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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P12904 | AAKG_YEAST | MKPTQDSQEKVSIEQQLAVESIRKFLNSKTSYDVLPVSYRLIVLDTSLLVKKSLNVLLQNSIVSAPLWDSKTSRFAGLLTTTDFINVIQYYFSNPDKFELVDKLQLDGLKDIERALGVDQLDTASIHPSRPLFEACLKMLESRSGRIPLIDQDEETHREIVVSVLTQYRILKFVALNCRETHFLKIPIGDLNIITQDNMKSCQMTTPVIDVIQMLTQGRVSSVPIIDENGYLINVYEAYDVLGLIKGGIYNDLSLSVGEALMRRSDDFEGVYTCTKNDKLSTIMDNIRKARVHRFFVVDDVGRLVGVLTLSDILKYILLG... | null | null | autophagy [GO:0006914]; filamentous growth [GO:0030447]; peroxisome organization [GO:0007031]; positive regulation of gluconeogenesis [GO:0045722]; regulation of cellular response to glucose starvation [GO:1904547]; regulation of invasive growth in response to glucose limitation [GO:2000217]; regulation of transcriptio... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear envelope lumen [GO:0005641]; nucleotide-activated protein kinase complex [GO:0031588]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | AMP binding [GO:0016208]; ATP binding [GO:0005524]; identical protein binding [GO:0042802]; protein kinase binding [GO:0019901]; protein kinase regulator activity [GO:0019887]; protein serine/threonine kinase activator activity [GO:0043539] | PF00571; | 3.10.580.10; | 5'-AMP-activated protein kinase gamma subunit family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17237508, ECO:0000269|PubMed:2481228, ECO:0000269|PubMed:3049255}. Cytoplasm {ECO:0000269|PubMed:17237508, ECO:0000269|PubMed:2481228}. | null | null | null | null | null | FUNCTION: Adenine nucleotides-binding subunit gamma of AMP-activated protein kinase (AMPK), an energy sensor protein kinase that plays a key role in regulating cellular energy metabolism. In response to reduction of intracellular ATP levels, AMPK activates energy-producing pathways and inhibits energy-consuming process... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P12908 | VP2_POVMC | MGAALTILVDLIEGLAEVSTLTGLSAEAILSGEALAALDGEITALTLEGVMSSETALATMGISEEVYGFVSTVPVFVNRTAGAIWLMQTVQGASTISLGIQRYLHNEEVPTVNRNMALIPWRDPALLDIYFPGVNQFAHALNVVHDWGHGLLHSVGRYVWQMVVQETQHRLEGAVRELTVRQTHTFLDGLARLLENTRWVVSNAPQSAIDAINRGASSASSGYSSLSDYYRQLGLNPPQRRALFNRIEGSMGNGGPTPAAHIQDESGEVIKFYQAQVVSHQRVTPDWMLPLILGLYGDITPTWATVIEEDGPQKKKRRL | null | null | symbiont entry into host cell [GO:0046718]; viral penetration into host nucleus [GO:0075732] | host cell [GO:0043657]; host cell endoplasmic reticulum membrane [GO:0044167]; host cell nucleus [GO:0042025]; membrane [GO:0016020]; viral capsid [GO:0019028] | DNA binding [GO:0003677]; structural molecule activity [GO:0005198] | PF00761; | null | Polyomaviruses capsid protein VP2 family | null | SUBCELLULAR LOCATION: [Isoform VP2]: Virion. Host nucleus. Host endoplasmic reticulum. Host endoplasmic reticulum membrane {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform VP3]: Virion. Host nucleus. Host endoplasmic reticulum. Host endoplasmic reticulum membrane {ECO:0000250}. | null | null | null | null | null | FUNCTION: [Isoform VP2]: Structural protein that resides within the core of the capsid surrounded by 72 VP1 pentamers. Participates in host cell receptor binding together with VP1. Following virus endocytosis and trafficking to the endoplasmic reticulum, VP2 and VP3 form oligomers and integrate into the endoplasmic ret... | Murine polyomavirus (strain Crawford small-plaque) (MPyV) |
P12911 | HBSAG_HBVCP | MGQNLSTSNPLGFFPEHQLDPAFKANTNNPDWDFNPKKDYWPEATKVGAGAFGPGFTPPHGGLLGLSPQAQGILTTLPANPPPASTNRQSGRQPTPLSPPLRDTHPQAMQWNSTTFHQALQDPRVRGLYFPAGGSSSGTLNPVPNTASHISSVFSTTGDPAPNMENITSGFLGPLLVLQAGFFLLTKILTIPQSLDSWWTSLNFLGGAPVCLGQNSQSPTSNHSPTSCPPICPGYRWMCLRRFIIFLFILLLCLIFLLVLLDYQGMLPVCPLIPGSSTTSTGPCKTCTTPAQGTSLIPSCCCTKPSDGNCTCIPIPSSWA... | null | null | caveolin-mediated endocytosis of virus by host cell [GO:0075513]; fusion of virus membrane with host endosome membrane [GO:0039654]; virion attachment to host cell [GO:0019062] | membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF00695; | null | Orthohepadnavirus major surface antigen family | PTM: Isoform M is N-terminally acetylated by host at a ratio of 90%, and N-glycosylated by host at the pre-S2 region. {ECO:0000250|UniProtKB:P03138, ECO:0000255|HAMAP-Rule:MF_04075}.; PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04075}. | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04075}. | null | null | null | null | null | FUNCTION: The large envelope protein exists in two topological conformations, one which is termed 'external' or Le-HBsAg and the other 'internal' or Li-HBsAg. In its external conformation the protein attaches the virus to cell receptors and thereby initiating infection. This interaction determines the species specifici... | Chimpanzee hepatitis B virus (isolate United Kingdom/LSH/1988) (HBVcpz) |
P12915 | POLG_BOVEV | MGAQLSRNTAGSHTTGTYATGGSTINYNNINYYSHAASAAQNKQDFTQDPSKFTQPIADVIKETAVPLKSPSAEACGYSDRVAQLTLGNSTITTQEAANICVAYGCWPAKLSDTDATSVDKPTEPGVSADAFYTLRSKPWQADSKGWYWKLPDALNNTGMFGQNAQFHYIYRGGWAVHVQCNATKFHQGTLLVLAIPEHQIATQEQPAFDRTMPGSEGGTFQEPFWLEDGTSLGNSLIYPHQWINLRTNNSATLILPYVNAIPMDSAIRHSNWTLAIIPVAPLKYAAETTPLVPITVTIAPMETEYNGLRRAIASNQGLP... | 2.7.7.48; 3.4.22.28; 3.4.22.29; 3.6.1.15 | COFACTOR: [RNA-directed RNA polymerase]: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P03300}; Note=Binds 2 magnesium ions that constitute a dinuclear catalytic metal center (By similarity). The magnesium ions are not prebound but only present for catalysis (By similarity). Requires the presence... | DNA replication [GO:0006260]; DNA-templated transcription [GO:0006351]; endocytosis involved in viral entry into host cell [GO:0075509]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; suppression by virus of host mRNA export from nucleus [GO:00... | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell nucleus [GO:0042025]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; metal ion binding [GO:0046872]; monoatomic ion channel activity [GO:0005216]; ribonucleoside triphosphate phosphatase activity [GO:0017111]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [G... | PF08727;PF00548;PF02226;PF00947;PF01552;PF00680;PF00073;PF00910; | 1.20.960.20;2.40.10.120;2.60.120.20;3.30.70.270;6.10.20.20;4.10.880.10;2.40.10.10; | Picornaviruses polyprotein family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo by the viral proteases yield processing intermediates and the mature proteins. {ECO:0000250|UniProtKB:P03300}.; PTM: [Capsid protein VP0]: Myristoylation is required for the formation of pentamers during virus assembly. Further assembly of 12 pentamers and... | SUBCELLULAR LOCATION: [Capsid protein VP0]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP4]: Virion.; SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000250|UniPro... | CATALYTIC ACTIVITY: [Protein 2C]: 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:0000250|UniProtKB:P03300}; CATALYTIC ACT... | null | null | null | null | FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). Capsid protein VP1 mainly forms t... | Bovine enterovirus (strain VG-5-27) (BEV) |
P12916 | POLG_HRV1B | MGAQVSRQNVGTHSTQNSVSNGSSLNYFNINYFKDAASSGASRLDFSQDPSKFTDPVKDVLEKGIPTLQSPSVEACGYSDRIIQITRGDSTITSQDVANAVVGYGVWPHYLTPQDATAIDKPTQPDTSSNRFYTLESKHWNGDSKGWWWKLPDALKEMGIFGENMYYHFLGRSGYTVHVQCNASKFHQGTLLVAMIPEHQLASAKNGSVTAGYNLTHPGEAGRVVGQQRDANLRQPSDDSWLNFDGTLLGNLLIFPHQFINLRSNNSATLIVPYVNAVPMDSMLRHNNWSLVIIPISPLRSETTSSNIRPITVSISPMCA... | 2.7.7.48; 3.4.22.28; 3.4.22.29; 3.6.1.15 | COFACTOR: [RNA-directed RNA polymerase]: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P03300}; Note=Binds 2 magnesium ions that constitute a dinuclear catalytic metal center (By similarity). The magnesium ions are not prebound but only present for catalysis (By similarity). Requires the presence... | DNA replication [GO:0006260]; DNA-templated transcription [GO:0006351]; endocytosis involved in viral entry into host cell [GO:0075509]; induction by virus of host autophagy [GO:0039520]; protein complex oligomerization [GO:0051259]; proteolysis [GO:0006508]; suppression by virus of host mRNA export from nucleus [GO:00... | host cell cytoplasmic vesicle membrane [GO:0044162]; host cell nucleus [GO:0042025]; membrane [GO:0016020]; T=pseudo3 icosahedral viral capsid [GO:0039618] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cysteine-type endopeptidase activity [GO:0004197]; metal ion binding [GO:0046872]; monoatomic ion channel activity [GO:0005216]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968]; structural mo... | PF08727;PF00548;PF02226;PF00947;PF01552;PF00680;PF00073;PF00910; | 1.20.960.20;2.60.120.20;3.30.70.270;3.40.50.300;6.10.20.20;4.10.880.10;2.40.10.10; | Picornaviruses polyprotein family | PTM: [Genome polyprotein]: Specific enzymatic cleavages in vivo by the viral proteases yield processing intermediates and the mature proteins. {ECO:0000250|UniProtKB:P03300}.; PTM: [Capsid protein VP0]: Myristoylation is required for the formation of pentamers during virus assembly. Further assembly of 12 pentamers and... | SUBCELLULAR LOCATION: [Capsid protein VP0]: Virion. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP4]: Virion.; SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000250|UniProtKB:P03300}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000250|UniPro... | CATALYTIC ACTIVITY: [Protein 2C]: 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:0000250|UniProtKB:P03300}; CATALYTIC ACT... | null | null | null | null | FUNCTION: [Capsid protein VP1]: Forms an icosahedral capsid of pseudo T=3 symmetry with capsid proteins VP2 and VP3 (By similarity). The capsid is 300 Angstroms in diameter, composed of 60 copies of each capsid protein and enclosing the viral positive strand RNA genome (By similarity). Capsid protein VP1 mainly forms t... | Human rhinovirus 1B (HRV-1B) |
P12919 | PDGFB_FELCA | MNRCWALFLSLCCYLRLVSAEGDPIPEELYKMLSDHSIRSFDDLQRLLHGDSVDEDRAELDLNSTRSHCGGELESLSRGRRSLGEAAGSPTVAEPAMIAECKTRTEVFEVSRRLIDRTNANFLVWPPCVEVQRCSGCCNNRNVQCRPTQVQLRLVQVRKIEIVRKRPVFKKATVTLEDHLACKCETVVAARPVTRSPGSSQEQRARTPQTRVTIRTVRVRRPPKGKHQKFKHTHDKKALKETLGA | null | null | cell chemotaxis [GO:0060326]; cellular response to mycophenolic acid [GO:0071506]; embryonic placenta development [GO:0001892]; heart development [GO:0007507]; metanephric glomerular mesangial cell development [GO:0072255]; monocyte chemotaxis [GO:0002548]; negative regulation of gene expression [GO:0010629]; negative ... | basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular space [GO:0005615] | growth factor activity [GO:0008083]; platelet-derived growth factor receptor binding [GO:0005161]; protein homodimerization activity [GO:0042803]; superoxide-generating NADPH oxidase activator activity [GO:0016176] | PF00341;PF04692; | 2.10.90.10; | PDGF/VEGF growth factor family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. Note=Released by platelets upon wounding. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Growth factor that plays an essential role in the regulation of embryonic development, cell proliferation, cell migration, survival and chemotaxis. Potent mitogen for cells of mesenchymal origin. Required for normal proliferation and recruitment of pericytes and vascular smooth muscle cells in the central ner... | Felis catus (Cat) (Felis silvestris catus) |
P12927 | NPH2_VACCW | MEKNLPDIFFFPNCVNVFSYKYSQDEFSNMSKTERDSFSLAVFPVIKHRWHNAHVVKHKGIYKVSTEARGKKVSPPSLGKPAHINLTAKQYIYSEHTISFECYSFLKCITNTEINSFDEYILRGLLEAGNSLQIFSNSVGKRTDTIGVLGNKYPFSKIPLASLTPKAQREIFSAWISHRPVVLTGGTGVGKTSQVPKLLLWFNYLFGGFSTLDKITNFHERPVILSLPRIALVRLHSNTILKSLGFKVLDGSPISLRYGSIPEELINKQPKKYGIVFSTHKLSLTKLFSYGTLIIDEVHEHDQIGDIIIAVARKHHTKID... | 3.6.4.13 | null | null | virion component [GO:0044423] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724] | PF00270;PF00271;PF12011; | 3.40.50.300; | DEAD box helicase family, DEAH subfamily | null | SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:4364421}. Note=Localizes to the virion core. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000269|PubMed:9573237}; | null | null | null | null | FUNCTION: NTP-dependent helicase that catalyzes unidirectional unwinding of 3'tailed duplex RNAs and plays an important role during transcription of early mRNAs, presumably by preventing R-loop formation behind the elongating RNA polymerase. Might also play a role in the export of newly synthesized mRNA chains out of t... | Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR)) |
P12928 | KPYR_RAT | MSVQENTLPQQLWPWIFRSQKDLAKSALSGAPGGPAGYLRRASVAQLTQELGTAFFQQQQLPAAMADTFLEHLCLLDIDSQPVAARSTSIIATIGPASRSVDRLKEMIKAGMNIARLNFSHGSHEYHAESIANIREATESFATSPLSYRPVAIALDTKGPEIRTGVLQGGPESEVEIVKGSQVLVTVDPKFQTRGDAKTVWVDYHNITRVVAVGGRIYIDDGLISLVVQKIGPEGLVTEVEHGGILGSRKGVNLPNTEVDLPGLSEQDLLDLRFGVQHNVDIIFASFVRKASDVLAVRDALGPEGQNIKIISKIENHEGV... | 2.7.1.40 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P30613}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P30613}; COFACTOR: Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:P30613}; | cellular response to epinephrine stimulus [GO:0071872]; cellular response to insulin stimulus [GO:0032869]; glycolytic process [GO:0006096]; phosphorylation [GO:0016310]; pyruvate biosynthetic process [GO:0042866]; response to ATP [GO:0033198]; response to cAMP [GO:0051591]; response to glucose [GO:0009749]; response t... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; kinase activity [GO:0016301]; magnesium ion binding [GO:0000287]; monosaccharide binding [GO:0048029]; potassium ion binding [GO:0030955]; pyruvate kinase activity [GO:0004743] | PF00224;PF02887; | 3.20.20.60;2.40.33.10;3.40.1380.20; | Pyruvate kinase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + pyruvate = ADP + H(+) + phosphoenolpyruvate; Xref=Rhea:RHEA:18157, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:58702, ChEBI:CHEBI:456216; EC=2.7.1.40; Evidence={ECO:0000250|UniProtKB:P30613}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:18159; Evidence... | null | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 5/5. {ECO:0000250|UniProtKB:P30613}. | null | null | FUNCTION: Pyruvate kinase that catalyzes the conversion of phosphoenolpyruvate to pyruvate with the synthesis of ATP, and which plays a key role in glycolysis. {ECO:0000250|UniProtKB:P30613}. | Rattus norvegicus (Rat) |
P12931 | SRC_HUMAN | MGSNKSKPKDASQRRRSLEPAENVHGAGGGAFPASQTPSKPASADGHRGPSAAFAPAAAEPKLFGGFNSSDTVTSPQRAGPLAGGVTTFVALYDYESRTETDLSFKKGERLQIVNNTEGDWWLAHSLSTGQTGYIPSNYVAPSDSIQAEEWYFGKITRRESERLLLNAENPRGTFLVRESETTKGAYCLSVSDFDNAKGLNVKHYKIRKLDSGGFYITSRTQFNSLQQLVAYYSKHADGLCHRLTTVCPTSKPQTQGLAKDAWEIPRESLRLEVKLGQGCFGEVWMGTWNGTTRVAIKTLKPGTMSPEAFLQEAQVMKKL... | 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-cell adhesion [GO:0098609]; c... | actin filament [GO:0005884]; caveola [GO:0005901]; cell junction [GO:0030054]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendritic filopodium [GO:1902737]; dendritic growth cone [GO:0044294]; extracellular exosome [GO:0070062]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234]; focal adhesion ... | ATP binding [GO:0005524]; ATPase binding [GO:0051117]; BMP receptor binding [GO:0070700]; cadherin binding [GO:0045296]; 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]; non-... | 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:0000269|PubMed:7525268}.; PTM: Dephosphorylated at Tyr-530 by PTPRJ (By similarity). Phosphorylated on Tyr-530 by c-Src kinase (CSK). The phosphorylated form is termed pp60c-src. Dephosphorylated by PTPRJ at Tyr-419. Normally maintained... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7525268}; Lipid-anchor {ECO:0000269|PubMed:22801373}. Mitochondrion inner membrane {ECO:0000269|PubMed:12615910}. Nucleus {ECO:0000269|PubMed:7853507}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:7525268}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:19307596... | 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... | Homo sapiens (Human) |
P12934 | HBSAG_HBVC3 | MGGWSSKPRQGMGTNLSVPNPLGFFPDHQLDPAFGANSHNPDWDFNPNKDHWPEANQVGAGAFGPGFTPPHGGLLGWSPQAQGVLTTVPVAPPPASTNRQSGRQPTPISPPLRDSHPQAMQWNSTTFHQALLDPRVRGLYFPAGGSSSGTVNPVPTTASPISSISSRTGDPAPNMENTTSGFLGPLLVLQAGFFLLTRILTIPQSLDSWWTSLNFLGGAPTCPGQNSQSPTSNHSPTSCPPICPGYRWMCLRRFIIFLFILLLCLIFLLVLLDYQGMLPVCPLLPGTSTTSTGPCKTCTIPAQGTSMFPSCCCTKPSDGN... | null | null | caveolin-mediated endocytosis of virus by host cell [GO:0075513]; fusion of virus membrane with host endosome membrane [GO:0039654]; virion attachment to host cell [GO:0019062] | membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF00695; | null | Orthohepadnavirus major surface antigen family | PTM: Isoform M is N-terminally acetylated by host at a ratio of 90%, and N-glycosylated by host at the pre-S2 region. {ECO:0000250|UniProtKB:P03138, ECO:0000255|HAMAP-Rule:MF_04075}.; PTM: Myristoylated. {ECO:0000255|HAMAP-Rule:MF_04075}. | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04075}. | null | null | null | null | null | FUNCTION: The large envelope protein exists in two topological conformations, one which is termed 'external' or Le-HBsAg and the other 'internal' or Li-HBsAg. In its external conformation the protein attaches the virus to cell receptors and thereby initiating infection. This interaction determines the species specifici... | Hepatitis B virus genotype C subtype adr (strain Japan/adr4/1983) (HBV-C) |
P12938 | CP2D3_RAT | MELLAGTGLWPMAIFTVIFILLVDLMHRRQRWTSRYPPGPVPWPVLGNLLQVDLCNMPYSMYKLQNRYGDVFSLQMGWKPVVVINGLKAVQELLVTCGEDTADRPEMPIFQHIGYGHKAKGVVLAPYGPEWREQRRFSVSTLRNFGVGKKSLEQWVTDEASHLCDALTAEAGRPLDPYTLLNKAVCNVIASLIYARRFDYGDPDFIKVLKILKESMGEQTGLFPEVLNMFPVLLRIPGLADKVFPGQKTFLTMVDNLVTEHKKTWDPDQPPRDLTDAFLAEIEKAKGNPESSFNDANLRLVVNDLFGAGMVTTSITLTWA... | 1.14.14.1 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; | arachidonic acid metabolic process [GO:0019369]; liver development [GO:0001889]; xenobiotic metabolic process [GO:0006805] | cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231] | aromatase activity [GO:0070330]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen [GO:... | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57... | null | null | null | null | FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. | Rattus norvegicus (Rat) |
P12939 | CP2DA_RAT | MELLNGTGLWPMAIFTVIFILLVDLMHRHQRWTSRYPPGPVPWPVLGNLLQVDPSNMPYSMYKLQHRYGDVFSLQMGWKPMVIVNRLKAVQEVLVTHGEDTADRPPVPIFKCLGVKPRSQGVVFASYGPEWREQRRFSVSTLRTFGMGKKSLEEWVTKEAGHLCDAFTAQNGRSINPKAMLNKALCNVIASLIFARRFEYEDPYLIRMLTLVEESLIEVSGFIPEVLNTFPALLRIPGLADKVFQGQKTFMAFLDNLLAENRTTWDPAQPPRNLTDAFLAEVEKAKGNPESSFNDENLRMVVVDLFTAGMVTTATTLTWA... | 1.14.14.1 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; | arachidonic acid metabolic process [GO:0019369]; xenobiotic metabolic process [GO:0006805] | cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231] | aromatase activity [GO:0070330]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activity [GO:0004497]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom of oxygen [GO:... | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57... | null | null | null | null | FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. | Rattus norvegicus (Rat) |
