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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P05327 | PHR_SYNP6 | MAAPILFWHRRDLRLSDNIGLAAARAQSAQLIGLFCLDPQILQSADMAPARVAYLQGCLQELQQRYQQAGSRLLLLQGDPQHLIPQLAQQLQAEAVYWNQDIEPYGRDRDGQVAAALKTAGIRAVQLWDQLLHSPDQILSGSGNPYSVYGPFWKNWQAQPKPTPVATPTELVDLSPEQLTAIAPLLLSELPTLKQLGFDWDGGFPVEPGETAAIARLQEFCDRAIADYDPQRNFPAEAGTSGLSPALKFGAIGIRQAWRAASAAHALSRSDEARNSIRVWQQELAWREFYQHALYHFPSLADGPYRSLWQQFPWENREAL... | 4.1.99.3 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Note=Binds 1 FAD per subunit.; COFACTOR: Name=coenzyme F420-(gamma-Glu)n; Xref=ChEBI:CHEBI:133980; Note=Binds 1 coenzyme F420 non-covalently per subunit.; | circadian regulation of gene expression [GO:0032922]; DNA repair [GO:0006281]; entrainment of circadian clock by photoperiod [GO:0043153] | cytoplasm [GO:0005737] | deoxyribodipyrimidine photo-lyase activity [GO:0003904]; DNA binding [GO:0003677]; FAD binding [GO:0071949] | PF00875;PF03441; | 1.25.40.80;1.10.579.10;3.40.50.620; | DNA photolyase class-1 family | null | null | CATALYTIC ACTIVITY: Reaction=cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA).; EC=4.1.99.3; | null | null | null | null | FUNCTION: Involved in repair of UV radiation-induced DNA damage. Catalyzes the light-dependent monomerization (300-600 nm) of cyclobutyl pyrimidine dimers (in cis-syn configuration), which are formed between adjacent bases on the same DNA strand upon exposure to ultraviolet radiation. | Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis nidulans) |
P05328 | TRPG_ASPNG | MADSGLVDHSPHHPTKAAQLSTASNVILIDNYDSFTWNVYQYLVLEGATVNVFRNDQITLEELIAKKPTQLVISPGPGHPETDAGISSAAIQYFSGKIPIFGVCMGQQCIITCFGGKVDVTGEILHGKTSPLKHDGKGAYEGLPGSLAVTRYHSLAGTHATIPDCLEVSSSVQLADDSNKDVIMGVRHKKLAVEGVQFHPESILTEYGRIMFRNFLKLTAGTWEGNGKHFGEQSSTTKATVPSNPPPKTDKKLSILERIYDHRRAAVAVQKTIPSQRPADLQAAYDLNLAPPQIPFPARLRQSPYPLSLMAEIKRASPSK... | 4.1.1.48; 4.1.3.27; 5.3.1.24 | null | glutamine metabolic process [GO:0006541]; tetrahydrofolate biosynthetic process [GO:0046654]; tryptophan biosynthetic process [GO:0000162] | cytosol [GO:0005829] | 4-amino-4-deoxychorismate synthase activity [GO:0046820]; anthranilate synthase activity [GO:0004049]; indole-3-glycerol-phosphate synthase activity [GO:0004425]; phosphoribosylanthranilate isomerase activity [GO:0004640] | PF00117;PF00218;PF00697; | 3.40.50.880;3.20.20.70; | null | null | null | CATALYTIC ACTIVITY: Reaction=N-(5-phospho-beta-D-ribosyl)anthranilate = 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate; Xref=Rhea:RHEA:21540, ChEBI:CHEBI:18277, ChEBI:CHEBI:58613; EC=5.3.1.24; CATALYTIC ACTIVITY: Reaction=1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate + H(+) = (1S,2R)-1-C-(indol-3-yl)... | null | PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 1/5.; PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5.; PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 4/5. | null | null | FUNCTION: Trifunctional enzyme bearing the Gln amidotransferase (GATase) domain of anthranilate synthase, indole-glycerolphosphate synthase, and phosphoribosylanthranilate isomerase activities. | Aspergillus niger |
P05341 | NIFS_AZOVI | MADVYLDNNATTRVDDEIVQAMLPFFTEQFGNPSSLHSFGNQVGMALKKARQSVQKLLGAEHDSEILFTSCGTESDSTAILSALKAQPERKTVITTVVEHPAVLSLCDYLASEGYTVHKLPVDKKGRLDLEHYASLLTDDVAVVSVMWANNETGTLFPIEEMARLADDAGIMFHTDAVQAVGKVPIDLKNSSIHMLSLCGHKLHAPKGVGVLYLRRGTRFRPLLRGGHQERGRRAGTENAASIIGLGVAAERALQFMEHENTEVNALRDKLEAGILAVVPHAFVTGDPDNRLPNTANIAFEYIEGEAILLLLNKVGIAAS... | 2.8.1.7 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:8464885}; | amino acid metabolic process [GO:0006520]; nitrogen fixation [GO:0009399] | null | cysteine desulfurase activity [GO:0031071]; iron-sulfur cluster binding [GO:0051536]; metal ion binding [GO:0046872]; pyridoxal phosphate binding [GO:0030170] | PF00266; | 1.10.260.50;3.90.1150.10;3.40.640.10; | Class-V pyridoxal-phosphate-dependent aminotransferase family, NifS/IscS subfamily | null | null | CATALYTIC ACTIVITY: Reaction=[sulfur carrier]-H + L-cysteine = [sulfur carrier]-SH + L-alanine; Xref=Rhea:RHEA:43892, Rhea:RHEA-COMP:14737, Rhea:RHEA-COMP:14739, ChEBI:CHEBI:29917, ChEBI:CHEBI:35235, ChEBI:CHEBI:57972, ChEBI:CHEBI:64428; EC=2.8.1.7; Evidence={ECO:0000269|PubMed:8464885}; | null | null | null | null | FUNCTION: Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Seems to participate in the biosynthesis of the nitrogenase metalloclusters by providing the inorganic sulfur required for the Fe-S core formation. {ECO:0000269|PubMed:8464885}. | Azotobacter vinelandii |
P05362 | ICAM1_HUMAN | MAPSSPRPALPALLVLLGALFPGPGNAQTSVSPSKVILPRGGSVLVTCSTSCDQPKLLGIETPLPKKELLLPGNNRKVYELSNVQEDSQPMCYSNCPDGQSTAKTFLTVYWTPERVELAPLPSWQPVGKNLTLRCQVEGGAPRANLTVVLLRGEKELKREPAVGEPAEVTTTVLVRRDHHGANFSCRTELDLRPQGLELFENTSAPYQLQTFVLPATPPQLVSPRVLEVDTQGTVVCSLDGLFPVSEAQVHLALGDQRLNPTVTYGNDSFSAKASVSVTAEDEGTQRLTCAVILGNQSQETLQTVTIYSFPAPNVILTKP... | null | null | adhesion of symbiont to host [GO:0044406]; cell adhesion [GO:0007155]; cell adhesion mediated by integrin [GO:0033627]; cellular response to amyloid-beta [GO:1904646]; cellular response to glucose stimulus [GO:0071333]; cellular response to leukemia inhibitory factor [GO:1990830]; establishment of endothelial barrier [... | cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; immunological synapse [GO:0001772]; membrane [GO:0016020]; membrane raft [GO:0045121]; plasm... | integrin binding [GO:0005178]; signaling receptor activity [GO:0038023]; transmembrane signaling receptor activity [GO:0004888]; virus receptor activity [GO:0001618] | PF21146;PF03921;PF13895; | 2.60.40.10; | Immunoglobulin superfamily, ICAM family | PTM: Monoubiquitinated, which is promoted by MARCH9 and leads to endocytosis. | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: ICAM proteins are ligands for the leukocyte adhesion protein LFA-1 (integrin alpha-L/beta-2). During leukocyte trans-endothelial migration, ICAM1 engagement promotes the assembly of endothelial apical cups through ARHGEF26/SGEF and RHOG activation. {ECO:0000269|PubMed:11173916, ECO:0000269|PubMed:17875742}.; ... | Homo sapiens (Human) |
P05364 | AMPC_ENTCL | MMRKSLCCALLLGISCSALATPVSEKQLAEVVANTITPLMKAQSVPGMAVAVIYQGKPHYYTFGKADIAANKPVTPQTLFELGSISKTFTGVLGGDAIARGEISLDDAVTRYWPQLTGKQWQGIRMLDLATYTAGGLPLQVPDEVTDNASLLRFYQNWQPQWKPGTTRLYANASIGLFGALAVKPSGMPYEQAMTTRVLKPLKLDHTWINVPKAEEAHYAWGYRDGKAVRVSPGMLDAQAYGVKTNVQDMANWVMANMAPENVADASLKQGIALAQSRYWRIGSMYQGLGWEMLNWPVEANTVVEGSDSKVALAPLPVAE... | 3.5.2.6 | null | antibiotic catabolic process [GO:0017001]; response to antibiotic [GO:0046677] | outer membrane-bounded periplasmic space [GO:0030288] | beta-lactamase activity [GO:0008800] | PF00144; | 3.40.710.10; | Class-C beta-lactamase family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=a beta-lactam + H2O = a substituted beta-amino acid; Xref=Rhea:RHEA:20401, ChEBI:CHEBI:15377, ChEBI:CHEBI:35627, ChEBI:CHEBI:140347; EC=3.5.2.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU10102}; | null | null | null | null | FUNCTION: This protein is a serine beta-lactamase with a substrate specificity for cephalosporins. | Enterobacter cloacae |
P05369 | FPPS_RAT | MNGDQKLDVHNQEKQNFIQHFSQIVKVLTEDELGHPEKGDAITRIKEVLEYNTVGGKYNRGLTVVQTFQELVEPRKQDAESLQRALTVGWCVELLQAFFLVLDDIMDSSYTRRGQICWYQKPGIGLDAINDALLLEAAIYRLLKFYCREQPYYLNLLELFLQSSYQTEIGQTLDLITAPQGQVDLGRYTEKRYKSIVKYKTAFYSFYLPIAAAMYMAGIDGEKEHANALKILLEMGEFFQIQDDYLDLFGDPSVTGKVGTDIQDNKCSWLVVQCLLRATPQQRQILEENYGQKDPEKVARVKALYEELDLRSVFFKYEED... | 2.5.1.1; 2.5.1.10 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250}; | cellular response to fatty acid [GO:0071398]; cholesterol biosynthetic process [GO:0006695]; farnesyl diphosphate biosynthetic process [GO:0045337]; geranyl diphosphate biosynthetic process [GO:0033384]; male gonad development [GO:0008584]; positive regulation of cell growth involved in cardiac muscle cell development ... | cytoplasm [GO:0005737]; mitochondrial matrix [GO:0005759]; peroxisome [GO:0005777] | 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: Key enzyme in isoprenoid biosynthesis which catalyzes the formation of farnesyl diphosphate (FPP), a precursor for several classes of essential metabolites including sterols, dolichols, carotenoids, and ubiquinones. FPP also serves as substrate for protein farnesylation and geranylgeranylation. Catalyzes the ... | Rattus norvegicus (Rat) |
P05370 | G6PD_RAT | MAEQVALSRTQVCGILREELYQGDAFHQADTHIFIIMGASGDLAKKKIYPTIWWLFRDGLLPEDTFIVGYARSRLTVDDIRKQSEPFFKVTPEERPKLEEFFARNSYVAGQYDDPASYKHLNSHMNALHQGMQANRLFYLALPPTVYEAVTKNIQEICMSQTGWNRIIVEKPFGRDLQSSNQLSNHISSLFREDQIYRIDHYLGKEMVQNLMVLRFANRIFGPIWNRDNIACVILTFKEPFGTEGRGGYFDEFGIIRDVMQNHLLQMLCLVAMEKPASTDSDDVRDEKVKVLKCISEVETDNVVLGQYVGNPSGEGEATN... | 1.1.1.49 | null | angiotensin-mediated vasoconstriction involved in regulation of systemic arterial blood pressure [GO:0001998]; angiotensin-mediated vasodilation involved in regulation of systemic arterial blood pressure [GO:0002033]; cellular response to oxidative stress [GO:0034599]; cholesterol biosynthetic process [GO:0006695]; ery... | centriolar satellite [GO:0034451]; cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231] | carbohydrate binding [GO:0030246]; glucose binding [GO:0005536]; glucose-6-phosphate dehydrogenase activity [GO:0004345]; identical protein binding [GO:0042802]; NADP binding [GO:0050661]; protein homodimerization activity [GO:0042803] | PF02781;PF00479; | 3.40.50.720; | Glucose-6-phosphate dehydrogenase family | PTM: Acetylated by ELP3 at Lys-403; acetylation inhibits its homodimerization and enzyme activity. Deacetylated by SIRT2 at Lys-403; deacetylation stimulates its enzyme activity (By similarity). {ECO:0000250|UniProtKB:P11413}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P11413}. Membrane {ECO:0000250|UniProtKB:P11413}; Peripheral membrane protein {ECO:0000250|UniProtKB:P11413}. | CATALYTIC ACTIVITY: Reaction=D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + H(+) + NADPH; Xref=Rhea:RHEA:15841, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783, ChEBI:CHEBI:57955, ChEBI:CHEBI:58349, ChEBI:CHEBI:61548; EC=1.1.1.49; Evidence={ECO:0000250|UniProtKB:P11413}; PhysiologicalDirection=left-to-right; ... | null | PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3. {ECO:0000250|UniProtKB:P11413}. | null | null | FUNCTION: Cytosolic glucose-6-phosphate dehydrogenase that catalyzes the first and rate-limiting step of the oxidative branch within the pentose phosphate pathway/shunt, an alternative route to glycolysis for the dissimilation of carbohydrates and a major source of reducing power and metabolic intermediates for fatty a... | Rattus norvegicus (Rat) |
P05371 | CLUS_RAT | MKILLLCVALLLTWDNGMVLGEQEFSDNELQELSTQGSRYVNKEIQNAVQGVKHIKTLIEKTNAERKSLLNSLEEAKKKKEGALDDTRDSEMKLKAFPEVCNETMMALWEECKPCLKHTCMKFYARVCRSGSGLVGRQLEEFLNQSSPFYFWMNGDRIDSLLESDRQQSQVLDAMQDSFTRASGIIDTLFQDRFFTHEPQDIHHFSPMGFPHKRPHFLYPKSRLVRSLMPLSHYGPLSFHNMFQPFFDMIHQAQQAMDVQLHSPALQFPDVDFLKEGEDDPTVCKEIRHNSTGCLKMKGQCEKCQEILSVDCSTNNPAQA... | null | null | cell morphogenesis [GO:0000902]; cellular response to growth factor stimulus [GO:0071363]; central nervous system myelin maintenance [GO:0032286]; chaperone-mediated protein complex assembly [GO:0051131]; chaperone-mediated protein folding [GO:0061077]; endocrine pancreas development [GO:0031018]; estrous cycle [GO:004... | aggresome [GO:0016235]; apical dendrite [GO:0097440]; cell surface [GO:0009986]; chromaffin granule [GO:0042583]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular space [GO:0005615]; growth cone [GO:0030426]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrial inner membrane [GO:0005743]; mi... | amyloid-beta binding [GO:0001540]; low-density lipoprotein particle receptor binding [GO:0050750]; misfolded protein binding [GO:0051787]; protein carrier chaperone [GO:0140597]; protein-containing complex binding [GO:0044877]; signaling receptor binding [GO:0005102]; tau protein binding [GO:0048156]; ubiquitin protein... | PF01093; | null | Clusterin family | PTM: Proteolytically cleaved on its way through the secretory system, probably within the Golgi lumen (PubMed:3415696, PubMed:3651384). Proteolytic cleavage is not necessary for its chaperone activity. All non-secreted forms are not proteolytically cleaved. Chaperone activity of uncleaved forms is dependent on a non-re... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3415696, ECO:0000269|PubMed:3651384}. Nucleus {ECO:0000250|UniProtKB:P10909}. Cytoplasm {ECO:0000250|UniProtKB:P10909}. Mitochondrion membrane {ECO:0000250|UniProtKB:P10909}; Peripheral membrane protein {ECO:0000250|UniProtKB:P10909}; Cytoplasmic side {ECO:0000250|UniP... | null | null | null | null | null | FUNCTION: Functions as extracellular chaperone that prevents aggregation of non native proteins. Prevents stress-induced aggregation of blood plasma proteins. Inhibits formation of amyloid fibrils by APP, APOC2, B2M, CALCA, CSN3, SNCA and aggregation-prone LYZ variants (in vitro). Does not require ATP. Maintains partia... | Rattus norvegicus (Rat) |
P05373 | HEM2_YEAST | MHTAEFLETEPTEISSVLAGGYNHPLLRQWQSERQLTKNMLIFPLFISDNPDDFTEIDSLPNINRIGVNRLKDYLKPLVAKGLRSVILFGVPLIPGTKDPVGTAADDPAGPVIQGIKFIREYFPELYIICDVCLCEYTSHGHCGVLYDDGTINRERSVSRLAAVAVNYAKAGAHCVAPSDMIDGRIRDIKRGLINANLAHKTFVLSYAAKFSGNLYGPFRDAACSAPSNGDRKCYQLPPAGRGLARRALERDMSEGADGIIVKPSTFYLDIMRDASEICKDLPICAYHVSGEYAMLHAAAEKGVVDLKTIAFESHQGFLR... | 4.2.1.24 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:10386874}; Note=Binds 1 zinc ion per monomer. {ECO:0000269|PubMed:10386874}; | heme biosynthetic process [GO:0006783]; protoporphyrinogen IX biosynthetic process [GO:0006782] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | porphobilinogen synthase activity [GO:0004655]; zinc ion binding [GO:0008270] | PF00490; | 3.20.20.70; | ALAD family | null | null | CATALYTIC ACTIVITY: Reaction=2 5-aminolevulinate = H(+) + 2 H2O + porphobilinogen; Xref=Rhea:RHEA:24064, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58126, ChEBI:CHEBI:356416; EC=4.2.1.24; | null | PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4. | null | null | FUNCTION: Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P05374 | CHO2_YEAST | MSSCKTTLSEMVGSVTKDRGTINVEARTRSSNVTFKPPVTHDMVRSLFDPTLKKSLLEKCIALAIISNFFICYWVFQRFGLQFTKYFFLVQYLFWRIAYNLGIGLVLHYQSHYETLTNCAKTHAIFSKIPQNKDANSNFSTNSNSFSEKFWNFIRKFCQYEIRSKMPKEYDLFAYPEEINVWLIFRQFVDLILMQDFVTYIIYVYLSIPYSWVQIFNWRSLLGVILILFNIWVKLDAHRVVKDYAWYWGDFFFLEESELIFDGVFNISPHPMYSIGYLGYYGLSLICNDYKVLLVSVFGHYSQFLFLKYVENPHIERTYG... | 2.1.1.17 | null | methylation [GO:0032259]; phosphatidylcholine biosynthetic process [GO:0006656] | cell periphery [GO:0071944]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789] | phosphatidylethanolamine N-methyltransferase activity [GO:0004608] | PF04191; | 1.20.120.1630;2.60.40.2840; | Class VI-like SAM-binding methyltransferase superfamily, CHO2 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03217, ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03217}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + S-adenosyl-L-methionine = 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11164, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:64573, ChEBI:CHEBI:64612; EC=2.1.1.17... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=60 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:2684666}; KM=110 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:2198947}; KM=57 uM for phosphatidylethanolamine (PE) {ECO:0000269|PubMed:2198947}; | PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03217, ECO:0000305|PubMed:2445736, ECO:0000305|PubMed:3066687}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.9. {ECO:0000269|PubMed:2684666}; | null | FUNCTION: Catalyzes the first step of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylethanolamine (PE) to phosphatidylmonomethylethanolamine (PMME). Preferentially converts di-C16:1 substrates. {ECO:0000255|HAMAP-Rule:MF_03217, ECO:0000269|PubMed:15258140, ECO:... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P05375 | PLMT_YEAST | MKESVQEIIQQLIHSVDLQSSKFQLAIVCTMFNPIFWNIVARMEYHKHSLTKMCGGARKGCYMLAATIFSLGIVRDMVYESALREQPTCSLITGENWTKLGVALFGLGQVLVLSSMYKLGITGTYLGDYFGILMDERVTGFPFNVSNNPMYQGSTLSFLGIALYKGKPAGLVVSAVVYFMYKIALRWEEPFTAMIYANRDKAKKNM | 2.1.1.17; 2.1.1.71 | null | methylation [GO:0032259]; phosphatidylcholine biosynthetic process [GO:0006656] | cell periphery [GO:0071944]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739] | phosphatidyl-N-dimethylethanolamine N-methyltransferase activity [GO:0080101]; phosphatidyl-N-methylethanolamine N-methyltransferase activity [GO:0000773]; phosphatidylethanolamine N-methyltransferase activity [GO:0004608] | PF04191; | 1.20.120.1630; | Class VI-like SAM-binding methyltransferase superfamily, PEMT/PEM2 methyltransferase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_03216, ECO:0000269|PubMed:14562095}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03216}. Mitochondrion membrane {ECO:0000255|HAMAP-Rule:MF_03216, ECO:0000269|PubMed:14576278}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:M... | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + S-adenosyl-L-methionine = 1,2-diacyl-sn-glycero-3-phospho-N-methylethanolamine + H(+) + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:11164, ChEBI:CHEBI:15378, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:64573, ChEBI:CHEBI:64612; EC=2.1.1.17... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=180 uM for S-adenosyl-L-methionine (in presence of phosphatidylethanolamine (PE) as substrate) {ECO:0000269|PubMed:2684666}; KM=190 uM for S-adenosyl-L-methionine (in presence of phosphatidyl-N-methylethanolamine (PMME) as substrate) {ECO:0000269|PubMed:2684666}; K... | PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis. {ECO:0000255|HAMAP-Rule:MF_03216, ECO:0000305|PubMed:6337128}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.1. {ECO:0000269|PubMed:2684666}; | null | FUNCTION: Catalyzes the second two steps of the methylation pathway of phosphatidylcholine biosynthesis, the SAM-dependent methylation of phosphatidylmonomethylethanolamine (PMME) to phosphatidyldimethylethanolamine (PDME) and of PDME to phosphatidylcholine (PC). Can also catalyze the first methylation reaction of PE t... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P05383 | KAPCB_PIG | MGNAATAKKGSEVESVKEFLAKAKEDFLKKWENPAPNNAGLEDFERKKTLGTGSFGRVMLVKHKATEQYYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVRLEFSFKDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDHQGYIQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVSDIKTHKWFATTDWIAIYQRKVEAPFIPKFR... | 2.7.11.11 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | negative regulation of TORC1 signaling [GO:1904262]; protein kinase A signaling [GO:0010737]; protein phosphorylation [GO:0006468] | cAMP-dependent protein kinase complex [GO:0005952]; cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | AMP-activated protein kinase activity [GO:0004679]; ATP binding [GO:0005524]; cAMP-dependent protein kinase activity [GO:0004691]; magnesium ion binding [GO:0000287]; protein serine kinase activity [GO:0106310] | PF00069; | 1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, cAMP subfamily | PTM: Asn-3 is deaminated to Asp in more than 25% of the proteins, giving rise to 2 major isoelectric variants, called CB and CA respectively (0.4 pH unit change). Deamidation proceeds via the so-called beta-aspartyl shift mechanism and yields either 'D-Asp-2' (major) or 'D-isoAsp-2' (minor), in addition to L-isomers. D... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P22694}. Cell membrane {ECO:0000250|UniProtKB:P22694}. Membrane {ECO:0000250|UniProtKB:P22694}; Lipid-anchor {ECO:0000250|UniProtKB:P22694}. Nucleus {ECO:0000250|UniProtKB:P05131}. Note=Translocates into the nucleus (monomeric catalytic subunit). The inactive holoe... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.11; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: Mediates cAMP-dependent signaling triggered by receptor binding to GPCRs. PKA activation regulates diverse cellular processes such as cell proliferation, the cell cycle, differentiation and regulation of microtubule dynamics, chromatin condensation and decondensation, nuclear envelope disassembly and reassemb... | Sus scrofa (Pig) |
