Entry stringlengths 6 10 | Entry Name stringlengths 5 11 | Sequence stringlengths 2 35.2k | EC number stringlengths 7 118 ⌀ | Cofactor stringlengths 38 1.77k ⌀ | Gene Ontology (biological process) stringlengths 18 11.3k ⌀ | Gene Ontology (cellular component) stringlengths 17 1.75k ⌀ | Gene Ontology (molecular function) stringlengths 24 2.09k ⌀ | Pfam stringlengths 8 232 ⌀ | Gene3D stringlengths 10 250 ⌀ | Protein families stringlengths 9 237 ⌀ | Post-translational modification stringlengths 16 8.52k ⌀ | Subcellular location [CC] stringlengths 29 6.18k ⌀ | Catalytic activity stringlengths 64 35.7k ⌀ | Kinetics stringlengths 69 11.7k ⌀ | Pathway stringlengths 27 908 ⌀ | pH dependence stringlengths 64 955 ⌀ | Temperature dependence stringlengths 70 1.16k ⌀ | Function [CC] stringlengths 17 15.3k ⌀ | Organism stringlengths 8 196 |
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P16035 | TIMP2_HUMAN | MGAAARTLRLALGLLLLATLLRPADACSCSPVHPQQAFCNADVVIRAKAVSEKEVDSGNDIYGNPIKRIQYEIKQIKMFKGPEKDIEFIYTAPSSAVCGVSLDVGGKKEYLIAGKAEGDGKMHITLCDFIVPWDTLSTTQKKSLNHRYQMGCECKITRCPMIPCYISSPDECLWMDWVTEKNINGHQAKFFACIKRSDGSCAWYRGAAPPKQEFLDIEDP | null | null | negative regulation of membrane protein ectodomain proteolysis [GO:0051045]; negative regulation of metallopeptidase activity [GO:1905049]; response to cytokine [GO:0034097]; response to hormone [GO:0009725] | collagen-containing extracellular matrix [GO:0062023]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; ficolin-1-rich granule lumen [GO:1904813]; specific granule lumen [GO:0035580]; tertiary granule lumen [GO:1904724] | metalloendopeptidase inhibitor activity [GO:0008191]; molecular function inhibitor activity [GO:0140678]; peptidase inhibitor activity [GO:0030414]; protease binding [GO:0002020]; zinc ion binding [GO:0008270] | PF00965; | 2.40.50.120;3.90.370.10; | Protease inhibitor I35 (TIMP) family | PTM: The activity of TIMP2 is dependent on the presence of disulfide bonds. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. Known to act on MMP-1, MMP-2, MMP-3, MMP-7, MMP-8, MMP-9, MMP-10, MMP-13, MMP-14, MMP-15, MMP-16 and MMP-19. {ECO:0000269|PubMed:11710594, ECO:0000269|PubMed:2554304, ECO:000... | Homo sapiens (Human) |
P16039 | NPM_CHICK | MEDSAMDMESMGPLRPQTFLFGCELKAEKEYQFKVDDEENEHQLSLRTVTLGAGAKDELHVVEAEALDYEGNPTKVVLASLKMSVQPTVSLGGFEITPPFVLRLKCGSGPVYVSGQHLVALEEEPESEDEEEDTKIGNASTKRPASGGGAKTPQKKPKLSEDDEDDDEDEDDDEDDEDDLDDDEEEIKTPMKKPAREPAGKNMQKAKQNGKDSKPSTPASKTKTPDSKKDKSLTPKTPKVPLSLEEIKAKMQASVDKGCSLPKLEPKFANYVKNCFRTEDQKVIQALWQWRQTL | null | null | cellular senescence [GO:0090398]; centrosome cycle [GO:0007098]; chromatin remodeling [GO:0006338]; DNA repair [GO:0006281]; negative regulation of cell population proliferation [GO:0008285]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of centrosome duplication [GO:0010824]; regul... | centrosome [GO:0005813]; cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; ribonucleoprotein complex [GO:1990904] | chromatin binding [GO:0003682]; histone binding [GO:0042393]; NF-kappaB binding [GO:0051059]; RNA binding [GO:0003723]; unfolded protein binding [GO:0051082] | PF16276;PF03066; | 1.10.10.2100;2.60.120.340; | Nucleoplasmin family | PTM: Phosphorylated. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus, nucleoplasm {ECO:0000250}. Nucleus, nucleolus {ECO:0000250}. Note=Generally nucleolar, but is translocated to the nucleoplasm in case of serum starvation or treatment with anticancer drugs. {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... | Gallus gallus (Chicken) |
