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 |
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
P07014 | SDHB_ECOLI | MRLEFSIYRYNPDVDDAPRMQDYTLEADEGRDMMLLDALIQLKEKDPSLSFRRSCREGVCGSDGLNMNGKNGLACITPISALNQPGKKIVIRPLPGLPVIRDLVVDMGQFYAQYEKIKPYLLNNGQNPPAREHLQMPEQREKLDGLYECILCACCSTSCPSFWWNPDKFIGPAGLLAAYRFLIDSRDTETDSRLDGLSDAFSVFRCHSIMNCVSVCPKGLNPTRAIGHIKSMLLQRNA | 1.3.5.1 | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Note=Binds 1 [2Fe-2S] cluster.; COFACTOR: Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; Note=Binds 1 [3Fe-4S] cluster.; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Note=Binds 1 [4Fe-4S] cluster.; | aerobic electron transport chain [GO:0019646]; aerobic respiration [GO:0009060]; respiratory electron transport chain [GO:0022904]; tricarboxylic acid cycle [GO:0006099] | membrane [GO:0016020]; plasma membrane [GO:0005886]; succinate dehydrogenase complex [GO:0045281] | 2 iron, 2 sulfur cluster binding [GO:0051537]; 3 iron, 4 sulfur cluster binding [GO:0051538]; 4 iron, 4 sulfur cluster binding [GO:0051539]; electron transfer activity [GO:0009055]; iron-sulfur cluster binding [GO:0051536]; metal ion binding [GO:0046872]; succinate dehydrogenase (quinone) activity [GO:0008177] | PF13085;PF13534; | 3.10.20.30;1.10.1060.10; | Succinate dehydrogenase/fumarate reductase iron-sulfur protein family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:16079137}; Peripheral membrane protein {ECO:0000269|PubMed:16079137}. | CATALYTIC ACTIVITY: Reaction=a quinone + succinate = a quinol + fumarate; Xref=Rhea:RHEA:40523, ChEBI:CHEBI:24646, ChEBI:CHEBI:29806, ChEBI:CHEBI:30031, ChEBI:CHEBI:132124; EC=1.3.5.1; | null | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; fumarate from succinate (bacterial route): step 1/1. | null | null | FUNCTION: Two distinct, membrane-bound, FAD-containing enzymes are responsible for the catalysis of fumarate and succinate interconversion; the fumarate reductase is used in anaerobic growth, and the succinate dehydrogenase is used in aerobic growth. | Escherichia coli (strain K12) |
P07017 | MCP2_ECOLI | MINRIRVVTLLVMVLGVFALLQLISGSLFFSSLHHSQKSFVVSNQLREQQGELTSTWDLMLQTRINLSRSAVRMMMDSSNQQSNAKVELLDSARKTLAQAATHYKKFKSMAPLPEMVATSRNIDEKYKNYYTALTELIDYLDYGNTGAYFAQPTQGMQNAMGEAFAQYALSSEKLYRDIVTDNADDYRFAQWQLAVIALVVVLILLVAWYGIRRMLLTPLAKIIAHIREIAGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREGSDAIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADN... | null | null | cellular response to amino acid stimulus [GO:0071230]; chemotaxis [GO:0006935]; detection of chemical stimulus [GO:0009593]; positive regulation of post-translational protein modification [GO:1901875]; protein homooligomerization [GO:0051260]; regulation of chemotaxis [GO:0050920]; signal complex assembly [GO:0007172];... | cell tip [GO:0051286]; methyl accepting chemotaxis protein complex [GO:0098561]; plasma membrane [GO:0005886] | identical protein binding [GO:0042802]; protein histidine kinase binding [GO:0043424]; protein homodimerization activity [GO:0042803]; transmembrane signaling receptor activity [GO:0004888] | PF00672;PF00015;PF02203; | 1.20.120.30;1.10.287.950; | Methyl-accepting chemotaxis (MCP) protein family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:22380631}; Multi-pass membrane protein {ECO:0000269|PubMed:22380631}. Note=Found predominantly at cell poles. | null | null | null | null | null | FUNCTION: Receptor for the attractant L-aspartate and related amino and dicarboxylic acids. Tar also mediates taxis to the attractant maltose via an interaction with the periplasmic maltose binding protein. Tar mediates taxis away from the repellents cobalt and nickel.; FUNCTION: Chemotactic-signal transducers respond ... | Escherichia coli (strain K12) |
P07024 | USHA_ECOLI | MKLLQRGVALALLTTFTLASETALAYEQDKTYKITVLHTNDHHGHFWRNEYGEYGLAAQKTLVDGIRKEVAAEGGSVLLLSGGDINTGVPESDLQDAEPDFRGMNLVGYDAMAIGNHEFDNPLTVLRQQEKWAKFPLLSANIYQKSTGERLFKPWALFKRQDLKIAVIGLTTDDTAKIGNPEYFTDIEFRKPADEAKLVIQELQQTEKPDIIIAATHMGHYDNGEHGSNAPGDVEMARALPAGSLAMIVGGHSQDPVCMAAENKKQVDYVPGTPCKPDQQNGIWIVQAHEWGKYVGRADFEFRNGEMKMVNYQLIPVNLK... | 3.1.3.5; 3.6.1.45 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 2 Zn(2+) ions per subunit.; | nucleotide catabolic process [GO:0009166] | outer membrane-bounded periplasmic space [GO:0030288] | 5'-nucleotidase activity [GO:0008253]; metal ion binding [GO:0046872]; nucleotide binding [GO:0000166]; UDP-sugar diphosphatase activity [GO:0008768]; XMP 5'-nucleosidase activity [GO:0106411] | PF02872;PF00149; | 3.60.21.10;3.90.780.10; | 5'-nucleotidase family | null | SUBCELLULAR LOCATION: Periplasm. Note=Exported from the cell, except a small proportion that is internally localized. | CATALYTIC ACTIVITY: Reaction=UDP-sugar + H2O = UMP + alpha-D-aldose 1-phosphate.; EC=3.6.1.45; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-phosphate + H2O = a ribonucleoside + phosphate; Xref=Rhea:RHEA:12484, ChEBI:CHEBI:15377, ChEBI:CHEBI:18254, ChEBI:CHEBI:43474, ChEBI:CHEBI:58043; EC=3.1.3.5; | null | null | null | null | FUNCTION: Degradation of external UDP-glucose to uridine monophosphate and glucose-1-phosphate, which can then be used by the cell. | Escherichia coli (strain K12) |
P07056 | UCRI_NEUCR | MAPVSIVSRAAMRAAAAPARAVRALTTSTALQGSSSSTFESPFKGESKAAKVPDFGKYMSKAPPSTNMLFSYFMVGTMGAITAAGAKSTIQEFLKNMSASADVLAMAKVEVDLNAIPEGKNVIIKWRGKPVFIRHRTPAEIEEANKVNVATLRDPETDADRVKKPEWLVMLGVCTHLGCVPIGEAGDYGGWFCPCHGSHYDISGRIRKGPAPLNLEIPLYEFPEEGKLVIG | 7.1.1.8 | COFACTOR: Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Evidence={ECO:0000255|PROSITE-ProRule:PRU00628}; Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|PROSITE-ProRule:PRU00628}; | mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122] | mitochondrial respiratory chain complex III [GO:0005750]; 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;PF02921; | 2.102.10.10;1.20.5.270; | Rieske iron-sulfur protein family | PTM: Processed by both the mitochondrial processing peptidase (MPP) and the mitochondrial intermediate protease (MIP). Initially, MPP removes 25 amino acids from the newly imported precursor in the mitochondrial matrix. This proteolytic processing is then followed by a second proteolytic cleavage by MIP, which removes ... | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:226365}; Single-pass membrane protein {ECO:0000250|UniProtKB:P08067}. | CATALYTIC ACTIVITY: Reaction=a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2 Fe(II)-[cytochrome c](out) + 2 H(+)(out); Xref=Rhea:RHEA:11484, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:132124; EC=7.1.1.8; Evidence={ECO:0000... | null | null | null | null | FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrom... | Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
P07064 | SOMA_ONCKE | MGQVFLLMPVLLVSCFLSQGAAIENQRLFNIAVSRVQHLHLLAQKMFNDFDGTLLPDERRQLNKIFLLDFCNSDSIVSPVDKHETQKSSVLKLLHISFRLIESWEYPSQTLIISNSLMVRNANQISEKLSDLKVGINLLITGSQDGVLSLDDNDSQQLPPYGNYYQNLGGDGNVRRNYELLACFKKDMHKVETYLTVAKCRKSLEANCTL | null | null | animal organ development [GO:0048513]; calcium ion homeostasis [GO:0055074]; chloride ion homeostasis [GO:0055064]; growth hormone receptor signaling pathway [GO:0060396]; hyperosmotic salinity response [GO:0042538]; magnesium ion homeostasis [GO:0010960]; positive regulation of gene expression [GO:0010628]; positive r... | cytosol [GO:0005829]; extracellular space [GO:0005615] | growth factor activity [GO:0008083]; growth hormone activity [GO:0070186]; growth hormone receptor binding [GO:0005131]; metal ion binding [GO:0046872] | PF00103; | 1.20.1250.10; | Somatotropin/prolactin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Growth hormone plays an important role in growth control and is involved in the regulation of several anabolic processes. Implicated as an osmoregulatory substance important for seawater adaptation. | Oncorhynchus keta (Chum salmon) (Salmo keta) |
P07071 | NRDD_BPT4 | MTIEKEIEGLIHKTNKDLLNENANKDSRVFPTQRDLMAGIVSKHIAKNMVPSFIMKAHESGIIHVHDIDYSPALPFTNCCLVDLKGMLENGFKLGNAQIETPKSIGVATAIMAQITAQVASHQYGGTTFANVDKVLSPYVKRTYAKHIEDAEKWQIADALNYAQSKTEKDVYDAFQAYEYEVNTLFSSNGQTPFVTITFGTGTDWTERMIQKAILKNRIKGLGRDGITPIFPKLVMFVEEGVNLYKDDPNYDIKQLALECASKRMYPDIISAKNNKAITGSSVPVSPMGCRSFLSVWKDSTGNEILDGRNNLGVVTLNLP... | 1.1.98.6 | null | 2'-deoxyribonucleotide biosynthetic process [GO:0009265]; DNA replication [GO:0006260] | anaerobic ribonucleoside-triphosphate reductase complex [GO:0031250] | metal ion binding [GO:0046872]; ribonucleoside-diphosphate reductase activity, thioredoxin disulfide as acceptor [GO:0004748]; ribonucleoside-triphosphate reductase activity [GO:0008998] | PF13597; | 3.20.70.20; | Anaerobic ribonucleoside-triphosphate reductase family | null | null | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + formate + H(+) = a 2'-deoxyribonucleoside 5'-triphosphate + CO2 + H2O; Xref=Rhea:RHEA:51476, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15740, ChEBI:CHEBI:16526, ChEBI:CHEBI:61557, ChEBI:CHEBI:61560; EC=1.1.98.6; Evidence={ECO:0000269|PubMed:8702830... | null | null | null | null | FUNCTION: Catalyzes the conversion of ribonucleotides into deoxyribonucleotides, which are required for DNA synthesis and repair. {ECO:0000269|PubMed:8051113, ECO:0000269|PubMed:8702830}. | Enterobacteria phage T4 (Bacteriophage T4) |
P07091 | S10A4_MOUSE | MARPLEEALDVIVSTFHKYSGKEGDKFKLNKTELKELLTRELPSFLGKRTDEAAFQKVMSNLDSNRDNEVDFQEYCVFLSCIAMMCNEFFEGCPDKEPRKK | null | null | positive regulation of canonical NF-kappaB signal transduction [GO:0043123] | collagen-containing extracellular matrix [GO:0062023]; cytosol [GO:0005829]; extracellular space [GO:0005615]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471] | actin binding [GO:0003779]; calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; chemoattractant activity [GO:0042056]; identical protein binding [GO:0042802]; RAGE receptor binding [GO:0050786]; transition metal ion binding [GO:0046914] | PF01023; | 1.10.238.10; | S-100 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P26447}. Nucleus {ECO:0000250|UniProtKB:P26447}. Cytoplasm {ECO:0000269|PubMed:8051043}. | null | null | null | null | null | FUNCTION: Calcium-binding protein that plays a role in various cellular processes including motility, angiogenesis, cell differentiation, apoptosis, and autophagy (PubMed:20519440). Increases cell motility and invasiveness by interacting with non-muscle myosin heavy chain (NMMHC) IIA/MYH9 (PubMed:8051043). Mechanistica... | Mus musculus (Mouse) |
P07092 | GDN_RAT | MNWHFPFFILTTVTLSSVYSQLNSLSLEELGSDTGIQVFNQIIKSQPHENVVISPHGIASILGMLQLGADGRTKKQLSTVMRYNVNGVGKVLKKINKAIVSKKNKDIVTVANAVFVRNGFKVEVPFAARNKEVFQCEVQSVNFQDPASACDAINFWVKNETRGMIDNLLSPNLIDSALTKLVLVNAVYFKGLWKSRFQPENTKKRTFVAGDGKSYQVPMLAQLSVFRSGSTKTPNGLWYNFIELPYHGESISMLIALPTESSTPLSAIIPHISTKTINSWMNTMVPKRMQLVLPKFTALAQTDLKEPLKALGITEMFEPS... | null | null | blood coagulation [GO:0007596]; cell differentiation [GO:0030154]; cerebellar granular layer morphogenesis [GO:0021683]; dense core granule biogenesis [GO:0061110]; detection of mechanical stimulus involved in sensory perception [GO:0050974]; embryo implantation [GO:0007566]; innervation [GO:0060384]; long-term synapti... | collagen-containing extracellular matrix [GO:0062023]; cytosol [GO:0005829]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; neuromuscular junction [GO:0031594]; neuronal cell body [GO:0043025]; platelet alpha granule [GO:0031091] | glycosaminoglycan binding [GO:0005539]; heparin binding [GO:0008201]; serine-type endopeptidase inhibitor activity [GO:0004867]; signaling receptor binding [GO:0005102] | PF00079; | 2.30.39.10;3.30.497.10;2.10.310.10; | Serpin family | null | SUBCELLULAR LOCATION: Secreted, extracellular space. | null | null | null | null | null | FUNCTION: Serine protease inhibitor with activity toward thrombin, trypsin, and urokinase. Promotes neurite extension by inhibiting thrombin. Binds heparin. {ECO:0000269|PubMed:2337608}. | Rattus norvegicus (Rat) |
P07093 | GDN_HUMAN | MNWHLPLFLLASVTLPSICSHFNPLSLEELGSNTGIQVFNQIVKSRPHDNIVISPHGIASVLGMLQLGADGRTKKQLAMVMRYGVNGVGKILKKINKAIVSKKNKDIVTVANAVFVKNASEIEVPFVTRNKDVFQCEVRNVNFEDPASACDSINAWVKNETRDMIDNLLSPDLIDGVLTRLVLVNAVYFKGLWKSRFQPENTKKRTFVAADGKSYQVPMLAQLSVFRCGSTSAPNDLWYNFIELPYHGESISMLIALPTESSTPLSAIIPHISTKTIDSWMSIMVPKRVQVILPKFTAVAQTDLKEPLKVLGITDMFDSS... | null | null | cell differentiation [GO:0030154]; cerebellar granular layer morphogenesis [GO:0021683]; detection of mechanical stimulus involved in sensory perception [GO:0050974]; innervation [GO:0060384]; long-term synaptic potentiation [GO:0060291]; mating plug formation [GO:0042628]; negative regulation of blood coagulation [GO:... | collagen-containing extracellular matrix [GO:0062023]; cytosol [GO:0005829]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; extracellular vesicle [GO:1903561]; neuromuscular junction [GO:0031594]; platelet alpha granule [GO:0031091] | glycosaminoglycan binding [GO:0005539]; heparin binding [GO:0008201]; serine-type endopeptidase inhibitor activity [GO:0004867]; signaling receptor binding [GO:0005102] | PF00079; | 2.30.39.10;3.30.497.10;2.10.310.10; | Serpin family | null | SUBCELLULAR LOCATION: Secreted, extracellular space. | null | null | null | null | null | FUNCTION: Serine protease inhibitor with activity toward thrombin, trypsin, and urokinase. Promotes neurite extension by inhibiting thrombin. Binds heparin. | Homo sapiens (Human) |
P07097 | THIL_SHIZO | MSTPSIVIASARTAVGSFNGAFANTPAHELGATVISAVLERAGVAAGEVNEVILGQVLPAGEGQNPARQAAMKAGVPQEATAWGMNQLCGSGLRAVALGMQQIATGDASIIVAGGMESMSMAPHCAHLAGGVKMGDFKMIDTMIKDGLTDAFYGYHMGTTAENVAKQWQLSRDEQDAFAVASQNKAEAAQKDGRFKDEIVPFIVKGRKGDITVDADEYIRHGATLDSMAKLRPAFDKEGTVTAGNASGLNDGAAAALLMSEAEASRRGIQPLGRIVSWATVGVDPKVMGTGPIPASRKALERAGWKIGDLDLVEANEAFA... | 2.3.1.9 | null | fatty acid beta-oxidation [GO:0006635]; poly-hydroxybutyrate biosynthetic process [GO:0042619] | cytosol [GO:0005829] | acetyl-CoA C-acetyltransferase activity [GO:0003985] | PF02803;PF00108; | 3.40.47.10; | Thiolase-like superfamily, Thiolase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=2 acetyl-CoA = acetoacetyl-CoA + CoA; Xref=Rhea:RHEA:21036, ChEBI:CHEBI:57286, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.9; Evidence={ECO:0000255|PROSITE-ProRule:PRU10020}; | null | PATHWAY: Biopolymer metabolism; poly-(R)-3-hydroxybutanoate biosynthesis. {ECO:0000305}.; PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 1/3. | null | null | null | Shinella zoogloeoides (Crabtreella saccharophila) |
P07098 | LIPF_HUMAN | MWLLLTMASLISVLGTTHGLFGKLHPGSPEVTMNISQMITYWGYPNEEYEVVTEDGYILEVNRIPYGKKNSGNTGQRPVVFLQHGLLASATNWISNLPNNSLAFILADAGYDVWLGNSRGNTWARRNLYYSPDSVEFWAFSFDEMAKYDLPATIDFIVKKTGQKQLHYVGHSQGTTIGFIAFSTNPSLAKRIKTFYALAPVATVKYTKSLINKLRFVPQSLFKFIFGDKIFYPHNFFDQFLATEVCSREMLNLLCSNALFIICGFDSKNFNTSRLDVYLSHNPAGTSVQNMFHWTQAVKSGKFQAYDWGSPVQNRMHYDQ... | 3.1.1.3 | null | lipid catabolic process [GO:0016042]; malate metabolic process [GO:0006108]; triglyceride metabolic process [GO:0006641] | extracellular region [GO:0005576]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrion [GO:0005739] | lipid binding [GO:0008289]; malate dehydrogenase activity [GO:0016615]; triglyceride lipase activity [GO:0004806] | PF00561; | 3.40.50.1820; | AB hydrolase superfamily, Lipase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P80035}. | CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Evidence={ECO:0000269|PubMed:10358049, ECO:0000269|PubMed:2243091}; CATALYTIC ACTIVITY: Reaction... | null | null | null | null | FUNCTION: Catalyzes the hydrolysis of triacylglycerols to yield free fatty acids, diacylglycerol, monoacylglycerol, and glycerol (PubMed:10358049, PubMed:2243091). Shows a preferential hydrolysis at the sn-3 position of triacylglycerol (PubMed:2243091). {ECO:0000269|PubMed:10358049, ECO:0000269|PubMed:2243091}. | Homo sapiens (Human) |
P07099 | HYEP_HUMAN | MWLEILLTSVLGFAIYWFISRDKEETLPLEDGWWGPGTRSAAREDDSIRPFKVETSDEEIHDLHQRIDKFRFTPPLEDSCFHYGFNSNYLKKVISYWRNEFDWKKQVEILNRYPHFKTKIEGLDIHFIHVKPPQLPAGHTPKPLLMVHGWPGSFYEFYKIIPLLTDPKNHGLSDEHVFEVICPSIPGYGFSEASSKKGFNSVATARIFYKLMLRLGFQEFYIQGGDWGSLICTNMAQLVPSHVKGLHLNMALVLSNFSTLTLLLGQRFGRFLGLTERDVELLYPVKEKVFYSLMRESGYMHIQCTKPDTVGSALNDSPVG... | 3.3.2.9 | null | arachidonic acid metabolic process [GO:0019369]; aromatic compound catabolic process [GO:0019439]; epoxide metabolic process [GO:0097176]; response to organic cyclic compound [GO:0014070]; response to toxic substance [GO:0009636]; xenobiotic metabolic process [GO:0006805] | endoplasmic reticulum membrane [GO:0005789] | cis-stilbene-oxide hydrolase activity [GO:0033961]; epoxide hydrolase activity [GO:0004301]; oxysterol binding [GO:0008142] | PF00561; | 3.40.50.1820; | Peptidase S33 family | null | SUBCELLULAR LOCATION: Microsome membrane {ECO:0000269|PubMed:24958911}; Single-pass type III membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P07687}; Single-pass type III membrane protein {ECO:0000250|UniProtKB:P07687}. | CATALYTIC ACTIVITY: Reaction=cis-stilbene oxide + H2O = (1R,2R)-hydrobenzoin; Xref=Rhea:RHEA:23900, ChEBI:CHEBI:15377, ChEBI:CHEBI:50004, ChEBI:CHEBI:50014; EC=3.3.2.9; Evidence={ECO:0000269|PubMed:24958911}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23901; Evidence={ECO:0000269|PubMed:24958911}; CATALYTIC A... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.8 uM for 8,9-EET {ECO:0000269|PubMed:22798687}; KM=0.4 uM for 11,12-EET {ECO:0000269|PubMed:22798687}; KM=0.9 uM for 14,15-EET {ECO:0000269|PubMed:22798687}; KM=5.8 uM for leukotoxin {ECO:0000269|PubMed:22798687}; Vmax=0.12 umol/min/mg enzyme with 8,9-EET as subs... | null | null | null | FUNCTION: Biotransformation enzyme that catalyzes the hydrolysis of arene and aliphatic epoxides to less reactive and more water soluble dihydrodiols by the trans addition of water (By similarity). Plays a role in the metabolism of endogenous lipids such as epoxide-containing fatty acids (PubMed:22798687). Metabolizes ... | Homo sapiens (Human) |
P07101 | TY3H_HUMAN | MPTPDATTPQAKGFRRAVSELDAKQAEAIMVRGQGAPGPSLTGSPWPGTAAPAASYTPTPRSPRFIGRRQSLIEDARKEREAAVAAAAAAVPSEPGDPLEAVAFEEKEGKAVLNLLFSPRATKPSALSRAVKVFETFEAKIHHLETRPAQRPRAGGPHLEYFVRLEVRRGDLAALLSGVRQVSEDVRSPAGPKVPWFPRKVSELDKCHHLVTKFDPDLDLDHPGFSDQVYRQRRKLIAEIAFQYRHGDPIPRVEYTAEEIATWKEVYTTLKGLYATHACGEHLEAFALLERFSGYREDNIPQLEDVSRFLKERTGFQLRP... | 1.14.16.2 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:P04177}; | aminergic neurotransmitter loading into synaptic vesicle [GO:0015842]; anatomical structure morphogenesis [GO:0009653]; animal organ morphogenesis [GO:0009887]; cellular response to alkaloid [GO:0071312]; cellular response to glucose stimulus [GO:0071333]; cellular response to growth factor stimulus [GO:0071363]; cellu... | axon [GO:0030424]; cytoplasm [GO:0005737]; cytoplasmic side of plasma membrane [GO:0009898]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; dendrite [GO:0030425]; melanosome membrane [GO:0033162]; mitochondrion [GO:0005739]; neuron projection [GO:0043005]; nucleus [GO:0005634]; perikaryon [GO:0043204]; perinuc... | amino acid binding [GO:0016597]; dopamine binding [GO:0035240]; enzyme binding [GO:0019899]; ferric iron binding [GO:0008199]; ferrous iron binding [GO:0008198]; identical protein binding [GO:0042802]; oxygen binding [GO:0019825]; protein domain specific binding [GO:0019904]; tetrahydrobiopterin binding [GO:0034617]; t... | PF00351;PF21417;PF12549; | 3.30.70.260;1.10.800.10; | Biopterin-dependent aromatic amino acid hydroxylase family | PTM: Phosphorylated on Ser-19, Ser-62 and Ser-71 by several protein kinases with different site specificities. Phosphorylation at Ser-62 and Ser-71 leads to an increase of TH activity (PubMed:7901013). Phosphorylation at Ser-71 activates the enzyme and also counteracts the feedback inhibition of TH by catecholamines (P... | SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P24529}. Nucleus {ECO:0000250|UniProtKB:P04177}. Cell projection, axon {ECO:0000250|UniProtKB:P24529}. Cytoplasm {ECO:0000250|UniProtKB:P04177}. Cytoplasmic vesicle, secretory vesicle, synaptic vesicle {ECO:0000250|UniProtKB:P04177}. Note=When p... | CATALYTIC ACTIVITY: Reaction=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-tyrosine + O2 = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + L-dopa; Xref=Rhea:RHEA:18201, ChEBI:CHEBI:15379, ChEBI:CHEBI:15642, ChEBI:CHEBI:57504, ChEBI:CHEBI:58315, ChEBI:CHEBI:59560; EC=1.14.16.2; Evidence={ECO:0000269|PubMed:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=39 uM for 6R-tetrahydrobiopterin {ECO:0000269|PubMed:24753243}; KM=5.1 uM for L-tyrosine {ECO:0000269|PubMed:24753243}; KM=35 uM for L-tyrosine (in presence of N-ethylmaleimide) {ECO:0000269|PubMed:34922205}; KM=15 uM for L-tyrosine {ECO:0000269|PubMed:34922205}; K... | PATHWAY: Catecholamine biosynthesis; dopamine biosynthesis; dopamine from L-tyrosine: step 1/2. {ECO:0000269|PubMed:17391063}. | null | null | FUNCTION: Catalyzes the conversion of L-tyrosine to L-dihydroxyphenylalanine (L-Dopa), the rate-limiting step in the biosynthesis of cathecolamines, dopamine, noradrenaline, and adrenaline. Uses tetrahydrobiopterin and molecular oxygen to convert tyrosine to L-Dopa (PubMed:15287903, PubMed:1680128, PubMed:17391063, Pub... | Homo sapiens (Human) |