P05386 | RLA1_HUMAN | MASVSELACIYSALILHDDEVTVTEDKINALIKAAGVNVEPFWPGLFAKALANVNIGSLICNVGAGGPAPAAGAAPAGGPAPSTAAAPAEEKKVEAKKEESEESDDDMGFGLFD | null | null | cytoplasmic translation [GO:0002181]; translation [GO:0006412]; translational elongation [GO:0006414] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; cytosolic ribosome [GO:0022626]; focal adhesion [GO:0005925] | 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 | PTM: Ubiquitinated at Lys-92 and Lys-93 by RNF14 and RNF25 in response to ribosome collisions (ribosome stalling). {ECO:0000269|PubMed:36638793}. | null | null | null | null | null | null | FUNCTION: Plays an important role in the elongation step of protein synthesis. | Homo sapiens (Human) |
P05387 | RLA2_HUMAN | MRYVASYLLAALGGNSSPSAKDIKKILDSVGIEADDDRLNKVISELNGKNIEDVIAQGIGKLASVPAGGAVAVSAAPGSAAPAAGSAPAAAEEKKDEKKEESEESDDDMGFGLFD | null | null | cytoplasmic translation [GO:0002181]; cytoplasmic translational elongation [GO:0002182]; translation [GO:0006412] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020] | 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. | Homo sapiens (Human) |
P05388 | RLA0_HUMAN | MPREDRATWKSNYFLKIIQLLDDYPKCFIVGADNVGSKQMQQIRMSLRGKAVVLMGKNTMMRKAIRGHLENNPALEKLLPHIRGNVGFVFTKEDLTEIRDMLLANKVPAAARAGAIAPCEVTVPAQNTGLGPEKTSFFQALGITTKISRGTIEILSDVQLIKTGDKVGASEATLLNMLNISPFSFGLVIQQVFDNGSIYNPEVLDITEETLHSRFLEGVRNVASVCLQIGYPTVASVPHSIINGYKRVLALSVETDYTFPLAEKVKAFLADPSAFVAAAPVAAATTAAPAAAAAPAKVEAKEESEESDEDMGFGLFD | null | null | cytoplasmic translation [GO:0002181]; ribosome biogenesis [GO:0042254]; translation [GO:0006412] | cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; cytosolic ribosome [GO:0022626]; endoplasmic reticulum [GO:0005783]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; nucleus [GO:00056... | large ribosomal subunit rRNA binding [GO:0070180]; RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735] | PF00428;PF00466;PF17777; | 3.30.70.1730;3.90.105.20; | Universal ribosomal protein uL10 family | PTM: Ubiquitinated at Lys-264 by RNF14 and RNF25 in response to ribosome collisions (ribosome stalling). {ECO:0000269|PubMed:36638793}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:19188445}. Cytoplasm {ECO:0000269|PubMed:19188445}. Note=Localized in cytoplasmic mRNP granules containing untranslated mRNAs (PubMed:17289661, PubMed:19188445). {ECO:0000269|PubMed:17289661, ECO:0000269|PubMed:19188445}. | null | null | null | null | null | FUNCTION: Ribosomal protein P0 is the functional equivalent of E.coli protein L10. | Homo sapiens (Human) |
P05408 | 7B2_HUMAN | MVSRMVSTMLSGLLFWLASGWTPAFAYSPRTPDRVSEADIQRLLHGVMEQLGIARPRVEYPAHQAMNLVGPQSIEGGAHEGLQHLGPFGNIPNIVAELTGDNIPKDFSEDQGYPDPPNPCPVGKTADDGCLENTPDTAEFSREFQLHQHLFDPEHDYPGLGKWNKKLLYEKMKGGERRKRRSVNPYLQGQRLDNVVAKKSVPHFSDEDKDPE | null | null | intracellular protein transport [GO:0006886]; neuropeptide signaling pathway [GO:0007218]; peptide hormone processing [GO:0016486]; regulation of hormone secretion [GO:0046883] | extracellular region [GO:0005576]; nucleus [GO:0005634]; secretory granule [GO:0030141] | enzyme inhibitor activity [GO:0004857]; enzyme regulator activity [GO:0030234]; GTP binding [GO:0005525]; unfolded protein binding [GO:0051082] | PF05281; | null | 7B2 family | PTM: Proteolytically cleaved in the Golgi by a furin-like convertase to generate bioactive peptides. {ECO:0000250|UniProtKB:P12961}.; PTM: Sulfated on tyrosine residues. {ECO:0000250|UniProtKB:P12961}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P01165}. Note=Neuroendocrine and endocrine secretory granules. {ECO:0000250|UniProtKB:P01165}. | null | null | null | null | null | FUNCTION: Acts as a molecular chaperone for PCSK2/PC2, preventing its premature activation in the regulated secretory pathway. Binds to inactive PCSK2 in the endoplasmic reticulum and facilitates its transport from there to later compartments of the secretory pathway where it is proteolytically matured and activated. A... | Homo sapiens (Human) |
P05412 | JUN_HUMAN | MTAKMETTFYDDALNASFLPSESGPYGYSNPKILKQSMTLNLADPVGSLKPHLRAKNSDLLTSPDVGLLKLASPELERLIIQSSNGHITTTPTPTQFLCPKNVTDEQEGFAEGFVRALAELHSQNTLPSVTSAAQPVNGAGMVAPAVASVAGGSGSGGFSASLHSEPPVYANLSNFNPGALSSGGGAPSYGAAGLAFPAQPQQQQQPPHHLPQQMPVQHPRLQALKEEPQTVPEMPGETPPLSPIDMESQERIKAERKRMRNRIAASKCRKRKLERIARLEEKVKTLKAQNSELASTANMLREQVAQLKQKVMNHVNSGC... | null | null | cellular response to cadmium ion [GO:0071276]; cellular response to reactive oxygen species [GO:0034614]; integrated stress response signaling [GO:0140467]; negative regulation by host of viral transcription [GO:0043922]; negative regulation of DNA binding [GO:0043392]; negative regulation of DNA-templated transcriptio... | chromatin [GO:0000785]; euchromatin [GO:0000791]; nuclear chromosome [GO:0000228]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]; transcription factor AP-1 complex [GO:0035976]; transcription regulator complex [GO:0005667] | cAMP response element binding [GO:0035497]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcripti... | PF00170;PF03957; | 1.20.5.170; | BZIP family, Jun subfamily | PTM: Ubiquitinated by the SCF(FBXW7), leading to its degradation (PubMed:14739463, PubMed:27458189). Ubiquitination takes place following phosphorylation, that promotes interaction with FBXW7 (PubMed:14739463). {ECO:0000269|PubMed:14739463, ECO:0000269|PubMed:27458189}.; PTM: Phosphorylated by CaMK4 and PRKDC; phosphor... | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Transcription factor that recognizes and binds to the AP-1 consensus motif 5'-TGA[GC]TCA-3' (PubMed:10995748, PubMed:22083952). Heterodimerizes with proteins of the FOS family to form an AP-1 transcription complex, thereby enhancing its DNA binding activity to the AP-1 consensus sequence 5'-TGA[GC]TCA-3' and ... | Homo sapiens (Human) |
P05413 | FABPH_HUMAN | MVDAFLGTWKLVDSKNFDDYMKSLGVGFATRQVASMTKPTTIIEKNGDILTLKTHSTFKNTEISFKLGVEFDETTADDRKVKSIVTLDGGKLVHLQKWDGQETTLVRELIDGKLILTLTHGTAVCTRTYEKEA | null | null | brown fat cell differentiation [GO:0050873]; cholesterol homeostasis [GO:0042632]; intracellular lipid transport [GO:0032365]; long-chain fatty acid transport [GO:0015909]; negative regulation of cell population proliferation [GO:0008285]; phospholipid homeostasis [GO:0055091]; positive regulation of long-chain fatty a... | cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; nucleus [GO:0005634] | cytoskeletal protein binding [GO:0008092]; long-chain fatty acid binding [GO:0036041]; oleic acid binding [GO:0070538] | PF00061; | 2.40.128.20; | Calycin superfamily, Fatty-acid binding protein (FABP) family | null | SUBCELLULAR LOCATION: Cytoplasm. | null | null | null | null | null | FUNCTION: FABPs are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters. | Homo sapiens (Human) |
P05414 | GOX_SPIOL | MEITNVNEYEAIAKQKLPKMVYDYYASGAEDQWTLAENRNAFSRILFRPRILIDVTNIDMTTTILGFKISMPIMIAPTAMQKMAHPEGEYATARAASAAGTIMTLSSWATSSVEEVASTGPGIRFFQLYVYKDRNVVAQLVRRAERAGFKAIALTVDTPRLGRREADIKNRFVLPPFLTLKNFEGIDLGKMDKANDSGLSSYVAGQIDRSLSWKDVAWLQTITSLPILVKGVITAEDARLAVQHGAAGIIVSNHGARQLDYVPATIMALEEVVKAAQGRIPVFLDGGVRRGTDVFKALALGAAGVFIGRPVVFSLAAEGE... | 1.1.3.15 | COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000269|PubMed:2644287, ECO:0000269|PubMed:2681790, ECO:0000269|PubMed:7705356, ECO:0000269|PubMed:9144771}; Note=Binds 1 FMN per subunit. {ECO:0000269|PubMed:2681790}; | fatty acid alpha-oxidation [GO:0001561]; lactate oxidation [GO:0019516]; oxidative photosynthetic carbon pathway [GO:0009854]; response to other organism [GO:0051707] | peroxisome [GO:0005777]; plasma membrane [GO:0005886] | (S)-2-hydroxy-acid oxidase activity [GO:0003973]; FMN binding [GO:0010181]; L-lactate dehydrogenase activity [GO:0004459] | PF01070; | 3.20.20.70; | FMN-dependent alpha-hydroxy acid dehydrogenase family | null | SUBCELLULAR LOCATION: Peroxisome. | CATALYTIC ACTIVITY: Reaction=glycolate + O2 = glyoxylate + H2O2; Xref=Rhea:RHEA:25311, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:29805, ChEBI:CHEBI:36655; EC=1.1.3.15; Evidence={ECO:0000269|PubMed:1324737, ECO:0000269|PubMed:7705356}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:25312; Evidence={ECO:000... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.2 mM for glycolate (at 25 degrees Celsius) {ECO:0000269|PubMed:1324737}; KM=1 mM for glycolate {ECO:0000269|PubMed:7705356}; KM=11.5 mM for L-lactate {ECO:0000269|PubMed:7705356}; KM=0.21 mM for O2 {ECO:0000269|PubMed:7705356}; KM=3 mM for L-2-hydroxbyutanoate {E... | PATHWAY: Photosynthesis; photorespiration; glycine from 2-phosphoglycolate: step 2/3. {ECO:0000305|PubMed:2644287}. | null | null | FUNCTION: Catalyzes the oxidation of glycolate to glyoxylate, with a reduction of O2 to H2O2 (PubMed:1324737, PubMed:7705356). Is a key enzyme in photorespiration in green plants (Probable). To a lesser extent, is also able to use L-lactate and 2-hydroxbyutanoate as substrate in vitro, but shows almost no activity with... | Spinacia oleracea (Spinach) |
P05423 | RPC4_HUMAN | MSEGNAAGEPSTPGGPRPLLTGARGLIGRRPAPPLTPGRLPSIRSRDLTLGGVKKKTFTPNIISRKIKEEPKEEVTVKKEKRERDRDRQREGHGRGRGRPEVIQSHSIFEQGPAEMMKKKGNWDKTVDVSDMGPSHIINIKKEKRETDEETKQILRMLEKDDFLDDPGLRNDTRNMPVQLPLAHSGWLFKEENDEPDVKPWLAGPKEEDMEVDIPAVKVKEEPRDEEEEAKMKAPPKAARKTPGLPKDVSVAELLRELSLTKEEELLFLQLPDTLPGQPPTQDIKPIKTEVQGEDGQVVLIKQEKDREAKLAENACTLAD... | null | null | defense response to virus [GO:0051607]; innate immune response [GO:0045087]; positive regulation of innate immune response [GO:0045089]; positive regulation of interferon-beta production [GO:0032728]; tRNA transcription by RNA polymerase III [GO:0042797] | cytosol [GO:0005829]; nucleoplasm [GO:0005654]; RNA polymerase III complex [GO:0005666] | chromatin binding [GO:0003682]; DNA binding [GO:0003677] | PF05132; | null | Eukaryotic RPC4/POLR3D RNA polymerase subunit family | PTM: Sumoylation on Lys-141 can serve as a signal to mark misfolded Pol III for proteasomal degradation. {ECO:0000269|PubMed:33558764}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:33335104}. | null | null | null | null | null | FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates (PubMed:12391170, PubMed:20413673, PubMed:33558764, PubMed:34675218, PubMed:35637192). Specific peripheric component of RNA polymerase III (Pol III) which synthesizes small non-co... | Homo sapiens (Human) |
P05425 | COPB_ENTHA | MNNGIDPENETNKKGAIGKNPEEKITVEQTNTKNNLQEHGKMENMDQHHTHGHMERHQQMDHGHMSGMDHSHMDHEDMSGMNHSHMGHENMSGMDHSMHMGNFKQKFWLSLILAIPIILFSPMMGMSFPFQVTFPGSNWVVLVLATILFIYGGQPFLSGAKMELKQKSPAMMTLIAMGITVAYVYSVYSFIANLINPHTHVMDFFWELATLIVIMLLGHWIEMNAVSNASDALQKLAELLPESVKRLKKDGTEETVSLKEVHEGDRLIVRAGDKMPTDGTIDKGHTIVDESAVTGESKGVKKQVGDSVIGGSINGDGTIE... | 7.2.2.8 | null | copper ion homeostasis [GO:0055070] | plasma membrane [GO:0005886] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; copper ion binding [GO:0005507]; P-type divalent copper transporter activity [GO:0043682]; P-type monovalent copper transporter activity [GO:0140581] | PF00122;PF00702; | 3.40.1110.10;2.70.150.10;3.40.50.1000; | Cation transport ATPase (P-type) (TC 3.A.3) family, Type IB subfamily | null | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. | CATALYTIC ACTIVITY: Reaction=ATP + Cu(+)(in) + H2O = ADP + Cu(+)(out) + H(+) + phosphate; Xref=Rhea:RHEA:25792, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:49552, ChEBI:CHEBI:456216; EC=7.2.2.8; Evidence={ECO:0000269|PubMed:7721839}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. {ECO:0000269|PubMed:7721839}; | null | FUNCTION: Involved in copper export. Can also export silver. {ECO:0000269|PubMed:7721839, ECO:0000269|PubMed:8037745, ECO:0000269|PubMed:8048974}. | Enterococcus hirae (strain ATCC 9790 / DSM 20160 / JCM 8729 / LMG 6399 / NBRC 3181 / NCIMB 6459 / NCDO 1258 / NCTC 12367 / WDCM 00089 / R) |
P05426 | RL7_RAT | MEAVPEKKKKVAAALGTLKKKKVPAVPETLKKKRRNFAELKVKRLRKKFALKTLRKARRKLIYEKAKHYHKEYRQMYRTEIRMARMARKAGNFYVPAEPKLAFVIRIRGINGVSPKVRKVLQLLRLRQIFNGTFVKLNKASVNMLRIVEPYIAWGYPNLKSVNELIYKRGYGKINKKRIALTDNSLVARSLGKFGIICMEDLIHEIYTVGKRFKEANNFLWPFKLSSPRGGMKKKTTHFVEGGDAGNREDQINRLIRRMN | null | null | liver regeneration [GO:0097421]; maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000463]; ribosomal large subunit biogenesis [GO:0042273]; rRNA processing [GO:0006364] | A band [GO:0031672]; cytoplasm [GO:0005737]; cytosolic large ribosomal subunit [GO:0022625]; cytosolic ribosome [GO:0022626]; postsynaptic density [GO:0014069]; ribonucleoprotein complex [GO:1990904]; ribosome [GO:0005840]; synapse [GO:0045202] | 5S rRNA binding [GO:0008097]; DNA binding [GO:0003677]; identical protein binding [GO:0042802]; mRNA binding [GO:0003729]; RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735] | PF00327;PF08079; | 3.30.1390.20; | Universal ribosomal protein uL30 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P18124}. | null | null | null | null | null | FUNCTION: Component of the large ribosomal subunit. The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. Binds to G-rich structures in 28S rRNA and in mRNAs. Plays a regulatory role in the translation apparatus; inhibits cell-free translation of mRNAs. {ECO:0000250|Un... | Rattus norvegicus (Rat) |
P05431 | FMM1_NEIMB | MNTLQKGFTLIELMIVIAIVGILAAVALPAYQDYTARAQVSEAILLAEGQKSAVTEYYLNHGEWPGNNTSAGVATSSEIKGKYVKSVEVKNGVVTAQMASSNVNNEIKGKKLSLWAKRQNGSVKWFCGQPVTRDKAKAANDDVTAAAAANGKKIDTKHLPSTCRDASDAS | null | null | cell adhesion [GO:0007155] | membrane [GO:0016020]; pilus [GO:0009289] | null | PF07963;PF00114; | 3.30.700.10; | N-Me-Phe pilin family | PTM: O-linked glycan has been reported to consist either of the Gal(alpha1-3) GlcNAc disaccharide, or the Gal(beta 1-4) Gal(alpha 1-3) 2,4-diacetamido-2,4,6-trideoxyhexose trisaccharide. {ECO:0000269|PubMed:7934852, ECO:0000269|PubMed:9515697}. | SUBCELLULAR LOCATION: Fimbrium. Membrane {ECO:0000255}; Single-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Major component of the type IV pilus (T4P) that plays a role in cellular adherence, microcolony formation as well as twitching motility. {ECO:0000269|PubMed:17121595, ECO:0000269|PubMed:27698424, ECO:0000269|PubMed:7934852}. | Neisseria meningitidis serogroup B (strain MC58) |
P05432 | ERRFI_RAT | MSTAGVAAQDIRVPLKTGFLHNGQALGNMKTCWGSRNEFEKNFLNIDPITMAYNLNSPAPEHLTTLGCASPSAPGSGHFFAERGPSPKSSLPPLVIPPSESSGQREEDQVLCGFKKLSVNGVCASTPPLTPIQSCSSPFPCAAPCDRSSRPLPPLPISEDPSLDEADCEVEFLTSADTDFLLEDCVPSDFKYDVPGRRSFRGCGQINYAYFDSPTVSVADLSCASDQNRVVPDPNPPPPQSHRRLRRSHSGPAGSFNKPAIRISSCTHRASPSSDEDKPEIPPRVPIPPRPAKPDYRRWSAEVTSNTYSDEDRPPKVPPR... | null | null | apoptotic process [GO:0006915]; bile acid biosynthetic process [GO:0006699]; cartilage development [GO:0051216]; cell migration [GO:0016477]; cellular hyperosmotic response [GO:0071474]; cellular response to dexamethasone stimulus [GO:0071549]; cellular response to epidermal growth factor stimulus [GO:0071364]; cellula... | cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | kinase binding [GO:0019900]; protein kinase binding [GO:0019901]; SH3 domain binding [GO:0017124]; small GTPase binding [GO:0031267] | PF09027;PF11555; | null | MIG6 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Nucleus {ECO:0000250}. Note=Associated with the plasma membrane of basal skin keratinocytes. Translocates into the nucleus of differentiating suprabasal keratinocytes (B... | null | null | null | null | null | FUNCTION: Negative regulator of EGFR signaling in skin morphogenesis. Acts as a negative regulator for several EGFR family members, including ERBB2, ERBB3 and ERBB4. Inhibits EGFR catalytic activity by interfering with its dimerization. Inhibits autophosphorylation of EGFR, ERBB2 and ERBB4. Important for normal keratin... | Rattus norvegicus (Rat) |
P05451 | REG1A_HUMAN | MAQTSSYFMLISCLMFLSQSQGQEAQTELPQARISCPEGTNAYRSYCYYFNEDRETWVDADLYCQNMNSGNLVSVLTQAEGAFVASLIKESGTDDFNVWIGLHDPKKNRRWHWSSGSLVSYKSWGIGAPSSVNPGYCVSLTSSTGFQKWKDVPCEDKFSFVCKFKN | null | null | antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; disruption of cell wall in another organism [GO:0044278]; positive regulation of cell population proliferation [GO:0008284]; response to peptide hormone [GO:0043434] | collagen-containing extracellular matrix [GO:0062023]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615] | growth factor activity [GO:0008083]; molecular function inhibitor activity [GO:0140678]; oligosaccharide binding [GO:0070492]; peptidoglycan binding [GO:0042834]; signaling receptor activity [GO:0038023] | PF00059; | 3.10.100.10; | null | PTM: The composition of the O-linked carbohydrate on Thr-27 is complex and varied. In the crystallographic structure, the attached sugar appears to be N-acetylglucosamine, typical of an intracellular protein, rather than N-acetylgalactosamine. {ECO:0000269|PubMed:2493268}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Might act as an inhibitor of spontaneous calcium carbonate precipitation. May be associated with neuronal sprouting in brain, and with brain and pancreas regeneration. | Homo sapiens (Human) |