P12943 | PHNS_MEGGA | MKFCTAVAVAMGMGPAFAPKVAEALTAKKRPSVVYLHNAECTGCSESLLRTVDPYVDELILDVISMDYHETLMAGAGHAVEEALHEAIKGDFVCVIEGGIPMGDGGYWGKVGRRNMYDICAEVAPKAKAVIAIGTCATYGGVQAAKPNPTGTVGVNEALGKLGVKAINIAGCPPNPMNFVGTVVHLLTKGMPELDKQGRPVMFFGETVHDNCPRLKHFEAGEFATSFGSPEAKKGYCLYELGCKGPDTYNNCPKQLFNQVNWPVQAGHPCIACSEPNFWDLYSPFYSA | 1.12.2.1 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Note=Binds 2 [4Fe-4S] clusters.; COFACTOR: Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; Note=Binds 1 [3Fe-4S] cluster.; | anaerobic respiration [GO:0009061] | [Ni-Fe] hydrogenase complex [GO:0044569]; ferredoxin hydrogenase complex [GO:0009375]; membrane [GO:0016020]; periplasmic space [GO:0042597] | 3 iron, 4 sulfur cluster binding [GO:0051538]; 4 iron, 4 sulfur cluster binding [GO:0051539]; cytochrome-c3 hydrogenase activity [GO:0047806]; electron transfer activity [GO:0009055]; ferredoxin hydrogenase activity [GO:0008901]; metal ion binding [GO:0046872] | PF14720;PF01058; | 4.10.480.10;3.40.50.700; | [NiFe]/[NiFeSe] hydrogenase small subunit family | null | SUBCELLULAR LOCATION: Periplasm. | CATALYTIC ACTIVITY: Reaction=2 Fe(III)-[cytochrome c3] + H2 = 2 Fe(II)-[cytochrome c3] + 2 H(+); Xref=Rhea:RHEA:20625, Rhea:RHEA-COMP:11576, Rhea:RHEA-COMP:11577, ChEBI:CHEBI:15378, ChEBI:CHEBI:18276, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.12.2.1; | null | null | null | null | null | Megalodesulfovibrio gigas (Desulfovibrio gigas) |
P12945 | NAT1_YEAST | MSRKRSTKPKPAAKIALKKENDQFLEALKLYEGKQYKKSLKLLDAILKKDGSHVDSLALKGLDLYSVGEKDDAASYVANAIRKIEGASASPICCHVLGIYMRNTKEYKESIKWFTAALNNGSTNKQIYRDLATLQSQIGDFKNALVSRKKYWEAFLGYRANWTSLAVAQDVNGERQQAINTLSQFEKLAEGKISDSEKYEHSECLMYKNDIMYKAASDNQDKLQNVLKHLNDIEPCVFDKFGLLERKATIYMKLGQLKDASIVYRTLIKRNPDNFKYYKLLEVSLGIQGDNKLKKALYGKLEQFYPRCEPPKFIPLTFLQ... | null | null | N-terminal protein amino acid acetylation [GO:0006474] | cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; NatA complex [GO:0031415] | ribosome binding [GO:0043022] | PF12569; | 1.25.40.1010;1.25.40.1040; | null | PTM: The N-terminus is blocked. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. | null | null | null | null | null | FUNCTION: Non-catalytic component of the NatA N-terminal acetyltransferase, which catalyzes acetylation of proteins beginning with Met-Ser, Met-Gly and Met-Ala. N-acetylation plays a role in normal eukaryotic translation and processing, protect against proteolytic degradation and protein turnover. NAT1 anchors ARD1 and... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P12946 | CTAA_BACSU | MNKALKALGVLTTFVMLIVLIGGALVTKTGSGQGCGRQWPLCHGRFFPELNPASIIEWSHRFASGISIILVLSLAFWSWRKITPIFRETTFLAIMSIIFLFLQALLGALAVVFGSNALIMALHFGISLISFASVLILTLLIFEADKSVRTLVKPLQIGKKMQFHMIGILIYSYIVVYTGAYVRHTESSLACPNVPLCSPLNNGLPTQFHEWVQMGHRAAALLLFVWIIVAAVHAITSYKDQKQIFWGWISCLIFITLQALSGIMIVYSELALGFALAHSFFIACLFGVLCYFLLLIARFRYESRQS | 1.17.99.9 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000255|HAMAP-Rule:MF_01664, ECO:0000269|PubMed:30397130, ECO:0000269|PubMed:7961419}; | heme A biosynthetic process [GO:0006784] | plasma membrane [GO:0005886] | metal ion binding [GO:0046872]; oxidoreductase activity, acting on NAD(P)H, heme protein as acceptor [GO:0016653] | PF02628; | null | COX15/CtaA family, Type 1 subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_01664, ECO:0000269|PubMed:12206660, ECO:0000269|PubMed:16321940, ECO:0000269|PubMed:30397130, ECO:0000269|PubMed:7961419}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_01664, ECO:0000269|PubMed:30397130}. | CATALYTIC ACTIVITY: Reaction=2 A + Fe(II)-heme o + H2O = 2 AH2 + Fe(II)-heme a; Xref=Rhea:RHEA:63388, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:17499, ChEBI:CHEBI:60530, ChEBI:CHEBI:61715; EC=1.17.99.9; Evidence={ECO:0000255|HAMAP-Rule:MF_01664, ECO:0000269|PubMed:15236569, ECO:0000269|PubMed:16321940}; Physiol... | null | PATHWAY: Porphyrin-containing compound metabolism; heme A biosynthesis; heme A from heme O: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01664, ECO:0000269|PubMed:12206660, ECO:0000305|PubMed:7961419}. | null | null | FUNCTION: Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A. {ECO:0000255|HAMAP-Rule... | Bacillus subtilis (strain 168) |
P12954 | SRS2_YEAST | MSSNNDLWLHLVSQLNTQQRAAALFDYTRGLQVIAGPGTGKTKVLTSRVAYLILHHHIHPRDIIVTTFTNKAANEMKERLQEMLRGAGVNISELLIGTFHSICLKILYRFGHLVDLQKDWRIIDEKEIDVILDDMIEKVPDQIRDYASSITRKVNLCMPSKNGDEWTIHPKLIKKQISKLKSNAILPEEYILDSNHDAALGYFYQIYQSELSKKNTLDFDDLLMYTFRLLTRVRVLSNIKHVLVDEFQDTNGIQLDLMFLFAKGNHHLSRGMTIVGDPDQSIYAFRNALAHNFLEMGRKCPIEYSTIILVENYRSSQKIL... | 5.6.2.4 | null | DNA duplex unwinding [GO:0032508]; DNA protection [GO:0042262]; DNA recombinase disassembly [GO:1990986]; DNA repair [GO:0006281]; double-strand break repair via nonhomologous end joining [GO:0006303]; negative regulation of DNA recombination [GO:0045910]; negative regulation of double-strand break repair via homologou... | cytosol [GO:0005829]; DNA helicase complex [GO:0033202]; nucleus [GO:0005634] | 3'-5' DNA helicase activity [GO:0043138]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; enzyme activator activity [GO:0008047]; isomerase activity [GO:0016853] | PF00580;PF13361; | 1.10.10.160;3.40.50.300; | Helicase family, UvrD subfamily | null | SUBCELLULAR LOCATION: Nucleus. | CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.; EC=5.6.2.4; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216... | null | null | null | null | FUNCTION: ATP-dependent DNA helicase involved in DNA repair at least for UV-induced lesions. The polarity of the helicase activity was determined to be 3' to 5'. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P12955 | PEPD_HUMAN | MAAATGPSFWLGNETLKVPLALFALNRQRLCERLRKNPAVQAGSIVVLQGGEETQRYCTDTGVLFRQESFFHWAFGVTEPGCYGVIDVDTGKSTLFVPRLPASHATWMGKIHSKEHFKEKYAVDDVQYVDEIASVLTSQKPSVLLTLRGVNTDSGSVCREASFDGISKFEVNNTILHPEIVECRVFKTDMELEVLRYTNKISSEAHREVMKAVKVGMKEYELESLFEHYCYSRGGMRHSSYTCICGSGENSAVLHYGHAGAPNDRTIQNGDMCLFDMGGEYYCFASDITCSFPANGKFTADQKAVYEAVLRSSRAVMGAM... | 3.4.13.9 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:17081196, ECO:0000269|PubMed:28677335}; Note=Binds 2 manganese ions per subunit. {ECO:0000269|PubMed:28677335}; | amino acid metabolic process [GO:0006520]; collagen catabolic process [GO:0030574]; negative regulation of programmed cell death [GO:0043069]; proteolysis [GO:0006508] | extracellular exosome [GO:0070062] | manganese ion binding [GO:0030145]; metalloaminopeptidase activity [GO:0070006]; metallocarboxypeptidase activity [GO:0004181]; peptidase activity [GO:0008233]; proline dipeptidase activity [GO:0102009] | PF05195;PF00557; | 3.90.230.10;3.40.350.10; | Peptidase M24B family, Eukaryotic-type prolidase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=H2O + Xaa-L-Pro dipeptide = an L-alpha-amino acid + L-proline; Xref=Rhea:RHEA:76407, ChEBI:CHEBI:15377, ChEBI:CHEBI:59869, ChEBI:CHEBI:60039, ChEBI:CHEBI:195196; EC=3.4.13.9; Evidence={ECO:0000269|PubMed:17081196, ECO:0000269|PubMed:35165443}; | null | null | null | null | FUNCTION: Dipeptidase that catalyzes the hydrolysis of dipeptides with a prolyl (Xaa-Pro) or hydroxyprolyl residue in the C-terminal position (PubMed:17081196, PubMed:35165443). The preferred dipeptide substrate is Gly-Pro, but other Xaa-Pro dipeptides, such as Ala-Pro, Met-Pro, Phe-Pro, Val-Pro and Leu-Pro, can be cle... | Homo sapiens (Human) |
P12956 | XRCC6_HUMAN | MSGWESYYKTEGDEEAEEEQEENLEASGDYKYSGRDSLIFLVDASKAMFESQSEDELTPFDMSIQCIQSVYISKIISSDRDLLAVVFYGTEKDKNSVNFKNIYVLQELDNPGAKRILELDQFKGQQGQKRFQDMMGHGSDYSLSEVLWVCANLFSDVQFKMSHKRIMLFTNEDNPHGNDSAKASRARTKAGDLRDTGIFLDLMHLKKPGGFDISLFYRDIISIAEDEDLRVHFEESSKLEDLLRKVRAKETRKRALSRLKLKLNKDIVISVGIYNLVQKALKPPPIKLYRETNEPVKTKTRTFNTSTGGLLLPSDTKRSQ... | 3.6.4.-; 4.2.99.- | null | activation of innate immune response [GO:0002218]; cellular hyperosmotic salinity response [GO:0071475]; cellular response to gamma radiation [GO:0071480]; cellular response to X-ray [GO:0071481]; DNA ligation [GO:0006266]; double-strand break repair via classical nonhomologous end joining [GO:0097680]; double-strand b... | chromosome, telomeric region [GO:0000781]; cytosol [GO:0005829]; DNA-dependent protein kinase complex [GO:0070418]; DNA-dependent protein kinase-DNA ligase 4 complex [GO:0005958]; extracellular region [GO:0005576]; ficolin-1-rich granule lumen [GO:1904813]; Ku70:Ku80 complex [GO:0043564]; membrane [GO:0016020]; nonhomo... | 5'-deoxyribose-5-phosphate lyase activity [GO:0051575]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent activity, acting on DNA [GO:0008094]; cyclin binding [GO:0030332]; damaged DNA binding [GO:0003684]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678]; double-stranded DNA bin... | PF02735;PF03730;PF03731;PF02037; | 1.10.1600.10;2.40.290.10;4.10.970.10;1.10.720.30;3.40.50.410; | Ku70 family | PTM: Phosphorylation by PRKDC may enhance helicase activity. Phosphorylation of Ser-51 does not affect DNA repair. {ECO:0000269|PubMed:10026262, ECO:0000269|PubMed:12547193, ECO:0000269|PubMed:9362500}.; PTM: ADP-ribosylated by PARP3. {ECO:0000269|PubMed:24598253}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22442688}. Chromosome {ECO:0000269|PubMed:22442688}. | null | null | null | null | null | FUNCTION: Single-stranded DNA-dependent ATP-dependent helicase that plays a key role in DNA non-homologous end joining (NHEJ) by recruiting DNA-PK to DNA (PubMed:11493912, PubMed:12145306, PubMed:20493174, PubMed:2466842, PubMed:7957065, PubMed:8621488, PubMed:9742108). Required for double-strand break repair and V(D)J... | Homo sapiens (Human) |
P12957 | CALD1_CHICK | MDDFERRRELRRQKREEMRLEAERLSYQRNDDDEEEAARERRRRARQERLRQKEEGDVSGEVTEKSEVNAQNSVAEEETKRSTDDEAALLERLARREERRQKRLQEALERQKEFDPTITDGSLSVPSRREVNNVEENEITGKEEKVETRQGRCEIEETETVTKSYQRNNWRQDGEEEGKKEEKDSEEEKPKEVPTEENQVDVAVEKSTDKEEVVETKTLAVNAENDTNAMLEGEQSITDAADKEKEEAEKEREKLEAEEKERLKAEEEKKAAEEKQKAEEEKKAAEERERAKAEEEKRAAEERERAKAEEERKAAEERER... | null | null | actin filament bundle assembly [GO:0051017]; angiogenesis [GO:0001525]; muscle contraction [GO:0006936]; negative regulation of calcium-dependent ATPase activity [GO:1903611] | actin cytoskeleton [GO:0015629]; myofibril [GO:0030016]; stress fiber [GO:0001725] | actin binding [GO:0003779]; calmodulin binding [GO:0005516]; myosin binding [GO:0017022]; myosin II binding [GO:0045159]; S100 protein binding [GO:0044548] | PF02029; | null | Caldesmon family | PTM: Phosphorylated in non-muscle cells. Phosphorylation by CDK1 during mitosis causes caldesmon to dissociate from microfilaments. Phosphorylation reduces caldesmon binding to actin, myosin, and calmodulin as well as its inhibition of actomyosin ATPase activity. Phosphorylation also occurs in both quiescent and dividi... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P13505}. Cytoplasm, myofibril {ECO:0000250|UniProtKB:P13505}. Cytoplasm, cytoskeleton, stress fiber {ECO:0000250|UniProtKB:P13505}. Note=On thin filaments in smooth muscle and on stress fibers in fibroblasts (nonmuscle). {ECO:0000250|UniProtKB:P13505}... | null | null | null | null | null | FUNCTION: Actin- and myosin-binding protein implicated in the regulation of actomyosin interactions in smooth muscle and nonmuscle cells (could act as a bridge between myosin and actin filaments). Stimulates actin binding of tropomyosin which increases the stabilization of actin filament structure. In muscle tissues, i... | Gallus gallus (Chicken) |
P12960 | CNTN1_MOUSE | MKMPLLVSHLLLISLTSCLGDFTWHRRYGHGVSEEDKGFGPIFEEQPINTIYPEESLEGKVSLNCRARASPFPVYKWRMNNGDVDLTNDRYSMVGGNLVINNPDKQKDAGVYYCLASNNYGMVRSTEATLSFGYLDPFPPEERPEVKVKEGKGMVLLCDPPYHFPDDLSYRWLLNEFPVFITMDKRRFVSQTNGNLYIANVESSDRGNYSCFVSSPSITKSVFSKFIPLIPIPERTTKPYPADIVVQFKDIYTMMGQNVTLECFALGNPVPDIRWRKVLEPMPSTAEISTSGAVLKIFNIQLEDEGLYECEAENIRGKDK... | null | null | axon guidance [GO:0007411]; brain development [GO:0007420]; cell-cell adhesion [GO:0098609]; central nervous system myelin formation [GO:0032289]; cerebellum development [GO:0021549]; gene expression [GO:0010467]; locomotory behavior [GO:0007626]; myelination [GO:0042552]; neuron projection development [GO:0031175]; No... | axon [GO:0030424]; myelin sheath [GO:0043209]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; presynaptic membrane [GO:0042734]; side of membrane [GO:0098552] | carbohydrate binding [GO:0030246]; cell-cell adhesion mediator activity [GO:0098632] | PF00041;PF07679;PF00047;PF13927; | 2.60.40.10; | Immunoglobulin superfamily, Contactin family | null | SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor, GPI-anchor. | null | null | null | null | null | FUNCTION: Contactins mediate cell surface interactions during nervous system development. Involved in the formation of paranodal axo-glial junctions in myelinated peripheral nerves and in the signaling between axons and myelinating glial cells via its association with CNTNAP1. Participates in oligodendrocytes generatio... | Mus musculus (Mouse) |
P12961 | 7B2_MOUSE | MASRLVSAMLSGLLFWLMFEWNPAFAYSPRTPDRVSETDIQRLLHGVMEQLGIARPRVEYPAHQAMNLVGPQSIEGGAHEGLQHLGPFGNIPNIVAELTGDNIPKDFSEDQGYPDPPNPCPLGKTADDGCLENAPDTAEFSREFQLDQHLFDPEHDYPGLGKWNKKLLYEKMKGGQRRKRRSVNPYLQGKRLDNVVAKKSVPHFSEEEKEAE | 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]; 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:0000269|PubMed:8034690}.; PTM: Sulfated on tyrosine residues. {ECO:0000269|PubMed:8034690}. | 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... | Mus musculus (Mouse) |
P12962 | CAF20_YEAST | MIKYTIDELFQLKPSLTLEVNFDAVEFRAIIEKVKQLQHLKEEEFNSHHVGHFGRRRSSHHHGRPKIKHNKPKVTTDSDGWCTFEAKKKGSGEDDEEETETTPTSTVPVATIAQETLKVKPNNKNISSNRPADTRDIVADKPILGFNAFAALESEDEDDEA | null | null | negative regulation of translation [GO:0017148]; positive regulation of cytoplasmic mRNA processing body assembly [GO:0010606]; positive regulation of translation [GO:0045727] | cytoplasm [GO:0005737] | eukaryotic initiation factor 4E binding [GO:0008190]; translation initiation factor activity [GO:0003743] | PF17052; | null | CAF20 family | PTM: Phosphorylated by casein kinase II complex (CK2). {ECO:0000269|PubMed:7592868}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. | null | null | null | null | null | FUNCTION: Acts as an inhibitor of cap-dependent translation. Competes with eIF4G1/TIF4631 and EAP1 for binding to eIF4E/TIF45 and interferes with the formation of the eIF4F complex, inhibiting translation and stabilizing mRNA. Binding affinity for eIF4E/TIF45 is 10-fold less than that of eIF4G1/TIF4631. Required for in... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P12968 | IAPP_MOUSE | MMCISKLPAVLLILSVALNHLRATPVRSGSNPQMDKRKCNTATCATQRLANFLVRSSNNLGPVLPPTNVGSNTYGKRNAAGDPNRESLDFLLV | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; amylin receptor signaling pathway [GO:0097647]; bone resorption [GO:0045453]; eating behavior [GO:0042755]; negative regulation of bone resorption [GO:0045779]; negative regulation of osteoclast differentiation [GO:0045671]; osteocl... | cytosol [GO:0005829]; extracellular space [GO:0005615] | hormone activity [GO:0005179]; identical protein binding [GO:0042802] | PF00214; | 6.10.250.2190; | Calcitonin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, while not affecting adipocyte glucose metabolism. | Mus musculus (Mouse) |
P12969 | IAPP_RAT | MRCISRLPAVLLILSVALGHLRATPVGSGTNPQVDKRKCNTATCATQRLANFLVRSSNNLGPVLPPTNVGSNTYGKRNVAEDPNRESLDFLLL | null | null | amylin receptor signaling pathway [GO:0097647]; bone resorption [GO:0045453]; eating behavior [GO:0042755]; glucose metabolic process [GO:0006006]; negative regulation of bone resorption [GO:0045779]; negative regulation of osteoclast differentiation [GO:0045671]; osteoclast differentiation [GO:0030316]; positive regul... | extracellular space [GO:0005615]; neuronal cell body [GO:0043025]; secretory granule [GO:0030141] | hormone activity [GO:0005179]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; receptor ligand activity [GO:0048018]; signaling receptor binding [GO:0005102] | PF00214; | 6.10.250.2190; | Calcitonin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Selectively inhibits insulin-stimulated glucose utilization and glycogen deposition in muscle, while not affecting adipocyte glucose metabolism. {ECO:0000250}. | Rattus norvegicus (Rat) |
P12970 | RL7A_MOUSE | MPKGKKAKGKKVAPAPAVVKKQEAKKVVNPLFEKRPKNFGIGQDIQPKRDLTRFVKWPRYIRLQRQRAILYKRLKVPPAINQFTQALDRQTATQLLKLAHKYRPETKQEKKQRLLARAEKKAAGKGDVPTKRPPVLRAGVNTVTTLVENKKAQLVVIAHDVDPIELVVFLPALCRKMGVPYCIIKGKARLGHLVHRKTCTTVAFTQVNSEDKGALAKLVEAIRTNYNDRYDEIRRHWGGNVLGPKSVARIAKLEKAKAKELATKLG | null | null | cytoplasmic translation [GO:0002181]; maturation of LSU-rRNA [GO:0000470]; translation at postsynapse [GO:0140242]; translation at presynapse [GO:0140236] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; membrane [GO:0016020]; nucleolus [GO:0005730]; postsynapse [GO:0098794]; presynapse [GO:0098793]; ribosome [GO:0005840]; synapse [GO:0045202] | RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735] | PF01248; | 3.30.1330.30; | Eukaryotic ribosomal protein eL8 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:36517592}. | null | null | null | null | null | FUNCTION: Component of the large ribosomal subunit (PubMed:36517592). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:36517592). {ECO:0000269|PubMed:36517592}. | Mus musculus (Mouse) |
P12978 | EBNA2_EBVB9 | MPTFYLALHGGQTYHLIVDTDSLGNPSLSVIPSNPYQEQLSDTPLIPLTIFVGENTGVPPPLPPPPPPPPPPPPPPPPPPPPPPPPPPSPPPPPPPPPPPQRRDAWTQEPSPLDRDPLGYDVGHGPLASAMRMLWMANYIVRQSRGDRGLILPQGPQTAPQARLVQPHVPPLRPTAPTILSPLSQPRLTPPQPLMMPPRPTPPTPLPPATLTVPPRPTRPTTLPPTPLLTVLQRPTELQPTPSPPRMHLPVLHVPDQSMHPLTHQSTPNDPDSPEPRSPTVFYNIPPMPLPPSQLPPPAAPAQPPPGVINDQQLHHLPSG... | null | null | DNA-templated viral transcription [GO:0039695]; positive regulation of DNA-templated transcription [GO:0045893]; symbiont-mediated perturbation of host cell cycle progression [GO:0044071]; symbiont-mediated perturbation of host transcription [GO:0052026]; symbiont-mediated suppression of host translation initiation [GO... | host cell nuclear matrix [GO:0044204]; host cell nucleus [GO:0042025] | protein serine/threonine phosphatase inhibitor activity [GO:0004865] | null | null | Herpesviridae EBNA2 family | PTM: Phosphorylated. {ECO:0000269|PubMed:2161150}. | SUBCELLULAR LOCATION: Host nucleus matrix {ECO:0000269|PubMed:2161150}. Note=Associated with the nuclear matrix. | null | null | null | null | null | FUNCTION: Plays a key role in the activation of the host resting B-cell and stimulation of B-cell proliferation. Acts by up-regulating the expression of viral EBNA1-6, LMP1, LMP2A and LMP2B genes, as well as several host genes including CD21, CD23 and MYC. Activates transcription by acting as an adapter molecule that b... | Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4) |