P07102 | PPA_ECOLI | MKAILIPFLSLLIPLTPQSAFAQSEPELKLESVVIVSRHGVRAPTKATQLMQDVTPDAWPTWPVKLGWLTPRGGELIAYLGHYQRQRLVADGLLAKKGCPQSGQVAIIADVDERTRKTGEAFAAGLAPDCAITVHTQADTSSPDPLFNPLKTGVCQLDNANVTDAILSRAGGSIADFTGHRQTAFRELERVLNFPQSNLCLKREKQDESCSLTQALPSELKVSADNVSLTGAVSLASMLTEIFLLQQAQGMPEPGWGRITDSHQWNTLLSLHNAQFYLLQRTPEVARSRATPLLDLIKTALTPHPPQKQAYGVTLPTSVL... | 3.1.3.-; 3.6.1.- | null | cellular response to anoxia [GO:0071454]; cellular response to phosphate starvation [GO:0016036]; dephosphorylation [GO:0016311]; lysosome organization [GO:0007040] | lysosome [GO:0005764]; outer membrane-bounded periplasmic space [GO:0030288] | 4-phytase activity [GO:0008707]; acid phosphatase activity [GO:0003993]; GTPase activity [GO:0003924]; inositol phosphate phosphatase activity [GO:0052745]; nucleotidase activity [GO:0008252]; sugar-phosphatase activity [GO:0050308] | PF00328; | 3.40.50.1240; | Histidine acid phosphatase family | null | SUBCELLULAR LOCATION: Periplasm {ECO:0000269|PubMed:10696472, ECO:0000269|PubMed:1429631, ECO:0000269|PubMed:8387749, ECO:0000269|PubMed:8407904}. | CATALYTIC ACTIVITY: Reaction=1D-myo-inositol hexakisphosphate + H2O = 1D-myo-inositol 1,2,3,4,5-pentakisphosphate + phosphate; Xref=Rhea:RHEA:68308, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:58130, ChEBI:CHEBI:177294; Evidence={ECO:0000269|PubMed:10696472, ECO:0000269|PubMed:11035187, ECO:0000269|PubMed:3071247... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.13 mM for phytate {ECO:0000269|Ref.8}; KM=0.63 mM for phytate {ECO:0000269|PubMed:10696472}; KM=15 uM for D-Ins(1,2,3,4,5)P5 {ECO:0000269|PubMed:11035187}; KM=0.35 mM for GTP {ECO:0000269|PubMed:6282821}; KM=1.8 mM for ppGpp {ECO:0000269|PubMed:6282821}; KM=0.15 ... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5 for phytase activity (PubMed:10696472, PubMed:8387749). Optimum pH is 2.5 for acid phosphatase activity (PubMed:6282821). Optimum pH is 2.5-3.0 for acid phosphatase activity (PubMed:10696472). {ECO:0000269|PubMed:10696472, ECO:0000269|PubMed:6282821, ECO:... | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 55 degrees Celsius for phytase activity (PubMed:8387749). Optimum temperature is 60 degrees Celsius for phytase activity (PubMed:10696472). {ECO:0000269|PubMed:10696472, ECO:0000269|PubMed:8387749}; | FUNCTION: Catalyzes the hydrolysis of phytate (or myo-inositol hexakisphosphate, an indigestible organic form of phosphorus that is found in many plant tissues) to myo-inositol and inorganic phosphate (PubMed:10696472, PubMed:11035187, PubMed:30712472, PubMed:8387749, Ref.8). Dephosphorylates phytate in a stereospecifi... | Escherichia coli (strain K12) |
P07103 | GUNZ_DICD3 | MPLSYLDKNPVIDSKKHALRKKLFLSCAYFGLSLACLSSNAWASVEPLSVNGNKIYAGEKAKSFAGNSLFWSNNGWGGEKFYTADTVASLKKDWKSSIVRAAMGVQESGGYLQDPAGNKAKVERVVDAAIANDMYAIIGWHSHSAENNRSEAIRFFQEMARKYGNKPNVIYEIYNEPLQVSWSNTIKPYAEAVISAIRAIDPDNLIIVGTPSWSQNVDEASRDPINAKNIAYTLHFYAGTHGESLRNKARQALNNGIALFVTEWGTVNADGNGGVNQTETDAWVTFMRDNNISNANWALNDKNEGASTYYPDSKNLTESG... | 3.2.1.4 | null | cellulose catabolic process [GO:0030245] | extracellular region [GO:0005576] | carbohydrate binding [GO:0030246]; cellulase activity [GO:0008810] | PF14600;PF00150; | 2.10.10.20;3.20.20.80; | Glycosyl hydrolase 5 (cellulase A) family | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4; | null | null | null | null | FUNCTION: Represents 97% of the global cellulase activity. | Dickeya dadantii (strain 3937) (Erwinia chrysanthemi (strain 3937)) |
P07107 | ACBP_BOVIN | MSQAEFDKAAEEVKHLKTKPADEEMLFIYSHYKQATVGDINTERPGMLDFKGKAKWDAWNELKGTSKEDAMKAYIDKVEELKKKYGI | null | null | fatty acid metabolic process [GO:0006631] | endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; mitochondrion [GO:0005739] | fatty-acyl-CoA binding [GO:0000062] | PF00887; | 1.20.80.10; | ACBP family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:17953517}. Golgi apparatus {ECO:0000269|PubMed:17953517}. Note=Golgi localization is dependent on ligand binding. {ECO:0000250|UniProtKB:P07108}. | null | null | null | null | null | FUNCTION: Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. It is also able to displace diazepam from the benzodiazepine (BZD) recognition site located on the GABA type A receptor. It is therefore possible that this protein also acts as... | Bos taurus (Bovine) |
P07108 | ACBP_HUMAN | MSQAEFEKAAEEVRHLKTKPSDEEMLFIYGHYKQATVGDINTERPGMLDFTGKAKWDAWNELKGTSKEDAMKAYINKVEELKKKYGI | null | null | fatty acid metabolic process [GO:0006631]; negative regulation of protein lipidation [GO:1903060]; phosphatidylcholine acyl-chain remodeling [GO:0036151]; positive regulation of CoA-transferase activity [GO:1905920]; positive regulation of phospholipid transport [GO:2001140] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794]; mitochondrion [GO:0005739]; perinuclear endoplasmic reticulum [GO:0097038]; protein-lipid complex [GO:0032994] | benzodiazepine receptor binding [GO:0030156]; fatty-acyl-CoA binding [GO:0000062]; identical protein binding [GO:0042802]; long-chain fatty acyl-CoA binding [GO:0036042] | PF00887; | 1.20.80.10; | ACBP family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:17953517, ECO:0000269|PubMed:21698759}. Golgi apparatus {ECO:0000269|PubMed:17953517, ECO:0000269|PubMed:21698759}. Note=Golgi localization is dependent on ligand binding (PubMed:17953517). {ECO:0000269|PubMed:17953517}. | null | null | null | null | null | FUNCTION: Binds medium- and long-chain acyl-CoA esters with very high affinity and may function as an intracellular carrier of acyl-CoA esters. It is also able to displace diazepam from the benzodiazepine (BZD) recognition site located on the GABA type A receptor. It is therefore possible that this protein also acts as... | Homo sapiens (Human) |
P07112 | MOBA2_ECOLX | MAIYHLTAKTGSRSGGQSARAKADYIQREGKYARDMDEVLHAESGHMPEFVERPADYWDAADLYERANGRLFKEVEFALPVELTLDQQKALASEFAQHLTGAERLPYTLAIHAGGGENPHCHLMISERINDGIERPAAQWFKRYNGKTPEKGGAQKTEALKPKAWLEQTREAWADHANRALERAGHDARIDHRTLEAQGIERLPGVHLGPNVVEMEGRGIRTDRADVALNIDTANAQIIDLQEYREAIDHERNRQSEEIQRHQRVSGADRTAGPEHGDTGRRSPAGHEPDPAGQRGAGGGVAESPAPDRGGMGGAGQRVA... | 2.7.7.101; 5.6.2.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:1738602, ECO:0000269|PubMed:8223650}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:1738602, ECO:0000269|PubMed:8223650}; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:1738602, ECO:0000269|PubMed:8223650}... | null | cytoplasm [GO:0005737]; DNA-directed RNA polymerase complex [GO:0000428] | DNA binding [GO:0003677]; DNA primase activity [GO:0003896]; DNA topoisomerase type I (single strand cut, ATP-independent) activity [GO:0003917]; metal ion binding [GO:0046872] | PF03389;PF16793; | 1.10.1240.50;3.30.930.30;3.30.1490.240;3.30.70.1790;1.20.5.460; | MobA/MobL family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=ATP-independent breakage of single-stranded DNA, followed by passage and rejoining.; EC=5.6.2.1; CATALYTIC ACTIVITY: Reaction=ssDNA + n NTP = ssDNA/pppN(pN)n-1 hybrid + (n-1) diphosphate.; EC=2.7.7.101; Evidence={ECO:0000269|PubMed:10217797}; | null | null | null | null | FUNCTION: Part of the relaxosome complex that is responsible for plasmid transfer during conjugation. Locally unwinds DNA and catalyzes the cleavage of one of the DNA strands at oriT. The cleaved strand is then transferred through the dedicated type IV secretion apparatus. MobA remains covalently linked at the 5' end o... | Escherichia coli |
P07117 | PUTP_ECOLI | MAISTPMLVTFCVYIFGMILIGFIAWRSTKNFDDYILGGRSLGPFVTALSAGASDMSGWLLMGLPGAVFLSGISESWIAIGLTLGAWINWKLVAGRLRVHTEYNNNALTLPDYFTGRFEDKSRILRIISALVILLFFTIYCASGIVAGARLFESTFGMSYETALWAGAAATILYTFIGGFLAVSWTDTVQASLMIFALILTPVIVIISVGGFGDSLEVIKQKSIENVDMLKGLNFVAIISLMGWGLGYFGQPHILARFMAADSHHSIVHARRISMTWMILCLAGAVAVGFFGIAYFNDHPALAGAVNQNAERVFIELAQI... | null | null | proline transport [GO:0015824]; short-chain fatty acid transport [GO:0015912]; transmembrane transport [GO:0055085] | plasma membrane [GO:0005886] | L-proline transmembrane transporter activity [GO:0015193]; proline:sodium symporter activity [GO:0005298]; sodium ion binding [GO:0031402] | PF00474; | 1.20.1730.10; | Sodium:solute symporter (SSF) (TC 2.A.21) family | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:3007935, ECO:0000269|PubMed:3512540, ECO:0000269|PubMed:3902503, ECO:0000269|PubMed:9756872}; Multi-pass membrane protein {ECO:0000269|PubMed:16079137, ECO:0000269|PubMed:9756872}. | CATALYTIC ACTIVITY: Reaction=L-proline(in) + Na(+)(in) = L-proline(out) + Na(+)(out); Xref=Rhea:RHEA:28967, ChEBI:CHEBI:29101, ChEBI:CHEBI:60039; Evidence={ECO:0000269|PubMed:1567896, ECO:0000269|PubMed:3512540, ECO:0000269|PubMed:9693004}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.5 uM for L-proline {ECO:0000269|PubMed:3512540}; KM=2 uM for L-proline (for Na(+)-driven transport) {ECO:0000269|PubMed:9693004}; KM=31 uM for Na(+) (in intact cells) {ECO:0000269|PubMed:9693004}; KM=730 uM for Na(+) (for reconstituted PutP in proteoliposomes) {E... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.0. {ECO:0000269|PubMed:3512540}; | null | FUNCTION: Catalyzes the sodium-dependent uptake of extracellular L-proline (PubMed:1567896, PubMed:3512540, PubMed:9693004). This protein is also capable of using lithium as the transport cation (PubMed:1567896, PubMed:9693004). Also catalyzes the uptake of propionate (PubMed:17088549). {ECO:0000269|PubMed:1567896, ECO... | Escherichia coli (strain K12) |
P07118 | SYV_ECOLI | MEKTYNPQDIEQPLYEHWEKQGYFKPNGDESQESFCIMIPPPNVTGSLHMGHAFQQTIMDTMIRYQRMQGKNTLWQVGTDHAGIATQMVVERKIAAEEGKTRHDYGREAFIDKIWEWKAESGGTITRQMRRLGNSVDWERERFTMDEGLSNAVKEVFVRLYKEDLIYRGKRLVNWDPKLRTAISDLEVENRESKGSMWHIRYPLADGAKTADGKDYLVVATTRPETLLGDTGVAVNPEDPRYKDLIGKYVILPLVNRRIPIVGDEHADMEKGTGCVKITPAHDFNDYEVGKRHALPMINILTFDGDIRESAQVFDTKGNE... | 6.1.1.9 | null | cytosolic valyl-tRNA aminoacylation [GO:0061475]; positive regulation of translational fidelity [GO:0045903]; valyl-tRNA aminoacylation [GO:0006438] | cytosol [GO:0005829] | aminoacyl-tRNA editing activity [GO:0002161]; ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; valine-tRNA ligase activity [GO:0004832] | PF08264;PF00133;PF10458; | 3.40.50.620;1.10.287.380;3.90.740.10; | Class-I aminoacyl-tRNA synthetase family, ValS type 1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=ATP + L-valine + tRNA(Val) = AMP + diphosphate + L-valyl-tRNA(Val); Xref=Rhea:RHEA:10704, Rhea:RHEA-COMP:9672, Rhea:RHEA-COMP:9708, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57762, ChEBI:CHEBI:78442, ChEBI:CHEBI:78537, ChEBI:CHEBI:456215; EC=6.1.1.9; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.1 uM for tRNA {ECO:0000269|PubMed:12475234}; KM=47 uM for valine {ECO:0000269|PubMed:12475234}; | null | null | null | FUNCTION: Catalyzes the attachment of valine to tRNA(Val). As ValRS can inadvertently accommodate and process structurally similar amino acids such as threonine, to avoid such errors, it has a 'posttransfer' editing activity that hydrolyzes mischarged Thr-tRNA(Val) in a tRNA-dependent manner. | Escherichia coli (strain K12) |
P07140 | ACES_DROME | MAISCRQSRVLPMSLPLPLTIPLPLVLVLSLHLSGVCGVIDRLVVQTSSGPVRGRSVTVQGREVHVYTGIPYAKPPVEDLRFRKPVPAEPWHGVLDATGLSATCVQERYEYFPGFSGEEIWNPNTNVSEDCLYINVWAPAKARLRHGRGANGGEHPNGKQADTDHLIHNGNPQNTTNGLPILIWIYGGGFMTGSATLDIYNADIMAAVGNVIVASFQYRVGAFGFLHLAPEMPSEFAEEAPGNVGLWDQALAIRWLKDNAHAFGGNPEWMTLFGESAGSSSVNAQLMSPVTRGLVKRGMMQSGTMNAPWSHMTSEKAVEI... | 3.1.1.7 | null | acetylcholine catabolic process [GO:0006581]; acetylcholine catabolic process in synaptic cleft [GO:0001507]; chemical synaptic transmission [GO:0007268]; choline catabolic process [GO:0042426]; choline metabolic process [GO:0019695] | cytoplasm [GO:0005737]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; side of membrane [GO:0098552]; synapse [GO:0045202]; synaptic cleft [GO:0043083] | acetylcholinesterase activity [GO:0003990]; cholinesterase activity [GO:0004104]; protein homodimerization activity [GO:0042803]; serine hydrolase activity [GO:0017171]; sulfate binding [GO:0043199] | PF00135; | 3.40.50.1820; | Type-B carboxylesterase/lipase family | PTM: Proteolytic cleavage into the 16 kDa subunit and the 55 kDa subunits originates from the hydrophilic peptide, aa 148-180, and is associated with excretion out of the cell. {ECO:0000269|PubMed:2975507}.; PTM: Neither N-glycosylation nor dimerization is required for enzyme activity or substrate specificity, but prot... | SUBCELLULAR LOCATION: Synapse. Cell membrane; Lipid-anchor, GPI-anchor. Note=Attached to the membrane of the neuronal cholinergic synapses by a GPI-anchor. | CATALYTIC ACTIVITY: Reaction=acetylcholine + H2O = acetate + choline + H(+); Xref=Rhea:RHEA:17561, ChEBI:CHEBI:15354, ChEBI:CHEBI:15355, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30089; EC=3.1.1.7; | null | null | null | null | FUNCTION: Rapidly hydrolyzes choline released into the synapse. It can hydrolyze butyrylthiocholine. | Drosophila melanogaster (Fruit fly) |
P07141 | CSF1_MOUSE | MTARGAAGRCPSSTWLGSRLLLVCLLMSRSIAKEVSEHCSHMIGNGHLKVLQQLIDSQMETSCQIAFEFVDQEQLDDPVCYLKKAFFLVQDIIDETMRFKDNTPNANATERLQELSNNLNSCFTKDYEEQNKACVRTFHETPLQLLEKIKNFFNETKNLLEKDWNIFTKNCNNSFAKCSSRDVVTKPDCNCLYPKATPSSDPASASPHQPPAPSMAPLAGLAWDDSQRTEGSSLLPSELPLRIEDPGSAKQRPPRSTCQTLESTEQPNHGDRLTEDSQPHPSAGGPVPGVEDILESSLGTNWVLEEASGEASEGFLTQEA... | null | null | branching involved in mammary gland duct morphogenesis [GO:0060444]; developmental process involved in reproduction [GO:0003006]; homeostasis of number of cells within a tissue [GO:0048873]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; macrophage colony-stimulating factor signaling pathway [... | CSF1-CSF1R complex [GO:1990682]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; nuclear body [GO:0016604]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886] | cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; identical protein binding [GO:0042802]; macrophage colony-stimulating factor receptor binding [GO:0005157]; protein homodimerization activity [GO:0042803] | PF05337; | 1.20.1250.10; | null | PTM: N-glycosylated. {ECO:0000250|UniProtKB:P09603}.; PTM: O-glycosylated; contains chondroitin sulfate. {ECO:0000269|PubMed:1733926}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}.; SUBCELLULAR LOCATION: [Processed macrophage colony-stimulating factor 1]: Secreted, extracellular space {ECO:0000250}. | null | null | null | null | null | FUNCTION: Cytokine that plays an essential role in the regulation of survival, proliferation and differentiation of hematopoietic precursor cells, especially mononuclear phagocytes, such as macrophages and monocytes. Promotes the release of pro-inflammatory chemokines, and thereby plays an important role in innate immu... | Mus musculus (Mouse) |
P07142 | CY1_NEUCR | MLARTCLRSTRTFASAKNGAFKFAKRSASTQSSGAAAESPLRLNIAAAAATAVAAGSIAWYYHLYGFASAMTPAEEGLHATKYPWVHEQWLKTFDHQALRRGFQVYREVCASCHSLSRVPYRALVGTILTVDEAKALAEENEYDTEPNDQGEIEKRPGKLSDYLPDPYKNDEAARFANNGALPPDLSLIVKARHGGCDYIFSLLTGYPDEPPAGASVGAGLNFNPYFPGTGIAMARVLYDGLVDYEDGTPASTSQMAKDVVEFLNWAAEPEMDDRKRMGMKVLVVTSVLFALSVYVKRYKWAWLKSRKIVYDPPKSPPPA... | 7.1.1.8 | COFACTOR: Name=heme c; Xref=ChEBI:CHEBI:61717; Evidence={ECO:0000250|UniProtKB:P07143}; Note=Binds 1 heme c group covalently per subunit. {ECO:0000250|UniProtKB:P07143}; | mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122] | mitochondrial respiratory chain complex III [GO:0005750] | heme binding [GO:0020037]; metal ion binding [GO:0046872]; ubiquinol-cytochrome-c reductase activity [GO:0008121] | PF02167; | 1.10.760.10;1.20.5.100; | Cytochrome c family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:226365}; Single-pass membrane protein {ECO:0000250|UniProtKB:P07143}. | CATALYTIC ACTIVITY: Reaction=a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2 Fe(II)-[cytochrome c](out) + 2 H(+)(out); Xref=Rhea:RHEA:11484, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:132124; EC=7.1.1.8; Evidence={ECO:0000... | null | null | null | null | FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrom... | Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) |
P07143 | CY1_YEAST | MFSNLSKRWAQRTLSKSFYSTATGAASKSGKLTQKLVTAGVAAAGITASTLLYADSLTAEAMTAAEHGLHAPAYAWSHNGPFETFDHASIRRGYQVYREVCAACHSLDRVAWRTLVGVSHTNEEVRNMAEEFEYDDEPDEQGNPKKRPGKLSDYIPGPYPNEQAARAANQGALPPDLSLIVKARHGGCDYIFSLLTGYPDEPPAGVALPPGSNYNPYFPGGSIAMARVLFDDMVEYEDGTPATTSQMAKDVTTFLNWCAEPEHDERKRLGLKTVIILSSLYLLSIWVKKFKWAGIKTRKFVFNPPKPRK | 7.1.1.8 | COFACTOR: Name=heme c; Xref=ChEBI:CHEBI:61717; Evidence={ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}; Note=Binds 1 heme c group covalently per subunit. {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}; | cellular respiration [GO:0045333]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122] | cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrial respiratory chain complex III [GO:0005750]; mitochondrion [GO:0005739] | heme binding [GO:0020037]; metal ion binding [GO:0046872]; ubiquinol-cytochrome-c reductase activity [GO:0008121] | PF02167; | 1.10.760.10;1.20.5.100; | Cytochrome c family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}; Single-pass membrane protein {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}. | CATALYTIC ACTIVITY: Reaction=a quinol + 2 Fe(III)-[cytochrome c](out) = a quinone + 2 Fe(II)-[cytochrome c](out) + 2 H(+)(out); Xref=Rhea:RHEA:11484, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15378, ChEBI:CHEBI:24646, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI:132124; EC=7.1.1.8; Evidence={ECO:0000... | null | null | null | null | FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrom... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07146 | TRY2_MOUSE | MSALLILALVGAAVAFPVDDDDKIVGGYTCRESSVPYQVSLNAGYHFCGGSLINDQWVVSAAHCYKYRIQVRLGEHNINVLEGNEQFVDSAKIIRHPNYNSWTLDNDIMLIKLASPVTLNARVASVPLPSSCAPAGTQCLISGWGNTLSNGVNNPDLLQCVDAPVLPQADCEASYPGDITNNMICVGFLEGGKDSCQGDSGGPVVCNGELQGIVSWGYGCAQPDAPGVYTKVCNYVDWIQNTIADN | 3.4.21.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250}; | collagen catabolic process [GO:0030574]; digestion [GO:0007586]; proteolysis [GO:0006508]; response to caffeine [GO:0031000]; response to nicotine [GO:0035094]; response to nutrient [GO:0007584] | collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; extracellular space [GO:0005615] | calcium ion binding [GO:0005509]; serine-type endopeptidase activity [GO:0004252] | PF00089; | 2.40.10.10; | Peptidase S1 family | null | SUBCELLULAR LOCATION: Secreted, extracellular space. | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.; EC=3.4.21.4; | null | null | null | null | null | Mus musculus (Mouse) |