P05452 | TETN_HUMAN | MELWGAYLLLCLFSLLTQVTTEPPTQKPKKIVNAKKDVVNTKMFEELKSRLDTLAQEVALLKEQQALQTVCLKGTKVHMKCFLAFTQTKTFHEASEDCISRGGTLGTPQTGSENDALYEYLRQSVGNEAEIWLGLNDMAAEGTWVDMTGARIAYKNWETEITAQPDGGKTENCAVLSGAANGKWFDKRCRDQLPYICQFGIV | null | null | bone mineralization [GO:0030282]; cellular response to organic substance [GO:0071310]; cellular response to transforming growth factor beta stimulus [GO:0071560]; ossification [GO:0001503]; positive regulation of plasminogen activation [GO:0010756] | collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; granular component [GO:0001652]; platelet dense granule lumen [GO:0031089] | calcium ion binding [GO:0005509]; carbohydrate binding [GO:0030246]; heparin binding [GO:0008201]; kringle domain binding [GO:0036143] | PF00059; | 3.10.100.10; | null | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Tetranectin binds to plasminogen and to isolated kringle 4. May be involved in the packaging of molecules destined for exocytosis. Plays a role in retinal function (PubMed:35331648). {ECO:0000269|PubMed:35331648}. | Homo sapiens (Human) |
P05453 | ERF3_YEAST | MSDSNQGNNQQNYQQYSQNGNQQQGNNRYQGYQAYNAQAQPAGGYYQNYQGYSGYQQGGYQQYNPDAGYQQQYNPQGGYQQYNPQGGYQQQFNPQGGRGNYKNFNYNNNLQGYQAGFQPQSQGMSLNDFQKQQKQAAPKPKKTLKLVSSSGIKLANATKKVGTKPAESDKKEEEKSAETKEPTKEPTKVEEPVKKEEKPVQTEEKTEEKSELPKVEDLKISESTHNTNNANVTSADALIKEQEEEVDDEVVNDMFGGKDHVSLIFMGHVDAGKSTMGGNLLYLTGSVDKRTIEKYEREAKDAGRQGWYLSWVMDTNKEER... | 3.6.5.- | null | nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay [GO:0000288]; translation [GO:0006412]; translational termination [GO:0006415] | cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; translation release factor complex [GO:0018444] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; identical protein binding [GO:0042802]; mRNA binding [GO:0003729]; translation release factor activity [GO:0003747] | PF00009;PF03144;PF03143; | 3.40.50.300;2.40.30.10; | TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family, ERF3 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {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; Evidence={ECO:0000269|PubMed:34413231}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000269|PubMed:34413231}... | null | null | null | null | FUNCTION: GTPase component of the eRF1-eRF3-GTP ternary complex, a ternary complex that mediates translation termination in response to the termination codons UAA, UAG and UGA (PubMed:34413231, PubMed:7556078). SUP35/eRF3 mediates SUP45/eRF1 delivery to stop codons: The eRF1-eRF3-GTP complex binds to a stop codon in th... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P05455 | LA_HUMAN | MAENGDNEKMAALEAKICHQIEYYFGDFNLPRDKFLKEQIKLDEGWVPLEIMIKFNRLNRLTTDFNVIVEALSKSKAELMEISEDKTKIRRSPSKPLPEVTDEYKNDVKNRSVYIKGFPTDATLDDIKEWLEDKGQVLNIQMRRTLHKAFKGSIFVVFDSIESAKKFVETPGQKYKETDLLILFKDDYFAKKNEERKQNKVEAKLRAKQEQEAKQKLEEDAEMKSLEEKIGCLLKFSGDLDDQTCREDLHILFSNHGEIKWIDFVRGAKEGIILFKEKAKEALGKAKDANNGNLQLRNKEVTWEVLEGEVEKEALKKIIE... | null | null | histone mRNA metabolic process [GO:0008334]; IRES-dependent viral translational initiation [GO:0075522]; nuclear histone mRNA catabolic process [GO:0071045]; positive regulation of translation [GO:0045727]; protein localization to cytoplasmic stress granule [GO:1903608]; tRNA 3'-end processing [GO:0042780]; tRNA 5'-lea... | chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904] | mRNA binding [GO:0003729]; poly(U) RNA binding [GO:0008266]; RNA binding [GO:0003723]; sequence-specific mRNA binding [GO:1990825]; tRNA binding [GO:0000049] | PF05383;PF00076;PF08777; | 3.30.70.330;1.10.10.10; | null | PTM: Phosphorylated. The phosphorylation sites are at the C-terminal part of the protein. {ECO:0000269|PubMed:9054510}.; PTM: The N-terminus is blocked. | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Binds to the 3' poly(U) terminus of nascent RNA polymerase III transcripts, protecting them from exonuclease digestion and facilitating their folding and maturation (PubMed:2470590, PubMed:3192525). In case of Coxsackievirus B3 infection, binds to the viral internal ribosome entry site (IRES) and stimulates t... | Homo sapiens (Human) |
P05458 | PTRA_ECOLI | MPRSTWFKALLLLVALWAPLSQAETGWQPIQETIRKSDKDNRQYQAIRLDNGMVVLLVSDPQAVKSLSALVVPVGSLEDPEAYQGLAHYLEHMSLMGSKKYPQADSLAEYLKMHGGSHNASTAPYRTAFYLEVENDALPGAVDRLADAIAEPLLDKKYAERERNAVNAELTMARTRDGMRMAQVSAETINPAHPGSKFSGGNLETLSDKPGNPVQQALKDFHEKYYSANLMKAVIYSNKPLPELAKMAADTFGRVPNKESKKPEITVPVVTDAQKGIIIHYVPALPRKVLRVEFRIDNNSAKFRSKTDELITYLIGNRSP... | 3.4.24.55 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.; | amyloid-beta metabolic process [GO:0050435]; hormone catabolic process [GO:0042447]; peptide catabolic process [GO:0043171]; proteolysis [GO:0006508]; proteolysis involved in protein catabolic process [GO:0051603] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; outer membrane-bounded periplasmic space [GO:0030288]; peroxisomal matrix [GO:0005782] | metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270] | PF00675;PF05193;PF16187; | 3.30.830.10; | Peptidase M16 family | null | SUBCELLULAR LOCATION: Periplasm. | CATALYTIC ACTIVITY: Reaction=Preferential cleavage of 16-Tyr-|-Leu-17 and 25-Phe-|-Tyr-26 bonds of oxidized insulin B chain. Also acts on other substrates of Mw less than 7 kDa such as insulin and glucagon.; EC=3.4.24.55; Evidence={ECO:0000255|PROSITE-ProRule:PRU10096}; | null | null | null | null | FUNCTION: Endopeptidase that degrades small peptides of less than 7 kDa, such as glucagon and insulin. | Escherichia coli (strain K12) |
P05480 | SRC_MOUSE | MGSNKSKPKDASQRRRSLEPSENVHGAGGAFPASQTPSKPASADGHRGPSAAFVPPAAEPKLFGGFNSSDTVTSPQRAGPLAGGVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLSTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRESERLLLNAENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFNSLQQLVAYYSKHADGLCHRLTTVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKLR... | 2.7.10.2 | null | adherens junction organization [GO:0034332]; angiotensin-activated signaling pathway [GO:0038166]; bone resorption [GO:0045453]; branching involved in mammary gland duct morphogenesis [GO:0060444]; cell adhesion [GO:0007155]; cell cycle [GO:0007049]; cell differentiation [GO:0030154]; cell migration [GO:0016477]; cell-... | actin filament [GO:0005884]; caveola [GO:0005901]; cell junction [GO:0030054]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; dendritic filopodium [GO:1902737]; dendritic growth cone [GO:0044294]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; focal adhesion [GO:00059... | ATP binding [GO:0005524]; BMP receptor binding [GO:0070700]; cell adhesion molecule binding [GO:0050839]; connexin binding [GO:0071253]; enzyme binding [GO:0019899]; ephrin receptor binding [GO:0046875]; heme binding [GO:0020037]; insulin receptor binding [GO:0005158]; integrin binding [GO:0005178]; kinase activity [GO... | 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: Myristoylated at Gly-2, and this is essential for targeting to membranes. {ECO:0000250}.; PTM: Dephosphorylated at Tyr-529 by PTPRJ (By similarity). Phosphorylated on Tyr-529 by c-Src kinase (CSK). The phosphorylated form is termed pp60c-src. Dephosphorylated by PTPRJ at Tyr-418. Normally maintained in an inactive... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12615910, ECO:0000269|PubMed:21525037}; Lipid-anchor {ECO:0000269|PubMed:22801373}. Mitochondrion inner membrane {ECO:0000269|PubMed:12615910}. Nucleus {ECO:0000269|PubMed:12615910}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:12615910}. Cytoplasm, perinuclear reg... | 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 protein tyrosine kinase which is activated following engagement of many different classes of cellular receptors including immune response receptors, integrins and other adhesion receptors, receptor protein tyrosine kinases, G protein-coupled receptors as well as cytokine receptors. Participates i... | Mus musculus (Mouse) |
P05484 | O17A_CONMA | MKLTCVVIVAVLLLTACQLITADDSRGTQKHRALRSTTKLSTSTRCKGKGAKCSRLMYDCCTGSCRSGKCG | null | null | null | extracellular region [GO:0005576]; host cell presynaptic membrane [GO:0044231] | calcium channel regulator activity [GO:0005246]; ion channel inhibitor activity [GO:0008200]; toxin activity [GO:0090729] | PF02950; | null | Conotoxin O1 superfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2441741, ECO:0000269|PubMed:4071055}. | null | null | null | null | null | FUNCTION: Omega-conotoxins act at presynaptic membranes, they bind and block voltage-gated calcium channels. This toxin blocks Cav2.2/CACNA1B calcium channels (IC(50)=0.67-208 nM) (PubMed:26344359, PubMed:34589389, PubMed:7826361). It acts by neutralizing the outer electronegativity and sterically hindering the ion acc... | Conus magus (Magical cone) |
P05496 | AT5G1_HUMAN | MQTAGALFISPALIRCCTRGLIRPVSASFLNSPVNSSKQPSYSNFPLQVARREFQTSVVSRDIDTAAKFIGAGAATVGVAGSGAGIGTVFGSLIIGYARNPSLKQQLFSYAILGFALSEAMGLFCLMVAFLILFAM | null | null | proton motive force-driven ATP synthesis [GO:0015986] | mitochondrial inner membrane [GO:0005743]; mitochondrial proton-transporting ATP synthase complex [GO:0005753]; mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) [GO:0000276]; mitochondrion [GO:0005739] | lipid binding [GO:0008289]; proton transmembrane transporter activity [GO:0015078] | PF00137; | 1.20.20.10; | ATPase C chain family | PTM: Trimethylated by ATPSCKMT at Lys-104. Methylation is required for proper incorporation of the C subunit into the ATP synthase complex and mitochondrial respiration. {ECO:0000269|PubMed:30530489}. | SUBCELLULAR LOCATION: Mitochondrion membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramemb... | Homo sapiens (Human) |
P05503 | COX1_RAT | MLVNRWLFSTNHKDIGTLYLLFGAWAGMVGTALSILIRAELGQPGALLGDDQIYNVIVTAHAFVMIFFMVMPMMIGGFGNWLVPLMIGAPDMAFPRMNNMSFWLLPPSFLLLLASSMVEAGAGTGWTVYPPLAGNLAHAGASVDLTIFSLHLAGVSSILGAINFITTIINMKPPAMTQYQTPLFVWSVLITAVLLLLSLPVLAAGITMLLTDRNLNTTFFDPAGGGDPILYQHLFWFFGHPEVYILILPGFGIISHVVTYYSGKKEPFGYMGMVWAMMSIGFLGFIVWAHHMFTVGLDVDTRAYFTSATMIIAIPTGVKV... | 7.1.1.9 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P00396}; Note=Binds 2 heme A groups non-covalently per subunit. {ECO:0000250|UniProtKB:P00396}; COFACTOR: Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250|UniProtKB:P00396}; Note=Binds a copper B center. {ECO:0000250|UniProtKB:P00... | cerebellum development [GO:0021549]; electron transport coupled proton transport [GO:0015990]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123]; response to copper ion [GO:0046688]; response to electrical stimulus [GO:0051602]; response to hypoxia [GO:0001666]; response to oxidative stress [GO:0006... | mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966]; mitochondrial respiratory chain complex III [GO:0005750]; mitochondrial respiratory chain complex IV [GO:0005751]; mitochondrion [GO:0005739]; respiratory chain complex IV [GO:0045277] | cytochrome-c oxidase activity [GO:0004129]; heme binding [GO:0020037]; metal ion binding [GO:0046872] | PF00115; | 1.20.210.10; | Heme-copper respiratory oxidase family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P00396}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P00396}. | CATALYTIC ACTIVITY: Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=7.1.1.9; Evidence={ECO:0000250|UniP... | null | PATHWAY: Energy metabolism; oxidative phosphorylation. {ECO:0000250|UniProtKB:P00401}. | null | null | FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple... | Rattus norvegicus (Rat) |
P05523 | FPG_ECOLI | MPELPEVETSRRGIEPHLVGATILHAVVRNGRLRWPVSEEIYRLSDQPVLSVQRRAKYLLLELPEGWIIIHLGMSGSLRILPEELPPEKHDHVDLVMSNGKVLRYTDPRRFGAWLWTKELEGHNVLTHLGPEPLSDDFNGEYLHQKCAKKKTAIKPWLMDNKLVVGVGNIYASESLFAAGIHPDRLASSLSLAECELLARVIKAVLLRSIEQGGTTLKDFLQSDGKPGYFAQELQVYGRKGEPCRVCGTPIVATKHAQRATFYCRQCQK | 3.2.2.23; 4.2.99.18 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:1689309}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:1689309}; | base-excision repair [GO:0006284]; DNA damage response [GO:0006974] | cytoplasm [GO:0005737] | 8-oxo-7,8-dihydroguanine DNA N-glycosylase activity [GO:0034039]; class I DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0140078]; damaged DNA binding [GO:0003684]; DNA N-glycosylase activity [GO:0019104]; DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0003906]; endonuclease activity [GO:0... | PF01149;PF06831;PF06827; | 1.10.8.50;3.20.190.10; | FPG family | null | null | CATALYTIC ACTIVITY: Reaction=Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine.; EC=3.2.2.23; CATALYTIC ACTIVITY: Reaction=2'-deoxyribonucleotide-(2'-deoxyribose 5'-phosphate)-2'-deoxyribonucleotide-DNA = a 3'-end 2'-deoxyribonucleotide-(2... | null | null | null | null | FUNCTION: Involved in base excision repair of DNA damaged by oxidation or by mutagenic agents. Acts as a DNA glycosylase that recognizes and removes damaged bases. Has a preference for oxidized purines, such as 7,8-dihydro-8-oxoguanine (8-oxoG) and its derivatives such as guanidinohydantoin:C and spiroiminodihydantoin:... | Escherichia coli (strain K12) |
P05524 | FGF3_MOUSE | MGLIWLLLLSLLEPSWPTTGPGTRLRRDAGGRGGVYEHLGGAPRRRKLYCATKYHLQLHPSGRVNGSLENSAYSILEITAVEVGVVAIKGLFSGRYLAMNKRGRLYASDHYNAECEFVERIHELGYNTYASRLYRTGSSGPGAQRQPGAQRPWYVSVNGKGRPRRGFKTRRTQKSSLFLPRVLGHKDHEMVRLLQSSQPRAPGEGSQPRQRRQKKQSPGDHGKMETLSTRATPSTQLHTGGLAVA | null | null | animal organ morphogenesis [GO:0009887]; cell differentiation [GO:0030154]; fibroblast growth factor receptor signaling pathway [GO:0008543]; organ induction [GO:0001759]; otic vesicle formation [GO:0030916]; positive regulation of cell division [GO:0051781]; positive regulation of cell population proliferation [GO:000... | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; extracellular space [GO:0005615]; Golgi apparatus [GO:0005794]; nucleus [GO:0005634] | fibroblast growth factor receptor binding [GO:0005104]; growth factor activity [GO:0008083] | PF00167; | 2.80.10.50; | Heparin-binding growth factors family | PTM: Glycosylated. | SUBCELLULAR LOCATION: [Isoform 1]: Nucleus.; SUBCELLULAR LOCATION: [Isoform 2]: Endoplasmic reticulum. Golgi apparatus. | null | null | null | null | null | FUNCTION: Plays an important role in the regulation of embryonic development, cell proliferation, and cell differentiation. Required for normal ear development (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
P05532 | KIT_MOUSE | MRGARGAWDLLCVLLVLLRGQTATSQPSASPGEPSPPSIHPAQSELIVEAGDTLSLTCIDPDFVRWTFKTYFNEMVENKKNEWIQEKAEATRTGTYTCSNSNGLTSSIYVFVRDPAKLFLVGLPLFGKEDSDALVRCPLTDPQVSNYSLIECDGKSLPTDLTFVPNPKAGITIKNVKRAYHRLCVRCAAQRDGTWLHSDKFTLKVRAAIKAIPVVSVPETSHLLKKGDTFTVVCTIKDVSTSVNSMWLKMNPQPQHIAQVKHNSWHRGDFNYERQETLTISSARVDDSGVFMCYANNTFGSANVTTTLKVVEKGFINISP... | 2.7.10.1 | null | actin cytoskeleton organization [GO:0030036]; B cell differentiation [GO:0030183]; cell chemotaxis [GO:0060326]; cell differentiation [GO:0030154]; cell population proliferation [GO:0008283]; chemotaxis [GO:0006935]; cytokine-mediated signaling pathway [GO:0019221]; detection of mechanical stimulus involved in sensory ... | acrosomal vesicle [GO:0001669]; cell surface [GO:0009986]; cell-cell junction [GO:0005911]; cytoplasmic side of plasma membrane [GO:0009898]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; fibrillar center [GO:0001650]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; cytokine binding [GO:0019955]; growth factor binding [GO:0019838]; metal ion binding [GO:0046872]; protease binding [GO:0002020]; protein homodimerization activity [GO:0042803]; protein tyrosine kinase activity [GO:0004713]; SH2 domain binding [GO:0042169]; stem cell factor receptor activity [... | PF00047;PF07714; | 2.60.40.10;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, CSF-1/PDGF receptor subfamily | PTM: Ubiquitinated by SOCS6. KIT is rapidly ubiquitinated after autophosphorylation induced by KITLG/SCF binding, leading to internalization and degradation (By similarity). {ECO:0000250}.; PTM: Autophosphorylated on tyrosine residues. KITLG/SCF binding promotes autophosphorylation of isoform 1 and isoform 2. Isoform 1... | SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm. Note=Detected in the cytoplasm of spermatozoa, especially in the equatorial and subacrosomal regio... | 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: Tyrosine-protein kinase that acts as a cell-surface receptor for the cytokine KITLG/SCF and plays an essential role in the regulation of cell survival and proliferation, hematopoiesis, stem cell maintenance, gametogenesis, mast cell development, migration and function, and in melanogenesis. In response to KIT... | Mus musculus (Mouse) |
P05533 | LY6A_MOUSE | MDTSHTTKSCLLILLVALLCAERAQGLECYQCYGVPFETSCPSITCPYPDGVCVTQEAAVIVDSQTRKVKNNLCLPICPPNIESMEILGTKVNVKTSCCQEDLCNVAVPNGGSTWTMAGVLLFSLSSVLLQTLL | null | null | acetylcholine receptor signaling pathway [GO:0095500]; response to bacterium [GO:0009617] | external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886]; synapse [GO:0045202] | acetylcholine receptor binding [GO:0033130]; acetylcholine receptor inhibitor activity [GO:0030550] | PF00021; | 2.10.60.10; | null | PTM: O-glycosylated. Not N-glycosylated. {ECO:0000269|PubMed:3033645}.; PTM: Not phosphorylated. | SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. | null | null | null | null | null | FUNCTION: T-cell activation. | Mus musculus (Mouse) |