P12979 | MYOG_MOUSE | MELYETSPYFYQEPHFYDGENYLPVHLQGFEPPGYERTELSLSPEARGPLEEKGLGTPEHCPGQCLPWACKVCKRKSVSVDRRRAATLREKRRLKKVNEAFEALKRSTLLNPNQRLPKVEILRSAIQYIERLQALLSSLNQEERDLRYRGGGGPQPMVPSECNSHSASCSPEWGNALEFGPNPGDHLLAADPTDAHNLHSLTSIVDSITVEDMSVAFPDETMPN | null | null | cell cycle [GO:0007049]; cellular response to estradiol stimulus [GO:0071392]; cellular response to growth factor stimulus [GO:0071363]; cellular response to lithium ion [GO:0071285]; cellular response to tumor necrosis factor [GO:0071356]; muscle cell differentiation [GO:0042692]; muscle organ development [GO:0007517]... | nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-DNA complex [GO:0032993] | chromatin DNA binding [GO:0031490]; cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA-binding transcription activator activity [GO:0001216]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding tran... | PF01586;PF00010; | 4.10.280.10; | null | PTM: Phosphorylated by CAMK2G on threonine and serine amino acids in a muscle activity-dependent manner. Phosphorylation of Thr-87 impairs both DNA-binding and trans-activation functions in contracting muscles (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:16424906}. Note=Recruited to late myogenic gene promoter regulatory sequences with SMARCA4/BRG1/BAF190A and SWI/SNF chromatin-remodeling enzymes to promote chromatin-remodeling and transcription initiation in developing embryos. | null | null | null | null | null | FUNCTION: Acts as a transcriptional activator that promotes transcription of muscle-specific target genes and plays a role in muscle differentiation, cell cycle exit and muscle atrophy. Essential for the development of functional embryonic skeletal fiber muscle differentiation. However is dispensable for postnatal skel... | Mus musculus (Mouse) |
P12980 | LYL1_HUMAN | MCPPQAQAEVGPTMTEKAEMVCAPSPAPAPPPKPASPGPPQVEEVGHRGGSSPPRLPPGVPVISLGHSRPPGVAMPTTELGTLRPPLLQLSTLGTAPPTLALHYHPHPFLNSVYIGPAGPFSIFPSSRLKRRPSHCELDLAEGHQPQKVARRVFTNSRERWRQQNVNGAFAELRKLLPTHPPDRKLSKNEVLRLAMKYIGFLVRLLRDQAAALAAGPTPPGPRKRPVHRVPDDGARRGSGRRAEAAARSQPAPPADPDGSPGGAARPIKMEQTALSPEVR | null | null | B cell differentiation [GO:0030183]; blood vessel maturation [GO:0001955]; definitive hemopoiesis [GO:0060216]; positive regulation of DNA-templated transcription [GO:0045893]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357] | chromatin [GO:0000785]; nucleoplasm [GO:0005654] | DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00010; | 4.10.280.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981}. | null | null | null | null | null | null | Homo sapiens (Human) |
P12982 | PP12_DROME | MGDVMNIDSIISRLLEVRGARPGKNVQLSEGEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYSENFFLLRGNHECASINRIYGFYDECKRRYSIKLWKTFTDCFNCLPVAAIVDEKIFCCHGGLSPDLTSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDTMGWGENDRGVSFTFGAEVVAKFLQKHEFDLICRAHQVVEDGYEFFAKRMLVTLFSAPNYCGEFDNAGAMMSVDDTLMCSFQILKPADKRKK | 3.1.3.16 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Binds 2 manganese ions per subunit. {ECO:0000250}; | adult locomotory behavior [GO:0008344]; axon guidance [GO:0007411]; chromosome condensation [GO:0030261]; chromosome segregation [GO:0007059]; learning or memory [GO:0007611]; locomotion [GO:0040011]; mitotic cell cycle [GO:0000278]; mitotic metaphase chromosome alignment [GO:0007080]; nervous system development [GO:00... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; polytene chromosome [GO:0005700]; protein phosphatase type 1 complex [GO:0000164] | metal ion binding [GO:0046872]; myosin phosphatase activity [GO:0017018]; protein serine/threonine phosphatase activity [GO:0004722] | PF00149;PF16891; | 3.60.21.10; | PPP phosphatase family, PP-1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000269|PubMed:18412953}; CATALYTIC ACTIVITY: Reaction=H... | null | null | null | null | FUNCTION: Is essential for the regulation of mitotic chromosomal segregation as well as regulation of chromatin condensation during interphase. {ECO:0000269|PubMed:1330679, ECO:0000269|PubMed:2175717}. | Drosophila melanogaster (Fruit fly) |
P12995 | BIOA_ECOLI | MTTDDLAFDQRHIWHPYTSMTSPLPVYPVVSAEGCELILSDGRRLVDGMSSWWAAIHGYNHPQLNAAMKSQIDAMSHVMFGGITHAPAIELCRKLVAMTPQPLECVFLADSGSVAVEVAMKMALQYWQAKGEARQRFLTFRNGYHGDTFGAMSVCDPDNSMHSLWKGYLPENLFAPAPQSRMDGEWDERDMVGFARLMAAHRHEIAAVIIEPIVQGAGGMRMYHPEWLKRIRKICDREGILLIADEIATGFGRTGKLFACEHAEIAPDILCLGKALTGGTMTLSATLTTREVAETISNGEAGCFMHGPTFMGNPLACAAA... | 2.6.1.62 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:1092681}; | biotin biosynthetic process [GO:0009102] | cytoplasm [GO:0005737] | adenosylmethionine-8-amino-7-oxononanoate transaminase activity [GO:0004015]; dethiobiotin synthase activity [GO:0004141]; protein homodimerization activity [GO:0042803]; pyridoxal phosphate binding [GO:0030170] | PF00202; | 3.90.1150.10;3.40.640.10; | Class-III pyridoxal-phosphate-dependent aminotransferase family, BioA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=(8S)-8-amino-7-oxononanoate + S-adenosyl-L-methionine = (7R,8S)-7,8-diammoniononanoate + S-adenosyl-4-methylsulfanyl-2-oxobutanoate; Xref=Rhea:RHEA:16861, ChEBI:CHEBI:16490, ChEBI:CHEBI:59789, ChEBI:CHEBI:149468, ChEBI:CHEBI:149469; EC=2.6.1.62; Evidence={ECO:0000269|PubMed:1092681, ECO:000... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.2 uM for KAPA {ECO:0000269|PubMed:1092682, ECO:0000269|PubMed:12379100}; KM=150 uM for SAM {ECO:0000269|PubMed:1092682, ECO:0000269|PubMed:12379100}; KM=21 uM for pyridoxamine phosphate (PMP) {ECO:0000269|PubMed:1092682, ECO:0000269|PubMed:12379100}; KM=32 uM for... | PATHWAY: Cofactor biosynthesis; biotin biosynthesis; 7,8-diaminononanoate from 8-amino-7-oxononanoate (SAM route): step 1/1. | null | null | FUNCTION: Catalyzes the transfer of the alpha-amino group from S-adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid (KAPA) to form 7,8-diaminopelargonic acid (DAPA) (PubMed:1092681, PubMed:1092682). It is the only animotransferase known to utilize SAM as an amino donor (PubMed:1092681, PubMed:1092682). Comple... | Escherichia coli (strain K12) |
P12996 | BIOB_ECOLI | MAHRPRWTLSQVTELFEKPLLDLLFEAQQVHRQHFDPRQVQVSTLLSIKTGACPEDCKYCPQSSRYKTGLEAERLMEVEQVLESARKAKAAGSTRFCMGAAWKNPHERDMPYLEQMVQGVKAMGLEACMTLGTLSESQAQRLANAGLDYYNHNLDTSPEFYGNIITTRTYQERLDTLEKVRDAGIKVCSGGIVGLGETVKDRAGLLLQLANLPTPPESVPINMLVKVKGTPLADNDDVDAFDFIRTIAVARIMMPTSYVRLSAGREQMNEQTQAMCFMAGANSIFYGCKLLTTPNPEEDKDLQLFRKLGLNPQQTAVLAG... | 2.8.1.6 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000269|PubMed:8142361}; Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine. {ECO:0000269|PubMed:8142361}; COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:00... | biotin biosynthetic process [GO:0009102] | null | 2 iron, 2 sulfur cluster binding [GO:0051537]; 4 iron, 4 sulfur cluster binding [GO:0051539]; biotin synthase activity [GO:0004076]; iron ion binding [GO:0005506]; protein homodimerization activity [GO:0042803] | PF06968;PF04055; | 3.20.20.70; | Radical SAM superfamily, Biotin synthase family | null | null | CATALYTIC ACTIVITY: Reaction=(4R,5S)-dethiobiotin + [sulfur carrier]-SH + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2 5'-deoxyadenosine + [sulfur carrier]-H + biotin + 2 L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:22060, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, Rhea:RHEA-COMP:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2 uM for dethiobiotin {ECO:0000269|PubMed:8142361}; | PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 2/2. | null | null | FUNCTION: Catalyzes the conversion of dethiobiotin (DTB) to biotin by the insertion of a sulfur atom into dethiobiotin via a radical-based mechanism. {ECO:0000269|PubMed:8142361}. | Escherichia coli (strain K12) |
P12998 | BIOF_ECOLI | MSWQEKINAALDARRAADALRRRYPVAQGAGRWLVADDRQYLNFSSNDYLGLSHHPQIIRAWQQGAEQFGIGSGGSGHVSGYSVVHQALEEELAEWLGYSRALLFISGFAANQAVIAAMMAKEDRIAADRLSHASLLEAASLSPSQLRRFAHNDVTHLARLLASPCPGQQMVVTEGVFSMDGDSAPLAEIQQVTQQHNGWLMVDDAHGTGVIGEQGRGSCWLQKVKPELLVVTFGKGFGVSGAAVLCSSTVADYLLQFARHLIYSTSMPPAQAQALRASLAVIRSDEGDARREKLAALITRFRAGVQDLPFTLADSCSAI... | 2.3.1.47 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:10642176}; | biotin biosynthetic process [GO:0009102] | null | 8-amino-7-oxononanoate synthase activity [GO:0008710]; protein homodimerization activity [GO:0042803]; pyridoxal phosphate binding [GO:0030170] | PF00155; | 3.90.1150.10;3.40.640.10; | Class-II pyridoxal-phosphate-dependent aminotransferase family, BioF subfamily | null | null | CATALYTIC ACTIVITY: Reaction=6-carboxyhexanoyl-[ACP] + H(+) + L-alanine = (8S)-8-amino-7-oxononanoate + CO2 + holo-[ACP]; Xref=Rhea:RHEA:42288, Rhea:RHEA-COMP:9685, Rhea:RHEA-COMP:9955, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57972, ChEBI:CHEBI:64479, ChEBI:CHEBI:78846, ChEBI:CHEBI:149468; EC=2.3.1.47; Eviden... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=25 uM for pimeloyl-CoA (at pH 7.5 and at 30 degrees Celsius) {ECO:0000269|PubMed:10642176}; KM=0.5 uM for L-alanine (at pH 7.5 and at 30 degrees Celsius) {ECO:0000269|PubMed:10642176}; | PATHWAY: Cofactor biosynthesis; biotin biosynthesis. {ECO:0000305|PubMed:3058702}. | null | null | FUNCTION: Catalyzes the decarboxylative condensation of pimeloyl-[acyl-carrier protein] and L-alanine to produce 8-amino-7-oxononanoate (AON), [acyl-carrier protein], and carbon dioxide. Can also use pimeloyl-CoA instead of pimeloyl-ACP as substrate, but it is believed that pimeloyl-ACP rather than pimeloyl-CoA is the ... | Escherichia coli (strain K12) |
P13000 | BIOD1_ECOLI | MSKRYFVTGTDTEVGKTVASCALLQAAKAAGYRTAGYKPVASGSEKTPEGLRNSDALALQRNSSLQLDYATVNPYTFAEPTSPHIISAQEGRPIESLVMSAGLRALEQQADWVLVEGAGGWFTPLSDTFTFADWVTQEQLPVILVVGVKLGCINHAMLTAQVIQHAGLTLAGWVANDVTPPGKRHAEYMTTLTRMIPAPLLGEIPWLAENPENAATGKYINLALL | 6.3.3.3 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_00336, ECO:0000269|PubMed:7669756, ECO:0000269|PubMed:7881906, ECO:0000269|PubMed:9576910, ECO:0000269|PubMed:9865950}; Note=Binds 1 Mg(2+) per subunit, in one structure a second Mg(2+) was seen. {ECO:0000269|PubMed:7669756, ECO:0000269|... | biotin biosynthetic process [GO:0009102] | cytosol [GO:0005829] | ATP binding [GO:0005524]; dethiobiotin synthase activity [GO:0004141]; magnesium ion binding [GO:0000287]; protein homodimerization activity [GO:0042803] | PF13500; | 3.40.50.300; | Dethiobiotin synthetase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00336}. | CATALYTIC ACTIVITY: Reaction=(7R,8S)-7,8-diammoniononanoate + ATP + CO2 = (4R,5S)-dethiobiotin + ADP + 3 H(+) + phosphate; Xref=Rhea:RHEA:15805, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:149469, ChEBI:CHEBI:149473, ChEBI:CHEBI:456216; EC=6.3.3.3; Evidence={ECO:0000255|HAMAP... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=15.2 uM for DAPA (at pH 7.5, 37 degrees Celsius) {ECO:0000269|PubMed:25801336}; KM=600 uM for NaHCO3 (at pH 7.5, 37 degrees Celsius) {ECO:0000269|PubMed:25801336}; KM=10.5 uM for ATP (at pH 7.5, 37 degrees Celsius) {ECO:0000269|PubMed:25801336}; KM=1.1 mM for CTP (... | PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00336}. | null | null | FUNCTION: Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring. Only CTP can partially replace ATP while diaminobiotin is only 37% as effective as 7,8-diaminope... | Escherichia coli (strain K12) |
P13001 | BIOH_ECOLI | MNNIWWQTKGQGNVHLVLLHGWGLNAEVWRCIDEELSSHFTLHLVDLPGFGRSRGFGALSLADMAEAVLQQAPDKAIWLGWSLGGLVASQIALTHPERVQALVTVASSPCFSARDEWPGIKPDVLAGFQQQLSDDFQRTVERFLALQTMGTETARQDARALKKTVLALPMPEVDVLNGGLEILKTVDLRQPLQNVSMPFLRLYGYLDGLVPRKVVPMLDKLWPHSESYIFAKAAHAPFISHPAEFCHLLVALKQRV | 3.1.1.85 | null | biotin biosynthetic process [GO:0009102] | cytoplasm [GO:0005737] | carboxylic ester hydrolase activity [GO:0052689]; pimelyl-[acyl-carrier protein] methyl ester esterase activity [GO:0090499] | PF00561; | 3.40.50.1820; | AB hydrolase superfamily, Carboxylesterase BioH family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=6-carboxyhexanoyl-[ACP] methyl ester + H2O = 6-carboxyhexanoyl-[ACP] + H(+) + methanol; Xref=Rhea:RHEA:42700, Rhea:RHEA-COMP:9955, Rhea:RHEA-COMP:10186, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17790, ChEBI:CHEBI:78846, ChEBI:CHEBI:82735; EC=3.1.1.85; Evidence={ECO:0000269|PubMed:1... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=229 uM for DMB-S-MMP (at Ph 7.9 and at room temperature) {ECO:0000269|PubMed:12732651, ECO:0000269|PubMed:17625941, ECO:0000269|PubMed:19307763}; KM=0.29 mM for pNP-acetate {ECO:0000269|PubMed:12732651, ECO:0000269|PubMed:17625941, ECO:0000269|PubMed:19307763}; KM=... | PATHWAY: Cofactor biosynthesis; biotin biosynthesis. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0-8.5. The activity is more than 90% in the pH range from 7 to 9. {ECO:0000269|PubMed:12732651, ECO:0000269|PubMed:17625941, ECO:0000269|PubMed:19307763}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is between 20 and 30 degrees Celsius. {ECO:0000269|PubMed:12732651, ECO:0000269|PubMed:17625941, ECO:0000269|PubMed:19307763}; | FUNCTION: The physiological role of BioH is to remove the methyl group introduced by BioC when the pimeloyl moiety is complete. It allows to synthesize pimeloyl-ACP via the fatty acid synthetic pathway through the hydrolysis of the ester bonds of pimeloyl-ACP esters. E.coli employs a methylation and demethylation strat... | Escherichia coli (strain K12) |
P13002 | ELF1_DROME | MSTSTATTSVITSNELSLSGHAHGHGHAHQLHQHTHSRLGVGVGVGILSDASLSPIQQGSGGHSGGGNTNSSPLAPNGVPLLTTMHRSPDSPQPELATMTNVNVLDLHTDNSKLYDKEAVFIYETPKVVMPADGGGGNNSDEGHAIDARIAAQMGNQAQQQQQQQQQTEHQPLAKIEFDENQIIRVVGPNGEQQQIISREIINGEHHILSRNEAGEHILTRIVSDPSKLMPNDNAVATAMYNQAQKMNNDHGQAVYQTSPLPLDASVLHYSGGNDSNVIKTEADIYEDHKKHAAAAAAAAGGGSIIYTTSDPNGVNVKQL... | null | null | chitin-based cuticle development [GO:0040003]; chitin-based embryonic cuticle biosynthetic process [GO:0008362]; epithelial cell morphogenesis [GO:0003382]; fibroblast growth factor receptor signaling pathway [GO:0008543]; ganglion mother cell fate determination [GO:0007402]; membrane organization [GO:0061024]; nervous... | nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein homodimerization activity [GO:0042803]; RNA polymerase II c... | PF04516; | null | Grh/CP2 family, Grainyhead subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20599892, ECO:0000269|PubMed:2792757}. | null | null | null | null | null | FUNCTION: Transcription factor that binds a CNS-specific regulatory element of the Dopa decarboxylase (Ddc) gene. Also interacts with sequences adjacent to other transcription units, including Ultrabithorax (Ubx) and engrailed (en). Activity in vivo may be required only at high levels transiently to activate the expres... | Drosophila melanogaster (Fruit fly) |
P13009 | METH_ECOLI | MSSKVEQLRAQLNERILVLDGGMGTMIQSYRLNEADFRGERFADWPCDLKGNNDLLVLSKPEVIAAIHNAYFEAGADIIETNTFNSTTIAMADYQMESLSAEINFAAAKLARACADEWTARTPEKPRYVAGVLGPTNRTASISPDVNDPAFRNITFDGLVAAYRESTKALVEGGADLILIETVFDTLNAKAAVFAVKTEFEALGVELPIMISGTITDASGRTLSGQTTEAFYNSLRHAEALTFGLNCALGPDELRQYVQELSRIAECYVTAHPNAGLPNAFGEYDLDADTMAKQIREWAQAGFLNIVGGCCGTTPQHIAA... | 2.1.1.13 | COFACTOR: Name=methylcob(III)alamin; Xref=ChEBI:CHEBI:28115; Evidence={ECO:0000269|PubMed:7992050}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:9398304}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:9398304}; | homocysteine metabolic process [GO:0050667]; methionine biosynthetic process [GO:0009086]; methylation [GO:0032259]; tetrahydrofolate interconversion [GO:0035999]; tetrahydrofolate metabolic process [GO:0046653] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | cobalamin binding [GO:0031419]; methionine synthase activity [GO:0008705]; zinc ion binding [GO:0008270] | PF02310;PF02607;PF02965;PF00809;PF02574; | 3.40.50.280;1.10.288.10;3.20.20.20;3.20.20.330;1.10.1240.10;3.10.196.10; | Vitamin-B12 dependent methionine synthase family | null | null | CATALYTIC ACTIVITY: Reaction=(6S)-5-methyl-5,6,7,8-tetrahydrofolate + L-homocysteine = (6S)-5,6,7,8-tetrahydrofolate + L-methionine; Xref=Rhea:RHEA:11172, ChEBI:CHEBI:18608, ChEBI:CHEBI:57453, ChEBI:CHEBI:57844, ChEBI:CHEBI:58199; EC=2.1.1.13; Evidence={ECO:0000269|PubMed:8652590, ECO:0000269|PubMed:9201956}; | null | PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetH route): step 1/1. | null | null | FUNCTION: Catalyzes the transfer of a methyl group from methyl-cobalamin to homocysteine, yielding enzyme-bound cob(I)alamin and methionine. Subsequently, remethylates the cofactor using methyltetrahydrofolate. {ECO:0000269|PubMed:8652590, ECO:0000269|PubMed:9201956}. | Escherichia coli (strain K12) |
P13010 | XRCC5_HUMAN | MVRSGNKAAVVLCMDVGFTMSNSIPGIESPFEQAKKVITMFVQRQVFAENKDEIALVLFGTDGTDNPLSGGDQYQNITVHRHLMLPDFDLLEDIESKIQPGSQQADFLDALIVSMDVIQHETIGKKFEKRHIEIFTDLSSRFSKSQLDIIIHSLKKCDISLQFFLPFSLGKEDGSGDRGDGPFRLGGHGPSFPLKGITEQQKEGLEIVKMVMISLEGEDGLDEIYSFSESLRKLCVFKKIERHSIHWPCRLTIGSNLSIRIAAYKSILQERVKKTWTVVDAKTLKKEDIQKETVYCLNDDDETEVLKEDIIQGFRYGSDI... | 3.6.4.- | null | activation of innate immune response [GO:0002218]; cellular hyperosmotic salinity response [GO:0071475]; cellular response to fatty acid [GO:0071398]; cellular response to gamma radiation [GO:0071480]; cellular response to leukemia inhibitory factor [GO:1990830]; cellular response to X-ray [GO:0071481]; DNA damage resp... | chromosome, telomeric region [GO:0000781]; cytosol [GO:0005829]; DNA-dependent protein kinase complex [GO:0070418]; DNA-dependent protein kinase-DNA ligase 4 complex [GO:0005958]; extracellular region [GO:0005576]; Ku70:Ku80 complex [GO:0043564]; membrane [GO:0016020]; nonhomologous end joining complex [GO:0070419]; nu... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent activity, acting on DNA [GO:0008094]; damaged DNA binding [GO:0003684]; DNA binding [GO:0003677]; DNA end binding [GO:0045027]; DNA helicase activity [GO:0003678]; double-stranded DNA binding [GO:0003690]; enzyme activator activity [GO:000804... | PF02735;PF03730;PF03731;PF08785; | 1.10.1600.10;2.40.290.10;1.25.40.240;3.40.50.410; | Ku80 family | PTM: ADP-ribosylated by PARP3. {ECO:0000269|PubMed:24598253}.; PTM: Phosphorylated on serine residues. Phosphorylation by PRKDC may enhance helicase activity. {ECO:0000269|PubMed:10026262}.; PTM: Sumoylated. {ECO:0000269|PubMed:15561718}.; PTM: Ubiquitinated by RNF8 via 'Lys-48'-linked ubiquitination following DNA dama... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:22442688, ECO:0000269|PubMed:32103174}. Nucleus, nucleolus {ECO:0000269|PubMed:22002106, ECO:0000269|PubMed:32103174}. Chromosome {ECO:0000269|PubMed:22442688}. | null | null | null | null | null | FUNCTION: Single-stranded DNA-dependent ATP-dependent helicase that plays a key role in DNA non-homologous end joining (NHEJ) by recruiting DNA-PK to DNA (PubMed:11493912, PubMed:12145306, PubMed:7957065, PubMed:8621488). Required for double-strand break repair and V(D)J recombination (PubMed:11493912, PubMed:12145306,... | Homo sapiens (Human) |
P13011 | SCD2_MOUSE | MPAHILQEISGAYSATTTITAPPSGGQQNGGEKFEKSSHHWGADVRPELKDDLYDPTYQDDEGPPPKLEYVWRNIILMALLHLGALYGITLVPSCKLYTCLFAYLYYVISALGITAGAHRLWSHRTYKARLPLRLFLIIANTMAFQNDVYEWARDHRAHHKFSETHADPHNSRRGFFFSHVGWLLVRKHPAVKEKGGKLDMSDLKAEKLVMFQRRYYKPGLLLMCFVLPTLVPWYCWGETFVNSLCVSTFLRYAVVLNATWLVNSAAHLYGYRPYDKNISSRENILVSMGAVGEGFHNYHHAFPYDYSASEYRWHINFTT... | 1.14.19.1 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:P13516}; Note=Expected to bind 2 Fe(2+) ions per subunit. {ECO:0000250|UniProtKB:P13516}; | monounsaturated fatty acid biosynthetic process [GO:1903966]; response to fatty acid [GO:0070542]; unsaturated fatty acid biosynthetic process [GO:0006636] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789] | iron ion binding [GO:0005506]; palmitoyl-CoA 9-desaturase activity [GO:0032896]; stearoyl-CoA 9-desaturase activity [GO:0004768] | PF00487; | null | Fatty acid desaturase type 1 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:16443825}; Multi-pass membrane protein {ECO:0000305|PubMed:16443825}. Microsome membrane {ECO:0000269|PubMed:16443825}. | CATALYTIC ACTIVITY: Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 + octadecanoyl-CoA = (9Z)-octadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:19721, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI... | null | null | null | null | FUNCTION: Stearoyl-CoA desaturase that utilizes O(2) and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates (PubMed:16443825). Catalyzes the insertion of a cis double bond at the delta-9 position into fatty acyl-CoA substrates including palmitoyl-CoA and ste... | Mus musculus (Mouse) |