P07147 | TYRP1_MOUSE | MKSYNVLPLAYISLFLMLFYQVWAQFPRECANIEALRRGVCCPDLLPSSGPGTDPCGSSSGRGRCVAVIADSRPHSRHYPHDGKDDREAWPLRFFNRTCQCNDNFSGHNCGTCRPGWRGAACNQKILTVRRNLLDLSPEEKSHFVRALDMAKRTTHPQFVIATRRLEDILGPDGNTPQFENISVYNYFVWTHYYSVKKTFLGTGQESFGDVDFSHEGPAFLTWHRYHLLQLERDMQEMLQEPSFSLPYWNFATGKNVCDVCTDDLMGSRSNFDSTLISPNSVFSQWRVVCESLEEYDTLGTLCNSTEGGPIRRNPAGNVG... | 1.14.18.- | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000250|UniProtKB:P17643}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P17643}; Note=Contains bound zinc ions after heterologous expression in insect cells. {ECO:0000250|UniProtKB:P17643}; | acetoacetic acid metabolic process [GO:0043438]; melanin biosynthetic process from tyrosine [GO:0006583]; melanin metabolic process [GO:0006582]; melanocyte differentiation [GO:0030318]; melanosome organization [GO:0032438]; pigmentation [GO:0043473]; positive regulation of melanin biosynthetic process [GO:0048023] | clathrin-coated endocytic vesicle membrane [GO:0030669]; endosome membrane [GO:0010008]; melanosome [GO:0042470]; melanosome membrane [GO:0033162] | identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; tyrosinase activity [GO:0004503] | PF00264; | 1.10.1280.10; | Tyrosinase family | PTM: Glycosylated. {ECO:0000269|PubMed:1537333}. | SUBCELLULAR LOCATION: Melanosome membrane {ECO:0000269|PubMed:17182842, ECO:0000269|PubMed:18650808, ECO:0000269|PubMed:26620560}; Single-pass type I membrane protein {ECO:0000269|PubMed:17182842}. Note=Located to mature stage III and IV melanosomes and apposed endosomal tubular membranes. Transported to pigmented mela... | CATALYTIC ACTIVITY: Reaction=2 5,6-dihydroxyindole-2-carboxylate + O2 = 2 H2O + 2 indole-5,6-quinone-2-carboxylate; Xref=Rhea:RHEA:68388, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16875, ChEBI:CHEBI:177869; Evidence={ECO:0000269|PubMed:7813420}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68389; Eviden... | null | PATHWAY: Pigment biosynthesis; melanin biosynthesis. {ECO:0000269|PubMed:2245916}. | null | null | FUNCTION: Plays a role in melanin biosynthesis (PubMed:2245916). Catalyzes the oxidation of 5,6-dihydroxyindole-2-carboxylic acid (DHICA) into indole-5,6-quinone-2-carboxylic acid (PubMed:7813420). May regulate or influence the type of melanin synthesized (PubMed:2245916, PubMed:7813420). Also to a lower extent, capabl... | Mus musculus (Mouse) |
P07148 | FABPL_HUMAN | MSFSGKYQLQSQENFEAFMKAIGLPEELIQKGKDIKGVSEIVQNGKHFKFTITAGSKVIQNEFTVGEECELETMTGEKVKTVVQLEGDNKLVTTFKNIKSVTELNGDIITNTMTLGDIVFKRISKRI | null | null | cellular response to hydrogen peroxide [GO:0070301]; cellular response to hypoxia [GO:0071456]; fatty acid transport [GO:0015908]; intestinal absorption [GO:0050892]; negative regulation of apoptotic process [GO:0043066]; negative regulation of cysteine-type endopeptidase activity involved in apoptotic process [GO:0043... | apical cortex [GO:0045179]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; peroxisomal matrix [GO:0005782]; protein-containing complex [GO:0032991] | antioxidant activity [GO:0016209]; bile acid binding [GO:0032052]; chromatin binding [GO:0003682]; fatty acid binding [GO:0005504]; heterocyclic compound binding [GO:1901363]; long-chain fatty acid transporter activity [GO:0005324]; oleic acid binding [GO:0070538]; phospholipid binding [GO:0005543] | PF14651; | 2.40.128.20; | Calycin superfamily, Fatty-acid binding protein (FABP) family | null | SUBCELLULAR LOCATION: Cytoplasm. | null | null | null | null | null | FUNCTION: Plays a role in lipoprotein-mediated cholesterol uptake in hepatocytes (PubMed:25732850). Binds cholesterol (PubMed:25732850). Binds free fatty acids and their coenzyme A derivatives, bilirubin, and some other small molecules in the cytoplasm. May be involved in intracellular lipid transport (By similarity). ... | Homo sapiens (Human) |
P07149 | FAS1_YEAST | MDAYSTRPLTLSHGSLEHVLLVPTASFFIASQLQEQFNKILPEPTEGFAADDEPTTPAELVGKFLGYVSSLVEPSKVGQFDQVLNLCLTEFENCYLEGNDIHALAAKLLQENDTTLVKTKELIKNYITARIMAKRPFDKKSNSALFRAVGEGNAQLVAIFGGQGNTDDYFEELRDLYQTYHVLVGDLIKFSAETLSELIRTTLDAEKVFTQGLNILEWLENPSNTPDKDYLLSIPISCPLIGVIQLAHYVVTAKLLGFTPGELRSYLKGATGHSQGLVTAVAIAETDSWESFFVSVRKAITVLFFIGVRCYEAYPNTSLP... | 1.3.1.9; 2.3.1.38; 2.3.1.39; 2.3.1.86; 3.1.2.14; 4.2.1.59 | null | long-chain fatty acid biosynthetic process [GO:0042759] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; fatty acid synthase complex [GO:0005835]; lipid droplet [GO:0005811]; mitochondrion [GO:0005739] | (3R)-3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase activity [GO:0004317]; (3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity [GO:0019171]; [acyl-carrier-protein] S-acetyltransferase activity [GO:0004313]; [acyl-carrier-protein] S-malonyltransferase activity [GO:0004314]; enoyl-[acyl-carrier-protein] r... | PF00698;PF08354;PF17951;PF17828;PF13452;PF01575;PF16073; | 1.20.1050.120;1.20.930.70;3.30.1120.100;3.30.70.3330;6.10.140.1400;6.10.60.10;6.20.240.10;3.20.20.70;3.10.129.10;3.40.366.10; | Fungal fatty acid synthetase subunit beta family | null | null | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain fatty acyl-CoA + n CO2 + n CoA + H2O + 2n NADP(+); Xref=Rhea:RHEA:22896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChE... | null | null | null | null | FUNCTION: Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The beta subunit contains domains for: [acyl-carrier-protein] acetyltransferase and malonyltransferase, S-acyl fatty acid synthase thioesterase, enoyl-[acyl-carrier-protein] reductase, and 3-hydroxy... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07150 | ANXA1_RAT | MAMVSEFLKQACYIEKQEQEYVQAVKSYKGGPGSAVSPYPSFNPSSDVAALHKAIMVKGVDEATIIDILTKRTNAQRQQIKAAYLQETGKPLDETLKKALTGHLEEVVLAMLKTPAQFDADELRAAMKGLGTDEDTLIEILTTRSNQQIREITRVYREELKRDLAKDITSDTSGDFRNALLALAKGDRCEDMSVNQDLADTDARALYEAGERRKGTDVNVFNTILTTRSYPHLRKVFQNYRKYSQHDMNKALDLELKGDIEKCLTTIVKCATSTPAFFAEKLYEAMKGAGTRHKTLIRIMVSRSEIDMNEIKVFYQKKYG... | null | null | actin cytoskeleton organization [GO:0030036]; adaptive immune response [GO:0002250]; alpha-beta T cell differentiation [GO:0046632]; arachidonic acid secretion [GO:0050482]; cell surface receptor signaling pathway [GO:0007166]; cellular response to glucocorticoid stimulus [GO:0071385]; cellular response to hydrogen per... | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; cell surface [GO:0009986]; cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; early endosome membrane [GO:0031901]; endosome [GO:0005768]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; lateral plasma membrane [G... | cadherin binding involved in cell-cell adhesion [GO:0098641]; calcium ion binding [GO:0005509]; calcium-dependent phospholipid binding [GO:0005544]; calcium-dependent protein binding [GO:0048306]; DNA/DNA annealing activity [GO:1990814]; double-stranded DNA helicase activity [GO:0036121]; identical protein binding [GO:... | PF00191; | 1.10.220.10; | Annexin family | PTM: Phosphorylated by protein kinase C, EGFR and TRPM7. Phosphorylated in response to EGF treatment. {ECO:0000250|UniProtKB:P04083}.; PTM: Sumoylated. {ECO:0000250|UniProtKB:P10107}.; PTM: Proteolytically cleaved by cathepsin CTSG to release the active N-terminal peptide Ac2-26. {ECO:0000250|UniProtKB:P04083}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12467520}. Cytoplasm {ECO:0000269|PubMed:12467520}. Cell projection, cilium {ECO:0000250|UniProtKB:P10107}. Basolateral cell membrane {ECO:0000250|UniProtKB:P51662}. Lateral cell membrane {ECO:0000250|UniProtKB:P10107}. Cell membrane {ECO:0000250|UniProtKB:P10107}; Peri... | null | null | null | null | null | FUNCTION: Plays important roles in the innate immune response as effector of glucocorticoid-mediated responses and regulator of the inflammatory process. Has anti-inflammatory activity. Plays a role in glucocorticoid-mediated down-regulation of the early phase of the inflammatory response. Contributes to the adaptive i... | Rattus norvegicus (Rat) |
P07151 | B2MG_RAT | MARSVTVIFLVLVSLAVVLAIQKTPQIQVYSRHPPENGKPNFLNCYVSQFHPPQIEIELLKNGKKIPNIEMSDLSFSKDWSFYILAHTEFTPTETDVYACRVKHVTLKEPKTVTWDRDM | null | null | amyloid fibril formation [GO:1990000]; antigen processing and presentation of endogenous peptide antigen via MHC class I [GO:0019885]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; antigen processing and presentation of exogenous protein antigen via MHC class Ib, TAP-de... | external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; HFE-transferrin receptor complex [GO:1990712]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; MHC class I peptide loading complex [GO:0042824]; MHC class I protein complex [GO:0042612]; MHC class II protein complex [... | identical protein binding [GO:0042802]; MHC class II protein complex binding [GO:0023026]; peptide antigen binding [GO:0042605]; protein homodimerization activity [GO:0042803]; structural molecule activity [GO:0005198] | PF07654; | 2.60.40.10; | Beta-2-microglobulin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Component of the class I major histocompatibility complex (MHC). Involved in the presentation of peptide antigens to the immune system. | Rattus norvegicus (Rat) |
P07154 | CATL1_RAT | MTPLLLLAVLCLGTALATPKFDQTFNAQWHQWKSTHRRLYGTNEEEWRRAVWEKNMRMIQLHNGEYSNGKHGFTMEMNAFGDMTNEEFRQIVNGYRHQKHKKGRLFQEPLMLQIPKTVDWREKGCVTPVKNQGQCGSCWAFSASGCLEGQMFLKTGKLISLSEQNLVDCSHDQGNQGCNGGLMDFAFQYIKENGGLDSEESYPYEAKDGSCKYRAEYAVANDTGFVDIPQQEKALMKAVATVGPISVAMDASHPSLQFYSSGIYYEPNCSSKDLDHGVLVVGYGYEGTDSNKDKYWLVKNSWGKEWGMDGYIKIAKDRNN... | 3.4.22.15 | null | adaptive immune response [GO:0002250]; antigen processing and presentation of peptide antigen [GO:0048002]; autophagic cell death [GO:0048102]; CD4-positive, alpha-beta T cell lineage commitment [GO:0043373]; cellular response to starvation [GO:0009267]; cellular response to thyroid hormone stimulus [GO:0097067]; colla... | apical plasma membrane [GO:0016324]; chromaffin granule [GO:0042583]; cytoplasmic vesicle [GO:0031410]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lysosome [GO:0005764]; microvillus [GO:0005902]; multivesicular body [GO:0005771]; nucleolus [GO:0005730]; nucleus [GO:0005634]; perika... | aminopeptidase activity [GO:0004177]; collagen binding [GO:0005518]; cysteine-type carboxypeptidase activity [GO:0016807]; cysteine-type endopeptidase activator activity involved in apoptotic process [GO:0008656]; cysteine-type endopeptidase activity [GO:0004197]; cysteine-type peptidase activity [GO:0008234]; endopept... | PF08246;PF00112; | 3.90.70.10; | Peptidase C1 family | PTM: During export along the endocytic pathway, pro-CTSL undergoes several proteolytic cleavages to generate the CTSL single-chain and two-chain mature forms, composed of a heavy chain linked to a light chain by disulfide bonds (By similarity). Autocleavage; produces the single-chain CTSL after cleavage of the propepti... | SUBCELLULAR LOCATION: Lysosome {ECO:0000269|PubMed:7777858}. Apical cell membrane {ECO:0000250|UniProtKB:P06797}; Peripheral membrane protein {ECO:0000250|UniProtKB:P06797}; Extracellular side {ECO:0000250|UniProtKB:P06797}. Cytoplasmic vesicle, secretory vesicle, chromaffin granule {ECO:0000250|UniProtKB:P25975}. Secr... | CATALYTIC ACTIVITY: Reaction=Specificity close to that of papain. As compared to cathepsin B, cathepsin L exhibits higher activity toward protein substrates, but has little activity on Z-Arg-Arg-NHMec, and no peptidyl-dipeptidase activity.; EC=3.4.22.15; Evidence={ECO:0000250|UniProtKB:P07711}; | null | null | null | null | FUNCTION: Thiol protease important for the overall degradation of proteins in lysosomes (By similarity). Plays a critical for normal cellular functions such as general protein turnover, antigen processing and bone remodeling. Involved in the solubilization of cross-linked TG/thyroglobulin and in the subsequent release ... | Rattus norvegicus (Rat) |
P07156 | HMGB1_CRIGR | VNFSEFSKKCSERWKTMSAKEKGKFEDMAKADKARYEREMKTYIPPKGETKKKFKDPNAPKRPPSAFFLFCSEYRPKIKGEHPGLSIGDVAKKLGEMWNNTAADDKQPYEKKAAKLKEKYEKDIAAYRAKGKPDAAKKGVVKAEKSKKKKEEEDDEEDEEDEEEEEEEEDEDEEEDDDDE | null | null | adaptive immune response [GO:0002250]; apoptotic cell clearance [GO:0043277]; autophagy [GO:0006914]; chemotaxis [GO:0006935]; DNA recombination [GO:0006310]; DNA repair [GO:0006281]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; negative regulation of RNA polymerase II transcription preiniti... | condensed chromosome [GO:0000793]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; endosome [GO:0005768]; extracellular region [GO:0005576]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | DNA binding, bending [GO:0008301] | PF00505;PF09011; | 1.10.30.10; | HMGB family | PTM: Phosphorylated at serine residues. Phosphorylation in both NLS regions is required for cytoplasmic translocation followed by secretion. {ECO:0000250|UniProtKB:P09429}.; PTM: Acetylated on multiple sites upon stimulation with LPS (By similarity). Acetylation on lysine residues in the nuclear localization signals (N... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P09429}. Chromosome {ECO:0000250|UniProtKB:P10103, ECO:0000250|UniProtKB:P63159}. Cytoplasm {ECO:0000250|UniProtKB:P09429}. Secreted {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P63158}. Cell membrane {ECO:0000250|UniProtKB:P09429, ECO:0000250|UniProtKB:P6315... | null | null | null | null | null | FUNCTION: Multifunctional redox sensitive protein with various roles in different cellular compartments. In the nucleus is one of the major chromatin-associated non-histone proteins and acts as a DNA chaperone involved in replication, transcription, chromatin remodeling, V(D)J recombination, DNA repair and genome stabi... | Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) |
P07170 | KAD2_YEAST | MSSSESIRMVLIGPPGAGKGTQAPNLQERFHAAHLATGDMLRSQIAKGTQLGLEAKKIMDQGGLVSDDIMVNMIKDELTNNPACKNGFILDGFPRTIPQAEKLDQMLKEQGTPLEKAIELKVDDELLVARITGRLIHPASGRSYHKIFNPPKEDMKDDVTGEALVQRSDDNADALKKRLAAYHAQTEPIVDFYKKTGIWAGVDASQPPATVWADILNKLGKD | 2.7.4.3 | null | ADP biosynthetic process [GO:0006172]; AMP metabolic process [GO:0046033]; ATP metabolic process [GO:0046034]; DNA replication initiation [GO:0006270]; nucleotide metabolic process [GO:0009117]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrial intermembrane space [GO:0005758]; mitochondrion [GO:0005739] | adenylate kinase activity [GO:0004017]; ATP binding [GO:0005524] | PF00406;PF05191; | 3.40.50.300; | Adenylate kinase family, AK2 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000255|HAMAP-Rule:MF_03168, ECO:0000269|PubMed:12045196, ECO:0000269|PubMed:2850178}. Mitochondrion intermembrane space {ECO:0000255|HAMAP-Rule:MF_03168, ECO:0000269|PubMed:12045196, ECO:0000269|PubMed:16823961, ECO:0000269|PubMed:22984289, ECO:0000269|PubMed:2850178}. Not... | CATALYTIC ACTIVITY: Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; Evidence={ECO:0000255|HAMAP-Rule:MF_03168, ECO:0000269|PubMed:2850178}; | null | null | null | null | FUNCTION: Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways. {ECO:... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07171 | CALB1_RAT | MAESHLQSSLITASQFFEIWLHFDADGSGYLEGKELQNLIQELLQARKKAGLELSPEMKTFVDQYGQRDDGKIGIVELAHVLPTEENFLLLFRCQQLKSCEEFMKTWRKYDTDHSGFIETEELKNFLKDLLEKANKTVDDTKLAEYTDLMLKLFDSNNDGKLELTEMARLLPVQENFLLKFQGIKMCGKEFNKAFELYDQDGNGYIDENELDALLKDLCEKNKQELDINNISTYKKNIMALSDGGKLYRTDLALILSAGDN | null | null | cellular response to organic substance [GO:0071310]; cochlea development [GO:0090102]; learning or memory [GO:0007611]; locomotory behavior [GO:0007626]; long-term memory [GO:0007616]; metanephric collecting duct development [GO:0072205]; metanephric connecting tubule development [GO:0072286]; metanephric distal convol... | axon [GO:0030424]; calyx of Held [GO:0044305]; cuticular plate [GO:0032437]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; neuron projection [GO:... | calcium ion binding [GO:0005509]; calcium ion binding involved in regulation of postsynaptic cytosolic calcium ion concentration [GO:0099567]; calcium ion binding involved in regulation of presynaptic cytosolic calcium ion concentration [GO:0099534]; vitamin D binding [GO:0005499]; zinc ion binding [GO:0008270] | PF00036;PF13499; | 1.10.238.10; | Calbindin family | null | null | null | null | null | null | null | FUNCTION: Buffers cytosolic calcium. May stimulate a membrane Ca(2+)-ATPase and a 3',5'-cyclic nucleotide phosphodiesterase. | Rattus norvegicus (Rat) |
P07173 | CYCR_BLAVI | MKQLIVNSVATVALASLVAGCFEPPPATTTQTGFRGLSMGEVLHPATVKAKKERDAQYPPALAAVKAEGPPVSQVYKNVKVLGNLTEAEFLRTMTAITEWVSPQEGCTYCHDENNLASEAKYPYVVARRMLEMTRAINTNWTQHVAQTGVTCYTCHRGTPLPPYVRYLEPTLPLNNRETPTHVERVETRSGYVVRLAKYTAYSALNYDPFTMFLANDKRQVRVVPQTALPLVGVSRGKERRPLSDAYATFALMMSISDSLGTNCTFCHNAQTFESWGKKSTPQRAIAWWGIRMVRDLNMNYLAPLNASLPASRLGRQGEA... | null | null | photosynthesis [GO:0015979]; photosynthesis, light reaction [GO:0019684] | plasma membrane light-harvesting complex [GO:0030077]; plasma membrane-derived chromatophore membrane [GO:0042717] | electron transfer activity [GO:0009055]; heme binding [GO:0020037]; iron ion binding [GO:0005506] | PF02276; | 1.10.468.10; | null | PTM: Binds 4 heme groups per subunit. {ECO:0000269|PubMed:10024457, ECO:0000269|PubMed:10736158, ECO:0000269|PubMed:22054235, ECO:0000269|PubMed:6392571, ECO:0000269|PubMed:9351808, ECO:0000269|Ref.7}.; PTM: After the signal sequence is removed, the N-terminal cysteine is modified to form a diacylglyceride thioether, b... | SUBCELLULAR LOCATION: Cellular chromatophore membrane {ECO:0000269|PubMed:10024457, ECO:0000269|PubMed:9351808}; Lipid-anchor {ECO:0000269|PubMed:22054235, ECO:0000269|Ref.4}. | null | null | null | null | null | FUNCTION: The reaction center of purple bacteria contains a tightly bound cytochrome molecule which re-reduces the photo oxidized primary electron donor. {ECO:0000269|PubMed:10736158}. | Blastochloris viridis (Rhodopseudomonas viridis) |
P07174 | TNR16_RAT | MRRAGAACSAMDRLRLLLLLILGVSSGGAKETCSTGLYTHSGECCKACNLGEGVAQPCGANQTVCEPCLDNVTFSDVVSATEPCKPCTECLGLQSMSAPCVEADDAVCRCAYGYYQDEETGHCEACSVCEVGSGLVFSCQDKQNTVCEECPEGTYSDEANHVDPCLPCTVCEDTERQLRECTPWADAECEEIPGRWIPRSTPPEGSDSTAPSTQEPEVPPEQDLVPSTVADMVTTVMGSSQPVVTRGTTDNLIPVYCSILAAVVVGLVAYIAFKRWNSCKQNKQGANSRPVNQTPPPEGEKLHSDSGISVDSQSLHDQQT... | null | null | axon guidance [GO:0007411]; cellular response to amyloid-beta [GO:1904646]; cellular response to oxidative stress [GO:0034599]; central nervous system development [GO:0007417]; circadian regulation of gene expression [GO:0032922]; circadian rhythm [GO:0007623]; detection of temperature stimulus [GO:0016048]; dorsal aor... | cell surface [GO:0009986]; cell-cell junction [GO:0005911]; clathrin-coated endocytic vesicle [GO:0045334]; cytoplasm [GO:0005737]; dendrite membrane [GO:0032590]; dendritic spine [GO:0043197]; external side of plasma membrane [GO:0009897]; growth cone [GO:0030426]; neuromuscular junction [GO:0031594]; neuronal cell bo... | amyloid-beta binding [GO:0001540]; calmodulin binding [GO:0005516]; coreceptor activity [GO:0015026]; death receptor activity [GO:0005035]; identical protein binding [GO:0042802]; nerve growth factor binding [GO:0048406]; neurotrophin binding [GO:0043121]; neurotrophin TRKA receptor binding [GO:0005168]; preprotein bin... | PF00531;PF18422;PF00020; | 6.10.250.1780;1.10.533.10;2.10.50.10; | null | PTM: Subject to intramembrane proteolytic cleavage by the gamma-secretase complex, giving rise to an intracellular fragment that is rapidly degraded via the proteasome. {ECO:0000269|PubMed:27056327}.; PTM: N- and O-glycosylated. {ECO:0000269|PubMed:20036257}.; PTM: Phosphorylated on serine residues. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20036257, ECO:0000269|PubMed:22155786, ECO:0000269|PubMed:24908487, ECO:0000269|PubMed:3027580}; Single-pass type I membrane protein {ECO:0000305}. Perikaryon {ECO:0000269|PubMed:22155786}. Cell projection, growth cone {ECO:0000269|PubMed:22155786}. Cell projectio... | null | null | null | null | null | FUNCTION: Low affinity receptor which can bind to NGF, BDNF, NTF3, and NTF4 (PubMed:15131306, PubMed:18596692, PubMed:3027580). Forms a heterodimeric receptor with SORCS2 that binds the precursor forms of NGF, BDNF and NTF3 with high affinity, and has much lower affinity for mature NGF and BDNF (PubMed:22155786, PubMed... | Rattus norvegicus (Rat) |