P05538 | DQB2_HUMAN | MSWKMALQIPGGFWAAAVTVMLVMLSTPVAEARDFPKDFLVQFKGMCYFTNGTERVRGVARYIYNREEYGRFDSDVGEFQAVTELGRSIEDWNNYKDFLEQERAAVDKVCRHNYEAELRTTLQRQVEPTVTISPSRTEALNHHNLLVCSVTDFYPAQIKVRWFRNDQEETAGVVSTSLIRNGDWTFQILVMLEITPQRGDIYTCQVEHPSLQSPITVEWRAQSESAQSKMLSGIGGFVLGLIFLGLGLIIRHRGQKGPRGPPPAGLLH | null | null | adaptive immune response [GO:0002250]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; immune response [GO:0006955]; peptide antigen assembly with MHC class II protein complex [GO:0002503]; positive regulation of immune response [GO:0050778]; positive regulation of T cell... | clathrin-coated endocytic vesicle membrane [GO:0030669]; endocytic vesicle membrane [GO:0030666]; ER to Golgi transport vesicle membrane [GO:0012507]; Golgi membrane [GO:0000139]; late endosome membrane [GO:0031902]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; lysosomal membrane [GO:0005765]; MHC class... | MHC class II protein complex binding [GO:0023026]; MHC class II receptor activity [GO:0032395]; peptide antigen binding [GO:0042605] | PF07654;PF00969; | 2.60.40.10; | MHC class II family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22407913}; Single-pass type I membrane protein {ECO:0000269|PubMed:22407913}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:22407913}; Single-pass type I membrane protein {ECO:0000269|PubMed:22407913}. Golgi apparatus, trans-Golgi network membrane {ECO:000026... | null | null | null | null | null | FUNCTION: Binds peptides derived from antigens that access the endocytic route of antigen presenting cells (APC) and presents them on the cell surface for recognition by the CD4 T-cells. The peptide binding cleft accommodates peptides of 10-30 residues. The peptides presented by MHC class II molecules are generated mos... | Homo sapiens (Human) |
P05539 | CO2A1_RAT | MIRLGAPQSLVLLTLLIATVLQCQGQDARKLGPKGQKGEPGDIKDIIGPKGPPGPQGPAGEQGPRGDRGDKGERGAPGPRGRDGEPGTPGNPGPPGPPGPPGPPGLGGGNFAAQMAGGFDEKAGGAQMGVMQGPMGPMGPRGPPGPAGAPGPQGFQGNPGEPGEPGVSGPIGPRGPPGPAGKPGDDGEAGKPGKAGERGLPGPQGARGFPGTPGLPGVKGHRGYPGLDGAKGEAGAPGVKGESGSPGENGSPGPMGPRGLPGERGRTGPAGAAGARGNDGQPGPAGPPGPVGPAGGPGFLGAPGAKGEAGPTGARGPEGA... | null | null | anterior head development [GO:0097065]; bone development [GO:0060348]; cartilage condensation [GO:0001502]; cartilage development [GO:0051216]; cartilage development involved in endochondral bone morphogenesis [GO:0060351]; cellular response to BMP stimulus [GO:0071773]; cellular response to insulin-like growth factor ... | basement membrane [GO:0005604]; collagen trimer [GO:0005581]; collagen type II trimer [GO:0005585]; collagen-containing extracellular matrix [GO:0062023]; cytoplasm [GO:0005737]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615] | extracellular matrix structural constituent conferring tensile strength [GO:0030020]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; MHC class II protein binding [GO:0042289]; platelet-derived growth factor binding [GO:0048407]; protein homodimerization activity [GO:0042803]; proteoglycan bindi... | PF01410;PF01391; | 2.60.120.1000; | Fibrillar collagen family | PTM: Contains mostly 4-hydroxyproline. Prolines at the third position of the tripeptide repeating unit (G-X-P) are 4-hydroxylated in some or all of the chains. {ECO:0000269|PubMed:21757687}.; PTM: Contains 3-hydroxyproline at a few sites. This modification occurs on the first proline residue in the sequence motif Gly-P... | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000255|PROSITE-ProRule:PRU00793}. | null | null | null | null | null | FUNCTION: Type II collagen is specific for cartilaginous tissues. It is essential for the normal embryonic development of the skeleton, for linear growth and for the ability of cartilage to resist compressive forces. | Rattus norvegicus (Rat) |
P05540 | CD4_RAT | MCRGFSFRHLLPLLLLQLSKLLVVTQGKTVVLGKEGGSAELPCESTSRRSASFAWKSSDQKTILGYKNKLLIKGSLELYSRFDSRKNAWERGSFPLIINKLRMEDSQTYVCELENKKEEVELWVFRVTFNPGTRLLQGQSLTLILDSNPKVSDPPIECKHKSSNIVKDSKAFSTHSLRIQDSGIWNCTVTLNQKKHSFDMKLSVLGFASTSITAYKSEGESAEFSFPLNLGEESLQGELRWKAEKAPSSQSWITFSLKNQKVSVQKSTSNPKFQLSETLPLTLQIPQVSLQFAGSGNLTLTLDRGILYQEVNLVVMKVTQ... | null | null | adaptive immune response [GO:0002250]; calcium-mediated signaling [GO:0019722]; cell adhesion [GO:0007155]; cell surface receptor signaling pathway [GO:0007166]; cellular response to granulocyte macrophage colony-stimulating factor stimulus [GO:0097011]; defense response to Gram-negative bacterium [GO:0050829]; helper ... | cell surface [GO:0009986]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]; external side of plasma membrane [GO:0009897]; membrane raft [GO:0045121]; plasma membrane [GO:0005886] | coreceptor activity [GO:0015026]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; immunoglobulin binding [GO:0019865]; interleukin-16 binding [GO:0042011]; interleukin-16 receptor activity [GO:0042012]; lipid binding [GO:0008289]; MHC class II protein binding [GO:0042289]; MHC class II protein comp... | PF05790;PF09191;PF00047;PF12104; | 2.60.40.10;1.20.5.900; | null | PTM: Palmitoylation and association with LCK contribute to the enrichment of CD4 in lipid rafts. {ECO:0000250|UniProtKB:P01730}.; PTM: Phosphorylated by PKC; phosphorylation plays an important role for CD4 internalization. {ECO:0000250|UniProtKB:P01730}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P01730}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P01730}. Note=Localizes to lipid rafts. {ECO:0000250|UniProtKB:P01730}. | null | null | null | null | null | FUNCTION: Integral membrane glycoprotein that plays an essential role in the immune response and serves multiple functions in responses against both external and internal offenses. In T-cells, functions primarily as a coreceptor for MHC class II molecule:peptide complex. The antigens presented by class II peptides are ... | Rattus norvegicus (Rat) |
P05543 | THBG_HUMAN | MSPFLYLVLLVLGLHATIHCASPEGKVTACHSSQPNATLYKMSSINADFAFNLYRRFTVETPDKNIFFSPVSISAALVMLSFGACCSTQTEIVETLGFNLTDTPMVEIQHGFQHLICSLNFPKKELELQIGNALFIGKHLKPLAKFLNDVKTLYETEVFSTDFSNISAAKQEINSHVEMQTKGKVVGLIQDLKPNTIMVLVNYIHFKAQWANPFDPSKTEDSSSFLIDKTTTVQVPMMHQMEQYYHLVDMELNCTVLQMDYSKNALALFVLPKEGQMESVEAAMSSKTLKKWNRLLQKGWVDLFVPKFSISATYDLGATL... | null | null | thyroid hormone transport [GO:0070327] | extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | serine-type endopeptidase inhibitor activity [GO:0004867] | PF00079; | 2.30.39.10;3.30.497.10;2.10.310.10; | Serpin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Major thyroid hormone transport protein in serum. | Homo sapiens (Human) |
P05545 | SPA3K_RAT | MAFIAALGLLMAGICPAVLCDGILGRDTLPHEDQGKGRQLHSLTLASINTDFTLSLYKKLALRNPDKNVVFSPLSISAALAILSLGAKDSTMEEILEVLKFNLTEITEEEIHQGFGHLLQRLSQPEDQAEINTGSALFIDKEQPILSEFQEKTRALYQAEAFVADFKQCNEAKKFINDYVSNQTQGKIAELFSELDERTSMVLVNYLLFKGKWKVPFNPNDTFESEFYLDEKRSVKVPMMKIKDLTTPYIRDEELSCSVLELKYTGNASALFILPDQGKMQQVESSLQPETLKKWKDSLRPRIISELRMPKFSISTDYNL... | null | null | null | extracellular space [GO:0005615] | serine-type endopeptidase inhibitor activity [GO:0004867] | PF00079; | 2.30.39.10;3.30.497.10; | Serpin family | PTM: N-glycosylated. {ECO:0000269|PubMed:1694763, ECO:0000269|PubMed:2440672}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | null | null | null | null | null | FUNCTION: Binds to and inhibits kallikreins. Inhibits trypsin but not chymotrypsin or elastase. {ECO:0000269|PubMed:1864837, ECO:0000269|PubMed:2440672}. | Rattus norvegicus (Rat) |
P05546 | HEP2_HUMAN | MKHSLNALLIFLIITSAWGGSKGPLDQLEKGGETAQSADPQWEQLNNKNLSMPLLPADFHKENTVTNDWIPEGEEDDDYLDLEKIFSEDDDYIDIVDSLSVSPTDSDVSAGNILQLFHGKSRIQRLNILNAKFAFNLYRVLKDQVNTFDNIFIAPVGISTAMGMISLGLKGETHEQVHSILHFKDFVNASSKYEITTIHNLFRKLTHRLFRRNFGYTLRSVNDLYIQKQFPILLDFKTKVREYYFAEAQIADFSDPAFISKTNNHIMKLTKGLIKDALENIDPATQMMILNCIYFKGSWVNKFPVEMTHNHNFRLNEREV... | null | null | blood coagulation [GO:0007596]; chemotaxis [GO:0006935] | endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | endopeptidase inhibitor activity [GO:0004866]; heparin binding [GO:0008201]; serine-type endopeptidase inhibitor activity [GO:0004867] | PF00079; | 2.30.39.10;3.30.497.10; | Serpin family | PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000269|PubMed:26091039}. | null | null | null | null | null | null | FUNCTION: Thrombin inhibitor activated by the glycosaminoglycans, heparin or dermatan sulfate. In the presence of the latter, HC-II becomes the predominant thrombin inhibitor in place of antithrombin III (AT-III). Also inhibits chymotrypsin, but in a glycosaminoglycan-independent manner. {ECO:0000269|PubMed:1939083}.; ... | Homo sapiens (Human) |
P05549 | AP2A_HUMAN | MLWKLTDNIKYEDCEDRHDGTSNGTARLPQLGTVGQSPYTSAPPLSHTPNADFQPPYFPPPYQPIYPQSQDPYSHVNDPYSLNPLHAQPQPQHPGWPGQRQSQESGLLHTHRGLPHQLSGLDPRRDYRRHEDLLHGPHALSSGLGDLSIHSLPHAIEEVPHVEDPGINIPDQTVIKKGPVSLSKSNSNAVSAIPINKDNLFGGVVNPNEVFCSVPGRLSLLSSTSKYKVTVAEVQRRLSPPECLNASLLGGVLRRAKSKNGGRSLREKLDKIGLNLPAGRRKAANVTLLTSLVEGEAVHLARDFGYVCETEFPAKAVAEF... | null | null | bone morphogenesis [GO:0060349]; cellular response to iron ion [GO:0071281]; embryonic cranial skeleton morphogenesis [GO:0048701]; embryonic forelimb morphogenesis [GO:0035115]; eyelid development in camera-type eye [GO:0061029]; inner ear morphogenesis [GO:0042472]; kidney development [GO:0001822]; negative regulatio... | chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; DNA binding [GO:0003677]; 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]; iden... | PF03299; | null | AP-2 family | PTM: Sumoylated on Lys-10; which inhibits transcriptional activity. {ECO:0000305|PubMed:12072434}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12586840}. | null | null | null | null | null | FUNCTION: Sequence-specific DNA-binding protein that interacts with inducible viral and cellular enhancer elements to regulate transcription of selected genes. AP-2 factors bind to the consensus sequence 5'-GCCNNNGGC-3' and activate genes involved in a large spectrum of important biological functions including proper e... | Homo sapiens (Human) |
P05554 | CEBPA_RAT | MESADFYEAEPRPPMSSHLQSPPHAPSNAAFGFPRGAGPAPPPAPPAAPEPLGGICEHETSIDISAYIDPAAFNDEFLADLFQHSRQQEKAKAAAGPAGGGGDFDYPGAPAGPGGAVMSAGAHGPPPGYGCAAAGYLDGRLEPLYERVGAPALRPLVIKQEPREEDEAKQLALAGLFPYQPPPPPPPPHPHASPAHLAAPHLQFQIAHCGQTTMHLQPGHPTPPPTPVPSPHPAPAMGAAGLPGPGGSLKGLAGPHPDLRTGGGGGGGAGAGKAKKSVDKNSNEYRVRRERNNIAVRKSRDKAKQRNVETQQKVLELTSD... | null | null | acute-phase response [GO:0006953]; animal organ regeneration [GO:0031100]; brown fat cell differentiation [GO:0050873]; cell differentiation [GO:0030154]; cell population proliferation [GO:0008283]; cellular response to lithium ion [GO:0071285]; cellular response to organic cyclic compound [GO:0071407]; cellular respon... | C/EBP complex [GO:1990647]; CHOP-C/EBP complex [GO:0036488]; nuclear matrix [GO:0016363]; nucleolus [GO:0005730]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; Rb-E2F complex [GO:0035189]; RNA polymerase II transcription regulator complex [GO:0090575]; transcription regulator complex [GO:0005667] | chromatin binding [GO:0003682]; chromatin DNA binding [GO:0031490]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981];... | PF07716; | 1.20.5.170; | BZIP family, C/EBP subfamily | PTM: Sumoylated, sumoylation blocks the inhibitory effect on cell proliferation by disrupting the interaction with SMARCA2. {ECO:0000269|PubMed:16735515}.; PTM: Phosphorylation at Ser-193 is required for interaction with CDK2, CDK4 and SWI/SNF complex leading to cell cycle inhibition. Dephosphorylated at Ser-193 by pro... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:8367486}.; SUBCELLULAR LOCATION: [Isoform 4]: Nucleus, nucleolus {ECO:0000269|PubMed:20075868}. | null | null | null | null | null | FUNCTION: Transcription factor that coordinates proliferation arrest and the differentiation of myeloid progenitors, adipocytes, hepatocytes, and cells of the lung and the placenta (PubMed:11672531, PubMed:16735515, PubMed:20176812, PubMed:8367486). Binds directly to the consensus DNA sequence 5'-T[TG]NNGNAA[TG]-3' act... | Rattus norvegicus (Rat) |
P05555 | ITAM_MOUSE | MTLKALLVTALALCHGFNLDTEHPMTFQENAKGFGQNVVQLGGTSVVVAAPQEAKAVNQTGALYQCDYSTSRCHPIPLQVPPEAVNMSLGLSLAVSTVPQQLLACGPTVHQNCKENTYVNGLCYLFGSNLLRPPQQFPEALRECPQQESDIVFLIDGSGSINNIDFQKMKEFVSTVMEQFKKSKTLFSLMQYSDEFRIHFTFNDFKRNPSPRSHVSPIKQLNGRTKTASGIRKVVRELFHKTNGARENAAKILVVITDGEKFGDPLDYKDVIPEADRAGVIRYVIGVGNAFNKPQSRRELDTIASKPAGEHVFQVDNFEA... | null | null | activated T cell proliferation [GO:0050798]; amyloid-beta clearance [GO:0097242]; cell adhesion [GO:0007155]; cell adhesion mediated by integrin [GO:0033627]; cell-cell adhesion [GO:0098609]; cell-matrix adhesion [GO:0007160]; cellular extravasation [GO:0045123]; complement receptor mediated signaling pathway [GO:00024... | cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; integrin alphaM-beta2 complex [GO:0034688]; integrin complex [GO:0008305]; membrane [GO:0016020]; membrane raft [GO:0045121]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | cargo receptor activity [GO:0038024]; complement component C3b binding [GO:0001851]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; integrin binding [GO:0005178]; metal ion binding [GO:0046872]; opsonin binding [GO:0001846] | PF01839;PF08441;PF20805;PF00357;PF21520;PF00092; | 1.20.5.930;2.130.10.130;2.60.40.1460;2.60.40.1510;2.60.40.1530;3.40.50.410; | Integrin alpha chain family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:8986723, ECO:0000269|PubMed:9862668}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P11215}. Membrane raft {ECO:0000250|UniProtKB:P11215}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P11215}. | null | null | null | null | null | FUNCTION: Integrin ITGAM/ITGB2 is implicated in various adhesive interactions of monocytes, macrophages and granulocytes as well as in mediating the uptake of complement-coated particles and pathogens (By similarity). It is identical with CR-3, the receptor for the iC3b fragment of the third complement component. It pr... | Mus musculus (Mouse) |
P05556 | ITB1_HUMAN | MNLQPIFWIGLISSVCCVFAQTDENRCLKANAKSCGECIQAGPNCGWCTNSTFLQEGMPTSARCDDLEALKKKGCPPDDIENPRGSKDIKKNKNVTNRSKGTAEKLKPEDITQIQPQQLVLRLRSGEPQTFTLKFKRAEDYPIDLYYLMDLSYSMKDDLENVKSLGTDLMNEMRRITSDFRIGFGSFVEKTVMPYISTTPAKLRNPCTSEQNCTSPFSYKNVLSLTNKGEVFNELVGKQRISGNLDSPEGGFDAIMQVAVCGSLIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGQCHLENNMYTMSHYYDYPSIA... | null | null | axon extension [GO:0048675]; B cell differentiation [GO:0030183]; basement membrane organization [GO:0071711]; calcium-independent cell-matrix adhesion [GO:0007161]; cardiac cell fate specification [GO:0060912]; cardiac muscle cell differentiation [GO:0055007]; cardiac muscle cell myoblast differentiation [GO:0060379];... | cell surface [GO:0009986]; cerebellar climbing fiber to Purkinje cell synapse [GO:0150053]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; dendritic spine [GO:0043197]; endosome membrane [GO:0010008]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; filopodium [GO:0030175]; foca... | actin binding [GO:0003779]; C-X3-C chemokine binding [GO:0019960]; cadherin binding [GO:0045296]; calcium ion binding [GO:0005509]; cell adhesion molecule binding [GO:0050839]; collagen binding involved in cell-matrix adhesion [GO:0098639]; coreceptor activity [GO:0015026]; fibronectin binding [GO:0001968]; integrin bi... | PF07974;PF18372;PF08725;PF07965;PF00362;PF17205; | 4.10.1240.30;1.20.5.100;2.10.25.10;3.30.1680.10;2.60.40.1510;3.40.50.410; | Integrin beta chain family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17158881, ECO:0000269|PubMed:32487760, ECO:0000269|PubMed:35687021, ECO:0000303|PubMed:10455171}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, invadopodium membrane {ECO:0000269|PubMed:10455171}; Single-pass type I membrane protein {ECO:0000... | null | null | null | null | null | FUNCTION: Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-1 and alpha-11/beta-1 are receptors for collagen. Integrins alpha-1/beta-1 and alpha-2/beta-2 recognize the proline-hydroxylated sequence G-F-P-G-E-R in collagen. Integrins alpha-2/beta-1, alpha-3/beta-1, alpha-4/beta-1, alpha-5/beta-1, alpha-8/beta-1, a... | Homo sapiens (Human) |
P05618 | CDGT_BACS0 | MKRFMKLTAVWTLWLSLTLGLLSPVHAAPDTSVSNKQNFSTDVIYQIFTDRFSDGNPANNPTGAAFDGSCTNLRLYCGGDWQGIINKINDGYLTGMGITAIWISQPVENIYSVINYSGVNNTAYHGYWARDFKKTNPAYGTMQDFKNLIDTAHAHNIKVIIDFAPNHTSPASSDDPSFAENGRLYDNGNLLGGYTNDTQNLFHHYGGTDFSTIENGIYKNLYDLADLNHNNSSVDVYLKDAIKMWLDLGVDGIRVDAVKHMPFGWQKSFMATINNYKPVFTFGEWFLGVNEISPEYHQFANESGMSLLDFRFAQKARQVF... | 2.4.1.19 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 2 calcium ions per subunit.; | carbohydrate metabolic process [GO:0005975] | extracellular region [GO:0005576] | alpha-amylase activity [GO:0004556]; cyclomaltodextrin glucanotransferase activity [GO:0043895]; metal ion binding [GO:0046872]; starch binding [GO:2001070] | PF00128;PF02806;PF00686;PF01833; | 3.20.20.80;2.60.40.1180;2.60.40.10; | Glycosyl hydrolase 13 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=Cyclizes part of a (1->4)-alpha-D-glucan chain by formation of a (1->4)-alpha-D-glucosidic bond.; EC=2.4.1.19; | null | null | null | null | null | Bacillus sp. (strain 1011) |
P05620 | VSP1_PROFL | MVLIRVLANLLILQLSYAQKSSELVIGGDECNINEHPFLVALYDAWSGRFLCGGTLINPEWVLTAAHCDSKNFKMKLGAHSKKVLNEDEQIRNPKEKFICPNKKNDEVLDKDIMLIKLDSPVSYSEHIAPLSLPSSPPSVGSVCRIMGWGSITPVEETFPDVPHCANINLLDDVECKPGYPELLPEYRTLCAGVLQGGIDTCGFDSGTPLICNGQFQGIVSYGGHPCGQSRKPGIYTKVFDYNAWIQSIIAGNTAATCLP | 3.4.21.74 | null | proteolysis [GO:0006508] | extracellular space [GO:0005615] | serine-type endopeptidase activity [GO:0004252]; toxin activity [GO:0090729] | PF00089; | 2.40.10.10; | Peptidase S1 family, Snake venom subfamily | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Xaa bond in fibrinogen, to form fibrin, and release fibrinopeptide A. The specificity of further degradation of fibrinogen varies with species origin of the enzyme.; EC=3.4.21.74; | null | null | null | null | FUNCTION: Thrombin-like snake venom serine protease that clots fibrinogen (FGA) by releasing fibrinopeptide A. According to PubMed:8585090, only cleaves rabbit fibrinogen, whereas no specificity is described in PubMed:3910643 (tests done on bovine fibrinogen). Also acts as a C3 convertase that independently cleaves hum... | Protobothrops flavoviridis (Habu) (Trimeresurus flavoviridis) |
