ECO:0000269|PubMed:2995028}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0-8.5. Reversibly inactivated below pH 4.5. {ECO:0000269|PubMed:2995028}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermostable. No loss of activity occurs after incubation for 2 hours at 60 degrees Celsius. Inactivated after incubation for 2 hours at 75 degrees Celsius, however 45% of activity remains after incubation for 20 minutes at 75 degrees Celsius. {ECO:0000269|PubMed:... | FUNCTION: This enzyme is a serine protease capable of degrading the native triple helix of collagen. Also cleaves the B chain of insulin at the 15-Leu-|-Try-16 and 22-Arg-|-Gly-23 bonds. Hydrolyzes casein, but not Px-Pro-Leu-Gly-Pro-DArg, BzArgNHPh, AcTyrNHPh, 2-naphthyl phosphate, 2-naphthyl butyrate, 2-naphthyl capry... | Hypoderma lineatum (Early cattle grub) (Common cattle grub) |
P08898 | H3_CAEEL | MARTKQTARKSTGGKAPRKQLATKAARKSAPASGGVKKPHRYRPGTVALREIRRYQKSTELLIRRAPFQRLVREIAQDFKTDLRFQSSAVMALQEACEAYLVGLFEDTNLCAIHAKRVTIMPKDIQLARRIRGERA | null | null | null | nucleosome [GO:0000786]; nucleus [GO:0005634] | DNA binding [GO:0003677]; methylated histone binding [GO:0035064]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125; | 1.10.20.10; | Histone H3 family | PTM: Phosphorylated at Ser-11 and Ser-29 during M phase. Phosphorylation of Ser-11 requires air-2 but not air-1. Dephosphorylated by gsp-1 and/or gsp-2 during chromosome segregation. {ECO:0000269|PubMed:10975519, ECO:0000269|PubMed:11807039, ECO:0000269|PubMed:12015116, ECO:0000269|PubMed:12837290, ECO:0000269|PubMed:1... | SUBCELLULAR LOCATION: Nucleus. Chromosome. | null | null | null | null | null | FUNCTION: Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is r... | Caenorhabditis elegans |
P08900 | SCX2_CENSU | KEGYLVSKSTGCKYECLKLGDNDYCLRECKQQYGKSSGGYCYAFACWCTHLYEQAVVWPLPNKTCN | null | null | defense response [GO:0006952] | extracellular space [GO:0005615] | sodium channel inhibitor activity [GO:0019871]; toxin activity [GO:0090729] | PF00537; | 3.30.30.10; | Long (4 C-C) scorpion toxin superfamily, Sodium channel inhibitor family, Beta subfamily | PTM: C-terminal amidation increases its affinity for sodium channels. {ECO:0000269|PubMed:2435711}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2435711}. | null | null | null | null | null | FUNCTION: Beta toxin that binds site-4 of sodium channels (Nav) and reduces peak current (observed on Nav1.6/SCN8A (IC(50)=307 nM)), shifts the voltage of activation toward more negative potentials (observed on Nav1.6, Nav1.1 (weak), Nav1.2 (weak), and Nav1.7 (weak)), and induces resurgent currents at negative voltages... | Centruroides suffusus (Durango bark scorpion) |
P08902 | LECA_DIOGR | ADTIVAVELDSYPNTDIGDPNYPHIGIDIKSIRSKSTARWNMQTGKVGTVHISYNSVAKRLSAVVSYSGSSSTTVSYDVDLNNVLPEWVRVGLSATTGLYKETNTILSWSFTSKLKTNSIADENSLHFSFHKFSQNPKDLILQGDAFTDSDGNLELTKVSSSGDPQGNSVGRALFYAPVHIWESSAVVASFDATFTFLIKSPDREPADGITFFIANTDTSIPSGSGGRLLGLFPDAN | null | null | null | null | carbohydrate binding [GO:0030246]; identical protein binding [GO:0042802]; mannose binding [GO:0005537]; metal ion binding [GO:0046872]; toxin activity [GO:0090729] | PF00139; | 2.60.120.200; | Leguminous lectin family | PTM: The beta and gamma chains are produced by partial