P07195 | LDHB_HUMAN | MATLKEKLIAPVAEEEATVPNNKITVVGVGQVGMACAISILGKSLADELALVDVLEDKLKGEMMDLQHGSLFLQTPKIVADKDYSVTANSKIVVVTAGVRQQEGESRLNLVQRNVNVFKFIIPQIVKYSPDCIIIVVSNPVDILTYVTWKLSGLPKHRVIGSGCNLDSARFRYLMAEKLGIHPSSCHGWILGEHGDSSVAVWSGVNVAGVSLQELNPEMGTDNDSENWKEVHKMVVESAYEVIKLKGYTNWAIGLSVADLIESMLKNLSRIHPVSTMVKGMYGIENEVFLSLPCILNARGLTSVINQKLKDDEVAQLKKS... | 1.1.1.27 | null | lactate metabolic process [GO:0006089]; NAD metabolic process [GO:0019674]; pyruvate metabolic process [GO:0006090] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; membrane raft [GO:0045121]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; oxidoreductase complex [GO:1990204] | identical protein binding [GO:0042802]; kinase binding [GO:0019900]; L-lactate dehydrogenase activity [GO:0004459]; NAD binding [GO:0051287] | PF02866;PF00056; | 3.90.110.10;3.40.50.720; | LDH/MDH superfamily, LDH family | null | SUBCELLULAR LOCATION: Cytoplasm. Mitochondrion inner membrane {ECO:0000269|PubMed:27618187}; Peripheral membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=(S)-lactate + NAD(+) = H(+) + NADH + pyruvate; Xref=Rhea:RHEA:23444, ChEBI:CHEBI:15361, ChEBI:CHEBI:15378, ChEBI:CHEBI:16651, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.27; Evidence={ECO:0000269|PubMed:11276087, ECO:0000269|PubMed:27618187}; PhysiologicalDirection=left-to-right; Xref=Rh... | null | PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1. {ECO:0000305|PubMed:27618187}. | null | null | FUNCTION: Interconverts simultaneously and stereospecifically pyruvate and lactate with concomitant interconversion of NADH and NAD(+). {ECO:0000269|PubMed:27618187}. | Homo sapiens (Human) |
P07196 | NFL_HUMAN | MSSFSYEPYYSTSYKRRYVETPRVHISSVRSGYSTARSAYSSYSAPVSSSLSVRRSYSSSSGSLMPSLENLDLSQVAAISNDLKSIRTQEKAQLQDLNDRFASFIERVHELEQQNKVLEAELLVLRQKHSEPSRFRALYEQEIRDLRLAAEDATNEKQALQGEREGLEETLRNLQARYEEEVLSREDAEGRLMEARKGADEAALARAELEKRIDSLMDEISFLKKVHEEEIAELQAQIQYAQISVEMDVTKPDLSAALKDIRAQYEKLAAKNMQNAEEWFKSRFTVLTESAAKNTDAVRAAKDEVSESRRLLKAKTLEIE... | null | null | anterograde axonal transport [GO:0008089]; axonal transport of mitochondrion [GO:0019896]; axonogenesis [GO:0007409]; cerebral cortex development [GO:0021987]; hippocampus development [GO:0021766]; intermediate filament organization [GO:0045109]; intermediate filament polymerization or depolymerization [GO:0045105]; lo... | axon [GO:0030424]; axon cytoplasm [GO:1904115]; cholinergic synapse [GO:0098981]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; growth cone [GO:0030426]; intermediate filament [GO:0005882]; neurofilament [GO:0005883]; neuromuscular junction [GO:0031594]; postsynaptic intermediate filament cytoskeleton [GO:0099160]; pre... | identical protein binding [GO:0042802]; phospholipase binding [GO:0043274]; protein domain specific binding [GO:0019904]; protein-containing complex binding [GO:0044877]; protein-macromolecule adaptor activity [GO:0030674]; structural constituent of cytoskeleton [GO:0005200]; structural constituent of postsynaptic inte... | PF00038;PF04732; | 1.20.5.170;1.20.5.500;1.20.5.1160; | Intermediate filament family | PTM: O-glycosylated. {ECO:0000250}.; PTM: Phosphorylated in the head and rod regions by the PKC kinase PKN1, leading to the inhibition of polymerization. {ECO:0000269|PubMed:8621664}.; PTM: Ubiquitinated in the presence of TRIM2 and UBE2D1. {ECO:0000250}. | SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000250|UniProtKB:P08551}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P08551}. | null | null | null | null | null | FUNCTION: Neurofilaments usually contain three intermediate filament proteins: NEFL, NEFM, and NEFH which are involved in the maintenance of neuronal caliber. May additionally cooperate with the neuronal intermediate filament proteins PRPH and INA to form neuronal filamentous networks (By similarity). {ECO:0000250|UniP... | Homo sapiens (Human) |
P07197 | NFM_HUMAN | MSYTLDSLGNPSAYRRVTETRSSFSRVSGSPSSGFRSQSWSRGSPSTVSSSYKRSMLAPRLAYSSAMLSSAESSLDFSQSSSLLNGGSGPGGDYKLSRSNEKEQLQGLNDRFAGYIEKVHYLEQQNKEIEAEIQALRQKQASHAQLGDAYDQEIRELRATLEMVNHEKAQVQLDSDHLEEDIHRLKERFEEEARLRDDTEAAIRALRKDIEEASLVKVELDKKVQSLQDEVAFLRSNHEEEVADLLAQIQASHITVERKDYLKTDISTALKEIRSQLESHSDQNMHQAEEWFKCRYAKLTEAAEQNKEAIRSAKEEIAEY... | null | null | neurofilament bundle assembly [GO:0033693] | axon [GO:0030424]; cytoplasm [GO:0005737]; intermediate filament [GO:0005882]; intermediate filament cytoskeleton [GO:0045111]; neurofibrillary tangle [GO:0097418]; neurofilament [GO:0005883]; postsynaptic intermediate filament cytoskeleton [GO:0099160] | microtubule binding [GO:0008017]; structural constituent of cytoskeleton [GO:0005200] | PF00038;PF04732; | 1.20.5.170;1.20.5.500;1.20.5.1160; | Intermediate filament family | PTM: There are a number of repeats of the tripeptide K-S-P, NFM is phosphorylated on a number of the serines in this motif. It is thought that phosphorylation of NFM results in the formation of interfilament cross bridges that are important in the maintenance of axonal caliber.; PTM: Phosphorylation seems to play a maj... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:P08553}. Cell projection, axon {ECO:0000250|UniProtKB:P08553}. | null | null | null | null | null | FUNCTION: Neurofilaments usually contain three intermediate filament proteins: NEFL, NEFM, and NEFH which are involved in the maintenance of neuronal caliber. May additionally cooperate with the neuronal intermediate filament proteins PRPH and INA to form neuronal filamentous networks (By similarity). {ECO:0000250|UniP... | Homo sapiens (Human) |
P07199 | CENPB_HUMAN | MGPKRRQLTFREKSRIIQEVEENPDLRKGEIARRFNIPPSTLSTILKNKRAILASERKYGVASTCRKTNKLSPYDKLEGLLIAWFQQIRAAGLPVKGIILKEKALRIAEELGMDDFTASNGWLDRFRRRHGVVSCSGVARARARNAAPRTPAAPASPAAVPSEGSGGSTTGWRAREEQPPSVAEGYASQDVFSATETSLWYDFLPDQAAGLCGGDGRPRQATQRLSVLLCANADGSEKLPPLVAGKSAKPRAGQAGLPCDYTANSKGGVTTQALAKYLKALDTRMAAESRRVLLLAGRLAAQSLDTSGLRHVQLAFFPPG... | null | null | null | chromosome [GO:0005694]; chromosome, centromeric region [GO:0000775]; condensed chromosome, centromeric region [GO:0000779]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; pericentric heterochromatin [GO:0005721] | centromeric DNA binding [GO:0019237]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; satellite DNA binding [GO:0003696]; sequence-specific DNA binding [GO:0043565] | PF09026;PF04218;PF03184;PF03221; | 1.10.287.1090;1.10.10.60; | null | PTM: Poly-ADP-ribosylated by PARP1. {ECO:0000250|UniProtKB:P27790}.; PTM: N-terminally methylated by METTL11A/NTM1. Alpha-N-methylation is stimulated in response to extracellular stimuli, including increased cell density and heat shock, and seems to facilitate binding to CENP-B boxes. Chromatin-bound CENP-B is primaril... | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00320, ECO:0000255|PROSITE-ProRule:PRU00583, ECO:0000269|PubMed:18072184}. Chromosome, centromere {ECO:0000269|PubMed:18072184}. | null | null | null | null | null | FUNCTION: Interacts with centromeric heterochromatin in chromosomes and binds to a specific 17 bp subset of alphoid satellite DNA, called the CENP-B box (PubMed:11726497). May organize arrays of centromere satellite DNA into a higher-order structure which then directs centromere formation and kinetochore assembly in ma... | Homo sapiens (Human) |
P07200 | TGFB1_PIG | MPPSGLRLLPLLLPLLWLLVLTPGRPAAGLSTCKTIDMELVKRKRIEAIRGQILSKLRLASPPSQGDVPPGPLPEAVLALYNSTRDRVAGESVEPEPEPEADYYAKEVTRVLMVESGNQIYDKFKGTPHSLYMLFNTSELREAVPEPVLLSRAELRLLRLKLKVEQHVELYQKYSNDSWRYLSNRLLAPSDSPEWLSFDVTGVVRQWLTRREAIEGFRLSAHCSCDSKDNTLHVEINGFNSGRRGDLATIHGMNRPFLLLMATPLERAQHLHSSRHRRALDTNYCFSSTEKNCCVRQLYIDFRKDLGWKWIHEPKGYHAN... | null | null | ATP biosynthetic process [GO:0006754]; cell-cell junction organization [GO:0045216]; cellular response to transforming growth factor beta stimulus [GO:0071560]; chondrocyte differentiation [GO:0002062]; epithelial to mesenchymal transition [GO:0001837]; extracellular matrix assembly [GO:0085029]; extrinsic apoptotic si... | blood microparticle [GO:0072562]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; nucleus [GO:0005634] | antigen binding [GO:0003823]; cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; identical protein binding [GO:0042802]; type I transforming growth factor beta receptor binding [GO:0034713]; type II transforming growth factor beta receptor binding [GO:0005114]; type III transforming growth factor beta... | PF00019;PF00688; | 2.60.120.970;2.10.90.10; | TGF-beta family | PTM: Transforming growth factor beta-1 proprotein: The precursor proprotein is cleaved in the Golgi apparatus by FURIN to form Transforming growth factor beta-1 (TGF-beta-1) and Latency-associated peptide (LAP) chains, which remain non-covalently linked, rendering TGF-beta-1 inactive. {ECO:0000250|UniProtKB:P01137}.; P... | SUBCELLULAR LOCATION: [Latency-associated peptide]: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P01137}.; SUBCELLULAR LOCATION: [Transforming growth factor beta-1]: Secreted {ECO:0000250|UniProtKB:P01137}. | null | null | null | null | null | FUNCTION: Transforming growth factor beta-1 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-1 (TGF-beta-1) chains, which constitute the regulatory and active subunit of TGF-beta-1, respectively. {ECO:0000250|UniProtKB:P01137}.; FUNCTION: [Latency-associated peptide]: Re... | Sus scrofa (Pig) |
P07202 | PERT_HUMAN | MRALAVLSVTLVMACTEAFFPFISRGKELLWGKPEESRVSSVLEESKRLVDTAMYATMQRNLKKRGILSPAQLLSFSKLPEPTSGVIARAAEIMETSIQAMKRKVNLKTQQSQHPTDALSEDLLSIIANMSGCLPYMLPPKCPNTCLANKYRPITGACNNRDHPRWGASNTALARWLPPVYEDGFSQPRGWNPGFLYNGFPLPPVREVTRHVIQVSNEVVTDDDRYSDLLMAWGQYIDHDIAFTPQSTSKAAFGGGADCQMTCENQNPCFPIQLPEEARPAAGTACLPFYRSSAACGTGDQGALFGNLSTANPRQQMNGL... | 1.11.1.8 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00298}; Note=Binds 1 Ca(2+) ion per heterodimer. {ECO:0000255|PROSITE-ProRule:PRU00298}; COFACTOR: Name=heme b; Xref=ChEBI:CHEBI:60344; Evidence={ECO:0000255|PROSITE-ProRule:PRU00298}; Note=Binds 1 heme b (iron(II)-protoporphyrin IX... | embryonic hemopoiesis [GO:0035162]; hormone biosynthetic process [GO:0042446]; hydrogen peroxide catabolic process [GO:0042744]; response to oxidative stress [GO:0006979]; thyroid hormone generation [GO:0006590] | cell surface [GO:0009986]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | calcium ion binding [GO:0005509]; heme binding [GO:0020037]; iodide peroxidase activity [GO:0004447]; peroxidase activity [GO:0004601] | PF03098;PF07645;PF00084; | 2.10.70.10;1.10.640.10;2.10.25.10; | Peroxidase family, XPO subfamily | PTM: Glycosylated.; PTM: Heme is covalently bound through a H(2)O(2)-dependent autocatalytic process. Heme insertion is important for the delivery of protein at the cell surface.; PTM: Cleaved in its N-terminal part. | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 3]: Cell surface. | CATALYTIC ACTIVITY: Reaction=2 H(+) + H2O2 + 2 iodide = diiodine + 2 H2O; Xref=Rhea:RHEA:23336, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16240, ChEBI:CHEBI:16382, ChEBI:CHEBI:17606; EC=1.11.1.8; Evidence={ECO:0000250|UniProtKB:P09933}; CATALYTIC ACTIVITY: Reaction=[thyroglobulin]-L-tyrosine + H(+) + H2O2 + iod... | null | PATHWAY: Hormone biosynthesis; thyroid hormone biosynthesis. | null | null | FUNCTION: Iodination and coupling of the hormonogenic tyrosines in thyroglobulin to yield the thyroid hormones T(3) and T(4). {ECO:0000250|UniProtKB:P09933}. | Homo sapiens (Human) |
P07203 | GPX1_HUMAN | MCAARLAAAAAAAQSVYAFSARPLAGGEPVSLGSLRGKVLLIENVASLUGTTVRDYTQMNELQRRLGPRGLVVLGFPCNQFGHQENAKNEEILNSLKYVRPGGGFEPNFMLFEKCEVNGAGAHPLFAFLREALPAPSDDATALMTDPKLITWSPVCRNDVAWNFEKFLVGPDGVPLRRYSRRFQTIDIEPDIEALLSQGPSCA | 1.11.1.12; 1.11.1.9 | null | angiogenesis involved in wound healing [GO:0060055]; arachidonic acid metabolic process [GO:0019369]; biological process involved in interaction with symbiont [GO:0051702]; blood vessel endothelial cell migration [GO:0043534]; cell redox homeostasis [GO:0045454]; cellular response to glucose stimulus [GO:0071333]; cell... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | glutathione peroxidase activity [GO:0004602]; phospholipid-hydroperoxide glutathione peroxidase activity [GO:0047066]; SH3 domain binding [GO:0017124] | PF00255; | 3.40.30.10; | Glutathione peroxidase family | PTM: During periods of oxidative stress, Sec-49 may react with a superoxide radical, irreversibly lose hydroselenide and be converted to dehydroalanine. {ECO:0000250|UniProtKB:P11352}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P11352}. Mitochondrion {ECO:0000250|UniProtKB:P11352}. | CATALYTIC ACTIVITY: Reaction=2 glutathione + H2O2 = glutathione disulfide + 2 H2O; Xref=Rhea:RHEA:16833, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.9; Evidence={ECO:0000269|PubMed:11115402, ECO:0000269|PubMed:36608588}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:1683... | null | null | null | null | FUNCTION: Catalyzes the reduction of hydroperoxides in a glutathione-dependent manner thus regulating cellular redox homeostasis (PubMed:11115402, PubMed:36608588). Can reduce small soluble hydroperoxides such as H2O2, cumene hydroperoxide and tert-butyl hydroperoxide, as well as several fatty acid-derived hydroperoxid... | Homo sapiens (Human) |
P07204 | TRBM_HUMAN | MLGVLVLGALALAGLGFPAPAEPQPGGSQCVEHDCFALYPGPATFLNASQICDGLRGHLMTVRSSVAADVISLLLNGDGGVGRRRLWIGLQLPPGCGDPKRLGPLRGFQWVTGDNNTSYSRWARLDLNGAPLCGPLCVAVSAAEATVPSEPIWEEQQCEVKADGFLCEFHFPATCRPLAVEPGAAAAAVSITYGTPFAARGADFQALPVGSSAAVAPLGLQLMCTAPPGAVQGHWAREAPGAWDCSVENGGCEHACNAIPGAPRCQCPAGAALQADGRSCTASATQSCNDLCEHFCVPNPDQPGSYSCMCETGYRLAADQ... | null | null | blood coagulation [GO:0007596]; blood coagulation, common pathway [GO:0072377]; female pregnancy [GO:0007565]; negative regulation of blood coagulation [GO:0030195]; negative regulation of fibrinolysis [GO:0051918]; negative regulation of platelet activation [GO:0010544]; proteolysis [GO:0006508]; response to cAMP [GO:... | apicolateral plasma membrane [GO:0016327]; cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; serine-type endopeptidase complex [GO:1905370]; vacuolar membrane [GO:0005774] | calcium ion binding [GO:0005509]; signaling receptor activity [GO:0038023]; transmembrane signaling receptor activity [GO:0004888] | PF12662;PF07645;PF14670;PF00059;PF09064; | 2.10.25.10;3.10.100.10; | null | PTM: N-glycosylated. {ECO:0000269|PubMed:8216207}.; PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000269|PubMed:8390446}. | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Thrombomodulin is a specific endothelial cell receptor that forms a 1:1 stoichiometric complex with thrombin. This complex is responsible for the conversion of protein C to the activated protein C (protein Ca). Once evolved, protein Ca scissions the activated cofactors of the coagulation mechanism, factor Va ... | Homo sapiens (Human) |
P07205 | PGK2_HUMAN | MSLSKKLTLDKLDVRGKRVIMRVDFNVPMKKNQITNNQRIKASIPSIKYCLDNGAKAVVLMSHLGRPDGVPMPDKYSLAPVAVELKSLLGKDVLFLKDCVGAEVEKACANPAPGSVILLENLRFHVEEEGKGQDPSGKKIKAEPDKIEAFRASLSKLGDVYVNDAFGTAHRAHSSMVGVNLPHKASGFLMKKELDYFAKALENPVRPFLAILGGAKVADKIQLIKNMLDKVNEMIIGGGMAYTFLKVLNNMEIGASLFDEEGAKIVKDIMAKAQKNGVRITFPVDFVTGDKFDENAQVGKATVASGISPGWMGLDCGPES... | 2.7.2.3 | null | canonical glycolysis [GO:0061621]; flagellated sperm motility [GO:0030317]; gluconeogenesis [GO:0006094]; glycolytic process [GO:0006096]; phosphorylation [GO:0016310] | cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]; sperm fibrous sheath [GO:0035686] | ADP binding [GO:0043531]; ATP binding [GO:0005524]; phosphoglycerate kinase activity [GO:0004618] | PF00162; | 3.40.50.1260; | Phosphoglycerate kinase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP; Xref=Rhea:RHEA:14801, ChEBI:CHEBI:30616, ChEBI:CHEBI:57604, ChEBI:CHEBI:58272, ChEBI:CHEBI:456216; EC=2.7.2.3; | null | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5. | null | null | FUNCTION: Essential for sperm motility and male fertility (PubMed:26677959). Not required for the completion of spermatogenesis (By similarity). {ECO:0000250|UniProtKB:P09041, ECO:0000269|PubMed:26677959}. | Homo sapiens (Human) |
P07207 | NOTCH_DROME | MQSQRSRRRSRAPNTWICFWINKMHAVASLPASLPLLLLTLAFANLPNTVRGTDTALVAASCTSVGCQNGGTCVTQLNGKTYCACDSHYVGDYCEHRNPCNSMRCQNGGTCQVTFRNGRPGISCKCPLGFDESLCEIAVPNACDHVTCLNGGTCQLKTLEEYTCACANGYTGERCETKNLCASSPCRNGATCTALAGSSSFTCSCPPGFTGDTCSYDIEECQSNPCKYGGTCVNTHGSYQCMCPTGYTGKDCDTKYKPCSPSPCQNGGICRSNGLSYECKCPKGFEGKNCEQNYDDCLGHLCQNGGTCIDGISDYTCRCP... | null | null | actin filament organization [GO:0007015]; asymmetric cell division [GO:0008356]; axon guidance [GO:0007411]; border follicle cell migration [GO:0007298]; cell dedifferentiation [GO:0043697]; cell differentiation [GO:0030154]; cell fate commitment [GO:0045165]; chaeta development [GO:0022416]; chaeta morphogenesis [GO:0... | adherens junction [GO:0005912]; apical plasma membrane [GO:0016324]; cell surface [GO:0009986]; CSL-Notch-Mastermind transcription factor complex [GO:1990433]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]; endocytic vesicle [GO:0030139]; endoplasmic reticulum [GO:0005783]; endoplasmic retic... | calcium ion binding [GO:0005509]; chromatin binding [GO:0003682]; histone acetyltransferase binding [GO:0035035]; Notch binding [GO:0005112]; transcription coactivator activity [GO:0003713]; transmembrane signaling receptor activity [GO:0004888]; WW domain binding [GO:0050699] | PF00023;PF12796;PF00008;PF07645;PF12661;PF06816;PF07684;PF00066; | 3.30.300.320;3.30.70.3310;1.25.40.20;2.10.25.10; | NOTCH family | PTM: Upon binding its ligands such as Delta or Serrate, it is cleaved (S2 cleavage) in its extracellular domain, close to the transmembrane domain. S2 cleavage is probably mediated by Kuz. It is then cleaved (S3 cleavage) downstream of its transmembrane domain, releasing it from the cell membrane. S3 cleavage requires ... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17329366}; Single-pass type I membrane protein {ECO:0000269|PubMed:17329366}. Endosome {ECO:0000269|PubMed:17329366}. Endosome, multivesicular body {ECO:0000269|PubMed:22162134}. Note=Transported to early endosomes by O-fut1 (PubMed:17329366). Targeting to the end... | null | null | null | null | null | FUNCTION: Essential signaling protein which has a major role in many developmental processes (PubMed:3935325). Functions as a receptor for membrane-bound ligands Delta and Serrate to regulate cell-fate determination (PubMed:10935637, PubMed:12909620, PubMed:15620650, PubMed:18243100). Upon ligand activation, and releas... | Drosophila melanogaster (Fruit fly) |
P07210 | POLG_HRV8A | MGAQVSRQNVGTHSTQNSVSNGSSLNYFNINYFKDAASSGASRLDFSQDPSKFTDPVKDVLEKGIPTLQSPTVEACGYSDRLIQITRGDSTITSQDTANAVVAYGVWPSYLTPDDATAIDKPTQPDTSSNRFYTLDSRSWTSASSGWWWKLPDALKNMGIFGENMFYHFLGRSGYTIHVQCNSSKFHQGLLIVAAIPEHQLASATSGNVSVGYNHTHPGEQGREVVPSRTSSDNKRPSDDSWLNFDGTLLGNLPIYPHQYINLRTNNSATLILPYVNAVPMDSMLRHNNWSLVIIPICPLQVQPGGTQSIPITVSISPMF... | 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;2.60.120.20;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... | Human rhinovirus A serotype 89 (strain 41467-Gallo) (HRV-89) |