P05622 | PGFRB_MOUSE | MGLPGVIPALVLRGQLLLSVLWLLGPQTSRGLVITPPGPEFVLNISSTFVLTCSGSAPVMWEQMSQVPWQEAAMNQDGTFSSVLTLTNVTGGDTGEYFCVYNNSLGPELSERKRIYIFVPDPTMGFLPMDSEDLFIFVTDVTETTIPCRVTDPQLEVTLHEKKVDIPLHVPYDHQRGFTGTFEDKTYICKTTIGDREVDSDTYYVYSLQVSSINVSVNAVQTVVRQGESITIRCIVMGNDVVNFQWTYPRMKSGRLVEPVTDYLFGVPSRIGSILHIPTAELSDSGTYTCNVSVSVNDHGDEKAINISVIENGYVRLLET... | 2.7.10.1 | null | adrenal gland development [GO:0030325]; aorta morphogenesis [GO:0035909]; blood vessel development [GO:0001568]; cardiac myofibril assembly [GO:0055003]; cardiac vascular smooth muscle cell differentiation [GO:0060947]; cell chemotaxis [GO:0060326]; cell migration involved in coronary angiogenesis [GO:0060981]; cell mi... | apical plasma membrane [GO:0016324]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; lysosomal lumen [GO:0043202]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]; ruffle [GO:0001726] | ATP binding [GO:0005524]; kinase activity [GO:0016301]; phosphatidylinositol 3-kinase binding [GO:0043548]; platelet-derived growth factor beta-receptor activity [GO:0005019]; platelet-derived growth factor binding [GO:0048407]; platelet-derived growth factor receptor activity [GO:0005017]; protein tyrosine kinase acti... | PF00047;PF13927;PF07714; | 2.60.40.10;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, CSF-1/PDGF receptor subfamily | PTM: Autophosphorylated on tyrosine residues upon ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit. Phosphorylation at Tyr-578, and to a lesser degree, Tyr-580 is important for interaction with SRC. Phosphorylation at Tyr... | SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Cytoplasmic vesicle {ECO:0000250}. Lysosome lumen {ECO:0000250}. Note=After ligand binding, the autophosphorylated receptor is ubiquitinated and internalized, leading to its degradation. | 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: Tyrosine-protein kinase that acts as a cell-surface receptor for homodimeric PDGFB and PDGFD and for heterodimers formed by PDGFA and PDGFB, and plays an essential role in the regulation of embryonic development, cell proliferation, survival, differentiation, chemotaxis and migration. Plays an essential role ... | Mus musculus (Mouse) |
P05623 | A70A_DROME | MKTLALFLVLVCVLGLVQSWEWPWNRKPTKFPIPSPNPRDKWCRLNLGPAWGGRC | null | null | adult feeding behavior [GO:0008343]; G protein-coupled receptor signaling pathway [GO:0007186]; multi-organism reproductive process [GO:0044703]; negative regulation of female receptivity [GO:0007621]; negative regulation of female receptivity, post-mating [GO:0045434]; regulation of egg-laying behavior [GO:0046662]; r... | extracellular region [GO:0005576]; extracellular space [GO:0005615] | G protein-coupled receptor binding [GO:0001664]; hormone activity [GO:0005179] | PF08138; | null | Drosophila sex peptide family | PTM: Sperm-bound protein is cleaved to release an active C-terminal peptide. Gradual release from stored sperm may function to prolong PMR and enhance male reproductive success. {ECO:0000269|PubMed:15694303}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3135120}. | null | null | null | null | null | FUNCTION: Male seminal protein which triggers short- and long-term post-mating behavioral responses (PMR) in female Drosophila (PubMed:15694303, PubMed:19249273, PubMed:19793753, PubMed:20308537, PubMed:24089336, PubMed:3135120). Binds initially to sperm where it is later cleaved to release an active peptide within the... | Drosophila melanogaster (Fruit fly) |
P05625 | RAF1_CHICK | MEHIQGAWKTISNGFGLKDSVFDGPNCISPTIVQQFGYQRRASDDGKISDTSKTSNTIRVFLPNKQRTVVNVRNGMTLHDCLMKALKVRGLQPECCAVFRLVTEPKGKKVRLDWNTDAASLIGEELQVDFLDHVPLTTHNFARKTFLKLAFCDICQKFLLNGFRCQTCGYKFHEHCSTKVPTMCVDWSNIRQLLLFPNSNISDSGVPALPPLTMRRMRESVSRIPVSSQHRYSTPHVFTFNTSNPSSEGTLSQRQRSTSTPNVHMVSTTMPVDSRIIEDAIRNHSESASPSALSGSPNNMSPTGWSQPKTPVPAQRERAP... | 2.7.11.1 | null | MAPK cascade [GO:0000165]; phosphorylation [GO:0016310]; Ras protein signal transduction [GO:0007265] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; MAP kinase kinase kinase activity [GO:0004709]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310] | PF00130;PF00069;PF02196; | 3.30.60.20;1.10.510.10; | Protein kinase superfamily, TKL Ser/Thr protein kinase family, RAF subfamily | PTM: Phosphorylation at Ser-259 inactivates kinase activity. Dephosphorylation of Ser-259 by a complex containing protein phosphatase 1 relieves inactivation, leading to stimulate RAF1 activity (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cell membrane {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000250|UniProtKB:P04049}; Physiolo... | null | null | null | null | FUNCTION: Serine/threonine-protein kinase that acts as a regulatory link between the membrane-associated Ras GTPases and the MAPK/ERK cascade, and this critical regulatory link functions as a switch determining cell fate decisions. RAF1 activation initiates a mitogen-activated protein kinase (MAPK) cascade that compris... | Gallus gallus (Chicken) |
P05626 | ATPF_YEAST | MSMSMGVRGLALRSVSKTLFSQGVRCPSMVIGARYMSSTPEKQTDPKAKANSIINAIPGNNILTKTGVLGTSAAAVIYAISNELYVINDESILLLTFLGFTGLVAKYLAPAYKDFADARMKKVSDVLNASRNKHVEAVKDRIDSVSQLQNVAETTKVLFDVSKETVELESEAFELKQKVELAHEAKAVLDSWVRYEASLRQLEQRQLAKSVISRVQSELGNPKFQEKVLQQSISEIEQLLSKLK | null | null | protein-containing complex assembly [GO:0065003]; proton motive force-driven ATP synthesis [GO:0015986] | mitochondrial inner membrane [GO:0005743]; mitochondrial proton-transporting ATP synthase complex [GO:0005753]; mitochondrial proton-transporting ATP synthase complex, coupling factor F(o) [GO:0000276]; mitochondrial proton-transporting ATP synthase, stator stalk [GO:0000274]; mitochondrion [GO:0005739] | proton-transporting ATP synthase activity, rotational mechanism [GO:0046933] | PF05405; | 1.20.5.2210; | Eukaryotic ATPase B chain family | null | SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane. | null | null | null | null | null | FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramemb... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P05627 | JUN_MOUSE | MTAKMETTFYDDALNASFLQSESGAYGYSNPKILKQSMTLNLADPVGSLKPHLRAKNSDLLTSPDVGLLKLASPELERLIIQSSNGHITTTPTPTQFLCPKNVTDEQEGFAEGFVRALAELHSQNTLPSVTSAAQPVSGAGMVAPAVASVAGAGGGGGYSASLHSEPPVYANLSNFNPGALSSGGGAPSYGAAGLAFPSQPQQQQQPPQPPHHLPQQIPVQHPRLQALKEEPQTVPEMPGETPPLSPIDMESQERIKAERKRMRNRIAASKCRKRKLERIARLEEKVKTLKAQNSELASTANMLREQVAQLKQKVMNHVN... | null | null | angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; axon regeneration [GO:0031103]; cell population proliferation [GO:0008283]; cellular response to anisomycin [GO:0072740]; cellular response to calcium ion [GO:0071277]; cellular response to potassium ion starvation [GO:0051365]; DNA-templated transcription [GO:... | chromatin [GO:0000785]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; transcription factor AP-1 complex [GO:0035976]; transcription regulator complex [GO:0005667]; transcription repressor complex [GO:0017053] | chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; double-stranded DNA binding [GO:000... | PF00170;PF03957; | 1.20.5.170; | BZIP family, Jun subfamily | PTM: Phosphorylated by CaMK4 and PRKDC; phosphorylation enhances the transcriptional activity. Phosphorylated by HIPK3. Phosphorylated by DYRK2 at Ser-246; this primes the protein for subsequent phosphorylation by GSK3B at Thr-242. Phosphorylated at Thr-242, Ser-246 and Ser-252 by GSK3B; phosphorylation reduces its abi... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P05412}. | null | null | null | null | null | FUNCTION: Transcription factor that recognizes and binds to the AP-1 consensus motif 5'-TGA[GC]TCA-3' (PubMed:14707112). Heterodimerizes with proteins of the FOS family to form an AP-1 transcription factor complex, thereby enhancing its DNA binding activity to the AP-1 consensus sequence 5'-TGA[GC]TCA-3' and enhancing ... | Mus musculus (Mouse) |
P05630 | ATPD_BOVIN | MLPSALLRRPGLGRLVRQVRLYAEAAAAQAPAAGPGQMSFTFASPTQVFFNSANVRQVDVPTQTGAFGILAAHVPTLQVLRPGLVVVHAEDGTTSKYFVSSGSVTVNADSSVQLLAEEAVTLDMLDLGAAKANLEKAQSELLGAADEATRAEIQIRIEANEALVKALE | null | null | aerobic respiration [GO:0009060]; mitochondrial proton-transporting ATP synthase complex assembly [GO:0033615]; proton motive force-driven ATP synthesis [GO:0015986]; proton transmembrane transport [GO:1902600] | mitochondrial envelope [GO:0005740]; mitochondrial proton-transporting ATP synthase complex [GO:0005753]; mitochondrial proton-transporting ATP synthase complex, catalytic sector F(1) [GO:0000275]; proton-transporting ATP synthase complex [GO:0045259] | proton transmembrane transporter activity [GO:0015078]; proton-transporting ATP synthase activity, rotational mechanism [GO:0046933] | PF02823;PF21335; | 1.20.5.440;2.60.15.10; | ATPase epsilon chain family | null | SUBCELLULAR LOCATION: Mitochondrion. Mitochondrion inner membrane. | null | null | null | null | null | FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramemb... | Bos taurus (Bovine) |
P05637 | APAH_ECOLI | MATYLIGDVHGCYDELIALLHKVEFTPGKDTLWLTGDLVARGPGSLDVLRYVKSLGDSVRLVLGNHDLHLLAVFAGISRNKPKDRLTPLLEAPDADELLNWLRRQPLLQIDEEKKLVMAHAGITPQWDLQTAKECARDVEAVLSSDSYPFFLDAMYGDMPNNWSPELRGLGRLRFITNAFTRMRFCFPNGQLDMYSKESPEEAPAPLKPWFAIPGPVAEEYSIAFGHWASLEGKGTPEGIYALDTGCCWGGTLTCLRWEDKQYFVQPSNRHKDLGEAAAS | 3.6.1.41 | null | nucleobase-containing small molecule interconversion [GO:0015949]; response to X-ray [GO:0010165]; RNA decapping [GO:0110154] | cytoplasm [GO:0005737] | bis(5'-nucleosyl)-tetraphosphatase (symmetrical) activity [GO:0008803]; bis(5'-nucleosyl)-tetraphosphatase activity [GO:0008796]; phosphatase activity [GO:0016791] | PF00149; | 3.60.21.10; | Ap4A hydrolase family | null | null | CATALYTIC ACTIVITY: Reaction=H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP + 2 H(+); Xref=Rhea:RHEA:24252, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58141, ChEBI:CHEBI:456216; EC=3.6.1.41; Evidence={ECO:0000269|PubMed:6317672}; | null | null | null | null | FUNCTION: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield ADP. {ECO:0000269|PubMed:6317672}. | Escherichia coli (strain K12) |
P05655 | LSC_BACSU | MNIKKFAKQATVLTFTTALLAGGATQAFAKETNQKPYKETYGISHITRHDMLQIPEQQKNEKYQVPEFDSSTIKNISSAKGLDVWDSWPLQNADGTVANYHGYHIVFALAGDPKNADDTSIYMFYQKVGETSIDSWKNAGRVFKDSDKFDANDSILKDQTQEWSGSATFTSDGKIRLFYTDFSGKHYGKQTLTTAQVNVSASDSSLNINGVEDYKSIFDGDGKTYQNVQQFIDEGNYSSGDNHTLRDPHYVEDKGHKYLVFEANTGTEDGYQGEESLFNKAYYGKSTSFFRQESQKLLQSDKKRTAELANGALGMIELND... | 2.4.1.10 | null | carbohydrate utilization [GO:0009758] | extracellular region [GO:0005576] | levansucrase activity [GO:0050053]; metal ion binding [GO:0046872] | PF02435; | null | Glycosyl hydrolase 68 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=[6)-beta-D-fructofuranosyl-(2->](n) alpha-D-glucopyranoside + sucrose = [6)-beta-D-fructofuranosyl-(2->](n+1) alpha-D-glucopyranoside + D-glucose; Xref=Rhea:RHEA:13653, Rhea:RHEA-COMP:13093, Rhea:RHEA-COMP:13094, ChEBI:CHEBI:4167, ChEBI:CHEBI:17992, ChEBI:CHEBI:134464; EC=2.4.1.10; Evidence... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=8 mM for sucrose {ECO:0000269|PubMed:18596022}; KM=9 mM for sucrose {ECO:0000269|PubMed:33303628}; KM=8.3 mM for sucrose (for hydrolysis, in the absence of levan F4) {ECO:0000269|PubMed:32553967}; KM=6.9 mM for sucrose (for hydrolysis, in the presence of 5 g/L leva... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6. {ECO:0000269|PubMed:18596022}; | null | FUNCTION: Catalyzes the synthesis of levan, a fructose polymer, by transferring the fructosyl moiety from sucrose to a growing acceptor molecule (PubMed:14517548, PubMed:18596022, PubMed:32553967, PubMed:33303628, PubMed:4206083). Also displays sucrose hydrolase activity (PubMed:18596022, PubMed:32553967, PubMed:333036... | Bacillus subtilis (strain 168) |
P05656 | SACC_BACSU | MKKRLIQVMIMFTLLLTMAFSADAADSSYYDEDYRPQYHFTPEANWMNDPNGMVYYAGEYHLFYQYHPYGLQWGPMHWGHAVSKDLVTWEHLPVALYPDEKGTIFSGSAVVDKNNTSGFQTGKEKPLVAIYTQDREGHQVQSIAYSNDKGRTWTKYAGNPVIPNPGKKDFRDPKVFWYEKEKKWVMVLAAGDRILIYTSKNLKQWTYASEFGQDQGSHGGVWECPDLFELPVDGNPNQKKWVMQVSVGNGAVSGGSGMQYFVGDFDGTHFKNENPPNKVLWTDYGRDFYAAVSWSDIPSTDSRRLWLGWMSNWQYANDVP... | 3.2.1.80 | null | sucrose catabolic process [GO:0005987] | cytoplasm [GO:0005737]; extracellular region [GO:0005576] | fructan beta-fructosidase activity [GO:0051669]; sucrose alpha-glucosidase activity [GO:0004575] | PF06439;PF08244;PF00251; | null | Glycosyl hydrolase 32 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10217495}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing (2->1)- and (2->6)-linked beta-D-fructofuranose residues in fructans.; EC=3.2.1.80; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.2 uM for levan (at pH 5.5 and 55 degrees Celsius) {ECO:0000269|PubMed:7646030}; KM=6.7 mM for inulin (at pH 5.5 and 55 degrees Celsius) {ECO:0000269|PubMed:7646030}; KM=64 mM for sucrose (at pH 5.5 and 55 degrees Celsius) {ECO:0000269|PubMed:7646030}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5 for inulin hydrolysis. {ECO:0000269|PubMed:7646030}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius for inulin hydrolysis. Is rapidly inactivated at 60 degrees Celsius. High stable at 50 and 55 degrees Celsius. {ECO:0000269|PubMed:7646030}; | FUNCTION: Exo-fructosidase that can hydrolyze both levan and inulin, leading to the production of free fructose. Is also able to hydrolyze sucrose and to a small extent raffinose, but not melezitose, stachylose, cellobiose, maltose, and lactose. {ECO:0000269|PubMed:7646030}. | Bacillus subtilis (strain 168) |
P05661 | MYSA_DROME | MPKPVANQEDEDPTPYLFVSLEQRRIDQSKPYDSKKSCWIPDEKEGYLLGEIKATKGDIVSVGLQGGEVRDIKSEKVEKVNPPKFEKIEDMADMTVLNTPCVLHNLRQRYYAKLIYTYSGLFCVAINPYKRYPVYTNRCAKMYRGKRRNEVPPHIFAISDGAYVDMLTNHVNQSMLITGESGAGKTENTKKVIAYFATVGASKKTDEAAKSKGSLEDQVVQTNPVLEAFGNAKTVRNDNSSRFGKFIRIHFGPTGKLAGADIETYLLEKARVISQQSLERSYHIFYQIMSGSVPGVKDICLLTDNIYDYHIVSQGKVTVA... | null | null | adult somatic muscle development [GO:0007527]; border follicle cell migration [GO:0007298]; epithelial cell migration, open tracheal system [GO:0007427]; flight [GO:0060361]; locomotion [GO:0040011]; mitotic actomyosin contractile ring contraction [GO:1902404]; muscle cell differentiation [GO:0042692]; muscle contracti... | A band [GO:0031672]; cytoplasm [GO:0005737]; mitotic actomyosin contractile ring [GO:0110085]; myosin filament [GO:0032982]; myosin II complex [GO:0016460]; polytene chromosome puff [GO:0005703]; sarcomere [GO:0030017]; striated muscle myosin thick filament [GO:0005863] | actin filament binding [GO:0051015]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; microfilament motor activity [GO:0000146]; protein homodimerization activity [GO:0042803]; structural constituent of muscle [GO:0008307] | PF00063;PF02736;PF01576; | 1.10.10.820;1.20.5.340;1.20.5.370;1.20.5.4820;1.20.58.530;3.40.850.10;2.30.30.360;1.20.120.720; | TRAFAC class myosin-kinesin ATPase superfamily, Myosin family | null | SUBCELLULAR LOCATION: Cytoplasm, myofibril. Note=Thick filaments of the myofibrils. | null | null | null | null | null | FUNCTION: Muscle contraction. | Drosophila melanogaster (Fruit fly) |
P05674 | POLS_EEVV8 | MFPFQPMYPMQPMPYRNPFAAPRRPWFPRTDPFLAMQVQELTRSMANLTFKQRRDAPPEGPSAKKPKKEASQKQKGGGQGKKKKNQGKKKAKTGPPNPKAQNGNKKKTNKKPGKRQRMVMKLESDKTFPIMLEGKINGYACVVGGKLFRPMHVEGKIDNDVLAALKTKKASKYDLEYADVPQNMRADTFKYTHEKPQGYYSWHHGAVQYENGRFTVPKGVGAKGDSGRPILDNQGRVVAIVLGGVNEGSRTALSVVMWNEKGVTVKYTPENCEQWSLVTTMCLLANVTFPCAQPPICYDRKPAETLAMLSVNVDNPGYDE... | 3.4.21.90 | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; proteolysis [GO:0006508]; symbiont-mediated suppression of host gene expression [GO:0039657]; symbiont-mediated suppression of host toll-like receptor signaling pathway [GO:0039722]; vir... | 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]; viral envelope [GO:0019031]; 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... | Venezuelan equine encephalitis virus (strain TC-83) (VEEV) |
P05690 | VIT2_CAEEL | MRSIIIASLVALALASSPAFERTFEPKTDYHYKFDGLVLSGLPSASSELSQSRISARARIQAVDDRYIHLQLVNIRMAASHLPESEQMPSLNSMEQRELSEEYKQMLELPLRAQLRNGLISELQFDKEDAEWSKNMKRAVVNMISFNPIAPRNEIEKIESSYDKEEQSEENTSFFTNEKTLEGDCQVAYTVIREQKKTIITKSINFDKCTERSEIAYGLRYSSECPECEKDTELIRPQTVYTYVLENEELKESEVRSLYTVNVNGQEVMKTETRSKLVLEENHSIKSHIKKVNGEKESIIYSSRWEQLVEDFFKNGDKAE... | null | null | null | cytoplasmic vesicle [GO:0031410]; extracellular region [GO:0005576]; vesicle lumen [GO:0031983]; yolk granule [GO:0042718] | lipid transporter activity [GO:0005319]; nutrient reservoir activity [GO:0045735] | PF09172;PF01347;PF00094; | 2.20.80.10;1.25.10.20; | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:26671266}. | null | null | null | null | null | FUNCTION: Precursor of the egg-yolk proteins that are sources of nutrients during embryonic development (Probable). Together with other vitellogenins, may play a role in modulating life-span, acting via induction of autophagy and lysosomal lipolysis (PubMed:26671266). {ECO:0000269|PubMed:26671266, ECO:0000305}. | Caenorhabditis elegans |
P05694 | METE_YEAST | MVQSAVLGFPRIGPNRELKKATEGYWNGKITVDELFKVGKDLRTQNWKLQKEAGVDIIPSNDFSFYDQVLDLSLLFNVIPDRYTKYDLSPIDTLFAMGRGLQRKATETEKAVDVTALEMVKWFDSNYHYVRPTFSKTTQFKLNGQKPVDEFLEAKELGIHTRPVLLGPVSYLFLGKADKDSLDLEPLSLLEQLLPLYTEILSKLASAGATEVQIDEPVLVLDLPANAQAAIKKAYTYFGEQSNLPKITLATYFGTVVPNLDAIKGLPVAALHVDFVRAPEQFDEVVAAIGNKQTLSVGIVDGRNIWKNDFKKSSAIVNKA... | 2.1.1.14 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; | methionine biosynthetic process [GO:0009086]; methylation [GO:0032259] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; plasma membrane [GO:0005886] | 5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity [GO:0003871]; methionine synthase activity [GO:0008705]; zinc ion binding [GO:0008270] | PF08267;PF01717; | 3.20.20.210; | Vitamin-B12 independent methionine synthase family | null | null | CATALYTIC ACTIVITY: Reaction=5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-methionine + tetrahydropteroyltri-L-glutamate; Xref=Rhea:RHEA:21196, ChEBI:CHEBI:57844, ChEBI:CHEBI:58140, ChEBI:CHEBI:58199, ChEBI:CHEBI:58207; EC=2.1.1.14; | null | PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetE route): step 1/1. | null | null | FUNCTION: Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P05696 | KPCA_RAT | MADVYPANDSTASQDVANRFARKGALRQKNVHEVKDHKFIARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPDTDDPRSKHKFKIHTYGSPTFCDHCGSLLYGLIHQGMKCDTCDMNVHKQCVINVPSLCGMDHTEKRGRIYLKAEVTDEKLHVTVRDAKNLIPMDPNGLSDPYVKLKLIPDPKNESKQKTKTIRSTLNPQWNESFTFKLKPSDKDRRLSVEIWDWDRTTRNDFMGSLSFGVSELMKMPASGWYKLLNQEEGEYYNVPIPEGDEEGNVELRQKFEKAKLGPAGNKVISP... | 2.7.11.13 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041, ECO:0000269|PubMed:10562545, ECO:0000269|PubMed:19346474}; Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 domain. {ECO:0000269|PubMed:10562545, ECO:0000269|PubMed:19346474}; | angiogenesis [GO:0001525]; cell adhesion [GO:0007155]; cell population proliferation [GO:0008283]; cellular response to carbohydrate stimulus [GO:0071322]; central nervous system neuron axonogenesis [GO:0021955]; chondrocyte differentiation [GO:0002062]; desmosome assembly [GO:0002159]; establishment of protein localiz... | alphav-beta3 integrin-PKCalpha complex [GO:0035866]; apical part of cell [GO:0045177]; axon [GO:0030424]; calyx of Held [GO:0044305]; ciliary basal body [GO:0036064]; cone photoreceptor outer segment [GO:0120199]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; endoplasmic reticulum [GO:0005783]; i... | ATP binding [GO:0005524]; calcium,diacylglycerol-dependent serine/threonine kinase activity [GO:0004698]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; enzyme binding [GO:0019899]; histone H3T6 kinase activity [GO:0035403]; integrin binding [GO:0005178]; lipid binding [GO:0008289]; protein kin... | PF00130;PF00168;PF00069;PF00433; | 3.30.60.20;2.60.40.150;1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, PKC subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15271671}. Cell membrane {ECO:0000269|PubMed:15271671, ECO:0000269|PubMed:19346474}; Peripheral membrane protein {ECO:0000305|PubMed:15271671}. Mitochondrion membrane {ECO:0000250|UniProtKB:P17252}; Peripheral membrane protein {ECO:0000250|UniProtKB:P17252}. Nucleus {... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that is involved in positive and negative regulation of cell proliferation, apoptosis, differentiation, migration and adhesion, cardiac hypertrophy, angiogenesis, platelet function and inflammation, by directly... | Rattus norvegicus (Rat) |