P13020 | GELS_MOUSE | MAPYRSSLLCALLLLALCALSPSHAATTSRGRAQERAPQSRVSEARPSTMVVEHPEFLKAGKEPGLQIWRVEKFDLVPVPPNLYGDFFTGDAYVILKTVQLRNGNLQYDLHYWLGNECSQDESGAAAIFTVQLDDYLNGRAVQHREVQGFESSTFSGYFKSGLKYKKGGVASGFKHVVPNEVVVQRLFQVKGRRVVRATEVPVSWDSFNNGDCFILDLGNNIYQWCGSGSNKFERLKATQVSKGIRDNERSGRAQVHVSEEGGEPEAMLQVLGPKPALPEGTEDTAKEDAANRRLAKLYKVSNGAGSMSVSLVADENPFA... | null | null | actin cytoskeleton organization [GO:0030036]; actin filament capping [GO:0051693]; actin filament depolymerization [GO:0030042]; actin filament polymerization [GO:0030041]; actin filament severing [GO:0051014]; actin polymerization or depolymerization [GO:0008154]; amyloid fibril formation [GO:1990000]; barbed-end acti... | actin cap [GO:0030478]; actin cytoskeleton [GO:0015629]; apical ectoplasmic specialization [GO:0061831]; basal ectoplasmic specialization [GO:0061832]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; glial filament [GO:0097426]; lamellipodium [GO:003002... | actin binding [GO:0003779]; actin filament binding [GO:0051015]; calcium ion binding [GO:0005509]; myosin II binding [GO:0045159]; phosphatidylinositol 3-kinase catalytic subunit binding [GO:0036313]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546] | PF00626; | 3.40.20.10; | Villin/gelsolin family | PTM: Phosphorylated on tyrosine residues in vitro. {ECO:0000250}. | SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytoskeleton.; SUBCELLULAR LOCATION: [Isoform 1]: Secreted. | null | null | null | null | null | FUNCTION: Calcium-regulated, actin-modulating protein that binds to the plus (or barbed) ends of actin monomers or filaments, preventing monomer exchange (end-blocking or capping). It can promote the assembly of monomers into filaments (nucleation) as well as sever filaments already formed (By similarity). Plays a role... | Mus musculus (Mouse) |
P13021 | CAPZB_DICDI | MTEKQLSCCLDLMRRLPPSQIEDNLAGLLDLVPDLTEDLLSSIDQPLKVAYDAVSKKDYLLCDYNRDADSYRSPWSNKYDPPLSGACYPSSKLRDIEVQANEIFEIYLNLYFEGGVSSVYCWDLDDNFAAVVLMKKTQDQSKKGQPMRGTWDSIHVVEVKLGKKDKAVYKLTSTVMLSIETDNDNTGKVNLAGSLTRQDEKEYTFNEVDTHCVNIGKMVEDMESKLRQTLETIYFGKTKEVVNTLRNATGNSELEKRKNLSNQIGSAIGNRG | null | null | actin cytoskeleton organization [GO:0030036]; barbed-end actin filament capping [GO:0051016]; cell morphogenesis [GO:0000902]; negative regulation of filopodium assembly [GO:0051490]; regulation of lamellipodium assembly [GO:0010591]; response to bacterium [GO:0009617] | cortical actin cytoskeleton [GO:0030864]; cytosol [GO:0005829]; F-actin capping protein complex [GO:0008290] | actin filament binding [GO:0051015]; lipid binding [GO:0008289] | PF01115; | 1.20.58.570;3.90.1150.210; | F-actin-capping protein beta subunit family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. | null | null | null | null | null | FUNCTION: F-actin-capping proteins bind in a Ca(2+)-independent manner to the fast growing ends of actin filaments (barbed end) thereby blocking the exchange of subunits at these ends. Unlike other capping proteins (such as gelsolin and severin), these proteins do not sever actin filaments. {ECO:0000269|PubMed:8982279}... | Dictyostelium discoideum (Social amoeba) |
P13029 | KATG_ECOLI | MSTSDDIHNTTATGKCPFHQGGHDQSAGAGTTTRDWWPNQLRVDLLNQHSNRSNPLGEDFDYRKEFSKLDYYGLKKDLKALLTESQPWWPADWGSYAGLFIRMAWHGAGTYRSIDGRGGAGRGQQRFAPLNSWPDNVSLDKARRLLWPIKQKYGQKISWADLFILAGNVALENSGFRTFGFGAGREDVWEPDLDVNWGDEKAWLTHRHPEALAKAPLGATEMGLIYVNPEGPDHSGEPLSAAAAIRATFGNMGMNDEETVALIAGGHTLGKTHGAGPTSNVGPDPEAAPIEEQGLGWASTYGSGVGADAITSGLEVVWTQ... | 1.11.1.21 | COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000269|PubMed:374409}; Note=Binds 2 heme B (iron-protoporphyrin IX) groups per tetramer. {ECO:0000269|PubMed:374409}; | cellular response to hydrogen peroxide [GO:0070301]; hydrogen peroxide catabolic process [GO:0042744]; response to oxidative stress [GO:0006979] | cytosol [GO:0005829] | catalase activity [GO:0004096]; heme binding [GO:0020037]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]; peroxidase activity [GO:0004601] | PF00141; | 1.10.520.10;1.10.420.10; | Peroxidase family, Peroxidase/catalase subfamily | PTM: The N-terminus is blocked.; PTM: Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not the peroxidase activity of the enzyme. {ECO:0000255|HAMAP-Rule:MF_01961}. | null | CATALYTIC ACTIVITY: Reaction=AH2 + H2O2 = A + 2 H2O; Xref=Rhea:RHEA:30275, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:17499; EC=1.11.1.21; Evidence={ECO:0000255|HAMAP-Rule:MF_01961}; CATALYTIC ACTIVITY: Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, C... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=35 mM for H(2)O(2) for the catalase reaction (at pH 5.5-6.0) {ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:374409}; KM=4.2 mM for H(2)O(2) for the catalase reaction (at pH 7.0) {ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:374409}; KM=3.9 mM for H(2)O(2) for ... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.25 for the peroxidase reaction and 7.5 for the catalase reaction. {ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:374409}; | null | FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Also displays NADH oxidase, INH lyase and isonicotinoyl-NAD synthase activities. {ECO:0000269|PubMed:18178143, ECO:0000269|PubMed:23416055, ECO:0000269|PubMed:374409}. | Escherichia coli (strain K12) |
P13035 | GLPD_ECOLI | METKDLIVIGGGINGAGIAADAAGRGLSVLMLEAQDLACATSSASSKLIHGGLRYLEHYEFRLVSEALAEREVLLKMAPHIAFPMRFRLPHRPHLRPAWMIRIGLFMYDHLGKRTSLPGSTGLRFGANSVLKPEIKRGFEYSDCWVDDARLVLANAQMVVRKGGEVLTRTRATSARRENGLWIVEAEDIDTGKKYSWQARGLVNATGPWVKQFFDDGMHLPSPYGIRLIKGSHIVVPRVHTQKQAYILQNEDKRIVFVIPWMDEFSIIGTTDVEYKGDPKAVKIEESEINYLLNVYNTHFKKQLSRDDIVWTYSGVRPLC... | 1.1.5.3 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; | glycerol catabolic process [GO:0019563]; glycerol-3-phosphate catabolic process [GO:0046168] | glycerol-3-phosphate dehydrogenase complex [GO:0009331]; plasma membrane [GO:0005886] | electron transfer activity [GO:0009055]; FAD binding [GO:0071949]; glycerol-3-phosphate dehydrogenase (quinone) activity [GO:0004368]; protein homodimerization activity [GO:0042803] | PF01266;PF16901; | 6.10.250.1890;1.10.8.870;3.30.9.10;3.50.50.60; | FAD-dependent glycerol-3-phosphate dehydrogenase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=a quinone + sn-glycerol 3-phosphate = a quinol + dihydroxyacetone phosphate; Xref=Rhea:RHEA:18977, ChEBI:CHEBI:24646, ChEBI:CHEBI:57597, ChEBI:CHEBI:57642, ChEBI:CHEBI:132124; EC=1.1.5.3; | null | PATHWAY: Polyol metabolism; glycerol degradation via glycerol kinase pathway; glycerone phosphate from sn-glycerol 3-phosphate (aerobic route): step 1/1. | null | null | FUNCTION: Conversion of glycerol 3-phosphate to dihydroxyacetone. Uses molecular oxygen or nitrate as electron acceptor. | Escherichia coli (strain K12) |
P13036 | FECA_ECOLI | MTPLRVFRKTTPLVNTIRLSLLPLAGLSFSAFAAQVNIAPGSLDKALNQYAAHSGFTLSVDASLTRGKQSNGLHGDYDVESGLQQLLDGSGLQVKPLGNNSWTLEPAPAPKEDALTVVGDWLGDARENDVFEHAGARDVIRREDFAKTGATTMREVLNRIPGVSAPENNGTGSHDLAMNFGIRGLNPRLASRSTVLMDGIPVPFAPYGQPQLSLAPVSLGNMDAIDVVRGGGAVRYGPQSVGGVVNFVTRAIPQDFGIEAGVEGQLSPTSSQNNPKETHNLMVGGTADNGFGTALLYSGTRGSDWREHSATRIDDLMLKS... | null | null | intracellular iron ion homeostasis [GO:0006879]; iron ion transport [GO:0006826]; regulation of DNA-templated transcription [GO:0006355]; response to iron ion starvation [GO:1990641]; siderophore-dependent iron import into cell [GO:0033214]; signal transduction involved in regulation of gene expression [GO:0023019] | cell outer membrane [GO:0009279]; membrane [GO:0016020]; transmembrane transporter complex [GO:1902495] | siderophore-iron transmembrane transporter activity [GO:0015343]; signaling receptor activity [GO:0038023] | PF07715;PF07660;PF00593; | 3.55.50.30;2.40.170.20;2.170.130.10; | TonB-dependent receptor family | null | SUBCELLULAR LOCATION: Cell outer membrane {ECO:0000255|PROSITE-ProRule:PRU01360}; Multi-pass membrane protein {ECO:0000255|PROSITE-ProRule:PRU01360}. | null | null | null | null | null | FUNCTION: FecA is the outer membrane receptor protein in the Fe(3+) dicitrate transport system. | Escherichia coli (strain K12) |
P13039 | FES_ECOLI | MTALKVGSESWWQSKHGPEWQRLNDEMFEVTFWWRDPQGSEEYSTIKRVWVYITGVTDHHQNSQPQSMQRIAGTNVWQWTTQLNANWRGSYCFIPTERDDIFSVPSPDRLELREGWRKLLPQAIADPLNLQSWKGGRGHAVSALEMPQAPLQPGWDCPQAPEIPAKEIIWKSERLKKSRRVWIFTTGDATAEERPLAVLLDGEFWAQSMPVWPVLTSLTHRQQLPPAVYVLIDAIDTTHRAHELPCNADFWLAVQQELLPLVKAIAPFSDRADRTVVAGQSFGGLSALYAGLHWPERFGCVLSQSGSYWWPHRGGQQEGV... | 3.1.1.108 | null | enterobactin catabolic process [GO:0046214]; siderophore-dependent iron import into cell [GO:0033214] | cytoplasm [GO:0005737] | enterochelin esterase activity [GO:0008849]; iron ion binding [GO:0005506] | PF11806;PF00756; | 3.40.50.1820;2.60.40.10; | Fes family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:1534808}. | CATALYTIC ACTIVITY: Reaction=Fe(III)-enterobactin + H(+) + 3 H2O = Fe(III)-[N-(2,3-dihydroxybenzoyl)-L-serine] + 2 N-(2,3-dihydroxybenzoyl)-L-serine; Xref=Rhea:RHEA:30111, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28199, ChEBI:CHEBI:58154, ChEBI:CHEBI:143010; EC=3.1.1.108; Evidence={ECO:0000269|PubMed:150859, E... | null | null | null | null | FUNCTION: Catalyzes the hydrolysis of ferric enterobactin (Fe-Ent) (PubMed:150859, PubMed:1534808, PubMed:8148617). Is responsible for the release of iron from ferric enterobactin (PubMed:1534808). Also catalyzes the hydrolysis of iron-free enterobactin (Ent) (PubMed:150859, PubMed:1534808, PubMed:8148617). Cleavage of... | Escherichia coli (strain K12) |
P13051 | UNG_HUMAN | MIGQKTLYSFFSPSPARKRHAPSPEPAVQGTGVAGVPEESGDAAAIPAKKAPAGQEEPGTPPSSPLSAEQLDRIQRNKAAALLRLAARNVPVGFGESWKKHLSGEFGKPYFIKLMGFVAEERKHYTVYPPPHQVFTWTQMCDIKDVKVVILGQDPYHGPNQAHGLCFSVQRPVPPPPSLENIYKELSTDIEDFVHPGHGDLSGWAKQGVLLLNAVLTVRAHQANSHKERGWEQFTDAVVSWLNQNSNGLVFLLWGSYAQKKGSAIDRKRHHVLQTAHPSPLSVYRGFFGCRHFSKTNELLQKSGKKPIDWKEL | 3.2.2.27 | null | base-excision repair [GO:0006284]; base-excision repair, AP site formation via deaminated base removal [GO:0097510]; depyrimidination [GO:0045008]; isotype switching [GO:0045190]; negative regulation of apoptotic process [GO:0043066]; somatic hypermutation of immunoglobulin genes [GO:0016446] | mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | damaged DNA binding [GO:0003684]; ribosomal small subunit binding [GO:0043024]; uracil DNA N-glycosylase activity [GO:0004844] | PF03167; | 3.40.470.10; | Uracil-DNA glycosylase (UDG) superfamily, UNG family | PTM: Isoform 1 is processed by cleavage of a transit peptide. | SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion.; SUBCELLULAR LOCATION: [Isoform 2]: Nucleus. | CATALYTIC ACTIVITY: Reaction=Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.; EC=3.2.2.27; Evidence={ECO:0000255|HAMAP-Rule:MF_03166}; | null | null | null | null | FUNCTION: Excises uracil residues from the DNA which can arise as a result of misincorporation of dUMP residues by DNA polymerase or due to deamination of cytosine. | Homo sapiens (Human) |
P13053 | VDR_RAT | MEATAASTSLPDPGDFDRNVPRICGVCGDRATGFHFNAMTCEGCKGFFRRSMKRKALFTCPFNGDCRITKDNRRHCQACRLKRCVDIGMMKEFILTDEEVQRKREMIMKRKEEEALKDSLRPKLSEEQQHIIAILLDAHHKTYDPTYADFRDFRPPVRMDGSTGSYSPRPTLSFSGNSSSSSSDLYTTSLDMMEPSGFSNLDLNGEDSDDPSVTLDLSPLSMLPHLADLVSYSIQKVIGFAKMIPGFRDLTSDDQIVLLKSSAIEVIMLRSNQSFTMDDMSWDCGSQDYKYDVTDVSKAGHTLELIEPLIKFQVGLKKLN... | null | null | animal organ morphogenesis [GO:0009887]; apoptotic process involved in mammary gland involution [GO:0060057]; apoptotic signaling pathway [GO:0097190]; bile acid signaling pathway [GO:0038183]; calcium ion transport [GO:0006816]; cell differentiation [GO:0030154]; cell morphogenesis [GO:0000902]; cellular response to a... | dense fibrillar component [GO:0001651]; euchromatin [GO:0000791]; heterochromatin [GO:0000792]; nuclear matrix [GO:0016363]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; receptor complex [GO:0043235]; RNA polymerase II transcription regulator complex [GO:0090575]; T-tubule [GO:0030315] | calcitriol binding [GO:1902098]; DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; lithocholic acid binding [GO:1902121]; lithocholic acid receptor activity [GO:0038186]; nuclear receptor activity [GO:0004879]; nuclear retinoid X receptor binding [GO:0046965]; RNA polymerase II cis-regul... | PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR1 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P11473, ECO:0000255|PROSITE-ProRule:PRU00407}. Cytoplasm {ECO:0000250|UniProtKB:P11473}. Note=Localizes mainly to the nucleus. Translocated into the nucleus via both ligand-dependent and ligand-independent pathways; ligand-independent nuclear translocation is mediate... | null | null | null | null | null | FUNCTION: Nuclear receptor for calcitriol, the active form of vitamin D3 which mediates the action of this vitamin on cells (PubMed:17227670). Enters the nucleus upon vitamin D3 binding where it forms heterodimers with the retinoid X receptor/RXR (By similarity). The VDR-RXR heterodimers bind to specific response eleme... | Rattus norvegicus (Rat) |
P13055 | E75BB_DROME | MEAVQAAAAATSSGGSSGSVPGSGSGSASKLIKTEPIDFEMLHLEENERQQDIEREPSSSNSNSNSNSLTPQRYTHVQVQTVPPRQPTGLTTPGGTQKVILTPRVEYVQQRATSSTGGGMKHVYSQQQGTAASRSAPPETTALLTTTSGTPQIIITRTLPSNQHLSRRHSASPSALHHYQQQQPQRQQSPPPLHHQQQQQQQHVRVIRDGRLYDEATVVVAARRHSVSPPPLHHHSRSAPVSPVIARRGGAAAYMDQQYQQRQTPPLAPPPPPPPPPPPPPPPQQQQQQYISTGVPPPTAAARKFVVSTSTRHVNVIASN... | null | null | cell differentiation [GO:0030154]; ecdysis, chitin-based cuticle [GO:0018990]; hormone-mediated signaling pathway [GO:0009755]; molting cycle, chitin-based cuticle [GO:0007591]; negative regulation of peptidoglycan recognition protein signaling pathway [GO:0061060]; negative regulation of transcription by RNA polymeras... | nucleus [GO:0005634] | DNA binding [GO:0003677]; heme binding [GO:0020037]; nuclear receptor activity [GO:0004879]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; zinc ion binding [GO:0008270] | PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR1 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}. | null | null | null | null | null | FUNCTION: Implicated in the regulation of ecdysone-triggered gene hierarchies. Probably plays a key role in mediating the regulation of the larval molt by 20-OH-ecdysone. {ECO:0000269|PubMed:8223281}. | Drosophila melanogaster (Fruit fly) |
P13056 | NR2C1_HUMAN | MATIEEIAHQIIEQQMGEIVTEQQTGQKIQIVTALDHNTQGKQFILTNHDGSTPSKVILARQDSTPGKVFLTTPDAAGVNQLFFTTPDLSAQHLQLLTDNSPDQGPNKVFDLCVVCGDKASGRHYGAVTCEGCKGFFKRSIRKNLVYSCRGSKDCIINKHHRNRCQYCRLQRCIAFGMKQDSVQCERKPIEVSREKSSNCAASTEKIYIRKDLRSPLTATPTFVTDSESTRSTGLLDSGMFMNIHPSGVKTESAVLMTSDKAESCQGDLSTLANVVTSLANLGKTKDLSQNSNEMSMIESLSNDDTSLCEFQEMQTNGDV... | null | null | cell differentiation [GO:0030154]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of retinoic acid receptor signaling pathway [GO:0048386] | chromatin [GO:0000785]; nucleoplasm [GO:0005654]; PML body [GO:0016605] | DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; histone deacetylase binding [GO:0042826]; nuclear receptor activity [GO:0004879]; nuclear steroid receptor activity [GO:000... | PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR2 subfamily | PTM: Sumoylation requires both PIAS1 and UBE2I. Sumoylation appears to dissociate NR2C1 from the PML nuclear bodies. Enhances the interaction with NRIP1 but inhibits interaction with KAT2B. In proliferating cells, stimulation by all-trans retinoic acid, activation of MAPK1-mediated phosphorylation and recruitment to PM... | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}. Nucleus, PML body {ECO:0000250}. Note=Recruited by HDAC3, after all-trans retinoic acid stimulated MAPK1-mediated Thr-223 phosphorylation, to PML bodies for subsequent sumoylation. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Orphan nuclear receptor. Binds the IR7 element in the promoter of its own gene in an autoregulatory negative feedback mechanism. Primarily repressor of a broad range of genes. Binds to hormone response elements (HREs) consisting of two 5'-AGGTCA-3' half site direct repeat consensus sequences. Together with NR... | Homo sapiens (Human) |
P13073 | COX41_HUMAN | MLATRVFSLVGKRAISTSVCVRAHESVVKSEDFSLPAYMDRRDHPLPEVAHVKHLSASQKALKEKEKASWSSLSMDEKVELYRIKFKESFAEMNRGSNEWKTVVGGAMFFIGFTALVIMWQKHYVYGPLPQSFDKEWVAKQTKRMLDMKVNPIQGLASKWDYEKNEWKK | null | null | cellular respiration [GO:0045333]; generation of precursor metabolites and energy [GO:0006091]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123] | cytosol [GO:0005829]; membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966]; mitochondrial respiratory chain complex IV [GO:0005751]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654] | cytochrome-c oxidase activity [GO:0004129] | PF02936; | 1.10.442.10; | Cytochrome c oxidase IV family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:30030519}; Single-pass membrane protein {ECO:0000269|PubMed:30030519}. | null | null | PATHWAY: Energy metabolism; oxidative phosphorylation. {ECO:0000250|UniProtKB:P00424}. | null | null | FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, comple... | Homo sapiens (Human) |
P13084 | NPM_RAT | MEDSMDMDMSPLRPQNYLFGCELKADKDYHFKVDNDENEHQLSLRTVSLGAGAKDELHIVEAEAMNYEGSPIKVTLATLKMSVQPTVSLGGFEITPPVVLRLKCGSGPVHISGQHLVAVEEDAESEDEDEEDVKLLGMSGKRSAPGGGNKVPQKKVKLDEDDDEDDEDDEDDEDDDDDDFDEEETEEKVPVKKSVRDTPAKNAQKSNQNGKDLKPSTPRSKGQESFKKQEKTPKTPKGPSSVEDIKAKMQASIEKGGSLPKVEAKFINYVKNCFRMTDQEAIQDLWQWRKSL | null | null | cardiac muscle hypertrophy [GO:0003300]; cell volume homeostasis [GO:0006884]; cellular response to hypoxia [GO:0071456]; cellular response to testosterone stimulus [GO:0071394]; cellular response to UV [GO:0034644]; cellular senescence [GO:0090398]; centrosome cycle [GO:0007098]; chromatin remodeling [GO:0006338]; cle... | centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; granular component [GO:0001652]; large ribosomal subunit [GO:0015934]; nuclear matrix [GO:0016363]; nuclear speck [GO:0016607]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; protein-... | ATP binding [GO:0005524]; chromatin binding [GO:0003682]; core promoter sequence-specific DNA binding [GO:0001046]; DNA binding [GO:0003677]; DNA-binding transcription factor binding [GO:0140297]; enzyme binding [GO:0019899]; histone binding [GO:0042393]; identical protein binding [GO:0042802]; molecular condensate sca... | PF16276;PF03066; | 1.10.10.2100;2.60.120.340; | Nucleoplasmin family | PTM: Acetylated at C-terminal lysine residues, thereby increasing affinity to histones. {ECO:0000250|UniProtKB:P06748}.; PTM: ADP-ribosylated. {ECO:0000250|UniProtKB:P06748}.; PTM: Phosphorylated at Ser-4 by PLK1 and PLK2. Phosphorylation at Ser-4 by PLK2 in S phase is required for centriole duplication and is sufficie... | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000250|UniProtKB:P06748}. Nucleus, nucleoplasm {ECO:0000250|UniProtKB:P06748}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:P06748}. Note=Generally nucleolar, but is translocated to the nucleoplasm in case of serum starvation or... | null | null | null | null | null | FUNCTION: Involved in diverse cellular processes such as ribosome biogenesis, centrosome duplication, protein chaperoning, histone assembly, cell proliferation, and regulation of tumor suppressors p53/TP53 and ARF. Binds ribosome presumably to drive ribosome nuclear export. Associated with nucleolar ribonucleoprotein s... | Rattus norvegicus (Rat) |