P07213 | TOM70_YEAST | MKSFITRNKTAILATVAATGTAIGAYYYYNQLQQQQQRGKKNTINKDEKKDTKDSQKETEGAKKSTAPSNPPIYPVSSNGEPDFSNKANFTAEEKDKYALALKDKGNQFFRNKKYDDAIKYYNWALELKEDPVFYSNLSACYVSVGDLKKVVEMSTKALELKPDYSKVLLRRASANEGLGKFADAMFDLSVLSLNGDFNDASIEPMLERNLNKQAMSKLKEKFGDIDTATATPTELSTQPAKERKDKQENLPSVTSMASFFGIFKPELTFANYDESNEADKELMNGLSNLYKRSPESYDKADESFTKAARLFEEQLDKNN... | null | null | protein import into mitochondrial matrix [GO:0030150]; protein insertion into mitochondrial inner membrane [GO:0045039]; protein insertion into mitochondrial outer membrane [GO:0045040]; protein targeting to mitochondrion [GO:0006626] | mitochondrial outer membrane [GO:0005741]; mitochondrial outer membrane translocase complex [GO:0005742]; mitochondrion [GO:0005739] | mitochondrion targeting sequence binding [GO:0030943]; protein-transporting ATPase activity [GO:0015450] | PF00515;PF13432;PF14559;PF13181; | 1.25.40.10; | Tom70 family | null | SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000269|PubMed:11502169}; Single-pass membrane protein {ECO:0000269|PubMed:11502169}. | null | null | null | null | null | FUNCTION: Component of the TOM (translocase of outer membrane) receptor complex responsible for the recognition and translocation of cytosolically synthesized mitochondrial preproteins. Together with TOM20 and TOM22 functions as the transit peptide receptor at the surface of the mitochondrion outer membrane and facilit... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07214 | SPRC_MOUSE | MRAWIFFLLCLAGRALAAPQQTEVAEEIVEEETVVEETGVPVGANPVQVEMGEFEDGAEETVEEVVADNPCQNHHCKHGKVCELDESNTPMCVCQDPTSCPAPIGEFEKVCSNDNKTFDSSCHFFATKCTLEGTKKGHKLHLDYIGPCKYIAPCLDSELTEFPLRMRDWLKNVLVTLYERDEGNNLLTEKQKLRVKKIHENEKRLEAGDHPVELLARDFEKNYNMYIFPVHWQFGQLDQHPIDGYLSHTELAPLRAPLIPMEHCTTRFFETCDLDNDKYIALEEWAGCFGIKEQDINKDLVI | null | null | bone development [GO:0060348]; cellular response to growth factor stimulus [GO:0071363]; lung development [GO:0030324]; pigmentation [GO:0043473]; regulation of cell population proliferation [GO:0042127]; regulation of synapse organization [GO:0050807] | basement membrane [GO:0005604]; collagen-containing extracellular matrix [GO:0062023]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; glutamatergic synapse [GO:0098978]; synapse [GO:0045202]; vesicle [GO:0031982] | calcium ion binding [GO:0005509]; collagen binding [GO:0005518]; extracellular matrix binding [GO:0050840] | PF09289;PF00050;PF10591; | 3.30.60.30;1.10.238.10; | SPARC family | PTM: N-glycosylated. {ECO:0000269|PubMed:3427055}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane {ECO:0000269|PubMed:3427055}. Note=In or around the basement membrane. | null | null | null | null | null | FUNCTION: Appears to regulate cell growth through interactions with the extracellular matrix and cytokines. Binds calcium and copper, several types of collagen, albumin, thrombospondin, PDGF and cell membranes. There are two calcium binding sites; an acidic domain that binds 5 to 8 Ca(2+) with a low affinity and an EF-... | Mus musculus (Mouse) |
P07221 | CASQ1_RABIT | MNAADRMGARVALLLLLVLGSPQSGVHGEEGLDFPEYDGVDRVINVNAKNYKNVFKKYEVLALLYHEPPEDDKASQRQFEMEELILELAAQVLEDKGVGFGLVDSEKDAAVAKKLGLTEEDSIYVFKEDEVIEYDGEFSADTLVEFLLDVLEDPVELIEGERELQAFENIEDEIKLIGYFKNKDSEHYKAFKEAAEEFHPYIPFFATFDSKVAKKLTLKLNEIDFYEAFMEEPVTIPDKPNSEEEIVNFVEEHRRSTLRKLKPESMYETWEDDMDGIHIVAFAEEADPDGYEFLEILKSVAQDNTDNPDLSIIWIDPDDF... | null | null | positive regulation of release of sequestered calcium ion into cytosol [GO:0051281]; positive regulation of store-operated calcium channel activity [GO:1901341]; protein polymerization [GO:0051258]; regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion [GO:0014809]; regulation of... | mitochondrial matrix [GO:0005759]; sarcoplasmic reticulum [GO:0016529]; sarcoplasmic reticulum lumen [GO:0033018]; sarcoplasmic reticulum membrane [GO:0033017]; Z disc [GO:0030018] | calcium ion binding [GO:0005509]; ion binding [GO:0043167]; magnesium ion binding [GO:0000287]; metal ion binding [GO:0046872]; potassium ion binding [GO:0030955]; protein homodimerization activity [GO:0042803] | PF01216; | 3.40.30.10; | Calsequestrin family | PTM: N-glycosylated. {ECO:0000269|PubMed:22170046}. | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:P31415}. Sarcoplasmic reticulum {ECO:0000250|UniProtKB:P31415}. Sarcoplasmic reticulum lumen {ECO:0000269|PubMed:15731387, ECO:0000269|PubMed:19230141, ECO:0000269|PubMed:8227022}. Mitochondrion matrix {ECO:0000250|UniProtKB:O09165}. Sarcoplasmic reticu... | null | null | null | null | null | FUNCTION: Calsequestrin is a high-capacity, moderate affinity, calcium-binding protein and thus acts as an internal calcium store in muscle. Calcium ions are bound by clusters of acidic residues at the protein surface, often at the interface between subunits. Can bind around 80 Ca(2+) ions. Regulates the release of lum... | Oryctolagus cuniculus (Rabbit) |
P07222 | NPM_XENLA | MEDSMDMDNIAPLRPQNFLFGCELKADKKEYSFKVEDDENEHQLSLRTVSLGASAKDELHVVEAEGINYEGKTIKIALASLKPSVQPTVSLGGFEITPPVILRLKSGSGPVYVSGQHLVALEDLESSDDEDEEHEPSPKNAKRIAPDSASKVPRKKTRLEEEEEDSDEDDDDDEDDDDEDDDEEEEETPVKKTDSTKSKAAQKLNHNGKASALSTTQKTPKTPEQKGKQDTKPQTPKTPKTPLSSEEIKAKMQTYLEKGNVLPKVEVKFANYVKNCFRTENQKVIEDLWKWRQSLKDGK | null | null | chromatin remodeling [GO:0006338]; DNA repair [GO:0006281]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of centrosome duplication [GO:0010824]; regulation of endodeoxyribonuclease activity [GO:0032071]; regulation of endoribonuclease activity [GO:0060699]; ribosomal large subunit ... | centrosome [GO:0005813]; cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; ribonucleoprotein complex [GO:1990904] | chromatin binding [GO:0003682]; histone binding [GO:0042393]; identical protein binding [GO:0042802]; RNA binding [GO:0003723] | PF16276;PF03066; | 1.10.10.2100;2.60.120.340; | Nucleoplasmin family | PTM: Phosphorylated. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. | null | null | null | null | null | FUNCTION: Acts as a chaperonin for the core histones H3, H2B and H4. Associated with nucleolar ribonucleoprotein structures and bind single-stranded nucleic acids. It may function in the assembly and/or transport of ribosome. May stimulate endonuclease activity on apurinic/apyrimidinic (AP) double-stranded DNA. May inh... | Xenopus laevis (African clawed frog) |
P07224 | PROS_BOVIN | MRVLGGRTGTLLACLALVLPVLEANFLSRQHASQVLIRRRRANTLLEETKKGNLERECIEELCNKEEAREIFENNPETEYFYPKYLGCLGSFRAGLFTAARLSTNAYPDLRSCVNAISDQCNPLPCNEDGFMTCKDGQATFTCICKSGWQGEKCESDINECKDPVNINGGCSQICENTPGSYHCSCKNGFVMLSNKKDCKDVDECVLKPSICGTAVCKNIPGDFECECAEGYKYNPVSKSCDDVDECAENLCAQLCVNYPGGYSCYCDGKKGFKLAQDQKSCEAVPVCLPLDLDKNYELLYLAEQFVGVVLYLKFRLPET... | null | null | blood coagulation [GO:0007596]; fibrinolysis [GO:0042730] | extracellular space [GO:0005615] | calcium ion binding [GO:0005509] | PF00008;PF07645;PF14670;PF00594;PF00054;PF02210; | 2.60.120.200;4.10.740.10;2.10.25.10; | null | PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000269|PubMed:2937785}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Anticoagulant plasma protein; it is a cofactor to activated protein C in the degradation of coagulation factors Va and VIIIa. It helps to prevent coagulation and stimulating fibrinolysis. | Bos taurus (Bovine) |
P07225 | PROS_HUMAN | MRVLGGRCGALLACLLLVLPVSEANFLSKQQASQVLVRKRRANSLLEETKQGNLERECIEELCNKEEAREVFENDPETDYFYPKYLVCLRSFQTGLFTAARQSTNAYPDLRSCVNAIPDQCSPLPCNEDGYMSCKDGKASFTCTCKPGWQGEKCEFDINECKDPSNINGGCSQICDNTPGSYHCSCKNGFVMLSNKKDCKDVDECSLKPSICGTAVCKNIPGDFECECPEGYRYNLKSKSCEDIDECSENMCAQLCVNYPGGYTCYCDGKKGFKLAQDQKSCEVVSVCLPLNLDTKYELLYLAEQFAGVVLYLKFRLPEI... | null | null | blood coagulation [GO:0007596]; fibrinolysis [GO:0042730] | blood microparticle [GO:0072562]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796]; Golgi membrane [GO:0000139]; plasma membrane [GO:0005886]; platelet alpha granule lumen [GO:0031093] | calcium ion binding [GO:0005509]; endopeptidase inhibitor activity [GO:0004866] | PF07645;PF14670;PF00594;PF12661;PF00054;PF02210; | 2.60.120.200;4.10.740.10;2.10.25.10; | null | PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Anticoagulant plasma protein; it is a cofactor to activated protein C in the degradation of coagulation factors Va and VIIIa. It helps to prevent coagulation and stimulating fibrinolysis. | Homo sapiens (Human) |
P07228 | ITB1_CHICK | MAETNLTLLTWAGILCCLIWSGSAQQGGSDCIKANAKSCGECIQAGPNCGWCKKTDFLQEGEPTSARCDDLAALKSKGCPEQDIENPRGSKRVLEDREVTNRKIGAAEKLKPEAITQIQPQKLVLQLRVGEPQTFSLKFKRAEDYPIDLYYLMDLSYSMKDDLENVKSLGTALMREMEKITSDFRIGFGSFVEKTVMPYISTTPAKLRNPCTGDQNCTSPFSYKNVLSLTSEGNKFNELVGKQHISGNLDSPEGGFDAIMQVAVCGDQIGWRNVTRLLVFSTDAGFHFAGDGKLGGIVLPNDGKCHLENNMYTMSHYYDY... | null | null | cell adhesion mediated by integrin [GO:0033627]; cell migration [GO:0016477]; cell-cell adhesion [GO:0098609]; integrin-mediated signaling pathway [GO:0007229]; muscle organ development [GO:0007517]; myoblast differentiation [GO:0045445]; myoblast fusion [GO:0007520] | cell surface [GO:0009986]; focal adhesion [GO:0005925]; integrin complex [GO:0008305]; lamellipodium [GO:0030027]; melanosome [GO:0042470]; plasma membrane [GO:0005886]; ruffle membrane [GO:0032587]; synapse [GO:0045202] | C-X3-C chemokine binding [GO:0019960]; collagen binding involved in cell-matrix adhesion [GO:0098639]; fibronectin binding [GO:0001968]; integrin binding [GO:0005178]; laminin binding [GO:0043236]; metal ion binding [GO:0046872]; protein kinase binding [GO:0019901]; protein tyrosine kinase binding [GO:1990782] | PF07974;PF18372;PF08725;PF07965;PF00362;PF17205; | 4.10.1240.30;1.20.5.100;2.10.25.10;3.30.1680.10;2.60.40.1510;3.40.50.410; | Integrin beta chain family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, invadopodium membrane {ECO:0000250|UniProtKB:P05556}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, ruffle membrane {ECO:0000250|UniProtKB:P05556}; Single-pass ty... | null | null | null | null | null | FUNCTION: Integrins alpha-1/beta-1, alpha-2/beta-1, alpha-10/beta-1 and alpha-11/beta-1 are receptors for collagen. Integrins alpha-1/beta-1 and alpha-2/beta-1 recognize the proline-hydroxylated sequence G-F-P-G-E-R in collagen. Integrins alpha-2/beta-1, alpha-3/beta-1, alpha-4/beta-1, alpha-5/beta-1, alpha-8/beta-1, a... | Gallus gallus (Chicken) |
P07231 | CKG_CONGE | MHLYTYLYLLVPLVTFHLILGTGTLDDGGALTERRSADATALKAEPVLLQKSAARSTDDNGKDRLTQMKRILKQRGNKARGEEELQENQELIREKSNGKR | null | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:10406223}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10406223, ECO:0000269|PubMed:26048991}; Note=Divalent cations stabilize the toxin the in alpha-helix conformation. {ECO:0000269|PubMed:10406223, ECO:0000269|PubMed:260... | null | extracellular region [GO:0005576]; host cell postsynaptic membrane [GO:0035792] | ion channel regulator activity [GO:0099106]; metal ion binding [GO:0046872]; toxin activity [GO:0090729] | null | null | Conotoxin B superfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:6501296}. | null | null | null | null | null | FUNCTION: Conantokins inhibit N-methyl-D-aspartate (NMDA) receptors. This toxin is selective for the NR2B/GRIN2B subunit. Induces sleep-like symptoms in young mice and hyperactivity in older mice. {ECO:0000269|PubMed:2165278}. | Conus geographus (Geography cone) (Nubecula geographus) |
P07237 | PDIA1_HUMAN | MLRRALLCLAVAALVRADAPEEEDHVLVLRKSNFAEALAAHKYLLVEFYAPWCGHCKALAPEYAKAAGKLKAEGSEIRLAKVDATEESDLAQQYGVRGYPTIKFFRNGDTASPKEYTAGREADDIVNWLKKRTGPAATTLPDGAAAESLVESSEVAVIGFFKDVESDSAKQFLQAAEAIDDIPFGITSNSDVFSKYQLDKDGVVLFKKFDEGRNNFEGEVTKENLLDFIKHNQLPLVIEFTEQTAPKIFGGEIKTHILLFLPKSVSDYDGKLSNFKTAAESFKGKILFIFIDSDHTDNQRILEFFGLKKEECPAVRLITL... | 5.3.4.1 | null | cellular response to hypoxia [GO:0071456]; cellular response to interleukin-7 [GO:0098761]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; insulin processing [GO:0030070]; interleukin-12-mediated signaling pathway [GO:0035722]; interleukin-23-mediated signaling pathway [GO:0038155]; peptidyl-pr... | cytoskeleton [GO:0005856]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum chaperone complex [GO:0034663]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum-Golgi intermediate compartment [GO:0005793]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO... | actin binding [GO:0003779]; enzyme binding [GO:0019899]; integrin binding [GO:0005178]; procollagen-proline 4-dioxygenase activity [GO:0004656]; protein disulfide isomerase activity [GO:0003756]; protein heterodimerization activity [GO:0046982]; protein-disulfide reductase activity [GO:0015035]; RNA binding [GO:0003723... | PF00085;PF13848; | 3.40.30.10; | Protein disulfide isomerase family | PTM: Phosphorylation of Ser-357 by FAM20C is induced by endoplasmic reticulum stress and results in a functional switch from oxidoreductase to molecular chaperone (PubMed:32149426). It also promotes interaction with ERN1 (PubMed:32149426). {ECO:0000269|PubMed:32149426}. | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:23475612, ECO:0000269|PubMed:32149426}. Endoplasmic reticulum lumen {ECO:0000269|PubMed:10636893, ECO:0000269|PubMed:23475612}. Melanosome {ECO:0000269|PubMed:12643545, ECO:0000269|PubMed:17081065}. Cell membrane {ECO:0000269|PubMed:21670307}; Peripheral m... | CATALYTIC ACTIVITY: Reaction=Catalyzes the rearrangement of -S-S- bonds in proteins.; EC=5.3.4.1; Evidence={ECO:0000269|PubMed:32149426}; | null | null | null | null | FUNCTION: This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to for... | Homo sapiens (Human) |
P07239 | DUSP_VACCW | MDKKSLYKYLLLRSTGDMHKAKSPTIMTRVTNNVYLGNYKNAMDAPSSEVKFKYVLNLTMDKYTLPNSNINIIHIPLVDDTTTDISKYFDDVTAFLSKCDQRNEPVLVHCAAGVNRSGAMILAYLMSKNKESLPMLYFLYVYHSMRDLRGAFVENPSFKRQIIEKYVIDKN | 3.1.3.-; 3.1.3.48 | null | dephosphorylation [GO:0016311]; negative regulation of MAPK cascade [GO:0043409]; symbiont-mediated suppression of host JAK-STAT cascade via inhibition of STAT1 activity [GO:0039563]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; virus-mediated perturbation of host def... | cytoplasm [GO:0005737]; host cell cytoplasm [GO:0030430]; virion component [GO:0044423] | MAP kinase tyrosine phosphatase activity [GO:0033550]; MAP kinase tyrosine/serine/threonine phosphatase activity [GO:0017017]; phosphatase activity [GO:0016791]; protein serine/threonine phosphatase activity [GO:0004722]; protein tyrosine/threonine phosphatase activity [GO:0008330] | PF00782; | 3.90.190.10; | Protein-tyrosine phosphatase family, Non-receptor class dual specificity subfamily | null | SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:21362620}. Host cytoplasm {ECO:0000269|PubMed:21362620}. Note=Approximately 200 molecules of OPG106 are packaged within the virion and are essential for the viability of the virus. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000269|PubMed:1848923}; CATALYTIC ACTIVITY: Reacti... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=87 uM for 3-O-methylfluorescein phosphate {ECO:0000269|PubMed:21362620}; | null | null | null | FUNCTION: Serine/tyrosine phosphatase which down-regulates cellular antiviral response by dephosphorylating activated host STAT1 and blocking interferon (IFN)-stimulated innate immune responses. Dephosphorylates the OPG144 protein. {ECO:0000269|PubMed:10438817, ECO:0000269|PubMed:11238845, ECO:0000269|PubMed:1848923, E... | Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR)) |
P07242 | PG110_VACCW | MAWSITNKADTSSFTKMAEIRAHLKNSAENKDKNEDIFPEDVIIPSTKPKTKRATTPRKPAATKRSTKKEEVEEEVVIEEYHQTTEKNSPSPGVSDIVESVAAVELDDSDGDDEPMVQVEAGKVNHSARSDLSDLKVATDNIVKDLKKIITRISAVSTVLEDVQAAGISRQFTSMTKAITTLSDLVTEGKSKVVRKKVKTCKK | null | null | viral DNA genome replication [GO:0039693]; viral transcription [GO:0019083] | host cell cytoplasm [GO:0030430]; viral envelope [GO:0019031] | translation elongation factor activity [GO:0003746] | PF03286; | null | Orthopoxvirus OPG110 family | PTM: Phosphorylated at multiple sites. Phosphorylation is necessary for cleavage activity. Phosphorylated by the viral B1R and F10 kinases (Probable). {ECO:0000305|PubMed:11001589, ECO:0000305|PubMed:18089571}. | SUBCELLULAR LOCATION: Virion. Host cytoplasm {ECO:0000269|PubMed:25855734}. Note=Early during viral infection, diffusely localizes within the cytoplasm. Following DNA replication, localizes specifically to virus factories. {ECO:0000269|PubMed:25855734}. | null | null | null | null | null | FUNCTION: Involved in the co-transcriptional or post-transcriptional endoribonucleolytic cleavage that generates sequence-homogeneous 3' ends during late transcription. Involved in postreplicative transcription elongation on intermediate and late genes. Also involved in DNA replication and in multiple steps of virion m... | Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR)) |
P07244 | PUR2_YEAST | MLNILVLGNGAREHVLVTKLAQSPTVGKIYVAPGNGGTATMDPSRVINWDITPDVANFARLQSMAVEHKINLVVPGPELPLVNGITSVFHSVGIPVFGPSVKAAQLEASKAFSKRFMSKHNIPTASYDVFTNPEEAISFLQAHTDKAFVIKADGIAAGKGVIIPSSIDESVQAIKDIMVTKQFGEEAGKQVVIEQFLEGDEISLLTIVDGYSHFNLPVAQDHKRIFDGDKGLNTGGMGAYAPAPVATPSLLKTIDSQIVKPTIDGMRRDGMPFVGVLFTGMILVKDSKTNQLVPEVLEYNVRFGDPETQAVLSLLDDQTD... | 6.3.3.1; 6.3.4.13 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Note=Binds two magnesium or manganese ions per subunit. {ECO:0000305}; | 'de novo' IMP biosynthetic process [GO:0006189]; adenine biosynthetic process [GO:0046084]; purine nucleobase metabolic process [GO:0006144]; purine nucleotide biosynthetic process [GO:0006164] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; phosphoribosylamine-glycine ligase activity [GO:0004637]; phosphoribosylformylglycinamidine cyclo-ligase activity [GO:0004641] | PF00586;PF02769;PF01071;PF02843;PF02844; | 3.40.50.20;3.30.1490.20;3.30.470.20;3.90.600.10;3.90.650.10;3.30.1330.10; | GARS family; AIR synthase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. | CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate; Xref=Rhea:RHEA:17453, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:58681, ChEBI:CHEBI:143788, ChEBI:CHEBI:456216; EC=6.3.4.13; Evid... | null | PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 2/2.; PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphat... | null | null | FUNCTION: Catalyzes the second and fifth step in the 'de novo' purine biosynthesis pathway; contains phosphoribosylamine--glycine ligase (GARS) and phosphoribosylformylglycinamidine cyclo-ligase (AIRS) activities. {ECO:0000250|UniProtKB:P20772}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07245 | C1TC_YEAST | MAGQVLDGKACAQQFRSNIANEIKSIQGHVPGFAPNLAIIQVGNRPDSATYVRMKRKAAEEAGIVANFIHLDESATEFEVLRYVDQLNEDPHTHGIIVQLPLPAHLDEDRITSRVLAEKDVDGFGPTNIGELNKKNGHPFFLPCTPKGIIELLHKANVTIEGSRSVVIGRSDIVGSPVAELLKSLNSTVTITHSKTRDIASYLHDADIVVVAIGQPEFVKGEWFKPRDGTSSDKKTVVIDVGTNYVADPSKKSGFKCVGDVEFNEAIKYVHLITPVPGGVGPMTVAMLMQNTLIAAKRQMEESSKPLQIPPLPLKLLTPV... | 1.5.1.5; 3.5.4.9; 6.3.4.3 | null | folic acid-containing compound metabolic process [GO:0006760]; histidine biosynthetic process [GO:0000105]; methionine biosynthetic process [GO:0009086]; purine nucleobase biosynthetic process [GO:0009113]; purine nucleotide biosynthetic process [GO:0006164]; tetrahydrofolate interconversion [GO:0035999] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | ATP binding [GO:0005524]; formate-tetrahydrofolate ligase activity [GO:0004329]; methenyltetrahydrofolate cyclohydrolase activity [GO:0004477]; methylenetetrahydrofolate dehydrogenase (NADP+) activity [GO:0004488] | PF01268;PF00763;PF02882; | 3.10.410.10;3.40.50.10860;3.40.50.720;3.40.50.300; | Tetrahydrofolate dehydrogenase/cyclohydrolase family; Formate--tetrahydrofolate ligase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095}. Nucleus {ECO:0000269|PubMed:14562095}. | CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = (6R)-5,10-methenyltetrahydrofolate + NADPH; Xref=Rhea:RHEA:22812, ChEBI:CHEBI:15636, ChEBI:CHEBI:57455, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.5.1.5; Evidence={ECO:0000269|PubMed:3514599, ECO:0000269|PubMed:8464869}; Physiological... | null | PATHWAY: One-carbon metabolism; tetrahydrofolate interconversion. | null | null | FUNCTION: Cytoplasmic isozyme of C-1-tetrahydrofolate synthase. The trifunctional enzyme catalyzes the interconversion of the one-carbon derivatives of tetrahydrofolate (THF) between different oxidation states by the enzymatic activities 10-formyltetrahydrofolate synthetase, 5,lO-methenyltetrahydrofolate cyclohydrolase... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07246 | ADH3_YEAST | MLRTSTLFTRRVQPSLFSRNILRLQSTAAIPKTQKGVIFYENKGKLHYKDIPVPEPKPNEILINVKYSGVCHTDLHAWHGDWPLPVKLPLVGGHEGAGVVVKLGSNVKGWKVGDLAGIKWLNGSCMTCEFCESGHESNCPDADLSGYTHDGSFQQFATADAIQAAKIQQGTDLAEVAPILCAGVTVYKALKEADLKAGDWVAISGAAGGLGSLAVQYATAMGYRVLGIDAGEEKEKLFKKLGGEVFIDFTKTKNMVSDIQEATKGGPHGVINVSVSEAAISLSTEYVRPCGTVVLVGLPANAYVKSEVFSHVVKSINIKG... | 1.1.1.1 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:P00330}; Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:P00330}; | amino acid catabolic process to alcohol via Ehrlich pathway [GO:0000947]; NADH oxidation [GO:0006116] | cytoplasm [GO:0005737]; mitochondrial inner membrane [GO:0005743]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | alcohol dehydrogenase (NAD+) activity [GO:0004022]; butanol dehydrogenase activity [GO:1990362]; zinc ion binding [GO:0008270] | PF08240;PF00107; | 3.90.180.10;3.40.50.720; | Zinc-containing alcohol dehydrogenase family | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:1101965, ECO:0000269|PubMed:2188098, ECO:0000269|PubMed:2943982}. Mitochondrion inner membrane {ECO:0000269|PubMed:2937632}. | CATALYTIC ACTIVITY: Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH; Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734, ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1; Evidence={ECO:0000305|PubMed:12702265}; CATALYTIC ACTIVITY: Reaction=a secondary alcohol + NAD(+) = a keto... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=240 uM for NAD(+) {ECO:0000269|PubMed:3546317}; KM=12 mM for ethanol {ECO:0000269|PubMed:3546317}; KM=0.44 mM for acetaldehyde {ECO:0000269|PubMed:3546317}; KM=70 uM for NADH {ECO:0000269|PubMed:3546317}; KM=11 mM for propanol {ECO:0000269|PubMed:3546317}; KM=7.7 m... | null | null | null | FUNCTION: Mitochondrial isozyme that reduces acetaldehyde to ethanol during the fermentation of glucose (Probable) (PubMed:22094012). Involved in the shuttling of mitochondrial reducing equivalents to the cytosol, where the redox balance is restored by NADH dehydrogenases on the external side of the mitochondrial inner... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07247 | KRUP_DROME | MSISMLQDAQTRTLAAALAGIKQEDVHLDRSMSLSPPMSANTSATSAAAIYPAMGLQQAAAASAFGMLSPTQLLAANRQAAAFMAQLPMSTLANTLFPHNPAALFGAWAAQQSLPPQGTHLHSPPASPHSPLSTPLGSGKHPLNSPNSTPQHHEPAKKARKLSVKKEFQTEISMSVNDMYHTSGGPISPPSSGSSPNSTHDGAGGNAGCVGVSKDPSRDKSFTCKICSRSFGYKHVLQNHERTHTGEKPFECPECHKRFTRDHHLKTHMRLHTGEKPYHCSHCDRQFVQVANLRRHLRVHTGERPYTCEICDGKFSDSNQ... | null | null | axon guidance [GO:0007411]; compound eye development [GO:0048749]; heterochromatin formation [GO:0031507]; Malpighian tubule bud morphogenesis [GO:0061332]; muscle organ development [GO:0007517]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [... | nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565] | PF00096; | 3.30.160.60; | Krueppel C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:3112773}. Note=Chromatin associated. | null | null | null | null | null | FUNCTION: Krueppel is a gap class segmentation protein. It is involved in the segmentation of the embryo and in the differentiation of the Malpighian tubules. | Drosophila melanogaster (Fruit fly) |