P05704 | MCP3_ECOLI | MNTTPSQRLGFLHHIRLVPLFACILGGILVLFALSSALAGYFLWQADRDQRDVTAEIEIRTGLANSSDFLRSARINMIQAGAASRIAEMEAMKRNIAQAESEIKQSQQGYRAYQNRPVKTPADEALDTELNQRFQAYITGMQPMLKYAKNGMFEAIINHESEQIRPLDNAYTDILNKAVKIRSTRANQLAELAHQRTRLGGMFMIGAFVLALVMTLITFMVLRRIVIRPLQHAAQRIEKIASGDLTMNDEPAGRNEIGRLSRHLQQMQHSLGMTVGTVRQGAEEIYRGTSEISAGNADLSSRTEEQAAAIEQTAASMEQL... | null | null | chemotaxis [GO:0006935]; signal transduction [GO:0007165] | methyl accepting chemotaxis protein complex [GO:0098561]; plasma membrane [GO:0005886] | protein homodimerization activity [GO:0042803]; transmembrane signaling receptor activity [GO:0004888] | PF00672;PF00015;PF02203; | 1.20.120.30;1.10.287.950; | Methyl-accepting chemotaxis (MCP) protein family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:22380631}; Multi-pass membrane protein {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:22380631}. Note=Found predominantly at cell poles. | null | null | null | null | null | FUNCTION: Mediates taxis to the sugars ribose and galactose via an interaction with the periplasmic ribose- or galactose-binding proteins.; FUNCTION: Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside... | Escherichia coli (strain K12) |
P05708 | HXK1_RAT | MIAAQLLAYYFTELKDDQVKKIDKYLYAMRLSDEILIDILTRFKKEMKNGLSRDYNPTASVKMLPTFVRSIPDGSEKGDFIALDLGGSSFRILRVQVNHEKNQNVSMESEIYDTPENIVHGSGTQLFDHVADCLGDFMEKKKIKDKKLPVGFTFSFPCRQSKIDEAVLITWTKRFKASGVEGADVVKLLNKAIKKRGDYDANIVAVVNDTVGTMMTCGYDDQQCEVGLIIGTGTNACYMEELRHIDLVEGDEGRMCINTEWGAFGDDGSLEDIRTEFDRELDRGSLNPGKQLFEKMVSGMYMGELVRLILVKMAKEGLLF... | 2.7.1.1 | null | canonical glycolysis [GO:0061621]; carbohydrate phosphorylation [GO:0046835]; establishment of protein localization to mitochondrion [GO:0072655]; fructose 6-phosphate metabolic process [GO:0006002]; glucose 6-phosphate metabolic process [GO:0051156]; glucose metabolic process [GO:0006006]; glycolytic process [GO:00060... | caveola [GO:0005901]; cytosol [GO:0005829]; membrane raft [GO:0045121]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; protein-containing complex [GO:0032991] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; fructokinase activity [GO:0008865]; glucokinase activity [GO:0004340]; glucosamine kinase activity [GO:0047931]; glucose binding [GO:0005536]; hexokinase activity [GO:0004396]; identical protein binding [GO:0042802]; mannokinase activity [GO:0019158]; pept... | PF00349;PF03727; | 3.30.420.40;3.40.367.20; | Hexokinase family | null | SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250|UniProtKB:P19367}; Peripheral membrane protein {ECO:0000250|UniProtKB:P19367}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P19367}. Note=The mitochondrial-binding peptide (MBP) region promotes association with the mitochondrial outer membrane. Dissociates fr... | CATALYTIC ACTIVITY: Reaction=a D-hexose + ATP = a D-hexose 6-phosphate + ADP + H(+); Xref=Rhea:RHEA:22740, ChEBI:CHEBI:4194, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:229467, ChEBI:CHEBI:456216; EC=2.7.1.1; Evidence={ECO:0000269|PubMed:13211595, ECO:0000269|PubMed:3579310, ECO:0000269|PubMed:5871820}; Physiolog... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=44 uM for D-glucose {ECO:0000269|PubMed:5871820}; KM=3.1 mM for D-fructose {ECO:0000269|PubMed:5871820}; KM=0.42 mM for ATP {ECO:0000269|PubMed:5871820}; | PATHWAY: Carbohydrate metabolism; hexose metabolism. {ECO:0000305|PubMed:5871820}.; PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 1/4. {ECO:0000305|PubMed:5871820}. | null | null | FUNCTION: Catalyzes the phosphorylation of various hexoses, such as D-glucose, D-glucosamine, D-fructose, D-mannose and 2-deoxy-D-glucose, to hexose 6-phosphate (D-glucose 6-phosphate, D-glucosamine 6-phosphate, D-fructose 6-phosphate, D-mannose 6-phosphate and 2-deoxy-D-glucose 6-phosphate, respectively) (PubMed:13211... | Rattus norvegicus (Rat) |
P05709 | SIM_DROME | MTNHRRVRKDCYESRLHDIAKTCAMKEKSKNAARTRREKENTEFCELAKLLPLPAAITSQLDKASVIRLTTSYLKMRQVFPDGLGEAWGSSPAMQRGATIKELGSHLLQTLDGFIFVVAPDGKIMYISETASVHLGLSQVELTGNSIFEYIHNYDQDEMNAILSLHPHINQHPLAQTHTPIGSPNGVQHPSAYDHDRGSHTIEIEKTFFLRMKCVLAKRNAGLTTSGFKVIHCSGYLKARIYPDRGDGQGSLIQNLGLVAVGHSLPSSAITEIKLHQNMFMFRAKLDMKLIFFDARVSQLTGYEPQDLIEKTLYQYIHAA... | null | null | adult walking behavior [GO:0007628]; axonogenesis [GO:0007409]; brain development [GO:0007420]; determination of genital disc primordium [GO:0035225]; ectoderm development [GO:0007398]; locomotion [GO:0040011]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of DNA-templated transcrip... | cytoplasm [GO:0005737]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein heterodimerization activity [GO:0046982]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory reg... | PF00010;PF00989;PF08447; | 4.10.280.10;3.30.450.20; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:3345560}. | null | null | null | null | null | FUNCTION: Transcription factor that functions as a master developmental regulator controlling midline development of the ventral nerve cord (PubMed:12221007, PubMed:1760843, PubMed:9840810). Required to correctly specify the formation of the central brain complex, which controls walking behavior (PubMed:12221007, PubMe... | Drosophila melanogaster (Fruit fly) |
P05710 | PRLR_RAT | MPSALAFVLLVLNISLLKGQSPPGKPEIHKCRSPDKETFTCWWNPGTDGGLPTNYSLTYSKEGEKTTYECPDYKTSGPNSCFFSKQYTSIWKIYIITVNATNQMGSSSSDPLYVDVTYIVEPEPPRNLTLEVKQLKDKKTYLWVKWSPPTITDVKTGWFTMEYEIRLKPEEAEEWEIHFTGHQTQFKVFDLYPGQKYLVQTRCKPDHGYWSRWSQESSVEMPNDFTLKDTTVWIIVAILSAVICLIMVWAVALKGYSMMTCIFPPVPGPKIKGFDTHLLEKGKSEELLSALGCQDFPPTSDCEDLLVEFLEVDDNEDERL... | null | null | cellular response to granulocyte macrophage colony-stimulating factor stimulus [GO:0097011]; cytokine-mediated signaling pathway [GO:0019221]; lactation [GO:0007595]; mammary gland alveolus development [GO:0060749]; mammary gland epithelial cell differentiation [GO:0060644]; mammary gland epithelium development [GO:006... | cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | cytokine binding [GO:0019955]; lipid binding [GO:0008289]; metal ion binding [GO:0046872]; peptide hormone binding [GO:0017046]; prolactin receptor activity [GO:0004925]; protein kinase binding [GO:0019901] | PF09067;PF00041; | 2.60.40.10; | Type I cytokine receptor family, Type 1 subfamily | null | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: This is a receptor for the anterior pituitary hormone prolactin. | Rattus norvegicus (Rat) |
P05712 | RAB2A_RAT | MAYAYLFKYIIIGDTGVGKSCLLLQFTDKRFQPVHDLTMGVEFGARMITIDGKQIKLQIWDTAGQESFRSITRSYYRGAAGALLVYDITRRDTFNHLTTWLEDARQHSNSNMVIMLIGNKSDLESRREVKKEEGEAFAREHGLIFMETSAKTASNVEEAFINTAKEIYEKIQEGVFDINNEANGIKIGPQHAATNASHGGNQGGQQAGGGCC | 3.6.5.2 | null | Golgi organization [GO:0007030]; protein transport [GO:0015031]; Rab protein signal transduction [GO:0032482]; vesicle-mediated transport [GO:0016192] | acrosomal vesicle [GO:0001669]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; melanosome [GO:0042470]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; perinuclear region of cytop... | GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Rab family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000250|UniProtKB:P61019}; Lipid-anchor {ECO:0000250|UniProtKB:P61019}; Cytoplasmic side {ECO:0000305}. Melanosome {ECO:0000250|UniProtKB:P61019}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P61019}; Lipid-anchor {ECO:000... | 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:P53994}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|Uni... | null | null | null | null | FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes. Rabs cycle between active GTP-bound and inactive GDP-bound states. In their active state, drive transport of vesicular carriers from donor organelles to acce... | Rattus norvegicus (Rat) |
P05714 | RAB4A_RAT | MAQTAMSETYDFLFKFLVIGNAGTGKSCLLHQFIEKKFKDDSNHTIGVEFGSKIINVGGKYVKLQIWDTAGQERFRSVTRSYYRGAAGALLVYDITSRETYNALTNWLTDARMLASQNIVIILCGNKKDLDADREVTFLEASRFAQENELMFLETSALTGENVEEAFMQCARKILNKIESGELDPERMGSGIQYGDAALRQLRSPRRTQAPSAQECGC | 3.6.5.2 | null | antigen processing and presentation [GO:0019882]; protein transport [GO:0015031]; Rab protein signal transduction [GO:0032482]; regulation of endocytosis [GO:0030100]; small GTPase-mediated signal transduction [GO:0007264]; vesicle-mediated transport [GO:0016192] | cytoplasm [GO:0005737]; early endosome membrane [GO:0031901]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; insulin-responsive compartment [GO:0032593]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; postsynaptic recycling endosome [GO:0098837]; recycling endosome [GO:0055037];... | ATPase activator activity [GO:0001671]; ATPase binding [GO:0051117]; G protein activity [GO:0003925]; GDP binding [GO:0019003]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; ionotropic glutamate receptor binding [GO:0035255]; syntaxin binding [GO:0019905] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Rab family | PTM: Serotonylation of Gln-72 by TGM2 during activation and aggregation of platelets leads to constitutive activation of GTPase activity. {ECO:0000250|UniProtKB:P56371}.; PTM: Phosphorylated by CDK1 kinase during mitosis. {ECO:0000250|UniProtKB:P20338}. | SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P20338}; Peripheral membrane protein {ECO:0000250|UniProtKB:P20338}. Cytoplasm {ECO:0000250|UniProtKB:P20338}. Early endosome membrane {ECO:0000269|PubMed:20098723}; Peripheral membrane protein {ECO:0000305}. Recycling endosome membrane {ECO:0000269|PubMed:20098723}... | 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:P20338}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|Uni... | null | null | null | null | FUNCTION: Small GTPase which cycles between an active GTP-bound and an inactive GDP-bound state (By similarity). Involved in protein transport. Plays a role in vesicular traffic. Mediates VEGFR2 endosomal trafficking to enhance VEGFR2 signaling (By similarity). Acts as a regulator of platelet alpha-granule release duri... | Rattus norvegicus (Rat) |
P05725 | DNE1_CHLRE | MNTKYNKEFLLYLAGFVDGDGSIIAQIKPNQSYKFKHQLSLTFQVTQKTQRRWFLDKLVDEIGVGYVRDRGSVSDYILSEIKPLHNFLTQLQPFLKLKQKQANLVLKIIEQLPSAKESPDKFLEVCTWVDQIAALNDSKTRKTTSETVRAVLDSLSEKKKSSP | 3.1.-.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:11276249, ECO:0000269|PubMed:12758074, ECO:0000269|PubMed:15518550}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:11276249, ECO:0000269|PubMed:12758074, ECO:0000269|PubMed:15518550}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evi... | intron homing [GO:0006314] | chloroplast [GO:0009507] | endonuclease activity [GO:0004519]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872] | PF00961; | 3.10.28.10; | LAGLIDADG endonuclease family | null | SUBCELLULAR LOCATION: Plastid, chloroplast. | null | null | null | null | null | FUNCTION: Endonuclease involved in group I intron homing. Recognizes and cleaves a 19-24 bp palindromic DNA site. | Chlamydomonas reinhardtii (Chlamydomonas smithii) |
P05737 | RL7A_YEAST | MAAEKILTPESQLKKSKAQQKTAEQVAAERAARKAANKEKRAIILERNAAYQKEYETAERNIIQAKRDAKAAGSYYVEAQHKLVFVVRIKGINKIPPKPRKVLQLLRLTRINSGTFVKVTKATLELLKLIEPYVAYGYPSYSTIRQLVYKRGFGKINKQRVPLSDNAIIEANLGKYGILSIDDLIHEIITVGPHFKQANNFLWPFKLSNPSGGWGVPRKFKHFIQGGSFGNREEFINKLVKSMN | null | null | cytoplasmic translation [GO:0002181]; maturation of LSU-rRNA [GO:0000470]; maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000463]; ribosomal large subunit biogenesis [GO:0042273] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625] | RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735] | PF00327;PF08079; | 3.30.1390.20; | Universal ribosomal protein uL30 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}. | null | null | null | null | null | FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains t... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P05739 | RL6B_YEAST | MTAQQAPKWYPSEDVAAPKKTRKAVRPQKLRASLVPGTVLILLAGRFRGKRVVYLKHLEDNTLLVTGPFKVNGVPLRRVNARYVIATSTKVSVEGVNVEKFNVEYFAKEKLTKKEKKEANLFPEQQTKEIKTERVEDQKVVDKALLAEIKKTPLLKQYLSASFSLKNGDKPHLLKF | null | null | cytoplasmic translation [GO:0002181]; ribosomal large subunit assembly [GO:0000027] | cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625] | RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735] | PF01159; | 2.30.30.30; | Eukaryotic ribosomal protein eL6 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}. | null | null | null | null | null | FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains t... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P05740 | RL17A_YEAST | MARYGATSTNPAKSASARGSYLRVSFKNTRETAQAINGWELTKAQKYLEQVLDHQRAIPFRRFNSSIGRTAQGKEFGVTKARWPAKSVKFVQGLLQNAAANAEAKGLDATKLYVSHIQVNQAPKQRRRTYRAHGRINKYESSPSHIELVVTEKEEAVAKAAEKKVVRLTSRQRGRIAAQKRIAA | null | null | cleavage in ITS2 between 5.8S rRNA and LSU-rRNA of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000448]; cytoplasmic translation [GO:0002181] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; preribosome, large subunit precursor [GO:0030687] | structural constituent of ribosome [GO:0003735] | PF00237; | 3.90.470.10; | Universal ribosomal protein uL22 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}. | null | null | null | null | null | FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains t... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P05744 | RL33A_YEAST | MAESHRLYVKGKHLSYQRSKRVNNPNVSLIKIEGVATPQDAQFYLGKRIAYVYRASKEVRGSKIRVMWGKVTRTHGNSGVVRATFRNNLPAKTFGASVRIFLYPSNI | null | null | cytoplasmic translation [GO:0002181]; ribosomal large subunit biogenesis [GO:0042273] | cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625] | structural constituent of ribosome [GO:0003735] | PF01247; | 2.40.10.190; | Eukaryotic ribosomal protein eL33 family | PTM: N-terminally acetylated by acetyltransferase NatA. {ECO:0000269|PubMed:10601260}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}. | null | null | null | null | null | FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains t... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P05745 | RL36A_YEAST | MTVKTGIAIGLNKGKKVTSMTPAPKISYKKGAASNRTKFVRSLVREIAGLSPYERRLIDLIRNSGEKRARKVAKKRLGSFTRAKAKVEEMNNIIAASRRH | null | null | cytoplasmic translation [GO:0002181] | cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625] | RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735] | PF01158; | 1.10.10.1760; | Eukaryotic ribosomal protein eL36 family | PTM: N-terminally acetylated by acetyltransferase NatA. {ECO:0000269|PubMed:10601260}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}. | null | null | null | null | null | FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains t... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P05748 | RL15A_YEAST | MGAYKYLEELQRKKQSDVLRFLQRVRVWEYRQKNVIHRAARPTRPDKARRLGYKAKQGFVIYRVRVRRGNRKRPVPKGATYGKPTNQGVNELKYQRSLRATAEERVGRRAANLRVLNSYWVNQDSTYKYFEVILVDPQHKAIRRDARYNWICDPVHKHREARGLTATGKKSRGINKGHKFNNTKAGRRKTWKRQNTLSLWRYRK | null | null | cytoplasmic translation [GO:0002181] | cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625] | RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735] | PF00827; | 3.40.1120.10; | Eukaryotic ribosomal protein eL15 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}. | null | null | null | null | null | FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains t... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P05750 | RS3_YEAST | MVALISKKRKLVADGVFYAELNEFFTRELAEEGYSGVEVRVTPTKTEVIIRATRTQDVLGENGRRINELTLLVQKRFKYAPGTIVLYAERVQDRGLSAVAQAESMKFKLLNGLAIRRAAYGVVRYVMESGAKGCEVVVSGKLRAARAKAMKFADGFLIHSGQPVNDFIDTATRHVLMRQGVLGIKVKIMRDPAKSRTGPKALPDAVTIIEPKEEEPILAPSVKDYRPAEETEAQAEPVEA | null | null | cytoplasmic translation [GO:0002181]; positive regulation of apoptotic signaling pathway [GO:2001235]; ribosomal small subunit export from nucleus [GO:0000056]; ribosomal subunit export from nucleus [GO:0000054] | 90S preribosome [GO:0030686]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; nucleus [GO:0005634]; preribosome, small subunit precursor [GO:0030688] | DNA-(apurinic or apyrimidinic site) endonuclease activity [GO:0003906]; RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735] | PF07650;PF00189; | 3.30.300.20;3.30.1140.32; | Universal ribosomal protein uS3 family | PTM: Ubiquitinated at Lys-212 in response to stalled ribosomes (PubMed:28757607, PubMed:28943311, PubMed:30718516, PubMed:30893611, PubMed:31819057). Ubiquitination leads to activation of the No-Go Decay (NGD) pathway and degradation of non-functional 18S rRNA: first monoubiquitinated at Lys-212 by MAG2, followed by fo... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}. | null | null | null | null | null | FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains t... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P05755 | RS9B_YEAST | MPRAPRTYSKTYSTPKRPYESSRLDAELKLAGEFGLKNKREIYRISFQLSKIRRAARDLLTRDEKDPKRLFEGNALIRRLVRVGVLSEDKKKLDYVLALKVEDFLERRLQTQVYKLGLAKSVHHARVLITQRHIAVGKQIVNIPSFMVRLDSEKHIDFAPTSPFGGARPGRVARRNAARKAEASGEAAEEAEDEE | null | null | maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000462]; positive regulation of translational fidelity [GO:0045903]; ribosomal small subunit biogenesis [GO:0042274]; translation [GO:0006412] | 90S preribosome [GO:0030686]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; nucleolus [GO:0005730]; small-subunit processome [GO:0032040] | rRNA binding [GO:0019843]; structural constituent of ribosome [GO:0003735] | PF00163;PF01479; | 3.10.290.10; | Universal ribosomal protein uS4 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}. Nucleus, nucleolus {ECO:0000269|PubMed:15590835}. | null | null | null | null | null | FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains t... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P05756 | RS13_YEAST | MGRMHSAGKGISSSAIPYSRNAPAWFKLSSESVIEQIVKYARKGLTPSQIGVLLRDAHGVTQARVITGNKIMRILKSNGLAPEIPEDLYYLIKKAVSVRKHLERNRKDKDAKFRLILIESRIHRLARYYRTVAVLPPNWKYESATASALVN | null | null | cytoplasmic translation [GO:0002181]; maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000462] | 90S preribosome [GO:0030686]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; nucleolus [GO:0005730] | small ribosomal subunit rRNA binding [GO:0070181]; structural constituent of ribosome [GO:0003735] | PF08069;PF00312; | 4.10.860.130;1.10.287.10; | Universal ribosomal protein uS15 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22096102}. | null | null | null | null | null | FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains t... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P05759 | RS31_YEAST | MQIFVKTLTGKTITLEVESSDTIDNVKSKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGGKKRKKKVYTTPKKIKHKHKKVKLAVLSYYKVDAEGKVTKLRRECSNPTCGAGVFLANHKDRLYCGKCHSVYKVNA | null | null | cytoplasmic translation [GO:0002181]; maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, LSU-rRNA,5S) [GO:0002109]; modification-dependent protein catabolic process [GO:0019941]; protein ubiquitination [GO:0016567]; ribosomal small subunit assembly [GO:0000028]; ribosome biogenesis [GO:0042254] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; nucleus [GO:0005634] | metal ion binding [GO:0046872]; protein tag activity [GO:0031386]; structural constituent of ribosome [GO:0003735]; ubiquitin protein ligase binding [GO:0031625] | PF01599;PF00240; | 6.20.50.150; | Ubiquitin family; Eukaryotic ribosomal protein eS31 family | null | SUBCELLULAR LOCATION: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.; SUBCELLULAR LOCATION: [Small ribosomal subunit protein eS31]: Cytoplasm {ECO:0000269|PubMed:22096102}. | null | null | null | null | null | FUNCTION: [Ubiquitin]: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polyme... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P05764 | RS21_SCHPO | MENEAGQLVDLYVPRKCSATNRIIQAKDHASVQINVCAVDAEGRQIPGEKTTYAISGFVRSKGESDDCINRLTTQDGLLEGVWSYQR | null | null | cytoplasmic translational elongation [GO:0002182]; endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000447]; endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:000... | cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627]; nucleus [GO:0005634] | structural constituent of ribosome [GO:0003735] | PF01249; | 3.30.1230.20; | Eukaryotic ribosomal protein eS21 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14623272, ECO:0000269|PubMed:16823372}. Nucleus {ECO:0000269|PubMed:16823372}. | null | null | null | null | null | FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains t... | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
P05769 | POLG_MVEV5 | MSKKPGGPGKPRVVNMLKRGIPRVFPLVGVKRVVMNLLDGRGPIRFVLALLAFFRFTALAPTKALMRRWKSVNKTTAMKHLTSFKKELGTLIDVVNKRGKKQKKRGGSETSVLMLIFMLIGFAAALKLSTFQGKIMMTVNATDIADVIAIPTPKGPNQCWIRAIDIGFMCDDTITYECPKLESGNDPEDIDCWCDKQAVYVNYGRCTRARHSKRSRRSITVQTHGESTLVNKKDAWLDSTKATRYLTKTENWIIRNPGYALVAVVLGWMLGSNTGQKVIFTVLLLLVAPAYSFNCLGMSSRDFIEGASGATWVDLVLEGD... | 2.1.1.56; 2.1.1.57; 2.7.7.48; 3.4.21.91; 3.6.1.15; 3.6.4.13 | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; induction by virus of host autophagy [GO:0039520]; proteolysis [GO:0006508]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity [GO:0039563]; symbion... | extracellular region [GO:0005576]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleus [GO:0042025]; host cell perinuclear region of cytoplasm [GO:0044220]; membrane [GO:0016020]; viral capsid [GO:0019028]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; double-stranded RNA binding [GO:0003725]; metal ion binding [GO:0046872]; mRNA (nucleoside-2'-O-)-methyltransferase activity [GO:0004483]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; protein dimerization activity [GO:0046983]; RNA he... | PF20907;PF01003;PF07652;PF21659;PF02832;PF00869;PF01004;PF00948;PF01005;PF01002;PF01350;PF01349;PF00972;PF20483;PF01570;PF01728;PF00949; | 1.10.10.930;1.10.260.90;1.20.1280.260;2.40.10.120;2.60.40.350;1.10.8.970;2.60.260.50;3.30.70.2840;3.40.50.300;2.60.98.10;3.40.50.150;3.30.67.10;3.30.387.10; | Class I-like SAM-binding methyltransferase superfamily, mRNA cap 0-1 NS5-type methyltransferase family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo yield mature proteins. Cleavages in the lumen of endoplasmic reticulum are performed by host signal peptidase, whereas cleavages in the cytoplasmic side are performed by serine protease NS3. Signal cleavage at the 2K-4B site requires a prior NS3 protease-m... | SUBCELLULAR LOCATION: [Capsid protein C]: Virion {ECO:0000250|UniProtKB:P17763}. Host nucleus {ECO:0000250|UniProtKB:P17763}. Host cytoplasm {ECO:0000250|UniProtKB:P06935}. Host cytoplasm, host perinuclear region {ECO:0000250|UniProtKB:P06935}.; SUBCELLULAR LOCATION: [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763... | CATALYTIC ACTIVITY: Reaction=Selective hydrolysis of -Xaa-Xaa-|-Yaa- bonds in which each of the Xaa can be either Arg or Lys and Yaa can be either Ser or Ala.; EC=3.4.21.91; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:... | null | null | null | null | FUNCTION: [Capsid protein C]: Plays a role in virus budding by binding to the cell membrane and gathering the viral RNA into a nucleocapsid that forms the core of a mature virus particle. During virus entry, may induce genome penetration into the host cytoplasm after hemifusion induced by the surface proteins. Can migr... | Murray valley encephalitis virus (strain MVE-1-51) (MVEV) |
P05770 | APOE_PAPAN | MKVLWAALLVTFLAGCQAKVEQPVEPETEPELRQQAEWQSGQPWELALGRFWDYLRWVQTLSEQVQEELLSPQVTQELTTLMDETMKELKAYKSELEEQLSPVAEETRARLSKELQAAQARLGADMEDVRSRLVQYRSEVQAMLGQSTEELRARLASHLRKLRKRLLRDADDLQKRLAVYQAGAREGAERGVSAIRERLGPLVEQGRVRAATVGSLASQPLQERAQALGERLRARMEEMGSRTRDRLDEVKEQVAEVRAKLEEQAQQISLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKVQAAVGASTAPVPSDNH | null | null | cholesterol catabolic process [GO:0006707]; cholesterol efflux [GO:0033344]; chylomicron remnant clearance [GO:0034382]; high-density lipoprotein particle assembly [GO:0034380]; intermediate-density lipoprotein particle clearance [GO:0071831]; lipoprotein biosynthetic process [GO:0042158]; lipoprotein catabolic process... | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; low-density lipoprotein particle [GO:0034362]; multivesicular body, internal vesicle ... | amyloid-beta binding [GO:0001540]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; low-density lipoprotein particle receptor binding [GO:0050750]; very-low-density lipoprotein particle receptor binding [GO:0070326] | PF01442; | 1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. {ECO:0000250|UniProtKB:P02649}.; PTM: Glycated in plasma VLDL. {ECO:0000250|UniProtKB:P02649}.; PTM: Phosphorylated by FAM20C in the extracellular ... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02649}. Extracellular vesicle {ECO:0000250|UniProtKB:P02649}. Endosome, multivesicular body {ECO:0000250|UniProtKB:P026... | null | null | null | null | null | FUNCTION: APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apolipoprot... | Papio anubis (Olive baboon) |
P05771 | KPCB_HUMAN | MADPAAGPPPSEGEESTVRFARKGALRQKNVHEVKNHKFTARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPASDDPRSKHKFKIHTYSSPTFCDHCGSLLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIQAHIDRDVLIVLVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLSFGISELQKASVDGWFKLLSQEEGEYFNVPVPPEGSEANEELRQKFERAKISQGTKVPEEK... | 2.7.11.13 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041}; Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 domain. {ECO:0000250|UniProtKB:P68403}; | adaptive immune response [GO:0002250]; apoptotic process [GO:0006915]; B cell activation [GO:0042113]; B cell receptor signaling pathway [GO:0050853]; calcium ion transport [GO:0006816]; cellular response to carbohydrate stimulus [GO:0071322]; dibenzo-p-dioxin metabolic process [GO:0018894]; intracellular calcium ion h... | brush border membrane [GO:0031526]; calyx of Held [GO:0044305]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; presynaptic cytosol [GO:0099523]; spectrin [GO:0008091] | ATP binding [GO:0005524]; calcium channel regulator activity [GO:0005246]; chromatin binding [GO:0003682]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; histone binding [GO:0042393]; histone H3T6 kinase activity [GO:0035403]; nuclear androgen receptor binding [GO:0050681]; nuclear receptor coa... | PF00130;PF00168;PF00069;PF00433; | 3.30.60.20;2.60.40.150;1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, PKC subfamily | PTM: Phosphorylation on Thr-500 within the activation loop renders it competent to autophosphorylate. Subsequent autophosphorylation of Thr-642 maintains catalytic competence, and autophosphorylation on Ser-661 appears to release the kinase into the cytosol. Autophosphorylation on other sites i.e. in the N-terminal and... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000269|PubMed:20228790}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13; Evidence={ECO:0000269|PubMed:20228790, ECO:00002... | null | null | null | null | FUNCTION: Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase involved in various cellular processes such as regulation of the B-cell receptor (BCR) signalosome, oxidative stress-induced apoptosis, androgen receptor-dependent transcription regulation, insulin signaling an... | Homo sapiens (Human) |
P05772 | KPCB_RABIT | MADPAAGQPPSEGEESTVRFARKGALRQKNVHEVKNHKFTARFFKQPTFCSHCTDFIWGFGKQGFQCQVCCFVVHKRCHEFVTFSCPGADKGPASDDPRSKHKFKIHTYSSPTFCDHCGSLLYGLIHQGMKCDTCMMNVHKRCVMNVPSLCGTDHTERRGRIYIQAHIDREVLIVVVRDAKNLVPMDPNGLSDPYVKLKLIPDPKSESKQKTKTIKCSLNPEWNETFRFQLKESDKDRRLSVEIWDWDLTSRNDFMGSLSFGISELQKAGVDGWFKLLSQEEGEYFNVPVPPEGSEGNEELRQKFERAKIGQGTKTPEEK... | 2.7.11.13 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041}; Note=Binds 3 Ca(2+) ions per subunit. The ions are bound to the C2 domain. {ECO:0000250|UniProtKB:P68403}; | adaptive immune response [GO:0002250]; apoptotic process [GO:0006915]; B cell activation [GO:0042113]; B cell receptor signaling pathway [GO:0050853]; intracellular signal transduction [GO:0035556]; negative regulation of glucose transmembrane transport [GO:0010829]; negative regulation of insulin receptor signaling pa... | cytoplasm [GO:0005737]; membrane [GO:0016020]; nucleus [GO:0005634] | ATP binding [GO:0005524]; chromatin binding [GO:0003682]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; histone binding [GO:0042393]; histone H3T6 kinase activity [GO:0035403]; nuclear androgen receptor binding [GO:0050681]; nuclear receptor coactivator activity [GO:0030374]; protein serine ki... | PF00130;PF00168;PF00069;PF00433; | 3.30.60.20;2.60.40.150;1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, PKC subfamily | PTM: Phosphorylation on 'Thr-499' of isoform beta-I, within the activation loop, renders it competent to autophosphorylate. Subsequent autophosphorylation of Thr-642 maintains catalytic competence, and autophosphorylation on Ser-661 appears to release the kinase into the cytosol. Similarly, isoform beta-II is autophosp... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: Calcium-activated, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase involved in various cellular processes such as regulation of the B-cell receptor (BCR) signalosome, oxidative stress-induced apoptosis, androgen receptor-dependent transcription regulation, insulin signaling an... | Oryctolagus cuniculus (Rabbit) |
P05777 | M1_I33A0 | MSLLTEVETYVLSIVPSGPLKAEIAQRLEDVFAGKNTDLEVLMEWLKTRPILSPLTKGILGFVFTLTVPSERGLQRRRFVQNALNGNGDPNNMDKAVKLYRKLKREITFHGAKEIALSYSAGALASCMGLIYNRMGAVTTEVAFGLVCATCEQIADSQHRSHRQMVTTTNPLIRHENRMVLASTTAKAMEQMAGSSEQAAEAMDIASQARQMVQAMRTIGTHPSSSAGLKDDLLENLQAYQKRMGVQMQRFK | null | null | viral budding from plasma membrane [GO:0046761] | host cell nucleus [GO:0042025]; membrane [GO:0016020]; virion membrane [GO:0055036] | RNA binding [GO:0003723]; structural constituent of virion [GO:0039660] | PF00598;PF08289; | 1.10.10.180;1.20.91.10; | Influenza viruses Matrix protein M1 family | null | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04068}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_04068}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_04068}. Host nucleus {ECO:0000255|HAMAP-Rule:MF_04068}. | null | null | null | null | null | FUNCTION: Plays critical roles in virus replication, from virus entry and uncoating to assembly and budding of the virus particle. M1 binding to ribonucleocapsids (RNPs) in nucleus seems to inhibit viral transcription. Interaction of viral NEP with M1-RNP is thought to promote nuclear export of the complex, which is ta... | Influenza A virus (strain A/Wilson-Smith/1933 H1N1) (Influenza A virus (strain A/WS/1933 H1N1)) |
P05779 | M2_I30A0 | MSLPTEVETPTRNEWGCRCNDSSDHITIAAKFIGILHLILWILDRLFFKCIYRRLKYGPKRGPSTEGVPDSMREEYRQKQQNAADVDDGHFVNIELE | null | null | protein complex oligomerization [GO:0051259]; suppression by virus of host autophagy [GO:0039521] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion membrane [GO:0055036] | monoatomic ion channel activity [GO:0005216]; proton transmembrane transporter activity [GO:0015078] | PF00599; | 6.10.250.1640; | Influenza viruses matrix protein M2 family | null | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04069}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04069}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04069}. Note=Abundantly expressed at the apical plasma membrane in infected polarized epithelial cells, in close proximit... | null | null | null | null | null | FUNCTION: Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is... | Influenza A virus (strain A/Swine/Iowa/15/1930 H1N1) |
P05780 | M2_I33A0 | MSLLTEVETPIRNEWGCRCNDSSDPLVIAANIIGILHLILWILDRLFFKCIYRRFKYGLKRGPSTEGVPESMREEYRKEQQNAVDVDDGHFVNIELE | null | null | protein complex oligomerization [GO:0051259]; suppression by virus of host autophagy [GO:0039521] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion membrane [GO:0055036] | monoatomic ion channel activity [GO:0005216]; proton transmembrane transporter activity [GO:0015078] | PF00599; | 6.10.250.1640; | Influenza viruses matrix protein M2 family | null | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04069, ECO:0000269|PubMed:1501289}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04069, ECO:0000269|PubMed:1501289}; Single-pass type III membrane protein {ECO:0000255|HAMAP-Rule:MF_04069, ECO:0000269|PubMed:1501289}. Note=Abundantly expressed at ... | null | null | null | null | null | FUNCTION: Forms a proton-selective ion channel that is necessary for the efficient release of the viral genome during virus entry. After attaching to the cell surface, the virion enters the cell by endocytosis. Acidification of the endosome triggers M2 ion channel activity. The influx of protons into virion interior is... | Influenza A virus (strain A/Wilson-Smith/1933 H1N1) (Influenza A virus (strain A/WS/1933 H1N1)) |
P05783 | K1C18_HUMAN | MSFTTRSTFSTNYRSLGSVQAPSYGARPVSSAASVYAGAGGSGSRISVSRSTSFRGGMGSGGLATGIAGGLAGMGGIQNEKETMQSLNDRLASYLDRVRSLETENRRLESKIREHLEKKGPQVRDWSHYFKIIEDLRAQIFANTVDNARIVLQIDNARLAADDFRVKYETELAMRQSVENDIHGLRKVIDDTNITRLQLETEIEALKEELLFMKKNHEEEVKGLQAQIASSGLTVEVDAPKSQDLAKIMADIRAQYDELARKNREELDKYWSQQIEESTTVVTTQSAEVGAAETTLTELRRTVQSLEIDLDSMRNLKASL... | null | null | anatomical structure morphogenesis [GO:0009653]; cell cycle [GO:0007049]; extrinsic apoptotic signaling pathway [GO:0097191]; Golgi to plasma membrane protein transport [GO:0043001]; hepatocyte apoptotic process [GO:0097284]; intermediate filament cytoskeleton organization [GO:0045104]; negative regulation of apoptotic... | adherens junction [GO:0005912]; cell periphery [GO:0071944]; centriolar satellite [GO:0034451]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; intermediate filament [GO:0005882]; keratin filament [GO:0045095]; microtubule organizing center [GO:0005815]; nucl... | cadherin binding involved in cell-cell adhesion [GO:0098641]; RNA binding [GO:0003723]; scaffold protein binding [GO:0097110]; structural molecule activity [GO:0005198] | PF00038; | 1.20.5.170;1.20.5.500;1.20.5.1160; | Intermediate filament family | PTM: Phosphorylation at Ser-34 increases during mitosis. Hyperphosphorylated at Ser-53 in diseased cirrhosis liver. Phosphorylation increases by IL-6. {ECO:0000269|PubMed:15368451, ECO:0000269|PubMed:16424149, ECO:0000269|PubMed:17213200, ECO:0000269|PubMed:7523419, ECO:0000269|PubMed:8609167, ECO:0000269|PubMed:952411... | SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250|UniProtKB:Q5BJY9}. Cytoplasm, perinuclear region. Nucleus, nucleolus {ECO:0000269|PubMed:22002106}. Cytoplasm {ECO:0000250|UniProtKB:Q5BJY9}. | null | null | null | null | null | FUNCTION: Involved in the uptake of thrombin-antithrombin complexes by hepatic cells (By similarity). When phosphorylated, plays a role in filament reorganization. Involved in the delivery of mutated CFTR to the plasma membrane. Together with KRT8, is involved in interleukin-6 (IL-6)-mediated barrier protection. {ECO:0... | Homo sapiens (Human) |