proteolytic processing of the lectin alpha chain by an asparaginyl endopeptidase. Mixture of 60% alpha lectin and 40% of its beta and gamma proteolytic fragments. | null | null | null | null | null | null | FUNCTION: D-mannose/D-glucose-binding lectin. Has anti-inflammatory activity in rats. Induces histamine release in mast cells from rat. Induces lymphocyte proliferation and IFNG production. Shows toxicity against the aquatic snail B.glabrata at concentrations higher than 50 ug/ml. {ECO:0000269|PubMed:10747944, ECO:0000... | Dioclea grandiflora (Mucana) |
P08904 | RNAS6_BOVIN | MGPHLLGRSSLLLLLLGMWWSVRPLCAVPKGLTKARWFEIQHIQPRLLQCNKAMSGVNNYTQHCKPENTFLHNVFQDVTAVCDMPNIICKNGRHNCHQSPKPVNLTQCNFIAGRYPDCRYHDDAQYKFFIVACDPPQKTDPPYHLVPVHLDKVV | 3.1.27.- | null | antibacterial humoral response [GO:0019731]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; innate immune response [GO:0045087] | extracellular space [GO:0005615]; lysosome [GO:0005764] | endonuclease activity [GO:0004519]; nucleic acid binding [GO:0003676]; RNA nuclease activity [GO:0004540] | PF00074; | 3.10.130.10; | Pancreatic ribonuclease family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q93091}. Lysosome {ECO:0000250|UniProtKB:Q93091}. Cytoplasmic granule {ECO:0000250|UniProtKB:Q93091}. | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5. {ECO:0000269|PubMed:3926759}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. Activity declines with increasing temperature, with loss of stability at 90 degrees Celsius. {ECO:0000269|PubMed:3926759}; | FUNCTION: Ribonuclease which shows a preference for the pyrimidines uridine and cytosine (PubMed:3926759). Has potent antimicrobial activity against a range of Gram-positive and Gram-negative bacteria, including P.aeruginosa, A.baumanii, M.luteus, S.aureus, E.faecalis, E.faecium, S.saprophyticus and E.coli (By similari... | Bos taurus (Bovine) |
P08905 | LYZ2_MOUSE | MKTLLTLGLLLLSVTAQAKVYERCEFARTLKRNGMAGYYGVSLADWVCLAQHESNYNTRATNYNRGDQSTDYGIFQINSRYWCNDGKTPRAVNACGINCSALLQDDITAAIQCAKRVVRDPQGIRAWVAWRAHCQNRDLSQYIRNCGV | 3.2.1.17 | null | defense response to bacterium [GO:0042742]; defense response to Gram-negative bacterium [GO:0050829]; defense response to Gram-positive bacterium [GO:0050830]; killing of cells of another organism [GO:0031640]; metabolic process [GO:0008152] | endoplasmic reticulum lumen [GO:0005788]; extracellular region [GO:0005576]; Golgi cis cisterna [GO:0000137]; Golgi stack [GO:0005795]; microvillus [GO:0005902]; rough endoplasmic reticulum lumen [GO:0048237]; secretory granule [GO:0030141]; trans-Golgi network transport vesicle [GO:0030140] | hydrolase activity, acting on glycosyl bonds [GO:0016798]; lysozyme activity [GO:0003796] | PF00062; | 1.10.530.10; | Glycosyl hydrolase 22 family | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: 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; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5. {ECO:0000269|PubMed:12613666}; | null | FUNCTION: Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Lyz2 is active against a range of Gram-positive and Gram-negative bacteria. More effective than Lyz1 in killing Gram-negative bacteri... | Mus musculus (Mouse) |
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