P13085 | PTHR_RAT | MLRRLVQQWSVLVFLLSYSVPSRGRSVEGLGRRLKRAVSEHQLLHDKGKSIQDLRRRFFLHHLIAEIHTAEIRATSEVSPNSKPAPNTKNHPVRFGSDDEGRYLTQETNKVETYKEQPLKTPGKKKKGKPGKRREQEKKKRRTRSAWPGTTGSGLLEDPQPHTSPTSTSLEPSSRTH | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; bone mineralization [GO:0030282]; chondrocyte differentiation [GO:0002062]; endochondral ossification [GO:0001958]; endoderm development [GO:0007492]; lung alveolus development [GO:0048286]; lung epithelial cell differentiation [GO:... | cytoplasm [GO:0005737]; extracellular region [GO:0005576]; nucleus [GO:0005634] | hormone activity [GO:0005179]; peptide hormone receptor binding [GO:0051428] | PF01279; | null | Parathyroid hormone family | PTM: There are several secretory forms, including osteostatin, arising from endoproteolytic cleavage of the initial translation product. Each of these secretory forms is believed to have one or more of its own receptors that mediates the normal paracrine, autocrine and endocrine actions (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. Secreted {ECO:0000250}. | null | null | null | null | null | FUNCTION: Neuroendocrine peptide which is a critical regulator of cellular and organ growth, development, migration, differentiation and survival and of epithelial calcium ion transport. Regulates endochondral bone development and epithelial-mesenchymal interactions during the formation of the mammary glands and teethR... | Rattus norvegicus (Rat) |
P13086 | SUCA_RAT | MTAAVVAAAATATMVSGSSGLAAARLLSRTFLLQQNGIRHGSYTASRKNIYIDKNTKVICQGFTGKQGTFHSQQALEYGTKLVGGTTPGKGGKKHLGLPVFNTVKEAKEKTGATASVIYVPPPFAAAAINEAIDAEIPLVVCITEGIPQQDMVRVKHKLTRQGKTRLIGPNCPGIINPGECKIGIMPGHIHKKGRIGIVSRSGTLTYEAVHQTTQVGLGQSLCIGIGGDPFNGTNFIDCLDVFLKDPATEGIVLIGEIGGHAEENAAEFLKEHNSGPKAKPVVSFIAGITAPPGRRMGHAGAIIAGGKGGAKEKISALQS... | 6.2.1.4; 6.2.1.5 | null | succinate metabolic process [GO:0006105]; succinyl-CoA metabolic process [GO:0006104]; tricarboxylic acid cycle [GO:0006099] | cytosol [GO:0005829]; mitochondrion [GO:0005739]; protein-containing complex [GO:0032991]; succinate-CoA ligase complex (ADP-forming) [GO:0009361]; succinate-CoA ligase complex (GDP-forming) [GO:0045244] | GDP binding [GO:0019003]; protein-containing complex binding [GO:0044877]; succinate-CoA ligase (ADP-forming) activity [GO:0004775]; succinate-CoA ligase (GDP-forming) activity [GO:0004776] | PF02629;PF00549; | 3.40.50.720;3.40.50.261; | Succinate/malate CoA ligase alpha subunit family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000255|HAMAP-Rule:MF_03222}. | CATALYTIC ACTIVITY: Reaction=ATP + CoA + succinate = ADP + phosphate + succinyl-CoA; Xref=Rhea:RHEA:17661, ChEBI:CHEBI:30031, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:456216; EC=6.2.1.5; Evidence={ECO:0000255|HAMAP-Rule:MF_03222}; CATALYTIC ACTIVITY: Reaction=CoA + GTP + s... | null | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinate from succinyl-CoA (ligase route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_03222}. | null | null | FUNCTION: Succinyl-CoA synthetase functions in the citric acid cycle (TCA), coupling the hydrolysis of succinyl-CoA to the synthesis of either ATP or GTP and thus represents the only step of substrate-level phosphorylation in the TCA. The alpha subunit of the enzyme binds the substrates coenzyme A and phosphate, while ... | Rattus norvegicus (Rat) |
P13096 | ESM5_DROME | MAPQSNNSTTFVSKTQHYLKVKKPLLERQRRARMNKCLDTLKTLVAEFQGDDAILRMDKAEMLEAALVFMRKQVVKQQAPVSPLPMDSFKNGYMNAVSEISRVMACTPAMSVDVGKTVMTHLGVEFQRMLQADQVQTSVTTSTPRPLSPASSGYHSDNEDSQSAASPKPVEETMWRPW | null | null | anterior/posterior pattern specification [GO:0009952]; cell differentiation [GO:0030154]; nervous system development [GO:0007399]; regulation of neurogenesis [GO:0050767]; regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; RNA polymerase II cis-regulatory region sequence-sp... | PF07527;PF00010; | 4.10.280.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Participates in the control of cell fate choice by uncommitted neuroectodermal cells in the embryo. Transcriptional repressor. Binds DNA on N-box motifs: 5'-CACNAG-3'. {ECO:0000269|PubMed:2540957}. | Drosophila melanogaster (Fruit fly) |
P13097 | ESM7_DROME | MATKYEMSKTYQYRKVMKPLLERKRRARINKCLDELKDLMAECVAQTGDAKFEKADILEVTVQHLRKLKESKKHVPANPEQSFRAGYIRAANEVSRALASLPRVDVAFGTTLMTHLGMRLNQLEQPMEQPQAVNTPLSIVCGSSSSSSTYSSASSCSSISPVSSGYASDNESLLQISSPGQVWRPW | null | null | anterior/posterior pattern specification [GO:0009952]; cell differentiation [GO:0030154]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nervous system development [GO:0007399]; regulation of neurogenesis [GO:0050767]; regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription factor binding [GO:0140297]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-s... | PF07527;PF00010; | 4.10.280.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Participates in the control of cell fate choice by uncommitted neuroectodermal cells in the embryo. Transcriptional repressor. Binds DNA on N-box motifs: 5'-CACNAG-3'. | Drosophila melanogaster (Fruit fly) |
P13098 | ESM8_DROME | MEYTTKTQIYQKVKKPMLERQRRARMNKCLDNLKTLVAELRGDDGILRMDKAEMLESAVIFMRQQKTPKKVAQEEQSLPLDSFKNGYMNAVNEVSRVMASTPGMSVDLGKSVMTHLGRVYKNLQQFHEAQSAADFIQNSMDCSSMDKAPLSPASSGYHSDCDSPAPSPQPMQQPLWRPW | null | null | anterior/posterior pattern specification [GO:0009952]; compound eye development [GO:0048749]; dendrite morphogenesis [GO:0048813]; mesoderm development [GO:0007498]; negative regulation of gene expression [GO:0010629]; regulation of neurogenesis [GO:0050767]; regulation of transcription by RNA polymerase II [GO:0006357... | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; RNA polymerase II cis-regulatory region sequence-sp... | PF07527;PF00010; | 4.10.280.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Participates in the control of cell fate choice by uncommitted neuroectodermal cells in the embryo (PubMed:2540957). Transcriptional repressor (PubMed:8001118). Binds DNA on N-box motifs: 5'-CACNAG-3' (PubMed:8001118). Part of the Notch signaling pathway (PubMed:22357926). {ECO:0000269|PubMed:22357926, ECO:00... | Drosophila melanogaster (Fruit fly) |
P13099 | TOP3_YEAST | MKVLCVAEKNSIAKAVSQILGGGRSTSRDSGYMYVKNYDFMFSGFPFARNGANCEVTMTSVAGHLTGIDFSHDSHGWGKCAIQELFDAPLNEIMNNNQKKIASNIKREARNADYLMIWTDCDREGEYIGWEIWQEAKRGNRLIQNDQVYRAVFSHLERQHILNAARNPSRLDMKSVHAVGTRIEIDLRAGVTFTRLLTETLRNKLRNQATMTKDGAKHRGGNKNDSQVVSYGTCQFPTLGFVVDRFERIRNFVPEEFWYIQLVVENKDNGGTTTFQWDRGHLFDRLSVLTFYETCIETAGNVAQVVDLKSKPTTKYRPLP... | 5.6.2.1 | null | DNA recombination [GO:0006310]; DNA repair [GO:0006281]; DNA topological change [GO:0006265]; double-strand break repair via homologous recombination [GO:0000724]; mitotic sister chromatid cohesion [GO:0007064]; reciprocal meiotic recombination [GO:0007131]; regulation of DNA recombination [GO:0000018]; telomere mainte... | nucleus [GO:0005634]; RecQ family helicase-topoisomerase III complex [GO:0031422] | DNA binding [GO:0003677]; DNA topoisomerase activity [GO:0003916]; DNA topoisomerase type I (single strand cut, ATP-independent) activity [GO:0003917] | PF01131;PF01751; | 3.40.50.140;1.10.460.10;2.70.20.10;1.10.290.10; | Type IA topoisomerase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.; EC=5.6.2.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU10131}; | null | null | null | null | FUNCTION: Releases the supercoiling and torsional tension of DNA introduced during the DNA replication and transcription by transiently cleaving and rejoining one strand of the DNA duplex. Introduces a single-strand break via transesterification at a target site in duplex DNA. The scissile phosphodiester is attacked by... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P13107 | CP2B3_RAT | MDTSVLLLLAVLLSFLLFLVRGHAKVHGHLPPGPRPLPLLGNLLQMDRGGFRKSFIQLQEKHGDVFTVYFGPRPVVMLCGTQTIREALVDHAEAFSGRGIIAVLQPIMQEYGVSFVNEERWKILRRLFVATMRDFGIGKQSVEDQIKEEAKCLVEELKNHQGVSLDPTFLFQCVTGNIICSIVFGERFDYRDRQFLRLLDLLYRTFSLISSFSSQMFEVYSDFLKYFPGVHREIYKNLKEVLDYIDHSVENHRATLDPNAPRDFIDTFLLHMEKEKLNHYTEFHHWNLMISVLFLFLAGTESTSNTLCYGFLLMLKYPHV... | 1.14.14.1 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; | cellular ketone metabolic process [GO:0042180]; epoxygenase P450 pathway [GO:0019373]; response to bacterium [GO:0009617]; response to organic cyclic compound [GO:0014070]; response to xenobiotic stimulus [GO:0009410]; steroid metabolic process [GO:0008202]; xenobiotic catabolic process [GO:0042178]; xenobiotic metabol... | cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231] | anandamide 11,12 epoxidase activity [GO:0062188]; anandamide 14,15 epoxidase activity [GO:0062189]; anandamide 8,9 epoxidase activity [GO:0062187]; arachidonic acid epoxygenase activity [GO:0008392]; aromatase activity [GO:0070330]; estrogen 2-hydroxylase activity [GO:0101021]; heme binding [GO:0020037]; iron ion bindi... | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57... | null | null | null | null | FUNCTION: Cytochromes P450 are a group of heme-thiolate monooxygenases. In liver microsomes, this enzyme is involved in an NADPH-dependent electron transport pathway. It oxidizes a variety of structurally unrelated compounds, including steroids, fatty acids, and xenobiotics. | Rattus norvegicus (Rat) |
P13109 | FGF2_RAT | MAAGSITSLPALPEDGGGAFPPGHFKDPKRLYCKNGGFFLRIHPDGRVDGVREKSDPHVKLQLQAEERGVVSIKGVCANRYLAMKEDGRLLASKCVTEECFFFERLESNNYNTYRSRKYSSWYVALKRTGQYKLGSKTGPGQKAILFLPMSAKS | null | null | angiogenesis [GO:0001525]; angiogenesis involved in coronary vascular morphogenesis [GO:0060978]; animal organ morphogenesis [GO:0009887]; branching involved in ureteric bud morphogenesis [GO:0001658]; canonical Wnt signaling pathway [GO:0060070]; cell differentiation [GO:0030154]; cell migration involved in sprouting ... | cytoplasm [GO:0005737]; extracellular space [GO:0005615]; nucleus [GO:0005634] | chemoattractant activity [GO:0042056]; chemokine binding [GO:0019956]; cytokine activity [GO:0005125]; fibroblast growth factor receptor binding [GO:0005104]; growth factor activity [GO:0008083]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; integrin binding [GO:0005178]; nuclear receptor coacti... | PF00167; | 2.80.10.50; | Heparin-binding growth factors family | PTM: Phosphorylation at Tyr-81 regulates FGF2 unconventional secretion. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P09038}. Nucleus {ECO:0000250|UniProtKB:P09038}. Note=Exported from cells by an endoplasmic reticulum (ER)/Golgi-independent mechanism (By similarity). Unconventional secretion of FGF2 occurs by direct translocation across the plasma membrane (By similarity). Bindin... | null | null | null | null | null | FUNCTION: Acts as a ligand for FGFR1, FGFR2, FGFR3 and FGFR4 (By similarity). Also acts as an integrin ligand which is required for FGF2 signaling (By similarity). Binds to integrin ITGAV:ITGB3 (By similarity). Plays an important role in the regulation of cell survival, cell division, cell differentiation and cell migr... | Rattus norvegicus (Rat) |
P13114 | CHSY_ARATH | MVMAGASSLDEIRQAQRADGPAGILAIGTANPENHVLQAEYPDYYFRITNSEHMTDLKEKFKRMCDKSTIRKRHMHLTEEFLKENPHMCAYMAPSLDTRQDIVVVEVPKLGKEAAVKAIKEWGQPKSKITHVVFCTTSGVDMPGADYQLTKLLGLRPSVKRLMMYQQGCFAGGTVLRIAKDLAENNRGARVLVVCSEITAVTFRGPSDTHLDSLVGQALFSDGAAALIVGSDPDTSVGEKPIFEMVSAAQTILPDSDGAIDGHLREVGLTFHLLKDVPGLISKNIVKSLDEAFKPLGISDWNSLFWIAHPGGPAILDQVE... | 2.3.1.74 | null | auxin polar transport [GO:0009926]; flavonoid biosynthetic process [GO:0009813]; polyketide biosynthetic process [GO:0030639]; regulation of anthocyanin biosynthetic process [GO:0031540]; response to auxin [GO:0009733]; response to gravity [GO:0009629]; response to jasmonic acid [GO:0009753]; response to oxidative stre... | endoplasmic reticulum [GO:0005783]; nucleus [GO:0005634]; plant-type vacuole membrane [GO:0009705] | chalcone synthase activity [GO:0102128]; naringenin-chalcone synthase activity [GO:0016210] | PF02797;PF00195; | 3.40.47.10; | Thiolase-like superfamily, Chalcone/stilbene synthases family | null | null | CATALYTIC ACTIVITY: Reaction=4-coumaroyl-CoA + 2 H(+) + 3 malonyl-CoA = 2',4,4',6'-tetrahydroxychalcone + 3 CO2 + 4 CoA; Xref=Rhea:RHEA:11128, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57355, ChEBI:CHEBI:57384, ChEBI:CHEBI:77645; EC=2.3.1.74; Evidence={ECO:0000255|PROSITE-ProRule:PRU10023}; | null | PATHWAY: Secondary metabolite biosynthesis; flavonoid biosynthesis. | null | null | FUNCTION: The primary product of this enzyme is 4,2',4',6'-tetrahydroxychalcone (also termed naringenin-chalcone or chalcone) which can under specific conditions spontaneously isomerize into naringenin. | Arabidopsis thaliana (Mouse-ear cress) |
P13128 | TACY_LISMO | MKKIMLVFITLILVSLPIAQQTEAKDASAFNKENSISSMAPPASPPASPKTPIEKKHADEIDKYIQGLDYNKNNVLVYHGDAVTNVPPRKGYKDGNEYIVVEKKKKSINQNNADIQVVNAISSLTYPGALVKANSELVENQPDVLPVKRDSLTLSIDLPGMTNQDNKIVVKNATKSNVNNAVNTLVERWNEKYAQAYPNVSAKIDYDDEMAYSESQLIAKFGTAFKAVNNSLNVNFGAISEGKMQEEVISFKQIYYNVNVNEPTRPSRFFGKAVTKEQLQALGVNAENPPAYISSVAYGRQVYLKLSTNSHSTKVKAAFD... | null | null | killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020] | cholesterol binding [GO:0015485]; identical protein binding [GO:0042802]; toxin activity [GO:0090729] | PF17440;PF01289; | 3.30.1040.20;3.40.30.40;2.60.40.1430;3.90.840.10; | Cholesterol-dependent cytolysin family | PTM: Phosphorylated. Phosphorylation does not appear to be required for ubiquitination or degradation. {ECO:0000269|PubMed:16441444}.; PTM: Ubiquitinated. {ECO:0000269|PubMed:16441444}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:24751541, ECO:0000269|PubMed:3110067}. Host membrane {ECO:0000269|PubMed:24751541, ECO:0000269|PubMed:3110067}; Multi-pass membrane protein {ECO:0000269|PubMed:3110067}. Host cell membrane {ECO:0000269|PubMed:3110067}; Multi-pass membrane protein {ECO:0000269|PubMed:31... | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5. Cytolytic activity is undetectable at pH 7.0. {ECO:0000269|PubMed:3110067}; | null | FUNCTION: A cholesterol-dependent pore-forming toxin, which is a major virulence factor required for the escape of bacteria from phagosomal vacuoles and entry into the host cytosol. After binding to target membranes, the protein undergoes a major conformation change, leading to its insertion in the host membrane and fo... | Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e) |
P13134 | KEX2_YEAST | MKVRKYITLCFWWAFSTSALVSSQQIPLKDHTSRQYFAVESNETLSRLEEMHPNWKYEHDVRGLPNHYVFSKELLKLGKRSSLEELQGDNNDHILSVHDLFPRNDLFKRLPVPAPPMDSSLLPVKEAEDKLSINDPLFERQWHLVNPSFPGSDINVLDLWYNNITGAGVVAAIVDDGLDYENEDLKDNFCAEGSWDFNDNTNLPKPRLSDDYHGTRCAGEIAAKKGNNFCGVGVGYNAKISGIRILSGDITTEDEAASLIYGLDVNDIYSCSWGPADDGRHLQGPSDLVKKALVKGVTEGRDSKGAIYVFASGNGGTRGD... | 3.4.21.61 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 3 Ca(2+) ions per subunit.; | peptide hormone processing [GO:0016486]; peptide pheromone maturation [GO:0007323]; protein processing [GO:0016485] | extracellular space [GO:0005615]; fungal-type vacuole [GO:0000324]; membrane [GO:0016020]; trans-Golgi network [GO:0005802] | metal ion binding [GO:0046872]; serine-type endopeptidase activity [GO:0004252] | PF01483;PF00082; | 2.60.120.260;3.40.50.200; | Peptidase S8 family, Furin subfamily | PTM: O-glycosylated. | SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane; Single-pass type I membrane protein. | CATALYTIC ACTIVITY: Reaction=Cleavage of -Lys-Arg-|-Xaa- and -Arg-Arg-|-Xaa- bonds to process yeast alpha-factor pheromone and killer toxin precursors.; EC=3.4.21.61; | null | null | null | null | FUNCTION: Processing of precursors of alpha-factors and killer toxin. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P13164 | IFM1_HUMAN | MHKEEHEVAVLGPPPSTILPRSTVINIHSETSVPDHVVWSLFNTLFLNWCCLGFIAFAYSVKSRDRKMVGDVTGAQAYASTAKCLNIWALILGILMTIGFILLLVFGSVTVYHIMLQIIQEKRGY | null | null | cell surface receptor signaling pathway [GO:0007166]; defense response to virus [GO:0051607]; negative regulation of cell migration [GO:0030336]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of viral entry into host cell [GO:0046597]; negative regulation of viral genome replica... | lysosomal membrane [GO:0005765]; membrane [GO:0016020]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991] | null | PF04505; | null | CD225/Dispanin family | PTM: Palmitoylation on membrane-proximal cysteines controls clustering in membrane compartments and antiviral activity. {ECO:0000305|PubMed:26354436}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1383329, ECO:0000269|PubMed:19499152, ECO:0000269|PubMed:25105503, ECO:0000269|PubMed:26354436}; Single-pass membrane protein {ECO:0000269|PubMed:19499152}. Lysosome membrane {ECO:0000269|PubMed:26354436}. | null | null | null | null | null | FUNCTION: IFN-induced antiviral protein which inhibits the entry of viruses to the host cell cytoplasm, permitting endocytosis, but preventing subsequent viral fusion and release of viral contents into the cytosol. Active against multiple viruses, including influenza A virus, SARS coronaviruses (SARS-CoV and SARS-CoV-2... | Homo sapiens (Human) |
P13180 | GLYCO_CHAV | MTSSVTISVVLLISFITPLYSYLSIAFPENTKLDWKPVTKNTRYCPMGGEWFLEPGLQEESFLSSTPIGATPSKSDGFLCHAAKWVTTCDFRWYGPKYITHSIHNIKPTRSDCDTALASYKSGTLVSLGFPPESCGYASVTDSEFLVIMITPHHVGVDDYRGHWVDPLFVGGECDQSYCDTIHNSSVWIPADQTKKNICGQSFTPLTVTVAYDKTKEIAAGGIVFKSKYHSHMEGARTCRLSYCGRNGIKFPNGEWVSLDVKTRIQEKHLLPLFKECPAGTEVRSTLQSDGAQVLTSEIQRILDYSLCQNTWDKVERKEP... | null | null | symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062] | membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF00974; | 2.30.29.130;2.30.30.640; | Vesiculovirus glycoprotein family | PTM: Glycosylated by host. Palmitoylated by host on Cys-498 (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Virion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. | null | null | null | null | null | FUNCTION: Attaches the virus to host cellular receptor, inducing endocytosis of the virion. In the endosome, the acidic pH induces conformational changes in the glycoprotein trimer, which trigger fusion between virus and cell membrane (By similarity). {ECO:0000250}. | Chandipura virus (strain I653514) (CHPV) |
P13183 | COX7B_BOVIN | MFPLAKNALSRLRVQSIQQAVARQIHQKRAPDFHDKYGNAVLASGATFCVAVWVYMATQIGIEWNPSPVGRVTPKEWREQ | null | null | central nervous system development [GO:0007417]; mitochondrial electron transport, cytochrome c to oxygen [GO:0006123] | mitochondrial respirasome [GO:0005746]; mitochondrion [GO:0005739]; respiratory chain complex IV [GO:0045277] | null | PF05392; | 4.10.51.10; | Cytochrome c oxidase VIIb family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:31533957}; Single-pass membrane protein {ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:31533957}. | null | null | PATHWAY: Energy metabolism; oxidative phosphorylation. {ECO:0000305|PubMed:27605664}. | 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... | Bos taurus (Bovine) |