P07248 | ADR1_YEAST | MANVEKPNDCSGFPVVDLNSCFSNGFNNEKQEIEMETDDSPILLMSSSASRENSNTFSVIQRTPDGKIITTNNNMNSKINKQLDKLPENLRLNGRTPSGKLRSFVCEVCTRAFARQEHLKRHYRSHTNEKPYPCGLCNRCFTRRDLLIRHAQKIHSGNLGETISHTKKVSRTITKARKNSASSVKFQTPTYGTPDNGNFLNRTTANTRRKASPEANVKRKYLKKLTRRASFSAQSASSYALPDQSSLEQHPKDRVKFSTPELVPLDLKNPELDSSFDLNMNLDLNLNLDSNFNIALNRSDSSGSTMNLDYKLPESANNYT... | null | null | chromatin organization [GO:0006325]; peroxisome organization [GO:0007031]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription from RNA polymerase II promoter by oleic acid [GO:0061429]; regulation of transcription by RNA polymerase II [GO:0006357] | chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; molecular adaptor activity [GO:0060090]; nucleic acid binding [GO:0003676]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II-specific DNA-binding trans... | PF00096; | 3.30.160.60; | null | PTM: Phosphorylation at Ser-230 by cAMP-dependent protein kinase A does not affect DNA binding but appears to prevent transcription of ADH2 during glucose repression. {ECO:0000269|PubMed:1549108}. | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Required for transcriptional activation of glucose-repressible alcohol dehydrogenase (ADH2). | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07249 | ARGR1_YEAST | MTSNSDGSSTSPVEKPITGDVETNEPTKPIRRLSTPSPEQDQEGDFDEEDDDDKFSVSTSTPTPTITKTKDSSDTSTVTRRKQPIRYIENKTRRHVTFSKRRHGIMKKAYELSVLTGANILLLILANSGLVYTFTTPKLEPVVREDEGKSLIRACINASDTPDATDTSPAQEQSPAN | null | null | arginine metabolic process [GO:0006525]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of arginine biosynthetic process [GO:1900079]; regulation of arginine catabolic process [GO:1900081]; regulation of arginine metabolic process [GO:0000821] | nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575] | cis-regulatory region sequence-specific DNA binding [GO:0000987]; 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]; serum response element binding [GO:0010736... | PF00319; | 3.40.1810.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00251, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:3311884}. | null | null | null | null | null | FUNCTION: With ARG81, ARG82 and MCM1, coordinates the expression of arginine anabolic and catabolic genes in response to arginine. {ECO:0000269|PubMed:10632874, ECO:0000269|PubMed:2274024, ECO:0000269|PubMed:3298999}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07250 | IPMK_YEAST | MDTVNNYRVLEHKAAGHDGTLTDGDGLLIFKPAFPQELEFYKAIQVRDVSRRKSSADGDAPLCSWMPTYLGVLNEGAKIEQSGDAALLKIDERLSDSTDNLDSIPVKSEKSKQYLVLENLLYGFSKPNILDIKLGKTLYDSKASLEKRERMKRVSETTTSGSLGFRICGMKIQKNPSVLNQLSLEYYEEEADSDYIFINKLYGRSRTDQNVSDAIELYFNNPHLSDARKHQLKKTFLKRLQLFYNTMLEEEVRMISSSLLFIYEGDPERWELLNDVDKLMRDDFIDDDDDDDDNDDDDDDDAEGSSEGPKDKKTTGSLSS... | 2.7.1.127; 2.7.1.151 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:17050532}; | arginine metabolic process [GO:0006525]; inositol phosphate biosynthetic process [GO:0032958]; macroautophagy [GO:0016236]; negative regulation of transcription by RNA polymerase II [GO:0000122]; phosphatidylinositol phosphate biosynthetic process [GO:0046854]; phosphorylation [GO:0016310]; positive regulation of trans... | cytoplasm [GO:0005737]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575] | 1-phosphatidylinositol-3-kinase activity [GO:0016303]; 1-phosphatidylinositol-4,5-bisphosphate 3-kinase activity [GO:0046934]; ATP binding [GO:0005524]; inositol hexakisphosphate kinase activity [GO:0000828]; inositol tetrakisphosphate 3-kinase activity [GO:0000824]; inositol tetrakisphosphate 6-kinase activity [GO:000... | PF03770; | 3.30.470.160; | Inositol phosphokinase (IPK) family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10632874, ECO:0000269|PubMed:16123124, ECO:0000269|PubMed:3311884}. | CATALYTIC ACTIVITY: Reaction=1D-myo-inositol 1,4,5-trisphosphate + 2 ATP = 1D-myo-inositol 1,3,4,5,6-pentakisphosphate + 2 ADP + 2 H(+); Xref=Rhea:RHEA:32359, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57733, ChEBI:CHEBI:203600, ChEBI:CHEBI:456216; EC=2.7.1.151; Evidence={ECO:0000269|PubMed:10574768}; CATALYTIC ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=15.3 uM for 1D-myo-inositol 1,4,5-trisphosphate {ECO:0000269|PubMed:11311242}; KM=7.1 uM for 1D-myo-inositol 1,4,5-trisphosphate {ECO:0000269|PubMed:7945194}; KM=62 uM for 1D-myo-inositol 1,3,4,5,6-pentakisphosphate {ECO:0000269|PubMed:11311242}; KM=30 uM for phosp... | null | null | null | FUNCTION: Inositol phosphate kinase with both monophosphoinositol and diphosphoinositol polyphosphate synthase activities. Able to phosphorylate inositol 1,4,5-trisphosphate (Ins(1,4,5)P3) on both the carbon-3 and carbon-6 positions to synthesize inositol 1,3,4,5-tetrakisphosphate (Ins(1,3,4,5)P4) and inositol 1,4,5,6-... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07251 | ATPA_YEAST | MLARTAAIRSLSRTLINSTKAARPAAAALASTRRLASTKAQPTEVSSILEERIKGVSDEANLNETGRVLAVGDGIARVFGLNNIQAEELVEFSSGVKGMALNLEPGQVGIVLFGSDRLVKEGELVKRTGNIVDVPVGPGLLGRVVDALGNPIDGKGPIDAAGRSRAQVKAPGILPRRSVHEPVQTGLKAVDALVPIGRGQRELIIGDRQTGKTAVALDTILNQKRWNNGSDESKKLYCVYVAVGQKRSTVAQLVQTLEQHDAMKYSIIVAATASEAAPLQYLAPFTAASIGEWFRDNGKHALIVYDDLSKQAVAYRQLSL... | null | null | proton motive force-driven ATP synthesis [GO:0015986] | cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrial nucleoid [GO:0042645]; mitochondrial proton-transporting ATP synthase complex [GO:0005753]; mitochondrial proton-transporting ATP synthase, catalytic core [GO:0005754]; mitochondrion [GO:000573... | ADP binding [GO:0043531]; ATP binding [GO:0005524]; proton-transporting ATP synthase activity, rotational mechanism [GO:0046933] | PF00006;PF00306;PF02874; | 2.40.30.20;1.20.150.20;3.40.50.300; | ATPase alpha/beta chains family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:11502169}. Note=Peripheral membrane protein. | null | null | null | null | null | FUNCTION: Mitochondrial membrane ATP synthase (F(1)F(0) ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F(1) - containing the extramemb... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07255 | COX9_YEAST | MTIAPITGTIKRRVIMDIVLGFSLGGVMASYWWWGFHMDKINKREKFYAELAERKKQEN | null | null | mitochondrial electron transport, cytochrome c to oxygen [GO:0006123] | mitochondrial respiratory chain complex IV [GO:0005751]; mitochondrion [GO:0005739] | cytochrome-c oxidase activity [GO:0004129] | null | null | Fungal cytochrome c oxidase subunit 7a family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:30598554}; Single-pass membrane protein {ECO:0000269|PubMed:30598554}. | null | null | PATHWAY: Energy metabolism; oxidative phosphorylation. | 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... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07256 | QCR1_YEAST | MLRTVTSKTVSNQFKRSLATAVATPKAEVTQLSNGIVVATEHNPSAHTASVGVVFGSGAANENPYNNGVSNLWKNIFLSKENSAVAAKEGLALSSNISRDFQSYIVSSLPGSTDKSLDFLNQSFIQQKANLLSSSNFEATKKSVLKQVQDFEENDHPNRVLEHLHSTAFQNTPLSLPTRGTLESLENLVVADLESFANNHFLNSNAVVVGTGNIKHEDLVNSIESKNLSLQTGTKPVLKKKAAFLGSEVRLRDDTLPKAWISLAVEGEPVNSPNYFVAKLAAQIFGSYNAFEPASRLQGIKLLDNIQEYQLCDNFNHFSL... | null | null | aerobic respiration [GO:0009060]; cellular respiration [GO:0045333]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]; protein processing involved in protein targeting to mitochondrion [GO:0006627]; proton transmembrane transport [GO:1902600] | mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex III [GO:0005750]; mitochondrion [GO:0005739] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222] | PF00675;PF05193; | 3.30.830.10; | Peptidase M16 family, UQCRC1/QCR1 subfamily | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:11502169, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}; Peripheral membrane protein {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}; Matrix side {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}. | null | null | null | null | null | FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrom... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07257 | QCR2_YEAST | MLSAARLQFAQGSVRRLTVSARDAPTKISTLAVKVHGGSRYATKDGVAHLLNRFNFQNTNTRSALKLVRESELLGGTFKSTLDREYITLKATFLKDDLPYYVNALADVLYKTAFKPHELTESVLPAARYDYAVAEQCPVKSAEDQLYAITFRKGLGNPLLYDGVERVSLQDIKDFADKVYTKENLEVSGENVVEADLKRFVDESLLSTLPAGKSLVSKSEPKFFLGEENRVRFIGDSVAAIGIPVNKASLAQYEVLANYLTSALSELSGLISSAKLDKFTDGGLFTLFVRDQDSAVVSSNIKKIVADLKKGKDLSPAINY... | null | null | aerobic respiration [GO:0009060]; cellular respiration [GO:0045333]; mitochondrial electron transport, ubiquinol to cytochrome c [GO:0006122]; proteolysis [GO:0006508]; proton transmembrane transport [GO:1902600] | mitochondrial crista [GO:0030061]; mitochondrial inner membrane [GO:0005743]; mitochondrial respiratory chain complex III [GO:0005750]; mitochondrion [GO:0005739] | metal ion binding [GO:0046872]; metalloendopeptidase activity [GO:0004222] | PF00675; | 3.30.830.10; | Peptidase M16 family, UQCRC2/QCR2 subfamily | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:11502169, ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:22984289, ECO:0000269|PubMed:30598554}; Peripheral membrane protein {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30598554}; Matrix side {ECO:0000269|PubMed:18390544, ECO:0000269|PubMed:30... | null | null | null | null | null | FUNCTION: Component of the ubiquinol-cytochrome c oxidoreductase, a multisubunit transmembrane complex that is part of the mitochondrial electron transport chain which drives oxidative phosphorylation. The respiratory chain contains 3 multisubunit complexes succinate dehydrogenase (complex II, CII), ubiquinol-cytochrom... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07258 | CARA_YEAST | MSSAATKATFCIQNGPSFEGISFGANKSVAGETVFTTSLVGYPESMTDPSYRGQILVFTQPLIGNYGVPSGEARDEYNLLKYFESPHIHVVGIVVAEYAYQYSHWTAVESLAQWCQREGVAAITGVDTRELVQYLREQGSSLGRITLADHDPVPYVNPMKTNLVAQVTTKKPFHVSALPGKAKANVALIDCGVKENIIRCLVKRGANVTVFPYDYRIQDVASEFDGIFLSNGPGNPELCQATISNVRELLNNPVYDCIPIFGICLGHQLLALASGASTHKLKYGNRAHNIPAMDLTTGQCHITSQNHGYAVDPETLPKDQ... | 6.3.5.5 | null | 'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; arginine biosynthetic process [GO:0006526]; glutamine metabolic process [GO:0006541]; pyrimidine nucleotide biosynthetic process [GO:0006221] | carbamoyl-phosphate synthase complex [GO:0005951]; cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494] | ATP binding [GO:0005524]; carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity [GO:0004088]; glutaminase activity [GO:0004359] | PF00988;PF00117; | 3.40.50.880;3.50.30.20; | CarA family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:200419, ECO:0000269|PubMed:205532}. | CATALYTIC ACTIVITY: Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359, ChEBI... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.25 mM for glutamine {ECO:0000269|PubMed:206535}; | PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1. {ECO:0000305|PubMed:5856369}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. {ECO:0000269|PubMed:206652}; | null | FUNCTION: Small subunit of the arginine-specific carbamoyl phosphate synthase (CPSase). CPSase catalyzes the formation of carbamoyl phosphate from the ammonia moiety of glutamine, carbonate, and phosphate donated by ATP, constituting the first step of 2 biosynthetic pathways, one leading to arginine and/or urea and the... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07259 | PYR1_YEAST | MATIAPTAPITPPMESTGDRLVTLELKDGTVLQGYSFGAEKSVAGELVFQTGMVGYPESVTDPSYEGQILVITYPLVGNYGVPDMHLRDELVEELPRYFESNRIHIAGLVISHYTDEYSHYLAKSSLGKWLQNEGIPAVYGVDTRSLTKHLRDAGSMLGRLSLEKSGSDRTISRSSSWRSAFDVPEWVDPNVQNLVSKVSINEPKLYVPPADNKHIELQTGPDGKVLRILAIDVGMKYNQIRCFIKRGVELKVVPWNYDFTKEDYDGLFISNGPGDPSVLDDLSQRLSNVLEAKKTPVFGICLGHQLIARAAGASTLKLK... | 2.1.3.2; 3.5.1.2; 6.3.4.16; 6.3.5.5 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409}; Note=Binds 4 Mg(2+) or Mn(2+) ions per subunit. {ECO:0000255|PROSITE-ProRule:PRU00409}; | 'de novo' pyrimidine nucleobase biosynthetic process [GO:0006207]; 'de novo' UMP biosynthetic process [GO:0044205]; citrulline biosynthetic process [GO:0019240]; glutamine metabolic process [GO:0006541]; negative regulation of pyrimidine nucleobase metabolic process [GO:0045984]; UTP biosynthetic process [GO:0006228] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane [GO:0016020]; mitochondrion [GO:0005739] | amino acid binding [GO:0016597]; aspartate carbamoyltransferase activity [GO:0004070]; ATP binding [GO:0005524]; carbamoyl-phosphate synthase (ammonia) activity [GO:0004087]; carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity [GO:0004088]; dihydroorotase activity [GO:0004151]; glutaminase activity [GO:000435... | PF02786;PF02787;PF00988;PF00117;PF02142;PF00185;PF02729; | 3.40.50.20;3.40.50.880;3.40.50.1370;3.30.1490.20;3.30.470.20;3.50.30.20;1.10.1030.10;3.20.20.140;3.40.50.1380; | CarA family; CarB family; Metallo-dependent hydrolases superfamily, DHOase family, CAD subfamily; Aspartate/ornithine carbamoyltransferase superfamily, ATCase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11015727, ECO:0000269|PubMed:14562095}. Note=Associates with membranes. {ECO:0000269|PubMed:11921093}. | CATALYTIC ACTIVITY: Reaction=2 ATP + H2O + hydrogencarbonate + L-glutamine = 2 ADP + carbamoyl phosphate + 2 H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:18633, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:58228, ChEBI:CHEBI:58359, ChEBI... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=30 mM for NH4(+) {ECO:0000269|PubMed:3281587}; KM=0.5 mM for glutamine {ECO:0000269|PubMed:182284}; KM=3 mM for hydrogencarbonate {ECO:0000269|PubMed:182284}; KM=16.6 mM for aspartate {ECO:0000269|PubMed:4575349, ECO:0000269|PubMed:6354093}; KM=1.18 mM for carbamoy... | PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3. {ECO:0000305|PubMed:5856369}.; PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3. {ECO:0000305|PubMed:5856369}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7 (for the CPSase reaction) (PubMed:3281587). Optimum pH is 8-9 (fro the ATCase reaction) (PubMed:4575349). {ECO:0000269|PubMed:3281587, ECO:0000269|PubMed:4575349}; | null | FUNCTION: Multifunctional protein that encodes the first 2 enzymatic activities of the de novo pyrimidine pathway: carbamoylphosphate synthetase (CPSase; EC 6.3.5.5) and aspartate transcarbamylase (ATCase; EC 2.1.3.2). The CPSase-function is accomplished in 2 steps, by a glutamine-dependent amidotransferase activity (G... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07260 | IF4E_YEAST | MSVEEVSKKFEENVSVDDTTATPKTVLSDSAHFDVKHPLNTKWTLWYTKPAVDKSESWSDLLRPVTSFQTVEEFWAIIQNIPEPHELPLKSDYHVFRNDVRPEWEDEANAKGGKWSFQLRGKGADIDELWLRTLLAVIGETIDEDDSQINGVVLSIRKGGNKFALWTKSEDKEPLLRIGGKFKQVLKLTDDGHLEFFPHSSANGRHPQPSITL | null | null | nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; positive regulation of formation of translation preinitiation complex [GO:1901195]; regulation of cell cycle [GO:0051726]; regulation of translational initiation [GO:0006446]; translational initiation [GO:0006413] | cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; eukaryotic translation initiation factor 4F complex [GO:0016281]; nucleus [GO:0005634]; ribosome [GO:0005840] | mRNA cap binding [GO:0098808]; phosphatidylinositol-3-phosphate binding [GO:0032266]; RNA 7-methylguanosine cap binding [GO:0000340]; translation initiation factor activity [GO:0003743] | PF01652; | 3.30.760.10; | Eukaryotic initiation factor 4E family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8119957}. Nucleus {ECO:0000269|PubMed:8119957}. | null | null | null | null | null | FUNCTION: Recognizes and binds the 7-methylguanosine (m7G)-containing mRNA cap during an early step in the initiation of protein synthesis and facilitates ribosome binding by inducing the unwinding of the mRNAs secondary structures. {ECO:0000269|PubMed:2685552, ECO:0000269|PubMed:8119957}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07261 | GCR1_YEAST | MVCTSTSSNFYSIAQYILQSYFKVNVDSLNSLKLVDLIVDQTYPDSLTLRKLNEGATGQPYDYFNTVSRDADISKCPIFALTIFFVIRWSHPNPPISIENFTTVPLLDSNFISLNSNPLLYIQNQNPNSNSSVKVSRSQTFEPSKELIDLVFPWLSYLKQDMLLIDRTNYKLYSLCELFEFMGRVAIQDLRYLSQHPLLLPNIVTFISKFIPELFQNEEFKGIGSIKNSNNNALNNVTGIETQFLNPSTEEVSQKVDSYFMELSKKLTTENIRLSQEITQLKADMNSVGNVCNQILLLQRQLLSGNQAIGSKSENIVSST... | null | null | carbon catabolite repression of transcription from RNA polymerase II promoter by glucose [GO:0000433]; nucleosome organization [GO:0034728]; positive regulation of ribosomal protein gene transcription by RNA polymerase II [GO:0060963]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive reg... | nuclear envelope [GO:0005635]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF12550; | null | null | PTM: Phosphorylated in a GCR2-dependent manner. {ECO:0000269|PubMed:9335588}. | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Transcriptional activator required for the expression of glycolytic and ribosomal genes. Forms a transcriptional activation complex with RAP1, RAP1 providing the specific DNA-binding function and GCR1 providing the activation function. Can also bind itself to DNA to a core 5'-CTTCC-3' sequence (CT box). CT bo... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07263 | SYH_YEAST | MLSRSLNKVVTSIKSSSIIRMSSATAAATSAPTANAANALKASKAPKKGKLQVSLKTPKGTKDWADSDMVIREAIFSTLSGLFKKHGGVTIDTPVFELREILAGKYGEDSKLIYNLEDQGGELCSLRYDLTVPFARYVAMNNIQSIKRYHIAKVYRRDQPAMTKGRMREFYQCDFDVAGTFESMVPDSECLSILVEGLTSLGIKDFKIKLNHRKILDGIFQIAGVKDEDVRKISSAVDKLDKSPWEAVKKEMTEEKGQSEETADKIGEYVKLNGSLKEIHAVLSADANITSNEKAKQGLDDIATLMKYTEAFDIDSFISF... | 6.1.1.21 | null | histidyl-tRNA aminoacylation [GO:0006427]; mitochondrial translation [GO:0032543] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739] | aminoacyl-tRNA ligase activity [GO:0004812]; ATP binding [GO:0005524]; histidine-tRNA ligase activity [GO:0004821]; identical protein binding [GO:0042802]; mRNA binding [GO:0003729]; RNA binding [GO:0003723] | PF03129;PF13393; | 3.40.50.800; | Class-II aminoacyl-tRNA synthetase family | null | SUBCELLULAR LOCATION: [Isoform Cytoplasmic]: Cytoplasm.; SUBCELLULAR LOCATION: [Isoform Mitochondrial]: Mitochondrion. | CATALYTIC ACTIVITY: Reaction=ATP + L-histidine + tRNA(His) = AMP + diphosphate + H(+) + L-histidyl-tRNA(His); Xref=Rhea:RHEA:17313, Rhea:RHEA-COMP:9665, Rhea:RHEA-COMP:9689, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57595, ChEBI:CHEBI:78442, ChEBI:CHEBI:78527, ChEBI:CHEBI:456215; EC=6.1.1.21; | null | null | null | null | FUNCTION: Catalyzes the aminoacylation of histidyl-tRNA in both the cytoplasm and the mitochondrion. {ECO:0000269|PubMed:1459448, ECO:0000269|PubMed:3521891}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07264 | LEUC_YEAST | MVYTPSKGPRTLYDKVFDAHVVHQDENGSFLLYIDRHLVHEVTSPQAFEGLENAGRKVRRVDCTLATVDHNIPTESRKNFKSLDTFIKQTDSRLQVKTLENNVKQFGVPYFGMSDARQGIVHTIGPEEGFTLPGTTVVCGDSHTSTHGAFGSLAFGIGTSEVEHVLATQTIIQAKSKNMRITVNGKLSPGITSKDLILYIIGLIGTAGGTGCVIEFAGEAIEALSMEARMSMCNMAIEAGARAGMIKPDETTFQYTKGRPLAPKGAEWEKAVAYWKTLKTDEGAKFDHEINIEAVDVIPTITWGTSPQDALPITGSVPDP... | 4.2.1.33 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250}; Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000250}; | amino acid biosynthetic process [GO:0008652]; leucine biosynthetic process [GO:0009098] | 3-isopropylmalate dehydratase complex [GO:0009316]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829] | 3-isopropylmalate dehydratase activity [GO:0003861]; 4 iron, 4 sulfur cluster binding [GO:0051539]; metal ion binding [GO:0046872] | PF00330;PF00694; | 3.30.499.10;3.20.19.10; | Aconitase/IPM isomerase family | null | null | CATALYTIC ACTIVITY: Reaction=(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate; Xref=Rhea:RHEA:32287, ChEBI:CHEBI:1178, ChEBI:CHEBI:35121; EC=4.2.1.33; | null | PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4. | null | null | FUNCTION: Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07267 | CARP_YEAST | MFSLKALLPLALLLVSANQVAAKVHKAKIYKHELSDEMKEVTFEQHLAHLGQKYLTQFEKANPEVVFSREHPFFTEGGHDVPLTNYLNAQYYTDITLGTPPQNFKVILDTGSSNLWVPSNECGSLACFLHSKYDHEASSSYKANGTEFAIQYGTGSLEGYISQDTLSIGDLTIPKQDFAEATSEPGLTFAFGKFDGILGLGYDTISVDKVVPPFYNAIQQDLLDEKRFAFYLGDTSKDTENGGEATFGGIDESKFKGDITWLPVRRKAYWEVKFEGIGLGDEYAELESHGAAIDTGTSLITLPSGLAEMINAEIGAKKGW... | 3.4.23.25 | null | autophagy [GO:0006914]; cytoplasm to vacuole targeting by the Cvt pathway [GO:0032258]; macroautophagy [GO:0016236]; microautophagy [GO:0016237]; pexophagy [GO:0000425]; proteolysis involved in protein catabolic process [GO:0051603] | endoplasmic reticulum [GO:0005783]; fungal-type vacuole [GO:0000324]; mitochondrion [GO:0005739]; protein-containing complex [GO:0032991] | aspartic-type endopeptidase activity [GO:0004190]; disordered domain specific binding [GO:0097718]; oligosaccharide binding [GO:0070492]; peptidase activity [GO:0008233] | PF00026; | 2.40.70.10; | Peptidase A1 family | null | SUBCELLULAR LOCATION: Vacuole. Note=Lysosome-like vacuoles. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of proteins with broad specificity for peptide bonds. Cleaves -Leu-Leu-|-Val-Tyr- bond in a synthetic substrate. Does not act on esters of Tyr or Arg.; EC=3.4.23.25; | null | null | null | null | FUNCTION: Aspartyl protease implicated in the post-translational regulation of S.cerevisiae vacuolar proteinases. Acts on YSCB, on YSCY and on itself. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07268 | PRZN_SERME | MQSTKKAIEITESNFAAATTGYDAVDDLLHYHERGNGIQINGKDSFSNEQAGLFITRENQTWNGYKVFGQPVKLTFSFPDYKFSSTNVAGDTGLSKFSAEQQQQAKLSLQSWADVANITFTEVAAGQKANITFGNYSQDRPGHYDYGTQAYAFLPNTIWQGQDLGGQTWYNVNQSNVKHPATEDYGRQTFTHEIGHALGLSHPGDYNAGEGNPTYRDVTYAEDTRQFSLMSYWSETNTGGDNGGHYAAAPLLDDIAAIQHLYGANLSTRTGDTVYGFNSNTGRDFLSTTSNSQKVIFAAWDAGGNDTFDFSGYTANQRIN... | 3.4.24.40 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Note=Binds 7 Ca(2+) ions per subunit.; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.; | collagen catabolic process [GO:0030574]; extracellular matrix organization [GO:0030198]; proteolysis [GO:0006508] | extracellular matrix [GO:0031012]; extracellular space [GO:0005615] | calcium ion binding [GO:0005509]; metalloendopeptidase activity [GO:0004222]; zinc ion binding [GO:0008270] | PF00353;PF00413;PF08548; | 3.40.390.10;2.150.10.10; | Peptidase M10B family | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Preferential cleavage of bonds with hydrophobic residues in P1'.; EC=3.4.24.40; | null | null | null | null | FUNCTION: Naturally present in the silkworm intestine and allows the emerging moth to dissolve its cocoon. | Serratia marcescens (strain ATCC 21074 / E-15) |
P07269 | PHO2_YEAST | MMEEFSYDHDFNTHFATDLDYLQHDQQQQQQQQHDQQHNQQQQPQPQPIQTQNLEHDHDQHTNDMSASSNASDSGPQRPKRTRAKGEALDVLKRKFEINPTPSLVERKKISDLIGMPEKNVRIWFQNRRAKLRKKQHGSNKDTIPSSQSRDIANDYDRGSTDNNLVTTTSTSSIFHDEDLTFFDRIPLNSNNNYYFFDICSITVGSWNRMKSGALQRRNFQSIKELRNLSPIKINNIMSNATDLMVLISKKNSEINYFFSAMANNTKILFRIFFPLSSVTNCSLTLETDDDIINSNNTSDKNNSNTNNDDDNDDNSNEDN... | null | null | cell differentiation [GO:0030154]; chromatin remodeling [GO:0006338]; positive regulation of DNA binding [GO:0043388]; positive regulation of phosphate metabolic process [GO:0045937]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription regulatory region DNA bindi... | cytosol [GO:0005829]; nucleus [GO:0005634] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565] | PF00046; | 1.10.10.60; | null | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Regulator in phosphate metabolism and acts as a derepressor of another central regulator PHO5. Binds to the upstream activator sequence (UAS) of PHO5. It also binds to the TRP4, HIS4, and CYC1 promoters. {ECO:0000269|PubMed:3049251}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07270 | PHO4_YEAST | MGRTTSEGIHGFVDDLEPKSSILDKVGDFITVNTKRHDGREDFNEQNDELNSQENHNSSENGNENENEQDSLALDDLDRAFELVEGMDMDWMMPSHAHHSPATTATIKPRLLYSPLIHTQSAVPVTISPNLVATATSTTSANKVTKNKSNSSPYLNKRRGKPGPDSATSLFELPDSVIPTPKPKPKPKQYPKVILPSNSTRRVSPVTAKTSSSAEGVVVASESPVIAPHGSSHSRSLSKRRSSGALVDDDKRESHKHAEQARRNRLAVALHELASLIPAEWKQQNVSAAPSKATTVEAACRYIRHLQQNVST | null | null | cellular response to phosphate starvation [GO:0016036]; chromatin remodeling [GO:0006338]; positive regulation of phosphate metabolic process [GO:0045937]; positive regulation of transcription by RNA polymerase II [GO:0045944] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | DNA-binding transcription factor activity [GO:0003700]; protein dimerization activity [GO:0046983]; sequence-specific DNA binding [GO:0043565] | PF00010; | 4.10.280.10; | null | PTM: Phosphorylated by the cyclin-CDK PHO80-PHO85 at five residues under high-phosphate conditions, preventing PHO4 from activating the structural PHO genes. Phosphorylation of Ser-114 and Ser-128 promotes nuclear export. Phosphorylation of Ser-152 decreases nuclear import. Phosphorylation of Ser-223 decreases the bind... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:8539622}. Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:8539622}. Note=Predominantly cytoplasmic under high-phosphate conditions and localized to the nucleus upon phosphate starvation. | null | null | null | null | null | FUNCTION: Transcriptional activator that regulates the expression of repressible phosphatase under phosphate starvation conditions. Binds to the upstream activating sequence (UAS) of several phosphatase encoding PHO genes. Inhibited by the cyclin-CDK PHO80-PHO85 under high-phosphate conditions. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07271 | PIF1_YEAST | MPKWIRSTLNHIIPRRPFICSFNSFLLLKNVSHAKLSFSMSSRGFRSNNFIQAQLKHPSILSKEDLDLLSDSDDWEEPDCIQLETEKQEKKIITDIHKEDPVDKKPMRDKNVMNFINKDSPLSWNDMFKPSIIQPPQLISENSFDQSSQKKSRSTGFKNPLRPALKKESSFDELQNNSISQERSLEMINENEKKKMQFGEKIAVLTQRPSFTELQNDQDDSNLNPHNGVKVKIPICLSKEQESIIKLAENGHNIFYTGSAGTGKSILLREMIKVLKGIYGRENVAVTASTGLAACNIGGITIHSFAGIGLGKGDADKLYK... | 3.6.4.12 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP-Rule:MF_03176, ECO:0000269|PubMed:8253734}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|HAMAP-Rule:MF_03176, ECO:0000269|PubMed:8253734}; Note=Mg(2+). To a lesser extent, can also use Mn(2+). {ECO:0000255|HAMAP-Rule:MF_03176, ECO:... | chromosome organization [GO:0051276]; DNA duplex unwinding [GO:0032508]; DNA recombination [GO:0006310]; DNA replication [GO:0006260]; DNA unwinding involved in DNA replication [GO:0006268]; double-strand break repair via break-induced replication [GO:0000727]; G-quadruplex DNA unwinding [GO:0044806]; mitochondrial gen... | mitochondrial inner membrane [GO:0005743]; mitochondrial membrane [GO:0031966]; mitochondrion [GO:0005739]; nuclear replication fork [GO:0043596]; nucleolus [GO:0005730]; replication fork [GO:0005657] | 5'-3' DNA helicase activity [GO:0043139]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA helicase activity [GO:0003678]; G-quadruplex DNA binding [GO:0051880]; single-stranded DNA binding [GO:0003697]; telomerase inhibitor activity [GO:0010521] | PF05970;PF21530; | 3.40.50.300; | Helicase family, PIF1 subfamily | PTM: Phosphorylated. Undergoes RAD53-dependent phosphorylation in response to loss of mtDNA. {ECO:0000269|PubMed:22927468}. | SUBCELLULAR LOCATION: [Isoform Nuclear]: Nucleus, nucleolus {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16816432}. Note=Mainly concentrated in the nucleolus, and occasionally redistributes to single nuclear foci outside the nucleolus, probably sites of DNA repair. {ECO:0000269|PubMed:16816432}.; SUBCELLULAR LOCATI... | 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=3.6.4.12; Evidence={ECO:0000255|HAMAP-Rule:MF_03176, ECO:0000269|PubMed:1849081, ECO:0000269|PubMed:23446274, ECO:0000269|PubMed:23596... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.3 mM for ATP {ECO:0000269|PubMed:8253734}; KM=0.4 mM for dATP {ECO:0000269|PubMed:8253734}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-9.5. {ECO:0000269|PubMed:8253734}; | null | FUNCTION: DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of both mitochondrial and nuclear genome stability. Efficiently unwinds G-quadruplex (G4) DNA structures and forked RNA-DNA hybrids. Appears to move along DNA in single nucleotide or base pair steps, powered by hydrolysis of 1 molecule o... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07272 | PPR1_YEAST | MKQKKFNSKKSNRTDLSKRGDSPNIGISKSRTACKRCRLKKIKCDQEFPSCKRCAKLEVPCVSLDPATGKDVPRSYVFFLEDRLAVMMRVLKEYGVDPTKIRGNIPATSDDEPFDLKKYSSVSSLGEEGILPHNGLLADYLVQKGNSMASSAITSKSMASPQTINVQRKEFLVNSKKQDGSALLPETGSPMTSDARAEELRRCNKEISALGTMRESSFNSFLGDSSGISFAKLVFTATNFRQDSGDDVLDEDIKQREQKYNGYAEAENNPHFDPLELPPRHAAEVMISRFFVDTNSQLPLLHRELFLKKYFEPIYGPWNP... | null | null | DNA-templated transcription [GO:0006351]; positive regulation of pyrimidine nucleotide biosynthetic process [GO:1900399]; positive regulation of transcription by RNA polymerase II [GO:0045944]; pyrimidine nucleotide biosynthetic process [GO:0006221] | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; sequence-specific DNA binding [GO:0043565]; zinc ion binding [GO:0008270] | PF04082;PF00172; | 4.10.240.10; | null | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Positive regulator of URA1 and URA3 expression. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07273 | TFS2_YEAST | MDSKEVLVHVKNLEKNKSNDAAVLEILHVLDKEFVPTEKLLRETKVGVEVNKFKKSTNVEISKLVKKMISSWKDAINKNKRSRQAQQHHQDHAPGNAEDKTTVGESVNGVQQPASSQSDAMKQDKYVSTKPRNSKNDGVDTAIYHHKLRDQVLKALYDVLAKESEHPPQSILHTAKAIESEMNKVNNCDTNEAAYKARYRIIYSNVISKNNPDLKHKIANGDITPEFLATCDAKDLAPAPLKQKIEEIAKQNLYNAQGATIERSVTDRFTCGKCKEKKVSYYQLQTRSADEPLTTFCTCEACGNRWKFS | null | null | DNA-templated transcription [GO:0006351]; maintenance of transcriptional fidelity during transcription elongation by RNA polymerase II [GO:0001193]; positive regulation of RNA polymerase II transcription preinitiation complex assembly [GO:0045899]; positive regulation of transcription elongation by RNA polymerase II [G... | nucleus [GO:0005634] | RNA polymerase II complex binding [GO:0000993]; RNA polymerase II complex recruiting activity [GO:0001139]; RNA polymerase II transcription regulatory region sequence-specific DNA binding [GO:0000977]; zinc ion binding [GO:0008270] | PF08711;PF01096;PF07500; | 2.20.25.10;1.20.930.10;1.10.472.30; | TFS-II family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Necessary for efficient RNA polymerase II transcription elongation past template-encoded arresting sites. The arresting sites in DNA have the property of trapping a certain fraction of elongating RNA polymerases that pass through, resulting in locked ternary complexes. Cleavage of the nascent transcript by S-... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07274 | PROF_YEAST | MSWQAYTDNLIGTGKVDKAVIYSRAGDAVWATSGGLSLQPNEIGEIVQGFDNPAGLQSNGLHIQGQKFMLLRADDRSIYGRHDAEGVVCVRTKQTVIIAHYPPTVQAGEATKIVEQLADYLIGVQY | null | null | intracellular transport [GO:0046907]; mitotic actomyosin contractile ring assembly [GO:1903475]; positive regulation of formin-nucleated actin cable assembly [GO:0090338]; sequestering of actin monomers [GO:0042989] | cell cortex [GO:0005938]; cytoskeleton [GO:0005856]; cytosol [GO:0005829] | actin monomer binding [GO:0003785]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546]; proline-rich region binding [GO:0070064] | PF00235; | 3.30.450.30; | Profilin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. | null | null | null | null | null | FUNCTION: Binds to actin and affects the structure of the cytoskeleton. At high concentrations, profilin prevents the polymerization of actin, whereas it enhances it at low concentrations. By binding to PIP2, it inhibits the formation of IP3 and DG. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07276 | RAD2_YEAST | MGVHSFWDIAGPTARPVRLESLEDKRMAVDASIWIYQFLKAVRDQEGNAVKNSHITGFFRRICKLLYFGIRPVFVFDGGVPVLKRETIRQRKERRQGKRESAKSTARKLLALQLQNGSNDNVKNSTPSSGSSVQIFKPQDEWDLPDIPGFKYDKEDARVNSNKTFEKLMNSINGDGLEDIDLDTINPASAEFEELPKATQYLILSSLRLKSRLRMGYSKEQLETIFPNSMDFSRFQIDMVKRRNFFTQKLINTTGFQDGGASKLNEEVINRISGQKSKEYKLTKTNNGWILGLGANDGSDAQKAIVIDDKDAGALVKQLD... | 3.1.-.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions per subunit. They probably participate in the reaction catalyzed by the enzyme. May bind an additional third magnesium ion after substrate binding. {ECO:0000250}; | nucleotide-excision repair [GO:0006289]; transcription by RNA polymerase II [GO:0006366] | nucleotide-excision repair factor 3 complex [GO:0000112]; nucleus [GO:0005634] | DNA endonuclease activity [GO:0004520]; metal ion binding [GO:0046872]; single-stranded DNA binding [GO:0003697]; single-stranded DNA endodeoxyribonuclease activity [GO:0000014] | PF00867;PF00752; | 1.10.150.20;3.40.50.1010; | XPG/RAD2 endonuclease family, XPG subfamily | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Single-stranded DNA endonuclease involved in excision repair of DNA damaged with UV light, bulky adducts, or cross-linking agents. Essential for the incision step of excision-repair. {ECO:0000269|PubMed:8247134}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07277 | ERG12_YEAST | MSLPFLTSAPGKVIIFGEHSAVYNKPAVAASVSALRTYLLISESSAPDTIELDFPDISFNHKWSINDFNAITEDQVNSQKLAKAQQATDGLSQELVSLLDPLLAQLSESFHYHAAFCFLYMFVCLCPHAKNIKFSLKSTLPIGAGLGSSASISVSLALAMAYLGGLIGSNDLEKLSENDKHIVNQWAFIGEKCIHGTPSGIDNAVATYGNALLFEKDSHNGTINTNNFKFLDDFPAIPMILTYTRIPRSTKDLVARVRVLVTEKFPEVMKPILDAMGECALQGLEIMTKLSKCKGTDDEAVETNNELYEQLLELIRINHG... | 2.7.1.36 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P17256}; | ergosterol biosynthetic process [GO:0006696]; farnesyl diphosphate biosynthetic process, mevalonate pathway [GO:0010142]; isopentenyl diphosphate biosynthetic process, mevalonate pathway [GO:0019287]; phosphorylation [GO:0016310] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | ATP binding [GO:0005524]; magnesium ion binding [GO:0000287]; mevalonate kinase activity [GO:0004496] | PF00288; | 3.30.230.10;3.30.70.890; | GHMP kinase family, Mevalonate kinase subfamily | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000305|PubMed:1645230}. | CATALYTIC ACTIVITY: Reaction=(R)-mevalonate + ATP = (R)-5-phosphomevalonate + ADP + H(+); Xref=Rhea:RHEA:17065, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:36464, ChEBI:CHEBI:58146, ChEBI:CHEBI:456216; EC=2.7.1.36; Evidence={ECO:0000269|PubMed:1645230}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17066; ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.13 mM for mevalonate {ECO:0000269|PubMed:1645230}; Vmax=27 nmol/min/mg enzyme {ECO:0000269|PubMed:1645230}; | PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via mevalonate pathway; isopentenyl diphosphate from (R)-mevalonate: step 1/3. {ECO:0000269|PubMed:1645230}. | null | null | FUNCTION: Mevalonate kinase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway (PubMed:1645230). ERG12 converts mevalonate into 5-phosphomevalonate (PubMed:1645230). The second module is carried out in the vacuole and involves the formation of farnesyl diphosphat... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07278 | KAPR_YEAST | MVSSLPKESQAELQLFQNEINAANPSDFLQFSANYFNKRLEQQRAFLKAREPEFKAKNIVLFPEPEESFSRPQSAQSQSRSRSSVMFKSPFVNEDPHSNVFKSGFNLDPHEQDTHQQAQEEQQHTREKTSTPPLPMHFNAQRRTSVSGETLQPNNFDDWTPDHYKEKSEQQLQRLEKSIRNNFLFNKLDSDSKRLVINCLEEKSVPKGATIIKQGDQGDYFYVVEKGTVDFYVNDNKVNSSGPGSSFGELALMYNSPRAATVVATSDCLLWALDRLTFRKILLGSSFKKRLMYDDLLKSMPVLKSLTTYDRAKLADALDT... | null | null | negative regulation of Ras protein signal transduction [GO:0046580]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein localization to bud neck [GO:0097271]; regulation of cytoplasmic mRNA processing body assembly [GO:0010603]; regulation of protein phosphorylation [GO:0001932] | cAMP-dependent protein kinase complex [GO:0005952]; chromatin [GO:0000785]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | cAMP binding [GO:0030552]; cAMP-dependent protein kinase inhibitor activity [GO:0004862]; identical protein binding [GO:0042802]; protein kinase A catalytic subunit binding [GO:0034236] | PF00027;PF02197; | 2.60.120.10; | CAMP-dependent kinase regulatory chain family | PTM: Phosphorylated by YAK1 in response to glucose starvation. Phosphorylated by MCK1 at Thr-129 upon TOR complex 1 (TORC1) inhibition. Thr-129 phosphorylation activates BCY1 to inhibit PKA. TORC1 inhibits phosphorylation of RxxS/T sites but has no effect on Ser-145 phosphorylation. The phosphorylation sites can be clu... | SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Cytoplasmic when phosphorylated. Nuclear when not phosphorylated. | null | null | null | null | null | FUNCTION: Regulatory subunit of the cyclic AMP-dependent protein kinase (PKA), an effector of the Ras/cAMP pathway. Inhibits PKA activity in the absence of cAMP. cAMP activates PKA and promotes growth and proliferation in response to good nutrient conditions. Together with ZDS1, provides a negative feedback control on ... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07280 | RS19A_YEAST | MPGVSVRDVAAQDFINAYASFLQRQGKLEVPGYVDIVKTSSGNEMPPQDAEGWFYKRAASVARHIYMRKQVGVGKLNKLYGGAKSRGVRPYKHIDASGSINRKVLQALEKIGIVEISPKGGRRISENGQRDLDRIAAQTLEEDE | null | null | ribosomal small subunit assembly [GO:0000028]; ribosomal small subunit biogenesis [GO:0042274]; ribosomal subunit export from nucleus [GO:0000054]; translation [GO:0006412] | cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627] | RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735] | PF01090; | 1.10.10.10; | Eukaryotic ribosomal protein eS19 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}. | null | null | null | null | null | FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains t... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07281 | RS19B_YEAST | MAGVSVRDVAAQDFINAYASFLQRQGKLEVPGYVDIVKTSSGNEMPPQDAEGWFYKRAASVARHIYMRKQVGVGKLNKLYGGAKSRGVRPYKHIDASGSINRKVLQALEKIGIVEISPKGGRRISENGQRDLDRIAAQTLEEDE | null | null | ribosomal small subunit assembly [GO:0000028]; ribosomal small subunit biogenesis [GO:0042274]; ribosomal subunit export from nucleus [GO:0000054]; translation [GO:0006412] | cytosol [GO:0005829]; cytosolic small ribosomal subunit [GO:0022627] | RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735] | PF01090; | 1.10.10.10; | Eukaryotic ribosomal protein eS19 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:22096102}. | null | null | null | null | null | FUNCTION: Component of the ribosome, a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell. The small ribosomal subunit (SSU) binds messenger RNAs (mRNAs) and translates the encoded message by selecting cognate aminoacyl-transfer RNA (tRNA) molecules. The large subunit (LSU) contains t... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07283 | PMM_YEAST | MSIAEFAYKEKPETLVLFDVDGTLTPARLTVSEEVRKTLAKLRNKCCIGFVGGSDLSKQLEQLGPNVLDEFDYSFSENGLTAYRLGKELASQSFINWLGEEKYNKLAVFILRYLSEIDLPKRRGTFLEFRNGMINVSPIGRNASTEERNEFERYDKEHQIRAKFVEALKKEFPDYGLTFSIGGQISFDVFPAGWDKTYCLQHVEKDGFKEIHFFGDKTMVGGNDYEIFVDERTIGHSVQSPDDTVKILTELFNL | 5.4.2.8 | null | GDP-mannose biosynthetic process [GO:0009298]; mannose metabolic process [GO:0006013]; protein N-linked glycosylation [GO:0006487] | cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829] | metal ion binding [GO:0046872]; phosphomannomutase activity [GO:0004615] | PF03332; | 3.30.1240.20;3.40.50.1000; | Eukaryotic PMM family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:3905826}. | CATALYTIC ACTIVITY: Reaction=alpha-D-mannose 1-phosphate = D-mannose 6-phosphate; Xref=Rhea:RHEA:11140, ChEBI:CHEBI:58409, ChEBI:CHEBI:58735; EC=5.4.2.8; Evidence={ECO:0000269|PubMed:3288631}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:11142; Evidence={ECO:0000305|PubMed:3288631}; | null | PATHWAY: Nucleotide-sugar biosynthesis; GDP-alpha-D-mannose biosynthesis; alpha-D-mannose 1-phosphate from D-fructose 6-phosphate: step 2/2. {ECO:0000305|PubMed:3288631}. | null | null | FUNCTION: Involved in the synthesis of the GDP-mannose and dolichol-phosphate-mannose required for a number of critical mannosyl transfer reactions such as folding and glycosylation of secretory proteins in the ER lumen. {ECO:0000269|PubMed:3288631}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07284 | SYSC_YEAST | MLDINQFIEDKGGNPELIRQSQKARNASVEIVDEIISDYKDWVKTRFELDELNKKFNKLQKDIGLKFKNKEDASGLLAEKEKLTQQKKELTEKEQQEDKDLKKKVFQVGNIVHPSVVVSNDEENNELVRTWKPEDLEAVGPIASVTGKPASLSHHEILLRLDGYDPDRGVKICGHRGYFFRNYGVFLNQALINYGLQFLAAKGYIPLQAPVMMNKELMSKTAQLSEFDEELYKVIDGEDEKYLIATSEQPISAYHSGEWFEKPQEQLPIHYVGYSSCFRREAGSHGKDAWGVFRVHAFEKIEQFVITEPEKSWEEFEKMI... | 6.1.1.11 | null | cytoplasmic translation [GO:0002181]; mitochondrial seryl-tRNA aminoacylation [GO:0070158]; seryl-tRNA aminoacylation [GO:0006434] | cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; mitochondrion [GO:0005739] | ATP binding [GO:0005524]; serine-tRNA ligase activity [GO:0004828]; tRNA binding [GO:0000049] | PF02403;PF00587; | 1.10.287.40; | Class-II aminoacyl-tRNA synthetase family, Type-1 seryl-tRNA synthetase subfamily | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P49591}. | CATALYTIC ACTIVITY: Reaction=ATP + L-serine + tRNA(Ser) = AMP + diphosphate + H(+) + L-seryl-tRNA(Ser); Xref=Rhea:RHEA:12292, Rhea:RHEA-COMP:9669, Rhea:RHEA-COMP:9703, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:33384, ChEBI:CHEBI:78442, ChEBI:CHEBI:78533, ChEBI:CHEBI:456215; EC=6.1.1.11; Evide... | null | null | null | null | FUNCTION: Catalyzes the attachment of serine to tRNA(Ser) in a two-step reaction: serine is first activated by ATP to form Ser-AMP and then transferred to the acceptor end of tRNA(Ser). {ECO:0000269|PubMed:3031581}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07286 | GPT_YEAST | MLRLFSLALITCLIYYSKNQGPSALVAAVGFGIAGYLATDMLIPRVGKSFIKIGLFGKDLSKPGRPVLPETIGAIPAAVYLFVMFIYIPFIFYKYMVITTSGGGHRDVSVVEDNGMNSNIFPHDKLSEYLSAILCLESTVLLGIADDLFDLRWRHKFFLPAIAAIPLLMVYYVDFGVTHVLIPGFMERWLKKTSVDLGLWYYVYMASMAIFCPNSINILAGVNGLEVGQCIVLAILALLNDLLYFSMGPLATRDSHRFSAVLIIPFLGVSLALWKWNRWPATVFVGDTYCYFAGMVFAVVGILGHFSKTMLLLFIPQIVN... | 2.7.8.15 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9H3H5}; | aerobic respiration [GO:0009060]; dolichol-linked oligosaccharide biosynthetic process [GO:0006488]; protein N-linked glycosylation [GO:0006487] | endoplasmic reticulum [GO:0005783]; UDP-N-acetylglucosamine transferase complex [GO:0043541] | glycosyltransferase activity [GO:0016757]; metal ion binding [GO:0046872]; UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase activity [GO:0003975] | PF00953; | null | Glycosyltransferase 4 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P23338}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9H3H5}. | CATALYTIC ACTIVITY: Reaction=a dolichyl phosphate + UDP-N-acetyl-alpha-D-glucosamine = N-acetyl-alpha-D-glucosaminyl-diphosphodolichol + UMP; Xref=Rhea:RHEA:13289, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9519, ChEBI:CHEBI:57683, ChEBI:CHEBI:57705, ChEBI:CHEBI:57865, ChEBI:CHEBI:58427; EC=2.7.8.15; Evidence={ECO:0000269|Pub... | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000305|PubMed:6096695}. | null | null | FUNCTION: UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase that operates in the biosynthetic pathway of dolichol-linked oligosaccharides, the glycan precursors employed in protein asparagine (N)-glycosylation. The assembly of dolichol-linked oligosaccharides begins on the cytosolic side... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P07288 | KLK3_HUMAN | MWVPVVFLTLSVTWIGAAPLILSRIVGGWECEKHSQPWQVLVASRGRAVCGGVLVHPQWVLTAAHCIRNKSVILLGRHSLFHPEDTGQVFQVSHSFPHPLYDMSLLKNRFLRPGDDSSHDLMLLRLSEPAELTDAVKVMDLPTQEPALGTTCYASGWGSIEPEEFLTPKKLQCVDLHVISNDVCAQVHPQKVTKFMLCAGRWTGGKSTCSGDSGGPLVCNGVLQGITSWGSEPCALPERPSLYTKVVHYRKWIKDTIVANP | 3.4.21.77 | null | negative regulation of angiogenesis [GO:0016525]; positive regulation of antibacterial peptide production [GO:0002803]; protein metabolic process [GO:0019538]; proteolysis [GO:0006508]; regulation of systemic arterial blood pressure [GO:0003073]; zymogen activation [GO:0031638] | extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; secretory granule [GO:0030141] | endopeptidase activity [GO:0004175]; hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides [GO:0016811]; serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236] | PF00089; | 2.40.10.10; | Peptidase S1 family, Kallikrein subfamily | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: -Tyr-|-Xaa-.; EC=3.4.21.77; | null | null | null | null | FUNCTION: Hydrolyzes semenogelin-1 thus leading to the liquefaction of the seminal coagulum. | Homo sapiens (Human) |
P07293 | CAC1S_RABIT | MEPSSPQDEGLRKKQPKKPLPEVLPRPPRALFCLTLQNPLRKACISIVEWKPFETIILLTIFANCVALAVYLPMPEDDNNSLNLGLEKLEYFFLTVFSIEAAMKIIAYGFLFHQDAYLRSGWNVLDFIIVFLGVFTAILEQVNVIQSNTAPMSSKGAGLDVKALRAFRVLRPLRLVSGVPSLQVVLNSIFKAMLPLFHIALLVLFMVIIYAIIGLELFKGKMHKTCYYIGTDIVATVENEKPSPCARTGSGRPCTINGSECRGGWPGPNHGITHFDNFGFSMLTVYQCITMEGWTDVLYWVNDAIGNEWPWIYFVTLILL... | null | null | calcium ion import across plasma membrane [GO:0098703]; calcium ion transmembrane transport [GO:0070588]; cellular response to caffeine [GO:0071313]; muscle contraction [GO:0006936]; positive regulation of muscle contraction [GO:0045933]; regulation of ryanodine-sensitive calcium-release channel activity [GO:0060314]; ... | L-type voltage-gated calcium channel complex [GO:1990454]; plasma membrane [GO:0005886]; T-tubule [GO:0030315] | calmodulin binding [GO:0005516]; high voltage-gated calcium channel activity [GO:0008331]; metal ion binding [GO:0046872]; transmembrane transporter binding [GO:0044325]; voltage-gated calcium channel activity [GO:0005245] | PF08763;PF16885;PF16905;PF00520; | 1.10.287.70;6.10.250.2180;6.10.250.2500;1.20.120.350; | Calcium channel alpha-1 subunit (TC 1.A.1.11) family, CACNA1S subfamily | PTM: The alpha-1S subunit is found in two isoforms in the skeletal muscle: a minor form of 212 kDa containing the complete amino acid sequence, and a major form of 190 kDa derived from the full-length form by post-translational proteolysis close to Phe-1690. {ECO:0000305|PubMed:3037387}.; PTM: Phosphorylated. Phosphory... | SUBCELLULAR LOCATION: Cell membrane, sarcolemma, T-tubule {ECO:0000269|PubMed:15201141, ECO:0000269|PubMed:25548159, ECO:0000269|PubMed:25667046, ECO:0000269|PubMed:26680202, ECO:0000269|PubMed:27580036, ECO:0000269|PubMed:27621462, ECO:0000269|PubMed:28112192, ECO:0000269|PubMed:29078335, ECO:0000269|PubMed:29467163, ... | null | null | null | null | null | FUNCTION: Pore-forming, alpha-1S subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents in skeletal muscle (PubMed:15201141, PubMed:25548159, PubMed:27621462, PubMed:29078335, PubMed:29467163, PubMed:9465115). Calcium channels containing the alpha-1S subunit play an important role in ex... | Oryctolagus cuniculus (Rabbit) |
P07305 | H10_HUMAN | MTENSTSAPAAKPKRAKASKKSTDHPKYSDMIVAAIQAEKNRAGSSRQSIQKYIKSHYKVGENADSQIKLSIKRLVTTGVLKQTKGVGASGSFRLAKSDEPKKSVAFKKTKKEIKKVATPKKASKPKKAASKAPTKKPKATPVKKAKKKLAATPKKAKKPKTVKAKPVKASKPKKAKPVKPKAKSSAKRAGKKK | null | null | chromosome condensation [GO:0030261]; heterochromatin formation [GO:0031507]; negative regulation of DNA recombination [GO:0045910]; nucleosome assembly [GO:0006334]; positive regulation of transcription regulatory region DNA binding [GO:2000679] | actin cytoskeleton [GO:0015629]; chromatin [GO:0000785]; euchromatin [GO:0000791]; Golgi apparatus [GO:0005794]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; nucleosome [GO:0000786]; nucleus [GO:0005634]; transcription repressor complex [GO:0017053] | chromatin DNA binding [GO:0031490]; double-stranded DNA binding [GO:0003690]; minor groove of adenine-thymine-rich DNA binding [GO:0003680]; nucleosomal DNA binding [GO:0031492]; nucleosome binding [GO:0031491]; RNA binding [GO:0003723]; structural constituent of chromatin [GO:0030527] | PF00538; | 1.10.10.10; | Histone H1/H5 family | PTM: Phosphorylated on Ser-17 in RNA edited version. {ECO:0000269|PubMed:18993075}.; PTM: ADP-ribosylated on Ser-104 in response to DNA damage. {ECO:0000269|PubMed:27723750}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00837, ECO:0000269|PubMed:18993075}. Chromosome {ECO:0000255|PROSITE-ProRule:PRU00837, ECO:0000269|PubMed:18993075}. Note=The RNA edited version has been localized to nuclear speckles. During mitosis, it appears in the vicinity of condensed chromosomes. | null | null | null | null | null | FUNCTION: Histones H1 are necessary for the condensation of nucleosome chains into higher-order structures. The histones H1.0 are found in cells that are in terminal stages of differentiation or that have low rates of cell division. | Homo sapiens (Human) |
P07306 | ASGR1_HUMAN | MTKEYQDLQHLDNEESDHHQLRKGPPPPQPLLQRLCSGPRLLLLSLGLSLLLLVVVCVIGSQNSQLQEELRGLRETFSNFTASTEAQVKGLSTQGGNVGRKMKSLESQLEKQQKDLSEDHSSLLLHVKQFVSDLRSLSCQMAALQGNGSERTCCPVNWVEHERSCYWFSRSGKAWADADNYCRLEDAHLVVVTSWEEQKFVQHHIGPVNTWMGLHDQNGPWKWVDGTDYETGFKNWRPEQPDDWYGHGLGGGEDCAHFTDDGRWNDDVCQRPYRWVCETELDKASQEPPLL | null | null | cellular response to extracellular stimulus [GO:0031668]; receptor-mediated endocytosis [GO:0006898] | external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; plasma membrane [GO:0005886] | asialoglycoprotein receptor activity [GO:0004873]; fucose binding [GO:0042806]; identical protein binding [GO:0042802]; mannose binding [GO:0005537]; metal ion binding [GO:0046872]; signaling receptor activity [GO:0038023] | PF00059;PF03954; | 3.10.100.10; | null | PTM: Phosphorylated on a cytoplasmic Ser residue. | SUBCELLULAR LOCATION: [Isoform H1a]: Membrane; Single-pass type II membrane protein.; SUBCELLULAR LOCATION: [Isoform H1b]: Secreted {ECO:0000269|PubMed:20886072}. | null | null | null | null | null | FUNCTION: Mediates the endocytosis of plasma glycoproteins to which the terminal sialic acid residue on their complex carbohydrate moieties has been removed. The receptor recognizes terminal galactose and N-acetylgalactosamine units. After ligand binding to the receptor, the resulting complex is internalized and transp... | Homo sapiens (Human) |
P07307 | ASGR2_HUMAN | MAKDFQDIQQLSSEENDHPFHQGEGPGTRRLNPRRGNPFLKGPPPAQPLAQRLCSMVCFSLLALSFNILLLVVICVTGSQSEGHGGAQLQAELRSLKEAFSNFSSSTLTEVQAISTHGGSVGDKITSLGAKLEKQQQDLKADHDALLFHLKHFPVDLRFVACQMELLHSNGSQRTCCPVNWVEHQGSCYWFSHSGKAWAEAEKYCQLENAHLVVINSWEEQKFIVQHTNPFNTWIGLTDSDGSWKWVDGTDYRHNYKNWAVTQPDNWHGHELGGSEDCVEVQPDGRWNDDFCLQVYRWVCEKRRNATGEVA | null | null | cell surface receptor signaling pathway [GO:0007166]; endocytosis [GO:0006897] | endoplasmic reticulum quality control compartment [GO:0044322]; external side of plasma membrane [GO:0009897]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886] | asialoglycoprotein receptor activity [GO:0004873]; fucose binding [GO:0042806]; mannose binding [GO:0005537]; signaling receptor activity [GO:0038023] | PF00059;PF03954; | 3.10.100.10; | null | null | SUBCELLULAR LOCATION: Membrane; Single-pass type II membrane protein. | null | null | null | null | null | FUNCTION: Mediates the endocytosis of plasma glycoproteins to which the terminal sialic acid residue on their complex carbohydrate moieties has been removed. The receptor recognizes terminal galactose and N-acetylgalactosamine units. After ligand binding to the receptor, the resulting complex is internalized and transp... | Homo sapiens (Human) |
P07308 | ACOD1_RAT | MPAHMLQEISSSYTTTTTITEPPSGNLQNGREKMKKVPLYLEEDIRPEMREDIHDPSYQDEEGPPPKLEYVWRNIILMALLHVGALYGITLIPSSKVYTLLWGIFYYLISALGITAGAHRLWSHRTYKARLPLRIFLIIANTMAFQNDVYEWARDHRAHHKFSETHADPHNSRRGFFFSHVGWLLVRKHPAVKEKGGKLDMSDLKAEKLVMFQRRYYKPGLLLMCFILPTLVPWYCWGETFLHSLFVSTFLRYTLVLNATWLVNSAAHLYGYRPYDKNIQSRENILVSLGAVGEGFHNYHHAFPYDYSASEYRWHINFTT... | 1.14.19.1 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000305|PubMed:2892838, ECO:0000305|PubMed:7947684}; Note=Expected to bind 2 Fe(2+) ions per subunit. {ECO:0000250|UniProtKB:P13516}; | brown fat cell differentiation [GO:0050873]; defense response to Gram-positive bacterium [GO:0050830]; fatty acid biosynthetic process [GO:0006633]; lipid biosynthetic process [GO:0008610]; lipid homeostasis [GO:0055088]; monounsaturated fatty acid biosynthetic process [GO:1903966]; positive regulation of cold-induced ... | endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020] | iron ion binding [GO:0005506]; metal ion binding [GO:0046872]; oxidoreductase activity [GO:0016491]; palmitoyl-CoA 9-desaturase activity [GO:0032896]; stearoyl-CoA 9-desaturase activity [GO:0004768] | null | null | Fatty acid desaturase type 1 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:O00767}; Multi-pass membrane protein {ECO:0000305}. Membrane {ECO:0000269|PubMed:2892838}; Multi-pass membrane protein {ECO:0000269|PubMed:2892838}. | 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:2892838, PubMed:7947684). Catalyzes the insertion of a cis double bond at the Delta-9 position into fatty acyl-CoA substrates including palmit... | Rattus norvegicus (Rat) |
P07313 | MYLK2_RABIT | MATENGAVELGIQSLSTDEASKGAASEESLAAEKDPAPPDPEKGPGPSDTKQDPDPSTPKKDANTPAPEKGDVVPAQPSAGGSQGPAGEGGQVEAPAEGSAGKPAALPQQTATAEASEKKPEAEKGPSGHQDPGEPTVGKKVAEGQAAARRGSPAFLHSPSCPAIIASTEKLPAQKPLSEASELIFEGVPATPGPTEPGPAKAEGGVDLLAESQKEAGEKAPGQADQAKVQGDTSRGIEFQAVPSERPRPEVGQALCLPAREEDCFQILDDCPPPPAPFPHRIVELRTGNVSSEFSMNSKEALGGGKFGAVCTCTEKSTG... | 2.7.11.18 | null | cardiac muscle tissue morphogenesis [GO:0055008]; phosphorylation [GO:0016310]; regulation of muscle filament sliding [GO:0032971]; striated muscle contraction [GO:0006941] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; calmodulin-dependent protein kinase activity [GO:0004683]; myosin light chain binding [GO:0032027]; myosin light chain kinase activity [GO:0004687] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11733062}. Note=Colocalizes with phosphorylated myosin light chain (RLCP) at filaments of the myofibrils. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[myosin light chain] = ADP + H(+) + O-phospho-L-seryl-[myosin light chain]; Xref=Rhea:RHEA:22004, Rhea:RHEA-COMP:13684, Rhea:RHEA-COMP:13685, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.18; CATALYTIC ACTIVITY: React... | null | null | null | null | FUNCTION: Implicated in the level of global muscle contraction and cardiac function (By similarity). Phosphorylates a specific serine in the N-terminus of a myosin light chain. {ECO:0000250}. | Oryctolagus cuniculus (Rabbit) |
P07314 | GGT1_RAT | MKNRFLVLGLVAVVLVFVIIGLCIWLPTTSGKPDHVYSRAAVATDAKRCSEIGRDMLQEGGSVVDAAIASLLCMGLINAHSMGIGGGLFFTIYNSTTRKAEVINAREMAPRLANTSMFNNSKDSEEGGLSVAVPGEIRGYELAHQRHGRLPWARLFQPSIQLARHGFPVGKGLARALDKKRDIIEKTPALCEVFCRQGKVLQEGETVTMPKLADTLQILAQEGARAFYNGSLTAQIVKDIQEAGGIMTVEDLNNYRAEVIEHPMSIGLGDSTLYVPSAPLSGPVLILILNILKGYNFSPKSVATPEQKALTYHRIVEAFR... | 2.3.2.2; 3.4.19.13; 3.4.19.14 | null | amino acid metabolic process [GO:0006520]; cellular response to oxidative stress [GO:0034599]; cysteine biosynthetic process [GO:0019344]; fatty acid metabolic process [GO:0006631]; glutamate metabolic process [GO:0006536]; glutathione biosynthetic process [GO:0006750]; glutathione catabolic process [GO:0006751]; hepat... | extracellular space [GO:0005615]; plasma membrane [GO:0005886]; vesicle [GO:0031982] | aminoacyltransferase activity [GO:0016755]; glutathione hydrolase activity [GO:0036374]; leukotriene C4 gamma-glutamyl transferase activity [GO:0103068]; leukotriene-C(4) hydrolase [GO:0002951]; peptidyltransferase activity [GO:0000048] | PF01019; | 1.10.246.130;3.60.20.40; | Gamma-glutamyltransferase family | PTM: N-glycosylated on both chains; contains sialic acid residues. It is not known if the sialic acid residues are present on N-linked or on O-linked glycans. {ECO:0000269|PubMed:6142889}.; PTM: O-glycosylated; close to the membrane anchor on the heavy chain and on the light chain. The sugar moieties are localized to t... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P19440}; Single-pass type II membrane protein {ECO:0000305|PubMed:6136502}. | CATALYTIC ACTIVITY: Reaction=an alpha-amino acid + an N-terminal (5-L-glutamyl)-[peptide] = 5-L-glutamyl amino acid + N-terminal L-alpha-aminoacyl-[peptide]; Xref=Rhea:RHEA:23904, Rhea:RHEA-COMP:9780, Rhea:RHEA-COMP:9795, ChEBI:CHEBI:77644, ChEBI:CHEBI:78597, ChEBI:CHEBI:78599, ChEBI:CHEBI:78608; EC=2.3.2.2; Evidence={... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=5.9 uM for leukotriene C(4) {ECO:0000269|PubMed:6122208}; KM=5.7 uM for glutathione {ECO:0000269|PubMed:6122208}; KM=5.8 uM for gamma-glutamyl-p-anilide {ECO:0000269|PubMed:6122208}; | PATHWAY: Sulfur metabolism; glutathione metabolism. {ECO:0000305|PubMed:6122208}.; PATHWAY: Lipid metabolism; leukotriene D4 biosynthesis. {ECO:0000305|PubMed:6122208}. | null | null | FUNCTION: Cleaves the gamma-glutamyl bond of extracellular glutathione (gamma-Glu-Cys-Gly), glutathione conjugates (such as maresin conjugate (13R)-S-glutathionyl-(14S)-hydroxy-(4Z,7Z,9E,11E,16Z,19Z)-docosahexaenoate, MCTR1) and other gamma-glutamyl compounds (such as leukotriene C4, LTC4) (By similarity) (PubMed:61222... | Rattus norvegicus (Rat) |
P07315 | CRGC_HUMAN | MGKITFYEDRAFQGRSYETTTDCPNLQPYFSRCNSIRVESGCWMLYERPNYQGQQYLLRRGEYPDYQQWMGLSDSIRSCCLIPQTVSHRLRLYEREDHKGLMMELSEDCPSIQDRFHLSEIRSLHVLEGCWVLYELPNYRGRQYLLRPQEYRRCQDWGAMDAKAGSLRRVVDLY | null | null | lens development in camera-type eye [GO:0002088]; visual perception [GO:0007601] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | structural constituent of eye lens [GO:0005212] | PF00030; | 2.60.20.10; | Beta/gamma-crystallin family | null | null | null | null | null | null | null | FUNCTION: Crystallins are the dominant structural components of the vertebrate eye lens. | Homo sapiens (Human) |
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