P05784 | K1C18_MOUSE | MSFTTRSTTFSTNYRSLGSVRTPSQRVRPASSAASVYAGAGGSGSRISVSRSVWGGSVGSAGLAGMGGIQTEKETMQDLNDRLASYLDKVKSLETENRRLESKIREHLEKKGPQGVRDWGHYFKIIEDLRAQIFANSVDNARIVLQIDNARLAADDFRVKYETELAMRQSVESDIHGLRKVVDDTNITRLQLETEIEALKEELLFMKKNHEEEVQGLEAQIASSGLTVEVDAPKSQDLSKIMADIRAQYEALAQKNREELDKYWSQQIEESTTVVTTKSAEIRDAETTLTELRRTLQTLEIDLDSMKNQNINLENSLGDV... | null | null | extrinsic apoptotic signaling pathway [GO:0097191]; Golgi to plasma membrane protein transport [GO:0043001]; hepatocyte apoptotic process [GO:0097284]; intermediate filament cytoskeleton organization [GO:0045104]; negative regulation of apoptotic process [GO:0043066]; tumor necrosis factor-mediated signaling pathway [G... | cell periphery [GO:0071944]; centriolar satellite [GO:0034451]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; intermediate filament [GO:0005882]; keratin filament [GO:0045095]; nuclear matrix [GO:0016363]; nucleolus [GO:0005730]; perinu... | scaffold protein binding [GO:0097110]; structural molecule activity [GO:0005198] | PF00038; | 1.20.5.170;1.20.5.500;1.20.5.1160; | Intermediate filament family | PTM: Phosphorylation increases by IL-6. {ECO:0000269|PubMed:17213200, ECO:0000269|PubMed:20724476}.; PTM: Proteolytically cleaved by caspases during epithelial cell apoptosis. Cleavage occurs at Asp-231 by either caspase-3, caspas-6 or caspase-7. {ECO:0000269|PubMed:9298992}.; PTM: O-GlcNAcylation increases solubility,... | SUBCELLULAR LOCATION: Nucleus matrix {ECO:0000250|UniProtKB:Q5BJY9}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P05783}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P05783}. Cytoplasm {ECO:0000250|UniProtKB:Q5BJY9}. | null | null | null | null | null | FUNCTION: When phosphorylated, plays a role in filament reorganization. Involved in the delivery of mutated CFTR to the plasma membrane. Involved in the uptake of thrombin-antithrombin complexes by hepatic cells (By similarity). Together with KRT8, is involved in interleukin-6 (IL-6)-mediated barrier protection. {ECO:0... | Mus musculus (Mouse) |
P05786 | K2C8_BOVIN | MSIRVTQKSYKVSTSAPRSFSSRSYTSGPGSRISSSAFSRVGSSSSFRGGLGTGMSMAGSYGGAPGLGGITAVTVNQSLLSPLKLEVDPNIQAVRTQEKEQIKTLNNKFASFIDKVRHLEQQNKVLETKWNLLQQQKTARSNIDNMFESYINNLRRQLETLAQEKLKLEVELGNMQGLVEDFKTKYEDEIQKRTDMENEFVIIKKDVDEAYMNKVELESRLEGLTDEINFYRQLYEEEIREMQSQISDTSVVLEMDNNRNLDLDGIIAEVKAQYEEIANRSRAEAEAMYQIKYEELQTLAGKHGDDLRRTKTEISEMNRN... | null | null | intermediate filament organization [GO:0045109]; keratinization [GO:0031424] | cytoplasm [GO:0005737]; extracellular space [GO:0005615]; keratin filament [GO:0045095]; nuclear matrix [GO:0016363]; nucleoplasm [GO:0005654] | 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: O-glycosylated. O-GlcNAcylation at multiple sites increases solubility, and decreases stability by inducing proteasomal degradation (By similarity). {ECO:0000250}.; PTM: O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q10758}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q10758}. Nucleus matrix {ECO:0000250|UniProtKB:Q10758}. | null | null | null | null | null | FUNCTION: Together with KRT19, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle. {ECO:0000250}. | Bos taurus (Bovine) |
P05787 | K2C8_HUMAN | MSIRVTQKSYKVSTSGPRAFSSRSYTSGPGSRISSSSFSRVGSSNFRGGLGGGYGGASGMGGITAVTVNQSLLSPLVLEVDPNIQAVRTQEKEQIKTLNNKFASFIDKVRFLEQQNKMLETKWSLLQQQKTARSNMDNMFESYINNLRRQLETLGQEKLKLEAELGNMQGLVEDFKNKYEDEINKRTEMENEFVLIKKDVDEAYMNKVELESRLEGLTDEINFLRQLYEEEIRELQSQISDTSVVLSMDNSRSLDMDSIIAEVKAQYEDIANRSRAEAESMYQIKYEELQSLAGKHGDDLRRTKTEISEMNRNISRLQAE... | null | null | cell differentiation involved in embryonic placenta development [GO:0060706]; extrinsic apoptotic signaling pathway [GO:0097191]; hepatocyte apoptotic process [GO:0097284]; intermediate filament organization [GO:0045109]; keratinization [GO:0031424]; response to hydrostatic pressure [GO:0051599]; response to other orga... | apicolateral plasma membrane [GO:0016327]; cell-cell junction [GO:0005911]; costamere [GO:0043034]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dystrophin-associated glycoprotein complex [GO:0016010]; extracellular exosome [GO:0070062]; intermediate filament [GO:0005882]; intermediate filament cytoskeleton [GO:004511... | protein-containing complex binding [GO:0044877]; scaffold protein binding [GO:0097110]; 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: Phosphorylation on serine residues is enhanced during EGF stimulation and mitosis. Ser-74 phosphorylation plays an important role in keratin filament reorganization. {ECO:0000269|PubMed:11781324, ECO:0000269|PubMed:11788583, ECO:0000269|PubMed:1374067, ECO:0000269|PubMed:9054461}.; PTM: O-glycosylated. O-GlcNAcyla... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:10973561, ECO:0000269|PubMed:19188445}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:Q10758}. Nucleus matrix {ECO:0000250|UniProtKB:Q10758}. | null | null | null | null | null | FUNCTION: Together with KRT19, helps to link the contractile apparatus to dystrophin at the costameres of striated muscle. {ECO:0000269|PubMed:16000376}. | Homo sapiens (Human) |
P05791 | ILVD_ECOLI | MPKYRSATTTHGRNMAGARALWRATGMTDADFGKPIIAVVNSFTQFVPGHVHLRDLGKLVAEQIEAAGGVAKEFNTIAVDDGIAMGHGGMLYSLPSRELIADSVEYMVNAHCADAMVCISNCDKITPGMLMASLRLNIPVIFVSGGPMEAGKTKLSDQIIKLDLVDAMIQGADPKVSDSQSDQVERSACPTCGSCSGMFTANSMNCLTEALGLSQPGNGSLLATHADRKQLFLNAGKRIVELTKRYYEQNDESALPRNIASKAAFENAMTLDIAMGGSTNTVLHLLAAAQEAEIDFTMSDIDKLSRKVPQLCKVAPSTQK... | 4.2.1.9 | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000255|HAMAP-Rule:MF_00012}; Note=Binds 1 [2Fe-2S] cluster per subunit. This cluster acts as a Lewis acid cofactor. {ECO:0000255|HAMAP-Rule:MF_00012}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00012}; | amino acid biosynthetic process [GO:0008652]; isoleucine biosynthetic process [GO:0009097]; valine biosynthetic process [GO:0009099] | cytosol [GO:0005829] | 2 iron, 2 sulfur cluster binding [GO:0051537]; 4 iron, 4 sulfur cluster binding [GO:0051539]; dihydroxy-acid dehydratase activity [GO:0004160]; hydro-lyase activity [GO:0016836]; iron-sulfur cluster binding [GO:0051536]; magnesium ion binding [GO:0000287] | PF00920; | 3.50.30.80; | IlvD/Edd family | null | null | CATALYTIC ACTIVITY: Reaction=(2R)-2,3-dihydroxy-3-methylbutanoate = 3-methyl-2-oxobutanoate + H2O; Xref=Rhea:RHEA:24809, ChEBI:CHEBI:11851, ChEBI:CHEBI:15377, ChEBI:CHEBI:49072; EC=4.2.1.9; Evidence={ECO:0000269|PubMed:13727223, ECO:0000269|PubMed:7771772, ECO:0000269|PubMed:8325851}; PhysiologicalDirection=left-to-rig... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.5 mM for racemic 2,3-dihydroxy-3-methylbutanoate {ECO:0000269|PubMed:8325851}; KM=0.75 mM for (2R)-2,3-dihydroxy-3-methylbutanoate {ECO:0000269|PubMed:8325851}; Note=Since only one of the isomers present in the racemic substrate is active, the corrected Km would ... | PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 3/4. {ECO:0000255|HAMAP-Rule:MF_00012, ECO:0000269|PubMed:3550695}.; PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 3/4. {ECO:0000255|HAMAP-Rule:MF_00012, ECO:0000269|PubMed:3550695... | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.8-7.9. {ECO:0000269|PubMed:13727223}; | null | FUNCTION: Functions in the biosynthesis of branched-chain amino acids. Catalyzes the dehydration of (2R,3R)-2,3-dihydroxy-3-methylpentanoate (2,3-dihydroxy-3-methylvalerate) into 2-oxo-3-methylpentanoate (2-oxo-3-methylvalerate) and of (2R)-2,3-dihydroxy-3-methylbutanoate (2,3-dihydroxyisovalerate) into 2-oxo-3-methylb... | Escherichia coli (strain K12) |
P05793 | ILVC_ECOLI | MANYFNTLNLRQQLAQLGKCRFMGRDEFADGASYLQGKKVVIVGCGAQGLNQGLNMRDSGLDISYALRKEAIAEKRASWRKATENGFKVGTYEELIPQADLVINLTPDKQHSDVVRTVQPLMKDGAALGYSHGFNIVEVGEQIRKDITVVMVAPKCPGTEVREEYKRGFGVPTLIAVHPENDPKGEGMAIAKAWAAATGGHRAGVLESSFVAEVKSDLMGEQTILCGMLQAGSLLCFDKLVEEGTDPAYAEKLIQFGWETITEALKQGGITLMMDRLSNPAKLRAYALSEQLKEIMAPLFQKHMDDIISGEFSSGMMADW... | 1.1.1.86 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:15654896, ECO:0000269|PubMed:23036858, ECO:0000269|PubMed:2653423}; Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:23036858, ECO:0000269|PubMed:2653423}; | amino acid biosynthetic process [GO:0008652]; isoleucine biosynthetic process [GO:0009097]; pantothenate biosynthetic process [GO:0015940]; valine biosynthetic process [GO:0009099] | cytosol [GO:0005829]; protein-containing complex [GO:0032991] | 2-dehydropantoate 2-reductase activity [GO:0008677]; identical protein binding [GO:0042802]; ketol-acid reductoisomerase activity [GO:0004455]; magnesium ion binding [GO:0000287]; NADP binding [GO:0050661] | PF01450;PF07991; | 3.40.50.720; | Ketol-acid reductoisomerase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:2653423}. | CATALYTIC ACTIVITY: Reaction=(2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-acetolactate + H(+) + NADPH; Xref=Rhea:RHEA:22068, ChEBI:CHEBI:15378, ChEBI:CHEBI:49072, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChEBI:CHEBI:58476; EC=1.1.1.86; Evidence={ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000269|PubMed:15654896, ECO:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.04 mM for NADPH {ECO:0000269|PubMed:21515217}; KM=0.042 mM for NADP {ECO:0000269|PubMed:9015391}; KM=0.073 mM for NADPH {ECO:0000269|PubMed:9015391}; KM=0.17 mM for 2-ketopantoate (at pH 8 and 37 degrees Celsius) {ECO:0000269|PubMed:15654896}; KM=0.206 mM for NAD... | PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 2/4. {ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000305|PubMed:2653423}.; PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 2/4. {ECO:0000255|HAMAP-Rule:MF_00435, ECO:0000305|PubMed:2653423... | null | null | FUNCTION: Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methy... | Escherichia coli (strain K12) |
P05803 | NRAM_I84A1 | MNPNQKILCTSATALVIGTIAVLIGIVNLGLNIGLHLKPSCNCSRSQPEATNASQTIINNYYNETNITQISNTNIQVEERASREFNNLTKGLCTINSWHIYGKDNAVRIGEDSDVLVTREPYVSCDPDECRFYALSQGTTIRGKHSNGTIHDRSQYRDLISWPLSSPPTVYNSRVECIGWSSTSCHDGRARMSICISGPNNNASAVIWYNRRPVTEINTWARNILRTQESECVCQNGVCPVVFTDGSATGPAETRIYYFKEGKILKWEPLTGTAKHIEECSCYGEQAGVTCTCRDNWQGSNRPVIQIDPVAMTHTSQYIC... | 3.2.1.18 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|HAMAP-Rule:MF_04071}; Note=Binds 1 Ca(2+) ion per subunit.; | carbohydrate metabolic process [GO:0005975]; viral budding from plasma membrane [GO:0046761] | host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; virion membrane [GO:0055036] | exo-alpha-(2->3)-sialidase activity [GO:0052794]; exo-alpha-(2->6)-sialidase activity [GO:0052795]; exo-alpha-(2->8)-sialidase activity [GO:0052796]; metal ion binding [GO:0046872] | PF00064; | 2.120.10.10; | Glycosyl hydrolase 34 family | PTM: N-glycosylated. {ECO:0000255|HAMAP-Rule:MF_04071, ECO:0000269|PubMed:7517697, ECO:0000269|PubMed:7994573}. | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04071}. Host apical cell membrane {ECO:0000255|HAMAP-Rule:MF_04071}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04071}. Note=Preferentially accumulates at the apical plasma membrane in infected polarized epithelial cells, which is the... | CATALYTIC ACTIVITY: Reaction=Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.; EC=3.2.1.18; Evidence={ECO:0000255|HAMAP-Rule:MF_04071}; | null | null | null | null | FUNCTION: Catalyzes the removal of terminal sialic acid residues from viral and cellular glycoconjugates. Cleaves off the terminal sialic acids on the glycosylated HA during virus budding to facilitate virus release. Additionally helps virus spread through the circulation by further removing sialic acids from the cell ... | Influenza A virus (strain A/Whale/Maine/1/1984 H13N9) |
P05804 | BGLR_ECOLI | MLRPVETPTREIKKLDGLWAFSLDRENCGIDQRWWESALQESRAIAVPGSFNDQFADADIRNYAGNVWYQREVFIPKGWAGQRIVLRFDAVTHYGKVWVNNQEVMEHQGGYTPFEADVTPYVIAGKSVRITVCVNNELNWQTIPPGMVITDENGKKKQSYFHDFFNYAGIHRSVMLYTTPNTWVDDITVVTHVAQDCNHASVDWQVVANGDVSVELRDADQQVVATGQGTSGTLQVVNPHLWQPGEGYLYELCVTAKSQTECDIYPLRVGIRSVAVKGEQFLINHKPFYFTGFGRHEDADLRGKGFDNVLMVHDHALMDW... | 3.2.1.31 | null | carbohydrate metabolic process [GO:0005975]; glucuronoside catabolic process [GO:0019391] | cytosol [GO:0005829]; extracellular space [GO:0005615]; protein-containing complex [GO:0032991] | beta-glucuronidase activity [GO:0004566]; carbohydrate binding [GO:0030246]; identical protein binding [GO:0042802]; signaling receptor binding [GO:0005102] | PF00703;PF02836;PF02837; | 2.60.120.260;3.20.20.80;2.60.40.10; | Glycosyl hydrolase 2 family | null | null | CATALYTIC ACTIVITY: Reaction=a beta-D-glucuronoside + H2O = an alcohol + D-glucuronate; Xref=Rhea:RHEA:17633, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:58720, ChEBI:CHEBI:83411; EC=3.2.1.31; Evidence={ECO:0000269|PubMed:21051639, ECO:0000269|PubMed:23690068, ECO:0000269|PubMed:26364932, ECO:0000269|PubMed:31056... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.13 mM for p-nitrophenyl-beta-D-glucuronide {ECO:0000269|PubMed:26364932}; Note=kcat is 120 sec(-1) with p-nitrophenyl-beta-D-glucuronide as substrate. {ECO:0000269|PubMed:26364932}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0-7.5.; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Resistant to thermal inactivation at 50 degrees Celsius.; | FUNCTION: Displays beta-glucuronidase activity with the artificial substrate p-nitrophenyl-beta-D-glucuronide (PNPG) and with 4-methylumbelliferyl-glucuronide (PubMed:21051639, PubMed:23690068, PubMed:26364932, PubMed:3105604, PubMed:33664385). Is likely capable of scavenging glucuronate from a range of chemically dist... | Escherichia coli (strain K12) |
P05806 | NPRE_BACCE | MKKKSLALVLATGMAVTTFGGTGSAFADSKNVLSTKKYNETVQSPEFISGDLTEATGKKAESVVFDYLNAAKGDYKLGEKSAQDSFKVKQVKKDAVTDSTVVRMQQVYEGVPVWGSTQVAHVSKDGSLKVLSGTVAPDLDKKEKLKNKNKIEGAKAIEIAQQDLGVTPKYEVEPKADLYVYQNGEETTYAYVVNLNFLDPSPGNYYYFIEADSGKVLNKFNTIDHVTNDDKSPVKQEAPKQDAKAVVKPVTGTNKVGTGKGVLGDTKSLNTTLSGSSYYLQDNTRGATIFTYDAKNRSTLPGTLWADADNVFNAAYDAAA... | 3.4.24.28 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 4 Ca(2+) ions per subunit.; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.; | proteolysis [GO:0006508] | extracellular region [GO:0005576] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222] | PF07504;PF03413;PF01447;PF02868; | 3.10.170.10;3.10.450.40;3.10.450.490;1.10.390.10; | Peptidase M4 family | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Similar, but not identical, to that of thermolysin.; EC=3.4.24.28; | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermolabile.; | FUNCTION: Extracellular zinc metalloprotease. | Bacillus cereus |
P05807 | NTP1_VACCW | MSKSHAAYIDYALRRTTNMPVEMMGSDVVRLKDYQHFVARVFLGLDSMHSLLLFHETGVGKTMTTVYILKHLKDIYTNWAIILLVKKALIEDPWMNTILRYAPEITKDCIFINYDDQNFRNKFFTNIKTINSKSRICVIIDECHNFISKSLIKEDGKIRPTRSVYNFLSKTIALKNHKMICLSATPIVNSVQEFTMLVNLLRPGSLQHQSLFENKRLVDEKELVSKLGGLCSYIVNNEFSIFDDVEGSASFAKKTVLMRYVNMSKKQEEIYQKAKLAEIKTGISSFRILRRMATTFTFDSFPERQNRDPGEYAQEIATLY... | 3.6.1.15 | null | DNA-templated transcription [GO:0006351] | virion component [GO:0044423] | ATP binding [GO:0005524]; ATP-dependent chromatin remodeler activity [GO:0140658]; DNA binding [GO:0003677]; ribonucleoside triphosphate phosphatase activity [GO:0017111] | PF00271;PF08469;PF00176; | 3.40.50.300; | Helicase family, NPH I subfamily | null | SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:16474121}. Note=Virion core enzyme. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474, ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15; Evidence={ECO:0000269|PubMed:22069335}; | null | null | null | null | FUNCTION: DNA-dependent ATPase that acts as a 5' to 3' translocase on single-stranded DNA and thereby plays a role in transcription termination of viral early genes (PubMed:27189950). Uses forward translocation in concert with the viral RNA polymerase RAP94/OPG109 subunit and the capping enzyme/VTF to catalyze release ... | Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR)) |
P05811 | CRYAB_MESAU | MDIAIHHPWIRRPFFPFHSPSRLFDQFFGEHLLESDLFSTATSLSPFYLRPPSFLRAPSWIDTGLSEMRMEKDRFSVNLDVKHFSPEELKVKVLGDVVEVHGKHEERQDEHGFISREFHRKYRIPADVDPLTITSSLSSDGVLTVNGPRKQASGPERTIPITREEKPAVTAAPKK | null | null | apoptotic process involved in morphogenesis [GO:0060561]; cellular response to gamma radiation [GO:0071480]; lens development in camera-type eye [GO:0002088]; muscle organ development [GO:0007517]; negative regulation of amyloid fibril formation [GO:1905907]; negative regulation of apoptotic process [GO:0043066]; negat... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; lysosome [GO:0005764]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; Z disc [GO:0030018] | amyloid-beta binding [GO:0001540]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; protein-containing complex binding [GO:0044877]; structural constituent of eye lens [GO:0005212]; unfolded protein binding [GO:0051082] | PF00525;PF00011; | 2.60.40.790; | Small heat shock protein (HSP20) family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P02511}. Nucleus {ECO:0000250|UniProtKB:P02511}. Secreted {ECO:0000250|UniProtKB:P02511}. Lysosome {ECO:0000250|UniProtKB:P23927}. Note=Translocates to the nucleus during heat shock and resides in sub-nuclear structures known as SC35 speckles or nuclear splicing sp... | null | null | null | null | null | FUNCTION: May contribute to the transparency and refractive index of the lens. Has chaperone-like activity, preventing aggregation of various proteins under a wide range of stress conditions. In lens epithelial cells, stabilizes the ATP6V1A protein, preventing its degradation by the proteasome (By similarity). {ECO:000... | Mesocricetus auratus (Golden hamster) |
P05813 | CRBA1_HUMAN | METQAEQQELETLPTTKMAQTNPTPGSLGPWKITIYDQENFQGKRMEFTSSCPNVSERSFDNVRSLKVESGAWIGYEHTSFCGQQFILERGEYPRWDAWSGSNAYHIERLMSFRPICSANHKESKMTIFEKENFIGRQWEISDDYPSLQAMGWFNNEVGSMKIQSGAWVCYQYPGYRGYQYILECDHHGGDYKHWREWGSHAQTSQIQSIRRIQQ | null | null | lens development in camera-type eye [GO:0002088]; negative regulation of cytokine production [GO:0001818]; negative regulation of ERK1 and ERK2 cascade [GO:0070373]; negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051898]; negative regulation of TOR signaling [GO:0032007];... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | structural constituent of eye lens [GO:0005212] | PF00030; | 2.60.20.10; | Beta/gamma-crystallin family | PTM: Specific cleavages in the N-terminal arm occur during lens maturation and give rise to several truncated forms. Cleavages do not seem to have adverse effects on solubility. {ECO:0000269|PubMed:15576560}.; PTM: S-methylation and glutathionylation occur in normal young lenses and do not seem to be detrimental. {ECO:... | null | null | null | null | null | null | FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens. | Homo sapiens (Human) |
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