P13185 | KIN1_YEAST | MDDYHVNTAFSMGRGNQQDDGNSESNSMHTQPSTMAPATLRMMGKSPQQQQQQNTPLMPPADIKYANNGNSHQAEQKERQVELEGKSRENAPKPNTTSQSRVSSSQGMPKQFHRKSLGDWEFVETVGAGSMGKVKLAKHRYTNEVCAVKIVNRATKAFLHKEQMLPPPKNEQDVLERQKKLEKEISRDKRTIREASLGQILYHPHICRLFEMCTLSNHFYMLFEYVSGGQLLDYIIQHGSIREHQARKFARGIASALIYLHANNIVHRDLKIENIMISDSSEIKIIDFGLSNIYDSRKQLHTFCGSLYFAAPELLKANPY... | 2.7.11.1 | null | exocytosis [GO:0006887]; intracellular signal transduction [GO:0035556]; microtubule cytoskeleton organization [GO:0000226]; phosphorylation [GO:0016310]; positive regulation of exocytosis [GO:0045921]; positive regulation of IRE1-mediated unfolded protein response [GO:1903896] | cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; tau-protein kinase activity [GO:0050321] | PF02149;PF00069; | 3.30.310.80;1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family, NIM1 subfamily | PTM: Autophosphorylated. {ECO:0000269|PubMed:1652871}. | SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Serine/threonine protein kinase involved in the regulation of exocytosis. Induces phosphorylation of SEC9 and its release from the plasma membrane to the cytosol. {ECO:0000269|PubMed:15563607, ECO:0000269|PubMed:1652871, ECO:0000269|PubMed:8203145}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P13186 | KIN2_YEAST | MPNPNTADYLVNPNFRTSKGGSLSPTPEAFNDTRVAAPATLRMMGKQSGPRNDQQQAPLMPPADIKQGKEQAAQRQNDASRPNGAVELRQFHRRSLGDWEFLETVGAGSMGKVKLVKHRQTKEICVIKIVNRASKAYLHKQHSLPSPKNESEILERQKRLEKEIARDKRTVREASLGQILYHPHICRLFEMCTMSNHFYMLFEYVSGGQLLDYIIQHGSLKEHHARKFARGIASALQYLHANNIVHRDLKIENIMISSSGEIKIIDFGLSNIFDYRKQLHTFCGSLYFAAPELLKAQPYTGPEVDIWSFGIVLYVLVCGK... | 2.7.11.1 | null | exocytosis [GO:0006887]; intracellular signal transduction [GO:0035556]; microtubule cytoskeleton organization [GO:0000226]; phosphorylation [GO:0016310]; positive regulation of exocytosis [GO:0045921]; positive regulation of IRE1-mediated unfolded protein response [GO:1903896] | cellular bud neck [GO:0005935]; cellular bud tip [GO:0005934]; cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; tau-protein kinase activity [GO:0050321] | PF02149;PF00069; | 3.30.310.80;1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family, NIM1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Peripheral membrane protein; Cytoplasmic side. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Serine/threonine protein kinase involved in the regulation of exocytosis. Induces phosphorylation of SEC9 and its release from the plasma membrane to the cytosol. {ECO:0000269|PubMed:15563607, ECO:0000269|PubMed:8203145}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P13195 | HEM1_RAT | METVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMEVGAKPAPRTVSTSAAQCQQVKETPPANEKEKTAKAAVQQAPDESQMAQTPDGTQLPPGHPSPSTSQSSGSKCPFLAAQLSQTGSSVFRKASLELQEDVQEMHAVRKEVAQSPVLPSLVNAKRDGEGPSPLLKNFQDIMRKQRPERVSHLLQDNLPKSVSTFQYDHFFEKKIDEKKNDHTYRVFKTVNRRAQIFPMADDYTDSLITKKQVSVWCSNDYLGMSRHPRVCGAVIETVKQHGAGAGGTRNISGTSKFHVELEQELADLHGKDAALLFSSCFVANDS... | 2.3.1.37 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:P13196}; | cellular response to insulin stimulus [GO:0032869]; cellular response to organic cyclic compound [GO:0071407]; erythrocyte development [GO:0048821]; heme A biosynthetic process [GO:0006784]; heme B biosynthetic process [GO:0006785]; heme biosynthetic process [GO:0006783]; heme O biosynthetic process [GO:0048034]; hemog... | mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | 5-aminolevulinate synthase activity [GO:0003870]; identical protein binding [GO:0042802]; pyridoxal phosphate binding [GO:0030170] | PF00155;PF09029; | 3.90.1150.10;3.40.640.10; | Class-II pyridoxal-phosphate-dependent aminotransferase family | PTM: In normoxia, is hydroxylated at Pro-578, promoting interaction with VHL, initiating ubiquitination and subsequent degradation via the proteasome. {ECO:0000250|UniProtKB:P13196}.; PTM: Ubiquitinated; in normoxia following hydroxylation and interaction with VHL, leading to its subsequent degradation via the proteaso... | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P22557}; Peripheral membrane protein {ECO:0000250|UniProtKB:P22557}. Note=Localizes to the matrix side of the mitochondrion inner membrane. {ECO:0000250|UniProtKB:P22557}. | CATALYTIC ACTIVITY: Reaction=glycine + H(+) + succinyl-CoA = 5-aminolevulinate + CO2 + CoA; Xref=Rhea:RHEA:12921, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:57305, ChEBI:CHEBI:356416; EC=2.3.1.37; Evidence={ECO:0000250|UniProtKB:P13196}; PhysiologicalDirection=left-to-right;... | null | PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from glycine: step 1/1. | null | null | FUNCTION: Catalyzes the pyridoxal 5'-phosphate (PLP)-dependent condensation of succinyl-CoA and glycine to form aminolevulinic acid (ALA), with CoA and CO2 as by-products. {ECO:0000250|UniProtKB:P13196}. | Rattus norvegicus (Rat) |
P13196 | HEM1_HUMAN | MESVVRRCPFLSRVPQAFLQKAGKSLLFYAQNCPKMMEVGAKPAPRALSTAAVHYQQIKETPPASEKDKTAKAKVQQTPDGSQQSPDGTQLPSGHPLPATSQGTASKCPFLAAQMNQRGSSVFCKASLELQEDVQEMNAVRKEVAETSAGPSVVSVKTDGGDPSGLLKNFQDIMQKQRPERVSHLLQDNLPKSVSTFQYDRFFEKKIDEKKNDHTYRVFKTVNRRAHIFPMADDYSDSLITKKQVSVWCSNDYLGMSRHPRVCGAVMDTLKQHGAGAGGTRNISGTSKFHVDLERELADLHGKDAALLFSSCFVANDSTL... | 2.3.1.37 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000305|PubMed:16234850}; | erythrocyte development [GO:0048821]; heme A biosynthetic process [GO:0006784]; heme B biosynthetic process [GO:0006785]; heme biosynthetic process [GO:0006783]; heme O biosynthetic process [GO:0048034]; hemoglobin biosynthetic process [GO:0042541]; protoporphyrinogen IX biosynthetic process [GO:0006782]; response to b... | cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654] | 5-aminolevulinate synthase activity [GO:0003870]; identical protein binding [GO:0042802]; pyridoxal phosphate binding [GO:0030170] | PF00155;PF09029; | 3.90.1150.10;3.40.640.10; | Class-II pyridoxal-phosphate-dependent aminotransferase family | PTM: In normoxia, is hydroxylated at Pro-576, promoting interaction with VHL, initiating ubiquitination and subsequent degradation via the proteasome. {ECO:0000269|PubMed:16234850}.; PTM: Ubiquitinated; in normoxia following hydroxylation and interaction with VHL, leading to its subsequent degradation via the proteasom... | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P22557}; Peripheral membrane protein {ECO:0000250|UniProtKB:P22557}. Note=Localizes to the matrix side of the mitochondrion inner membrane. {ECO:0000250|UniProtKB:P22557}. | CATALYTIC ACTIVITY: Reaction=glycine + H(+) + succinyl-CoA = 5-aminolevulinate + CO2 + CoA; Xref=Rhea:RHEA:12921, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:57305, ChEBI:CHEBI:356416; EC=2.3.1.37; Evidence={ECO:0000269|PubMed:16234850, ECO:0000269|PubMed:17975826}; Physiolog... | null | PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from glycine: step 1/1. | null | null | FUNCTION: Catalyzes the pyridoxal 5'-phosphate (PLP)-dependent condensation of succinyl-CoA and glycine to form aminolevulinic acid (ALA), with CoA and CO2 as by-products. {ECO:0000269|PubMed:16234850, ECO:0000269|PubMed:17975826}. | Homo sapiens (Human) |
P13199 | ICP27_SHV21 | MEDIIEGGISSDDDFDSSDSSSDEEESDTSPQIMKSDVTMASPPSTPEPSPDVSASTSNLKRERQRSPITWEHQSPLSRVYRSPSPMRFGKRPRISSNSTSRSCKTSWADRVREAAAQRRPSRPFRKPYSHPRNGPLRNGPPRAPPLLKLFDISILPKSGEPKLFLPVPSLPCQEAEKTNDKYVLAMAQRAMHDVPISSKQLTANLLPVKFKPLLSIVRYTPNYYYWVSMRKETIASANLCTVAAFLDESLCWGQQYLKNDFIFSENGKDIILDTSSALLSQLVHKIKMLPFCHCLMQTTPQDHIVKQVCYLIASNNRIL... | null | null | regulation of DNA-templated transcription [GO:0006355] | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025] | metal ion binding [GO:0046872]; molecular adaptor activity [GO:0060090]; RNA binding [GO:0003723] | PF05459; | null | HHV-1 ICP27 protein family | null | SUBCELLULAR LOCATION: Host cytoplasm {ECO:0000250}. Host nucleus {ECO:0000269|PubMed:21253573}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Probably acts as a viral splicing factor that regulates viral RNA splicing. Functions as a multifunctional regulator of the expression of viral lytic genes (By similarity). Early protein that promotes the accumulation and nuclear export of viral intronless RNA transcripts by interacting with mRNAs and cellula... | Saimiriine herpesvirus 2 (strain 11) (SaHV-2) (Herpesvirus saimiri) |
P13201 | GB_HCMVT | MESRIWCLVVCVNLCIVCLGAAVSSSSTRGTSATHSHHSSHTTSAAHSRSGSVSQRVTSSQTVSHGVNETIYNTTLKYGDVVGVNTTKYPYRVCSMAQGTDLIRFERNIVCTSMKPINEDLDEGIMVVYKRNIVAHTFKVRVYQKVLTFRRSYAYIHTTYLLGSNTEYVAPPMWEIHHINSHSQCYSSYSRVIAGTVFVAYHRDSYENKTMQLMPDDYSNTHSTRYVTVKDQWHSRGSTWLYRETCNLNCMVTITTARSKYPYHFFATSTGDVVDISPFYNGTNRNASYFGENADKFFIFPNYTIVSDFGRPNSALETHR... | null | null | symbiont entry into host cell [GO:0046718]; virion attachment to host cell [GO:0019062] | host cell endosome membrane [GO:0044175]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF17416;PF17417;PF00606;PF12154; | 1.20.5.1890;2.30.29.100;2.30.30.1230;6.10.250.3280; | Herpesviridae glycoprotein B family | PTM: A proteolytic cleavage by host furin generates two subunits that remain linked by disulfide bonds. {ECO:0000250}. | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Host cell membrane {ECO:0000255|HAMAP-Rule:MF_04032}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04032}. Host endosome membrane {ECO:0000255|HAMAP-Rule:MF_0... | null | null | null | null | null | FUNCTION: Envelope glycoprotein that plays a role in host cell entry, cell to-cell virus transmission, and fusion of infected cells. May be involved in the initial attachment via binding to heparan sulfate together with the gM/gN complex that binds heparin with higher affinity. Interacts with host integrin ITGB1, PDGFR... | Human cytomegalovirus (strain Towne) (HHV-5) (Human herpesvirus 5) |
P13203 | GLCDH_THEAC | MTEQKAIVTDAPKGGVKYTTIDMPEPEHYDAKLSPVYIGICGTDRGEVAGALSFTYNPEGENFLVLGHEALLRVDDARDNGYIKKGDLVVPLVRRPGKCINCRIGRQDNCSIGDPDKHEAGITGLHGFMRDVIYDDIEYLVKVEDPELGRIAVLTEPLKNVMKAFEVFDVVSKRSIFFGDDSTLIGKRMVIIGSGSEAFLYSFAGVDRGFDVTMVNRHDETENKLKIMDEFGVKFANYLKDMPEKIDLLVDTSGDPTTTFKFLRKVNNNGVVILFGTNGKAPGYPVDGEDIDYIVERNITIAGSVDAAKIHYVQALQSLS... | 1.1.1.120; 1.1.1.47; 1.1.1.48 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000255|HAMAP-Rule:MF_02127}; | galactose catabolic process via D-galactonate [GO:0033498]; non-phosphorylated glucose catabolic process [GO:0019595]; protein tetramerization [GO:0051262] | null | galactose 1-dehydrogenase (NADP+) activity [GO:0047910]; galactose 1-dehydrogenase activity [GO:0019151]; galactose binding [GO:0005534]; glucose 1-dehydrogenase (NAD+) activity [GO:0047934]; glucose 1-dehydrogenase (NADP+) activity [GO:0047935]; glucose 1-dehydrogenase [NAD(P)] activity [GO:0047936]; glucose binding [... | PF08240;PF16912; | 3.90.180.10;3.40.50.720; | Zinc-containing alcohol dehydrogenase family, Glucose 1-dehydrogenase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=D-glucose + NAD(+) = D-glucono-1,5-lactone + H(+) + NADH; Xref=Rhea:RHEA:14293, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378, ChEBI:CHEBI:16217, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.47; Evidence={ECO:0000269|PubMed:2803257, ECO:0000269|PubMed:8436115}; CATALYTIC ACTIVITY: Reaction=D-glucos... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=10 mM for glucose {ECO:0000269|PubMed:2803257}; KM=0.113 mM for NADP(+) {ECO:0000269|PubMed:2803257}; Note=The KM value for NAD(+) is superior to 30 mM, it could not be defined precisely as it was impossible to reach saturation of the enzyme.; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Thermostable. Retains full catalytic activity after 9 hours at 55 degrees Celsius, and at 75 degrees Celsius the half-life is approximately 3 hours. {ECO:0000269|PubMed:2803257}; | FUNCTION: Catalyzes the NAD(P)(+)-dependent oxidation of D-glucose to D-gluconate via gluconolactone. Is also significantly active with galactose as substrate, but not with mannose or glucose 6-phosphate. Can utilize both NAD(+) and NADP(+) as electron acceptor, with a marked preference for NADP(+). Physiologically, ma... | Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) |
P13205 | ANFB_RAT | MDLQKVLPQMILLLLFLNLSPLGGHSHPLGSPSQSPEQSTMQKLLELIREKSEEMAQRQLSKDQGPTKELLKRVLRSQDSAFRIQERLRNSKMAHSSSCFGQKIDRIGAVSRLGCDGLRLF | null | null | blood vessel diameter maintenance [GO:0097746]; cardiac muscle hypertrophy in response to stress [GO:0014898]; cell growth involved in cardiac muscle cell development [GO:0061049]; cellular response to mechanical stimulus [GO:0071260]; cGMP biosynthetic process [GO:0006182]; cGMP-mediated signaling [GO:0019934]; corona... | cytoplasm [GO:0005737]; extracellular space [GO:0005615]; perinuclear region of cytoplasm [GO:0048471]; protein-containing complex [GO:0032991] | hormone activity [GO:0005179]; hormone receptor binding [GO:0051427]; signaling receptor binding [GO:0005102] | PF00212; | null | Natriuretic peptide family | PTM: The precursor molecule is proteolytically cleaved by the endoprotease Furin to produce brain natriuretic peptide 45 (PubMed:9252368). May undergo further proteolytic cleavage by various proteases such as DPP4, MME and possibly FAP, to give rise to a variety of shorter peptides (By similarity). May be cleaved at Se... | SUBCELLULAR LOCATION: [Brain natriuretic peptide 45]: Secreted {ECO:0000269|PubMed:2525379, ECO:0000269|PubMed:2528349}. | null | null | null | null | null | FUNCTION: [Brain natriuretic peptide 45]: Cardiac hormone that plays a key role in mediating cardio-renal homeostasis (PubMed:2525380, PubMed:9252368). May also function as a paracrine antifibrotic factor in the heart (By similarity). Acts by specifically binding and stimulating NPR1 to produce cGMP, which in turn acti... | Rattus norvegicus (Rat) |
P13207 | EDN3_RAT | MELGLWLLLGLTVTSAAAALPAQPGNAGQERGPGRSGDQEEKRVPAHHRPRRCTCFTYKDKECVYYCHLDIIWINTPEQTVPYGLSNHRGSLRGKRSSGPVPESSQSSPQTRLRCACSGVDDKACAYFCAHVTSYSRRAEKAAAEEKQETGGPRQRLKSRTDKVHQP | null | null | axon extension [GO:0048675]; axon guidance [GO:0007411]; cell population proliferation [GO:0008283]; cell surface receptor signaling pathway [GO:0007166]; establishment of localization in cell [GO:0051649]; intracellular calcium ion homeostasis [GO:0006874]; intracellular magnesium ion homeostasis [GO:0010961]; melanoc... | extracellular space [GO:0005615] | bombesin receptor binding [GO:0031705]; endothelin B receptor binding [GO:0031708]; hormone activity [GO:0005179] | PF00322; | null | Endothelin/sarafotoxin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Endothelins are endothelium-derived vasoconstrictor peptides. | Rattus norvegicus (Rat) |
P13208 | SRTX_ATREN | MALLPRLAAGGLLLLLALAALEGKPAPSALSQLLEKRSEDQAAAGRIIDGGDTKQAARDPSPQRNVEPLCSCKDMSDKECLNFCHQDVIWRDTKQAARDPSPQRNVEPLCTCNDMTDEECLNFCHQDVIWRDTKQAARDPSPQRNVEPLCSCKDMTDKECLYFCHQDVIWRDTKQAARDPSPQRNVEPLCTCNDMTDEECLNFCHQDVIWRDTKQAARDPSPQRNVEPLCTCNDMTDEECLNFCHQDVIWRDTKQAARDPSPQRNVEPLCTCKDMTDKECLYFCHQGIIWRDTKQAARDPSPQRNVEPLCSCKDMSDKEC... | null | null | intracellular calcium ion homeostasis [GO:0006874]; regulation of systemic arterial blood pressure by endothelin [GO:0003100]; regulation of vasoconstriction [GO:0019229]; vein smooth muscle contraction [GO:0014826] | extracellular space [GO:0005615] | endothelin B receptor binding [GO:0031708]; hormone activity [GO:0005179]; toxin activity [GO:0090729] | PF00322; | null | Endothelin/sarafotoxin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2845579, ECO:0000269|PubMed:3176048}. | null | null | null | null | null | FUNCTION: Vasoconstrictor activity. These toxins cause cardiac arrest probably as a result of coronary vasospasm. {ECO:0000269|PubMed:21889567}.; FUNCTION: [Sarafotoxin-B]: Vasoconstrictor activity. Causes cardiac arrest probably as a result of coronary vasospasm (By similarity). Displays high agonistic activities towa... | Atractaspis engaddensis (Israeli burrowing asp) (Israeli mole viper) |
P13214 | ANXA4_BOVIN | MAAKGGTVKAASGFNAAEDAQTLRKAMKGLGTDEDAIINVLAYRSTAQRQEIRTAYKTTIGRDLMDDLKSELSGNFEQVILGMMTPTVLYDVQELRKAMKGAGTDEGCLIEILASRTPEEIRRINQTYQLQYGRSLEDDIRSDTSFMFQRVLVSLSAGGRDESNYLDDALMRQDAQDLYEAGEKKWGTDEVKFLTVLCSRNRNHLLHVFDEYKRIAQKDIEQSIKSETSGSFEDALLAIVKCMRNKSAYFAERLYKSMKGLGTDDDTLIRVMVSRAEIDMLDIRANFKRLYGKSLYSFIKGDTSGDYRKVLLILCGGDD | null | null | null | apical plasma membrane [GO:0016324]; chromaffin granule membrane [GO:0042584]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; zymogen granule membrane [GO:0042589] | calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; carbohydrate binding [GO:0030246]; chondroitin sulfate binding [GO:0035374]; heparin binding [GO:0008201]; phosphatidylserine binding [GO:0001786] | PF00191; | 1.10.220.10; | Annexin family | null | SUBCELLULAR LOCATION: Zymogen granule membrane {ECO:0000250|UniProtKB:P50994}; Peripheral membrane protein {ECO:0000250|UniProtKB:P50994}. | null | null | null | null | null | FUNCTION: May play a role in alveolar type II cells through interaction with the surfactant protein SFTPA1 (SP-A). | Bos taurus (Bovine) |
P13217 | PIPA_DROME | MTKKYEFDWIIPVPPELTTGCVFDRWFENEKETKENDFERDALFKVDEYGFFLYWKSEGRDGDVIELCQVSDIRAGGTPKDPKILDKVTKKNGTNIPELDKRSLTICSNTDYINITYHHVICPDAATAKSWQKNLRLITHNNRATNVCPRVNLMKHWMRLSYCVEKSGKIPVKTLAKTFASGKTEKLVYTCIKDAGLPDDKNATMTKEQFTFDKFYALYHKVCPRNDIEELFTSITKGKQDFISLEQFIQFMNDKQRDPRMNEILYPLYEEKRCTEIINDYELDEEKKKNVQMSLDGFKRYLMSDENAPVFLDRLDFYME... | 3.1.4.11 | null | adult locomotory behavior [GO:0008344]; calcium-mediated signaling [GO:0019722]; cellular response to light stimulus [GO:0071482]; circadian rhythm [GO:0007623]; deactivation of rhodopsin mediated signaling [GO:0016059]; detection of chemical stimulus involved in sensory perception of bitter taste [GO:0001580]; diacylg... | inaD signaling complex [GO:0016027]; rhabdomere [GO:0016028] | calcium ion binding [GO:0005509]; phosphatidylinositol phospholipase C activity [GO:0004435]; phospholipase C activity [GO:0004629] | PF00168;PF06631;PF09279;PF17787;PF00388;PF00387; | 2.30.29.240;2.60.40.150;1.10.238.10;3.20.20.190;1.20.1230.10; | null | null | null | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:33179, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:58456, ChEBI:CHEBI:203600; EC=3.1.4.11; Evidence={EC... | null | null | null | null | FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes (By similarity). Essential component of the phototransduction pathway (PubMed:2457447). Essential downstream component of ... | Drosophila melanogaster (Fruit fly) |
P13221 | AATC_RAT | MAPPSFFAQVPQAPPVLVFKLIADFRDDPDPRKVNLGVGAYRTDDSQPWVLPVVRKVEQKIANDHSLNHEYLPILGLAEFRSCASQLVLGDNSPALRENRVGGVQSLGGTGALRIGADFLGRWYNGTDNKNTPVYVSSPTWENHNGVFSAAGFKDIRSYRYWDAEKRGLDLQGFLNDLENAPEFSIFVLHACAHNPTGTDPTEEEWKQIAAVMKRRFLFPFFDSAYQGFASGDLEKDAWAIRYFVSEGFELFCAQSFSKNFGLYNERVGNLTVVGKEHDSVLRVLSQMEKIVRITWSNPPAQGARIVATTLSNPELFKEW... | 2.6.1.1; 2.6.1.3 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; | 2-oxoglutarate metabolic process [GO:0006103]; aspartate biosynthetic process [GO:0006532]; aspartate catabolic process [GO:0006533]; aspartate metabolic process [GO:0006531]; cellular response to insulin stimulus [GO:0032869]; cellular response to mechanical stimulus [GO:0071260]; dicarboxylic acid metabolic process [... | axon terminus [GO:0043679]; cytoplasm [GO:0005737]; cytosol [GO:0005829] | carboxylic acid binding [GO:0031406]; L-aspartate:2-oxoglutarate aminotransferase activity [GO:0004069]; L-cysteine transaminase activity [GO:0047801]; phosphatidylserine decarboxylase activity [GO:0004609]; pyridoxal phosphate binding [GO:0030170] | PF00155; | 3.90.1150.10;3.40.640.10; | Class-I pyridoxal-phosphate-dependent aminotransferase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + L-aspartate = L-glutamate + oxaloacetate; Xref=Rhea:RHEA:21824, ChEBI:CHEBI:16452, ChEBI:CHEBI:16810, ChEBI:CHEBI:29985, ChEBI:CHEBI:29991; EC=2.6.1.1; Evidence={ECO:0000269|PubMed:3053674, ECO:0000269|PubMed:7113743}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=22.2 mM for L-cysteine {ECO:0000269|PubMed:7113743}; KM=0.06 mM for 2-oxoglutarate {ECO:0000269|PubMed:7113743}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9.7. {ECO:0000269|PubMed:7113743}; | null | FUNCTION: Biosynthesis of L-glutamate from L-aspartate or L-cysteine. Important regulator of levels of glutamate, the major excitatory neurotransmitter of the vertebrate central nervous system. Acts as a scavenger of glutamate in brain neuroprotection. The aspartate aminotransferase activity is involved in hepatic gluc... | Rattus norvegicus (Rat) |
P13224 | GP1BB_HUMAN | MGSGPRGALSLLLLLLAPPSRPAAGCPAPCSCAGTLVDCGRRGLTWASLPTAFPVDTTELVLTGNNLTALPPGLLDALPALRTAHLGANPWRCDCRLVPLRAWLAGRPERAPYRDLRCVAPPALRGRLLPYLAEDELRAACAPGPLCWGALAAQLALLGLGLLHALLLVLLLCRLRRLRARARARAAARLSLTDPLVAERAGTDES | null | null | blood coagulation, intrinsic pathway [GO:0007597]; cell adhesion [GO:0007155]; cell surface receptor signaling pathway [GO:0007166]; megakaryocyte development [GO:0035855]; platelet activation [GO:0030168]; positive regulation of platelet activation [GO:0010572]; release of sequestered calcium ion into cytosol [GO:0051... | glycoprotein Ib-IX-V complex [GO:1990779]; plasma membrane [GO:0005886] | identical protein binding [GO:0042802]; transmembrane signaling receptor activity [GO:0004888] | null | 3.80.10.10; | null | null | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Gp-Ib, a surface membrane protein of platelets, participates in the formation of platelet plugs by binding to von Willebrand factor, which is already bound to the subendothelium. | Homo sapiens (Human) |
P13231 | HATA_DICDI | MGNRAFKSHHGHFLSAEGEAVKTHHGHHDHHTHFHVENHGGKVALKTHCGKYLSIGDHKQVYLSHHLHGDHSLFHLEHHGGKVSIKGHHHHYISADHHGHVSTKEHHDHDTTFEEIII | null | null | actin filament polymerization [GO:0030041]; hyperosmotic response [GO:0006972]; response to acidic pH [GO:0010447] | actin cytoskeleton [GO:0015629]; cortical cytoskeleton [GO:0030863]; cytosol [GO:0005829]; phagocytic vesicle [GO:0045335]; plasma membrane [GO:0005886] | actin filament binding [GO:0051015]; actin monomer binding [GO:0003785]; fatty acid binding [GO:0005504]; lipid binding [GO:0008289]; protein-macromolecule adaptor activity [GO:0030674] | PF06268; | 2.80.10.50; | Hisactophilin family | PTM: Phosphorylated. {ECO:0000269|PubMed:7822284}. | SUBCELLULAR LOCATION: Cytoplasm. Cell membrane; Lipid-anchor; Cytoplasmic side. | null | null | null | null | null | FUNCTION: May act as an intracellular pH sensor that links chemotactic signals to responses in the microfilament system of the cells by nucleating actin polymerization or stabilizing the filaments. | Dictyostelium discoideum (Social amoeba) |
P13232 | IL7_HUMAN | MFHVSFRYIFGLPPLILVLLPVASSDCDIEGKDGKQYESVLMVSIDQLLDSMKEIGSNCLNNEFNFFKRHICDANKEGMFLFRAARKLRQFLKMNSTGDFDLHLLKVSEGTTILLNCTGQVKGRKPAALGEAQPTKSLEENKSLKEQKKLNDLCFLKRLLQEIKTCWNKILMGTKEH | null | null | animal organ morphogenesis [GO:0009887]; B cell proliferation [GO:0042100]; bone resorption [GO:0045453]; cell-cell signaling [GO:0007267]; cytokine-mediated signaling pathway [GO:0019221]; extrinsic apoptotic signaling pathway [GO:0097191]; homeostasis of number of cells within a tissue [GO:0048873]; humoral immune re... | collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; interleukin-7 receptor binding [GO:0005139] | PF01415; | 1.20.1250.50; | IL-7/IL-9 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25870237}. | null | null | null | null | null | FUNCTION: Hematopoietic cytokine that plays an essential role in the development, expansion, and survival of naive and memory T-cells and B-cells thereby regulating the number of mature lymphocytes and maintaining lymphoid homeostasis (PubMed:25870237, PubMed:7527823). Mechanistically, exerts its biological effects thr... | Homo sapiens (Human) |
P13233 | CN37_RAT | MSTSFARKSHTFLPKIFFRKMSSSGAKDKPELQFPFLQDEDTVATLHECKTLFILRGLPGSGKSTLARLIVEKYHNGTKMVSADAYKIIPGSRADFSEEYKRLDEDLAGYCRRDIRVLVLDDTNHERERLDQLFEMADQYQYQVVLVEPKTAWRLDCAQLKEKNQWQLSLDDLKKLKPGLEKDFLPLYFGWFLTKKSSETLRKAGQVFLEELGNHKAFKKELRHFISGDEPKEKLDLVSYFGKRPPGVLHCTTKFCDYGKATGAEEYAQQDVVRRSYGKAFKLSISALFVTPKTAGAQVVLNEQELQLWPSDLDKPSSSE... | 3.1.4.37 | null | adult locomotory behavior [GO:0008344]; axonogenesis [GO:0007409]; cyclic nucleotide catabolic process [GO:0009214]; forebrain development [GO:0030900]; oligodendrocyte differentiation [GO:0048709]; regulation of mitochondrial membrane permeability [GO:0046902]; response to lipopolysaccharide [GO:0032496]; response to ... | cell projection [GO:0042995]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; melanosome [GO:0042470]; membrane [GO:0016020]; microvillus [GO:0005902]; mitochondrial inner membrane [GO:0005743]; mitochondrial outer membrane [GO:0005741]; myelin sheath [GO:0043209]; myelin sheath abaxonal region [GO:0035748]; ... | 2',3'-cyclic-nucleotide 3'-phosphodiesterase activity [GO:0004113]; cyclic nucleotide binding [GO:0030551]; RNA binding [GO:0003723] | PF13671;PF05881; | 3.90.1740.10;3.40.50.300; | 2H phosphoesterase superfamily, CNPase family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P16330}; Lipid-anchor {ECO:0000250|UniProtKB:P16330}. Melanosome {ECO:0000250|UniProtKB:P09543}. Note=Firmly bound to membrane structures of brain white matter. {ECO:0000250|UniProtKB:P16330}. | CATALYTIC ACTIVITY: Reaction=a nucleoside 2',3'-cyclic phosphate + H2O = a nucleoside 2'-phosphate + H(+); Xref=Rhea:RHEA:14489, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:66954, ChEBI:CHEBI:78552; EC=3.1.4.37; Evidence={ECO:0000250|UniProtKB:P06623}; | null | null | null | null | FUNCTION: Catalyzes the formation of 2'-nucleotide products from 2',3'-cyclic substrates (By similarity). May participate in RNA metabolism in the myelinating cell, CNP is the third most abundant protein in central nervous system myelin (By similarity). {ECO:0000250|UniProtKB:P06623, ECO:0000250|UniProtKB:P16330}. | Rattus norvegicus (Rat) |
P13234 | KCC4_RAT | MLKVTVPSCPSSPCSSVTSSTENLVPDYWIDGSKRDPLSDFFEVESELGRGATSIVYRCKQKGTQKPYALKVLKKTVDKKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLELVTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPDAPLKIADFGLSKIVEHQVLMKTVCGTPGYCAPEILRGCAYGPEVDMWSVGIITYILLCGFEPFYDERGDQFMFRRILNCEYYFISPWWDEVSLNAKDLVKKLIVLDPKKRLTTFQALQHPWVTGKAANFVHMDTAQKKLQEFNARR... | 2.7.11.17 | null | adaptive immune response [GO:0002250]; inflammatory response [GO:0006954]; intracellular signal transduction [GO:0035556]; long-term memory [GO:0007616]; myeloid dendritic cell differentiation [GO:0043011]; neuron-neuron synaptic transmission [GO:0007270]; nucleocytoplasmic transport [GO:0006913]; phosphorylation [GO:0... | cytoplasm [GO:0005737]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; postsynapse [GO:0098794] | ATP binding [GO:0005524]; calcium-dependent protein serine/threonine kinase activity [GO:0009931]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]; protein serine kinase activity [GO:0106310] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family, CaMK subfamily | PTM: Phosphorylated by CaMKK1 and CaMKK2 on Thr-196. Dephosphorylated by protein phosphatase 2A. Autophosphorylated on Ser-11 and Ser-12 (By similarity). {ECO:0000250}.; PTM: Glycosylation at Ser-185 modulates the phosphorylation of CaMK4 at Thr-196 and negatively regulates its activity toward CREB1 in basal conditions... | SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Localized in hippocampal neuron nuclei. In spermatids, associated with chromatin and nuclear matrix. {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=2.7.11.17; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: [Isoform 1]: Calcium/calmodulin-dependent protein kinase that operates in the calcium-triggered CaMKK-CaMK4 signaling cascade and regulates, mainly by phosphorylation, the activity of several transcription activators, such as CREB1, MEF2D, JUN and RORA, which play pivotal roles in immune response, inflammatio... | Rattus norvegicus (Rat) |
P13236 | CCL4_HUMAN | MKLCVTVLSLLMLVAAFCSPALSAPMGSDPPTACCFSYTARKLPRNFVVDYYETSSLCSQPAVVFQTKRSKQVCADPSESWVQEYVYDLELN | null | null | cell adhesion [GO:0007155]; cell-cell signaling [GO:0007267]; cellular response to interleukin-1 [GO:0071347]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to type II interferon [GO:0071346]; chemokine-mediated signaling pathway [GO:0070098]; eosinophil chemotaxis [GO:0048245]; establishme... | extracellular region [GO:0005576]; extracellular space [GO:0005615] | CCR chemokine receptor binding [GO:0048020]; CCR1 chemokine receptor binding [GO:0031726]; CCR5 chemokine receptor binding [GO:0031730]; chemokine activity [GO:0008009]; cytokine activity [GO:0005125]; identical protein binding [GO:0042802] | PF00048; | 2.40.50.40; | Intercrine beta (chemokine CC) family | PTM: N-terminal processed form MIP-1-beta(3-69) is produced by proteolytic cleavage after secretion from peripheral blood lymphocytes. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Monokine with inflammatory and chemokinetic properties. Binds to CCR5. One of the major HIV-suppressive factors produced by CD8+ T-cells. Recombinant MIP-1-beta induces a dose-dependent inhibition of different strains of HIV-1, HIV-2, and simian immunodeficiency virus (SIV). The processed form MIP-1-beta(3-69... | Homo sapiens (Human) |
P13242 | PYRG_BACSU | MTKYIFVTGGVVSSLGKGIVAASLGRLLKNRGLNVTIQKFDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDINLNKFSNVTTGKIYSTVLKKERRGDYLGGTVQVIPHITNELKDRVYRAGKETNADVVITEIGGTVGDIESLPFLEAIRQMKSDIGRENVMYIHCTLVPYIKAAGELKTKPTQHSVKELRSLGIQPNIIVVRTEMPISQDMKDKIALFCDIDTKAVIECEDADNLYSIPLELQKQGLDKLVCEHMKLACKEAEMSEWKELVNKVSNLSQTITIGLVGKYVELPDAYISVVESLRHAGYAF... | 6.3.4.2 | null | 'de novo' CTP biosynthetic process [GO:0044210]; CTP biosynthetic process [GO:0006241]; glutamine metabolic process [GO:0006541]; pyrimidine nucleobase biosynthetic process [GO:0019856] | cytoophidium [GO:0097268]; cytosol [GO:0005829] | ATP binding [GO:0005524]; CTP synthase activity [GO:0003883]; glutaminase activity [GO:0004359]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872] | PF06418;PF00117; | 3.40.50.880;3.40.50.300; | CTP synthase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-glutamine + UTP = ADP + CTP + 2 H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:26426, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:37563, ChEBI:CHEBI:43474, ChEBI:CHEBI:46398, ChEBI:CHEBI:58359, ChEBI:CHEBI:456216; EC=6.3.4.2; Evidenc... | null | PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2. {ECO:0000255|HAMAP-Rule:MF_01227}. | null | null | FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates. {ECO:0000255|HAMAP-Rule:MF_01227}. | Bacillus subtilis (strain 168) |
P13254 | MEGL_PSEPU | MHGSNKLPGFATRAIHHGYDPQDHGGALVPPVYQTATFTFPTVEYGAACFAGEQAGHFYSRISNPTLNLLEARMASLEGGEAGLALASGMGAITSTLWTLLRPGDEVLLGNTLYGCTFAFLHHGIGEFGVKLRHVDMADLQALEAAMTPATRVIYFESPANPNMHMADIAGVAKIARKHGATVVVDNTYCTPYLQRPLELGADLVVHSATKYLSGHGDITAGIVVGSQALVDRIRLQGLKDMTGAVLSPHDAALLMRGIKTLNLRMDRHCANAQVLAEFLARQPQVELIHYPGLASFPQYTLARQQMSQPGGMIAFELKG... | 4.4.1.11; 4.4.1.2 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:17289792, ECO:0000269|PubMed:22785484, ECO:0000269|PubMed:6742420}; | transsulfuration [GO:0019346] | cytoplasm [GO:0005737] | homocysteine desulfhydrase activity [GO:0047982]; methionine gamma-lyase activity [GO:0018826]; pyridoxal phosphate binding [GO:0030170] | PF01053; | 3.90.1150.10;3.40.640.10; | Trans-sulfuration enzymes family, L-methionine gamma-lyase subfamily | null | null | CATALYTIC ACTIVITY: Reaction=H2O + L-methionine = 2-oxobutanoate + methanethiol + NH4(+); Xref=Rhea:RHEA:23800, ChEBI:CHEBI:15377, ChEBI:CHEBI:16007, ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:57844; EC=4.4.1.11; Evidence={ECO:0000269|PubMed:22785484, ECO:0000269|PubMed:6742420}; CATALYTIC ACTIVITY: Reaction=H2O... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1 mM for L-methionine {ECO:0000269|PubMed:6742420}; KM=0.5 mM for L-methionine {ECO:0000269|PubMed:22785484}; KM=1.1 mM for DL-homocysteine {ECO:0000269|PubMed:22785484}; KM=0.2 mM for L-cysteine {ECO:0000269|PubMed:22785484}; KM=0.7 mM for S-methyl-L-cysteine {ECO... | null | null | null | FUNCTION: Catalyzes the alpha,gamma-elimination of L-methionine to produce methanethiol, 2-oxobutanoate and ammonia (PubMed:6742420, PubMed:8586629). Is involved in L-methionine catabolism (PubMed:9190812). In fact, shows a multicatalytic function since it also catalyzes gamma-replacement of L-methionine with thiol com... | Pseudomonas putida (Arthrobacter siderocapsulatus) |
P13255 | GNMT_RAT | MVDSVYRTRSLGVAAEGIPDQYADGEAARVWQLYIGDTRSRTAEYKAWLLGLLRQHGCHRVLDVACGTGVDSIMLVEEGFSVTSVDASDKMLKYALKERWNRRKEPAFDKWVIEEANWLTLDKDVPAGDGFDAVICLGNSFAHLPDSKGDQSEHRLALKNIASMVRPGGLLVIDHRNYDYILSTGCAPPGKNIYYKSDLTKDITTSVLTVNNKAHMVTLDYTVQVPGAGRDGAPGFSKFRLSYYPHCLASFTELVQEAFGGRCQHSVLGDFKPYRPGQAYVPCYFIHVLKKTG | 2.1.1.20 | null | glycine metabolic process [GO:0006544]; glycogen metabolic process [GO:0005977]; methionine metabolic process [GO:0006555]; methylation [GO:0032259]; one-carbon metabolic process [GO:0006730]; protein homotetramerization [GO:0051289]; regulation of gluconeogenesis [GO:0006111]; S-adenosylhomocysteine metabolic process ... | cytosol [GO:0005829]; methyltransferase complex [GO:0034708] | folic acid binding [GO:0005542]; glycine binding [GO:0016594]; glycine N-methyltransferase activity [GO:0017174]; identical protein binding [GO:0042802]; S-adenosyl-L-methionine binding [GO:1904047]; S-adenosylmethionine-dependent methyltransferase activity [GO:0008757]; selenol Se-methyltransferase activity [GO:009860... | PF13649; | 3.30.46.10;3.40.50.150; | Class I-like SAM-binding methyltransferase superfamily, Glycine N-methyltransferase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:6587377}. | CATALYTIC ACTIVITY: Reaction=glycine + S-adenosyl-L-methionine = H(+) + S-adenosyl-L-homocysteine + sarcosine; Xref=Rhea:RHEA:19937, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305, ChEBI:CHEBI:57433, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789; EC=2.1.1.20; Evidence={ECO:0000269|PubMed:12859184, ECO:0000269|PubMed:3838667}; Physiologic... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=36 uM for S-adenosyl-L-methionine {ECO:0000269|PubMed:12859184}; KM=0.43 uM for glycine {ECO:0000269|PubMed:12859184}; | null | null | null | FUNCTION: Catalyzes the methylation of glycine by using S-adenosylmethionine (AdoMet) to form N-methylglycine (sarcosine) with the concomitant production of S-adenosylhomocysteine (AdoHcy), a reaction regulated by the binding of 5-methyltetrahydrofolate. Possible crucial role in the regulation of tissue concentration o... | Rattus norvegicus (Rat) |
P13259 | PCY1_YEAST | MANPTTGKSSIRAKLSNSSLSNLFKKNKNKRQREETEEQDNEDKDESKNQDENKDTQLTPRKRRRLTKEFEEKEARYTNELPKELRKYRPKGFRFNLPPTDRPIRIYADGVFDLFHLGHMKQLEQCKKAFPNVTLIVGVPSDKITHKLKGLTVLTDKQRCETLTHCRWVDEVVPNAPWCVTPEFLLEHKIDYVAHDDIPYVSADSDDIYKPIKEMGKFLTTQRTNGVSTSDIITKIIRDYDKYLMRNFARGATRQELNVSWLKKNELEFKKHINEFRSYFKKNQTNLNNASRDLYFEVREILLKKTLGKKLYSKLIGNEL... | 2.7.7.15 | null | CDP-choline pathway [GO:0006657]; phosphatidylcholine biosynthetic process [GO:0006656] | membrane [GO:0016020]; NLS-dependent protein nuclear import complex [GO:0042564]; nuclear envelope [GO:0005635]; nucleus [GO:0005634] | choline-phosphate cytidylyltransferase activity [GO:0004105]; phosphatidylcholine binding [GO:0031210] | PF01467; | 3.40.50.620; | Cytidylyltransferase family | null | SUBCELLULAR LOCATION: Membrane. Note=Most of its activity is membrane-associated. | CATALYTIC ACTIVITY: Reaction=CTP + H(+) + phosphocholine = CDP-choline + diphosphate; Xref=Rhea:RHEA:18997, ChEBI:CHEBI:15378, ChEBI:CHEBI:33019, ChEBI:CHEBI:37563, ChEBI:CHEBI:58779, ChEBI:CHEBI:295975; EC=2.7.7.15; Evidence={ECO:0000269|PubMed:2826147}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18998; Evid... | null | PATHWAY: Phospholipid metabolism; phosphatidylcholine biosynthesis; phosphatidylcholine from phosphocholine: step 1/2. {ECO:0000305|PubMed:2826147}. | null | null | FUNCTION: Catalyzes the key rate-limiting step in the CDP-choline pathway for phosphatidylcholine biosynthesis. {ECO:0000269|PubMed:2826147}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P13264 | GLSK_RAT | MMRLRGSAMLRELLLRPPAAVGGVLRRTQPLGTLCRRPRGGSRPAAGLVAAARLHPWWGGGGRAKGPGSGGLSSSPSEILQELGKGGTPPQQQQQQQQQPGASPPAAPGPKDSPGETDAFGNSEGKEMVAAGDNKVKQGLLPSLEDLLFYTIAEGQEKIPVHKFITALKSTGLRTSDPRLKECMDMLRLTLQTTSDGVMLDKDLFKKCVQSNIVLLTQAFRRKFVIPDFMSFTSHIDELYESAKKQSGGKVADYIPQLAKFSPDLWGVSVCTVDGQRHSIGDTKVPFCLQSCVKPLKYAIAVNDLGTEYVHRYVGKEPSG... | 3.5.1.2 | null | chemical synaptic transmission [GO:0007268]; glutamate biosynthetic process [GO:0006537]; glutamine catabolic process [GO:0006543]; intracellular glutamate homeostasis [GO:0090461]; protein homotetramerization [GO:0051289]; regulation of respiratory gaseous exchange by nervous system process [GO:0002087]; suckling beha... | cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; synapse [GO:0045202] | glutaminase activity [GO:0004359]; identical protein binding [GO:0042802] | PF12796;PF17959;PF04960; | 1.10.238.210;1.25.40.20;3.40.710.10; | Glutaminase family | PTM: Synthesized as a 74-kDa cytosolic precursor which is proteolytically processed by the mitochondrial-processing peptidase (MPP) via a 72-kDa intermediate to yield the mature mitochondrial 68- and 65-kDa subunits. {ECO:0000269|PubMed:1918000, ECO:0000269|PubMed:1991024, ECO:0000269|PubMed:7836378}. | SUBCELLULAR LOCATION: [Isoform 1]: Mitochondrion {ECO:0000269|PubMed:1991024}. Cytoplasm, cytosol {ECO:0000269|PubMed:1991024}. Note=The 74-kDa cytosolic precursor is translocated into the mitochondria and processed via a 72-kDa intermediate to yield the mature 68 and 65-kDa subunits. {ECO:0000269|PubMed:1991024}.; SUB... | CATALYTIC ACTIVITY: Reaction=H2O + L-glutamine = L-glutamate + NH4(+); Xref=Rhea:RHEA:15889, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:29985, ChEBI:CHEBI:58359; EC=3.5.1.2; Evidence={ECO:0000269|PubMed:1991024, ECO:0000269|PubMed:22228304}; | null | null | null | null | FUNCTION: Catalyzes the first reaction in the primary pathway for the renal catabolism of glutamine. Plays a role in maintaining acid-base homeostasis. Regulates the levels of the neurotransmitter glutamate, the main excitatory neurotransmitter in the brain. {ECO:0000250|UniProtKB:D3Z7P3}. | Rattus norvegicus (Rat) |
P13265 | GPC3_RAT | MAGTVRTACLLVAMLLGLGCLGQAQPPPPPDATCHQVRSFFQRLQPGLKWVPETPVPGSDLQVCLPKGPTCCSRKMEEKYQLTARLNMEQLLQSASMELKFLIIQNAAVFQEAFEIVVRHAKNYTNAMFKNNYPSLTPQAFEFVGEFFTDVSLYILGSDINVDDMVNELFDSLFPVIYTQMMNPGLPESVLDINECLRGARRDLKVFGSFPKLIMTQVSKSLQVTRIFLQALNLGIEVINTTDHLKFSKDCGRMLTRMWYCSYCQGLMMVKPCGGYCNVVMQGCMAGVVEIDKYWREYILSLEELVNGMYRIYDMENVLL... | null | null | animal organ morphogenesis [GO:0009887]; anterior/posterior axis specification [GO:0009948]; body morphogenesis [GO:0010171]; bone mineralization [GO:0030282]; branching involved in ureteric bud morphogenesis [GO:0001658]; canonical Wnt signaling pathway [GO:0060070]; cell migration [GO:0016477]; cell migration involve... | cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; lysosome [GO:0005764]; plasma membrane [GO:0005886]; side of membrane [GO:0098552] | peptidyl-dipeptidase inhibitor activity [GO:0060422] | PF01153; | null | Glypican family | PTM: O-glycosylated; contains heparan sulfate and/or chondroitin sulfate. {ECO:0000250|UniProtKB:P51654}.; PTM: Cleaved intracellularly by a furin-like convertase to generate 2 subunits, alpha and beta, which remain associated through disulfide bonds and are associated with the cell surface via the GPI-anchor. This pro... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:7487896}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:7487896}; Extracellular side {ECO:0000269|PubMed:7487896}. | null | null | null | null | null | FUNCTION: Cell surface proteoglycan (By similarity). Negatively regulates the hedgehog signaling pathway when attached via the GPI-anchor to the cell surface by competing with the hedgehog receptor PTC1 for binding to hedgehog proteins (By similarity). Binding to the hedgehog protein SHH triggers internalization of the... | Rattus norvegicus (Rat) |
P13272 | UCRI_BOVIN | MLSVAARSGPFAPVLSATSRGVAGALRPLVQAAVPATSESPVLDLKRSVLCRESLRGQAAGRPLVASVSLNVPASVRYSHTDIKVPDFSDYRRPEVLDSTKSSKESSEARKGFSYLVTATTTVGVAYAAKNVVSQFVSSMSASADVLAMSKIEIKLSDIPEGKNMAFKWRGKPLFVRHRTKKEIDQEAAVEVSQLRDPQHDLERVKKPEWVILIGVCTHLGCVPIANAGDFGGYYCPCHGSHYDASGRIRKGPAPLNLEVPSYEFTSDDMVIVG | 7.1.1.8 | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000269|PubMed:9651245}; Note=Binds 1 [2Fe-2S] cluster per subunit. Fe-S cluster delivery to the Rieske protein is mediated by components of the iron sulfur (Fe-S) cluster assembly machinery that reside in the mitochondrial matrix (including HSC20 ... | mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122] | mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex III [GO:0005750]; mitochondrion [GO:0005739]; plasma membrane [GO:0005886] | 2 iron, 2 sulfur cluster binding [GO:0051537]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]; ubiquinol-cytochrome-c reductase activity [GO:0008121] | PF00355;PF09165;PF02921; | 2.102.10.10;1.20.5.270; | Rieske iron-sulfur protein family | PTM: Proteolytic processing is necessary for the correct insertion of UQCRFS1 in the complex III dimer. Several fragments are generated during UQCRFS1 insertion, most probably due to the endogenous matrix-processing peptidase (MPP) activity of the 2 core protein subunits UQCRC1/QCR1 and UQCRC2/QCR2, which are homologou... | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q5ZLR5}; Single-pass membrane protein {ECO:0000250|UniProtKB:Q5ZLR5}. | CATALYTIC ACTIVITY: Reaction=a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2 Fe(II)-[cytochrome c](out) + 2 H(+)(out); Xref=Rhea:RHEA:11484, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:132124; EC=7.1.1.8; Evidence={ECO:0000... | null | null | null | null | FUNCTION: [Cytochrome b-c1 complex subunit Rieske, mitochondrial]: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succi... | Bos taurus (Bovine) |
P13280 | GLYG_RABIT | MTDQAFVTLTTNDAYAKGALVLGSSLKQHRTSRRLAVLTTPQVSDTMRKALEIVFDEVITVDILDSGDSAHLTLMKRPELGVTLTKLHCWSLTQYSKCVFMDADTLVLANIDDLFEREELSAAPDPGWPDCFNSGVFVYQPSVETYNQLLHVASEQGSFDGGDQGLLNTFFNSWATTDIRKHLPFIYNLSSISIYSYLPAFKAFGANAKVVHFLGQTKPWNYTYDTKTKSVRSEGHDPTMTHPQFLNVWWDIFTTSVVPLLQQFGLVQDTCSYQHVEDVSGAVSHLSLGETPATTQPFVSSEERKERWEQGQADYMGADS... | 2.4.1.186 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:12051921, ECO:0000269|PubMed:1281472, ECO:0000269|PubMed:15849187, ECO:0000269|PubMed:22128147, ECO:0000269|PubMed:22226635, ECO:0000269|PubMed:2526735, ECO:0000269|PubMed:8143846}; Note=Divalent metal ions. Required for self-glucosylation. Man... | glycogen biosynthetic process [GO:0005978] | cytoplasm [GO:0005737] | glycogenin glucosyltransferase activity [GO:0008466]; manganese ion binding [GO:0030145]; protein homodimerization activity [GO:0042803]; UDP-alpha-D-glucose:glucosyl-glycogenin alpha-D-glucosyltransferase activity [GO:0102751] | PF01501; | null | Glycosyltransferase 8 family, Glycogenin subfamily | PTM: Self-glycosylated by the transfer of glucose residues from UDP-glucose to itself, forming an alpha-1,4-glycan of around 10 residues attached to Tyr-195. {ECO:0000269|PubMed:10049511, ECO:0000269|PubMed:22128147, ECO:0000269|PubMed:22226635, ECO:0000269|PubMed:7771798, ECO:0000269|PubMed:8143846}.; PTM: Phosphoryla... | null | CATALYTIC ACTIVITY: Reaction=L-tyrosyl-[glycogenin] + UDP-alpha-D-glucose = alpha-D-glucosyl-L-tyrosyl-[glycogenin] + H(+) + UDP; Xref=Rhea:RHEA:23360, Rhea:RHEA-COMP:14604, Rhea:RHEA-COMP:14605, ChEBI:CHEBI:15378, ChEBI:CHEBI:46858, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:140573; EC=2.4.1.186; Evidence={ECO:... | null | PATHWAY: Glycan biosynthesis; glycogen biosynthesis. {ECO:0000269|PubMed:1281472, ECO:0000269|PubMed:15849187, ECO:0000269|PubMed:2526735}. | null | null | FUNCTION: Glycogenin participates in the glycogen biosynthetic process along with glycogen synthase and glycogen branching enzyme. It self-glucosylates, via an inter-subunit mechanism, to form an oligosaccharide primer that serves as substrate for glycogen synthase. {ECO:0000269|PubMed:10049511, ECO:0000269|PubMed:1281... | Oryctolagus cuniculus (Rabbit) |
P13284 | GILT_HUMAN | MTLSPLLLFLPPLLLLLDVPTAAVQASPLQALDFFGNGPPVNYKTGNLYLRGPLKKSNAPLVNVTLYYEALCGGCRAFLIRELFPTWLLVMEILNVTLVPYGNAQEQNVSGRWEFKCQHGEEECKFNKVEACVLDELDMELAFLTIVCMEEFEDMERSLPLCLQLYAPGLSPDTIMECAMGDRGMQLMHANAQRTDALQPPHEYVPWVTVNGKPLEDQTQLLTLVCQLYQGKKPDVCPSSTSSLRSVCFK | 1.8.-.- | null | antigen processing and presentation of exogenous peptide antigen via MHC class I [GO:0042590]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; negative regulation of fibroblast proliferation [GO:0048147]; protein stabilization [GO:0050821] | cell junction [GO:0030054]; cytosol [GO:0005829]; extracellular region [GO:0005576]; intracellular membrane-bounded organelle [GO:0043231]; lysosomal lumen [GO:0043202]; lysosome [GO:0005764] | oxidoreductase activity, acting on a sulfur group of donors [GO:0016667]; oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor [GO:0016671] | PF03227; | null | GILT family | PTM: N-glycosylated. Sugar chains contain mannose-6-phosphate. {ECO:0000269|PubMed:10639150, ECO:0000269|PubMed:10852914}.; PTM: Synthesized as a 35 kDa precursor which is then processed into the mature 30 kDa form via cleavage of N-terminal and C-terminal propeptides. Processing of the precursor is mediated by multipl... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:10639150, ECO:0000269|PubMed:3136170}. Lysosome {ECO:0000269|PubMed:10639150, ECO:0000269|PubMed:3136170}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1200 uM for F(ab')2 fragment when denatured {ECO:0000269|PubMed:10639150}; KM=10 uM for F(ab')2 fragment {ECO:0000269|PubMed:10639150}; Note=Kinetic parameters shown are for mature enzyme.; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4-5. {ECO:0000269|PubMed:10639150}; | null | FUNCTION: Lysosomal thiol reductase that can reduce protein disulfide bonds. May facilitate the complete unfolding of proteins destined for lysosomal degradation. Plays an important role in antigen processing. Facilitates the generation of MHC class II-restricted epitodes from disulfide bond-containing antigen by the e... | Homo sapiens (Human) |
P13285 | LMP2_EBVB9 | MGSLEMVPMGAGPPSPGGDPDGYDGGNNSQYPSASGSSGNTPTPPNDEERESNEEPPPPYEDPYWGNGDRHSDYQPLGTQDQSLYLGLQHDGNDGLPPPPYSPRDDSSQHIYEEAGRGSMNPVCLPVIVAPYLFWLAAIAASCFTASVSTVVTATGLALSLLLLAAVASSYAAAQRKLLTPVTVLTAVVTFFAICLTWRIEDPPFNSLLFALLAAAGGLQGIYVLVMLVLLILAYRRRWRRLTVCGGIMFLACVLVLIVDAVLQLSPLLGAVTVVSMTLLLLAFVLWLSSPGGLGTLGAALLTLAAALALLASLILGTLN... | null | null | symbiont-mediated perturbation of host protein ubiquitination [GO:0039648]; viral latency [GO:0019042] | host cell endomembrane system [GO:0033645]; host cell perinuclear region of cytoplasm [GO:0044220]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020] | null | PF07415; | null | Herpesviridae LMP-2 family | PTM: [Isoform LMP2A]: Phosphorylated on cytoplasmic N-terminal tyrosine residues, possibly by human LYN. {ECO:0000269|PubMed:1710288}.; PTM: Can be ubiquitinated by human ITCH and WWP2 on the N-terminus in a lysine-independent manner. {ECO:0000269|PubMed:12202215}. | SUBCELLULAR LOCATION: [Isoform LMP2A]: Host cell membrane {ECO:0000269|PubMed:11163230, ECO:0000269|PubMed:11961256}; Multi-pass membrane protein {ECO:0000269|PubMed:11163230, ECO:0000269|PubMed:11961256}. Note=Isoform LMP2A is localized in plasma membrane lipid rafts. {ECO:0000269|PubMed:11163230}.; SUBCELLULAR LOCATI... | null | null | null | null | null | FUNCTION: [Isoform LMP2A]: Maintains EBV latent infection of B-lymphocyte, by preventing lytic reactivation of the virus in response to surface immunoglobulin (sIg) cross-linking. Acts like a dominant negative inhibitor of the sIg-associated protein tyrosine kinases, LYN and SYK. Also blocks translocation of the B-cell... | Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4) |
P13286 | PHKG1_RAT | MTRDEALPDSHSAQNFYENYEPKEILGRGVSSVVRRCIHKPTCQEYAVKIIDITGGGSFSSEEVQELREATLKEVDILQKVSGHPNIIQLKDTYETNTFFFLVFDLMKRGELFDYLTEKVTLTEKETRKIMRALLEVVCTLHKLNIVHRDLKPENILLDDNMNIKLTDFGFSCQLQPGEKLREVCGTPSYLAPEIIQCSMDEGHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMDGKYQFGSPEWDDYSDTVKDLVSRFLVVQPQDRCSAEEALAHPFFQEYVVEEVRHFSPRGKFKVICLTVLASVRIYY... | 2.7.11.1; 2.7.11.19; 2.7.11.26 | null | glycogen biosynthetic process [GO:0005978]; glycogen metabolic process [GO:0005977]; phosphorylation [GO:0016310] | phosphorylase kinase complex [GO:0005964] | ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; enzyme binding [GO:0019899]; phosphorylase kinase activity [GO:0004689]; protein serine kinase activity [GO:0106310]; tau-protein kinase activity [GO:0050321] | PF12330;PF00069; | 1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family | null | null | CATALYTIC ACTIVITY: Reaction=2 ATP + phosphorylase b = 2 ADP + phosphorylase a.; EC=2.7.11.19; CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[tau protein] = ADP + H(+) + O-phospho-L-seryl-[tau protein]; Xref=Rhea:RHEA:12801, Rhea:RHEA-COMP:13701, Rhea:RHEA-COMP:13702, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:3061... | null | null | null | null | FUNCTION: Catalytic subunit of the phosphorylase b kinase (PHK), which mediates the neural and hormonal regulation of glycogen breakdown (glycogenolysis) by phosphorylating and thereby activating glycogen phosphorylase. In vitro, phosphorylates PYGM, TNNI3, MAPT/TAU, GAP43 and NRGN/RC3 (By similarity). {ECO:0000250}. | Rattus norvegicus (Rat) |
P13288 | KR2_EBVB9 | MDVNMAAELSPTNSSSSGELSVSPEPPRETQAFLGKVTVIDYFTFQHKHLKVTNIDDMTETLYVKLPENMTRCDHLPITCEYLLGRGSYGAVYAHADNATVKLYDSVTELYHELMVCDMIQIGKATAEDGQDKALVDYLSACTSCHALFMPQFRCSLQDYGHWHDGSIEPLVRGFQGLKDAVYFLNRHCGLFHSDISPSNILVDFTDTMWGMGRLVLTDYGTASLHDRNKMLDVRLKSSKGRQLYRLYCQREPFSIAKDTYKPLCLLSKCYILRGAGHIPDPSACGPVGAQTALRLDLQSLGYSLLYGIMHLADSTHKIP... | 2.7.11.1 | null | modulation by virus of host chromatin organization [GO:0039525]; phosphorylation [GO:0016310]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of IRF3 activity [GO:0039548]; virus-mediated perturbation of host defense response [GO:0019049] | host cell nuclear envelope [GO:0044199]; host cell nucleus [GO:0042025]; viral tegument [GO:0019033] | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | null | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Virion tegument. Host nucleus {ECO:0000269|PubMed:22398289, ECO:0000269|PubMed:22623767}. Note=the protein is present at discrete sites in nuclei, called replication compartments where viral DNA replication occurs. | 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:0000269|PubMed:31291580}; CATALYTIC... | null | null | null | null | FUNCTION: Plays many key roles by phosphorylating several proteins including the viral DNA processivity factor BMRF1, EBNA1 or EBNA2. Modifies the host nuclear envelope structure and induces the redistribution of nuclear envelope-associated proteins by phosphorylating host nucleoporins. Subsequently, promotes the nucle... | Epstein-Barr virus (strain B95-8) (HHV-4) (Human herpesvirus 4) |
P13296 | TNFA_CAPHI | MSTKSMIRDVELAEEVLSKKAGGPQGSRSCWCLSLFSFLLVAGATTLFCLLHFGVIGPQREEQSPAGPSFNRPLVQTLRSSSQASSNKPVAHVVANISAPGQLRWGDSYANALKANGVELKDNQLVVPTDGLYLIYSQVLFRGHGCPSTPLFLTHTISRIAVSYQTKVNILSAIKSPCHRETPEGAEAKPWYEPIYQGGVFQLEKGDRLSAEINQPEYLDYAESGQVYFGIIAL | null | null | extrinsic apoptotic signaling pathway via death domain receptors [GO:0008625]; immune response [GO:0006955]; necroptotic signaling pathway [GO:0097527]; negative regulation of protein-containing complex disassembly [GO:0043242]; positive regulation of apoptotic process [GO:0043065]; positive regulation of JUN kinase ac... | cell surface [GO:0009986]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | cytokine activity [GO:0005125]; tumor necrosis factor receptor binding [GO:0005164] | PF00229; | 2.60.120.40; | Tumor necrosis factor family | PTM: The soluble form derives from the membrane form by proteolytic processing. The membrane-bound form is further proteolytically processed by SPPL2A or SPPL2B through regulated intramembrane proteolysis producing TNF intracellular domains (ICD1 and ICD2) released in the cytosol and TNF C-domain 1 and C-domain 2 secre... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Tumor necrosis factor, membrane form]: Membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Tumor necrosis factor, soluble form]: Secreted {ECO:00... | null | null | null | null | null | FUNCTION: Cytokine that binds to TNFRSF1A/TNFR1 and TNFRSF1B/TNFBR. It is mainly secreted by macrophages and can induce cell death of certain tumor cell lines. It is potent pyrogen causing fever by direct action or by stimulation of interleukin-1 secretion and is implicated in the induction of cachexia, Under certain c... | Capra hircus (Goat) |
P13297 | MSX1_MOUSE | MAPAAAMTSLPLGVKVEDSAFAKPAGGGVGQAPGAAAATATAMGTDEEGAKPKVPASLLPFSVEALMADHRKPGAKESVLVASEGAQAAGGSVQHLGTRPGSLGAPDAPSSPRPLGHFSVGGLLKLPEDALVKAESPEKLDRTPWMQSPRFSPPPARRLSPPACTLRKHKTNRKPRTPFTTAQLLALERKFRQKQYLSIAERAEFSSSLSLTETQVKIWFQNRRAKAKRLQEAELEKLKMAAKPMLPPAAFGLSFPLGGPAAVAAAAGASLYSASGPFQRAALPVAPVGLYTAHVGYSMYHLT | null | null | activation of meiosis [GO:0090427]; anterior/posterior pattern specification [GO:0009952]; BMP signaling pathway [GO:0030509]; bone morphogenesis [GO:0060349]; cartilage development [GO:0051216]; cartilage morphogenesis [GO:0060536]; cell morphogenesis [GO:0000902]; cell surface receptor signaling pathway involved in h... | nuclear periphery [GO:0034399]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | cis-regulatory region sequence-specific DNA binding [GO:0000987]; 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:000122... | PF00046; | 1.10.10.60; | Msh homeobox family | PTM: Sumoylated by PIAS1, desumoylated by SENP1 (PubMed:16678795). Sumoylation of Lys-15 and Lys-133 not required for interaction with H1-5, transcriptional repression, inhibition of myoblast differentiation, or binding to gene promoters (PubMed:16600910). {ECO:0000269|PubMed:16600910, ECO:0000269|PubMed:16678795}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16600910, ECO:0000269|PubMed:22629437, ECO:0000269|PubMed:23371388}. Note=Interaction with EHMT2/G9a is required for localization to the nuclear periphery (PubMed:22629437). Interaction with PIAS1 is required for localization to the nuclear periphery (PubMed:16600910). ... | null | null | null | null | null | FUNCTION: Acts as a transcriptional repressor (PubMed:22629437, PubMed:23371388, PubMed:7823952). Capable of transcription autoinactivation (PubMed:10215616). Binds to the consensus sequence 5'-C/GTAAT-3' in downstream activin regulatory elements (DARE) in the gene promoter, thereby repressing the transcription of CGA/... | Mus musculus (Mouse) |
P13299 | TEV1_BPT4 | MKSGIYQIKNTLNNKVYVGSAKDFEKRWKRHFKDLEKGCHSSIKLQRSFNKHGNVFECSILEEIPYEKDLIIERENFWIKELNSKINGYNIADATFGDTCSTHPLKEEIIKKRSETVKAKMLKLGPDGRKALYSKPGSKNGRWNPETHKFCKCGVRIQTSAYTCSKCRNRSGENNSFFNHKHSDITKSKISEKMKGKKPSNIKKISCDGVIFDCAADAARHFKISSGLVTYRVKSDKWNWFYINA | 3.1.-.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; | intron homing [GO:0006314]; negative regulation of DNA-templated transcription [GO:0045892]; nucleic acid metabolic process [GO:0090304] | transcription repressor complex [GO:0017053] | DNA binding [GO:0003677]; DNA-binding transcription repressor activity [GO:0001217]; double-stranded DNA endonuclease activity [GO:1990238]; endonuclease activity [GO:0004519]; sequence-specific DNA binding [GO:0043565]; zinc ion binding [GO:0008270] | PF01541;PF20987; | 3.40.1440.10; | null | null | null | null | null | null | null | null | FUNCTION: This endonuclease is specific to the thymidylate synthase (td) gene splice junction and is involved in intron homing. | Enterobacteria phage T4 (Bacteriophage T4) |
P13304 | ANTIH_BPT4 | MALKATALFAMLGLSFVLSPSIEANVDPHFDKFMESGIRHVYMLFENKSVESSEQFYSFMRTTYKNDPCSSDFECIERGAEMAQSYARIMNIKLETE | null | null | killing of cells of another organism [GO:0031640] | host cell periplasmic space [GO:0044229]; host cell plasma membrane [GO:0020002] | DNA binding [GO:0003677]; molecular function inhibitor activity [GO:0140678] | null | null | T4likevirus antiholin family | PTM: Disulfide bond is required for functionality. {ECO:0000255|HAMAP-Rule:MF_04105, ECO:0000269|PubMed:22389108}. | SUBCELLULAR LOCATION: Host periplasm {ECO:0000255|HAMAP-Rule:MF_04105, ECO:0000269|PubMed:34456892}. | null | null | null | null | null | FUNCTION: Involved in lysis inhibition. Senses superinfections and inhibits the holin, thereby delaying the host cell lysis timing. The genomic DNA from the superinfecting phage bound to the complex holin-antiholin probably serves as a signal for the lysis inhibition and blocks the holin multimerization. {ECO:0000255|H... | Enterobacteria phage T4 (Bacteriophage T4) |
P13314 | ACB2_BPT4 | MIEDIKGYKPHTEEKIGKVNAIKDAEVRLGLIFDALYDEFWEALDNCEDCEFAKNYAESLDQLTIAKTKLKEASMWACRAVFQPEEKY | null | null | null | null | nucleotide binding [GO:0000166] | null | null | Acb2 family | null | null | null | null | null | null | null | FUNCTION: Antagonizes CBASS (cyclic oligonucleotide-based antiphage signaling system) (Probable) (PubMed:36848932). Binds and sequesters host-produced 3',3'-cyclic GMP-AMP (cGAMP) with a dissociation constant of about 30 nM; each homohexamer binds 3 cGAMP molecules with 1 cGAMP molecule binding to 2 monomers (PubMed:36... | Enterobacteria phage T4 (Bacteriophage T4) |
Subsets and Splits
No community queries yet
The top public SQL queries from the community will appear here once available.