P16043 | SLIB_MOUSE | MLLWVLFVILILTSGSHCSLPPSPPFRMQRHVDAIFTTNYRKLLSQLYARKVIQDIMNKQGERIQEQRARLSRQEDSMWTEDKQMTLESILQGFPRMKPSADA | null | null | adenohypophysis development [GO:0021984]; adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; adenylate cyclase-modulating G protein-coupled receptor signaling pathway [GO:0007188]; growth hormone secretion [GO:0030252]; hormone secretion [GO:0046879]; multicellular organism growth [... | axon terminus [GO:0043679]; extracellular space [GO:0005615]; perikaryon [GO:0043204]; terminal bouton [GO:0043195] | growth hormone-releasing hormone activity [GO:0016608]; growth hormone-releasing hormone receptor binding [GO:0031770]; neuropeptide hormone activity [GO:0005184]; peptide hormone receptor binding [GO:0051428] | PF00123; | null | Glucagon family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: GRF is released by the hypothalamus and acts on the adenohypophyse to stimulate the secretion of growth hormone. | Mus musculus (Mouse) |
P16045 | LEG1_MOUSE | MACGLVASNLNLKPGECLKVRGEVASDAKSFVLNLGKDSNNLCLHFNPRFNAHGDANTIVCNTKEDGTWGTEHREPAFPFQPGSITEVCITFDQADLTIKLPDGHEFKFPNRLNMEAINYMAADGDFKIKCVAFE | null | null | apoptotic process [GO:0006915]; cell-cell adhesion [GO:0098609]; heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0007157]; myoblast differentiation [GO:0045445]; negative regulation of cell-substrate adhesion [GO:0010812]; negative regulation of neuron projection development [GO:0010977]... | cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; cytosol [GO:0005829]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; galectin complex [GO:1990724] | carbohydrate binding [GO:0030246]; galactose binding [GO:0005534]; galactoside binding [GO:0016936]; identical protein binding [GO:0042802]; lactose binding [GO:0030395]; laminin binding [GO:0043236] | PF00337; | 2.60.120.200; | null | null | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P09382}. Cytoplasm {ECO:0000250|UniProtKB:P09382}. Secreted {ECO:0000250|UniProtKB:P09382}. Note=Can be secreted; the secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10; it results in p... | null | null | null | null | null | FUNCTION: Lectin that binds beta-galactoside and a wide array of complex carbohydrates. Plays a role in regulating apoptosis, cell proliferation and cell differentiation. Inhibits CD45 protein phosphatase activity and therefore the dephosphorylation of Lyn kinase. Strong inducer of T-cell apoptosis. {ECO:0000250|UniPro... | Mus musculus (Mouse) |
P16046 | SCAF_SCMVC | MADPVYVGGFLVRYDEPPGEAELFLPSGVVDRWLRDCRGPLPLNVNHDESATVGYVAGLQNVRAGLFCLGRVTSPKFLDIVQKASEKSELVSRGPPSESSLRPDGVLEFLSGSYSGLSLSSRRDINAADGAAGDAETACFKHVALCSVGRRRGTLAVYGRQPDWVMERFPDLTEADREALRNQLSGSGEVAAKESAESSAAAAVDPFQSDSYGLLGNSVDALYIQERLPKLRYDKRLVGVTARESYVKASVSPAEQETCDIKVEKERPKEPEQSHVPTESMSHPMSAVATPAASTVAPSQAPLALAHDGVYLPKDAFFSL... | 3.4.21.97 | null | nuclear capsid assembly [GO:0039708]; proteolysis [GO:0006508]; viral release from host cell [GO:0019076] | host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025] | identical protein binding [GO:0042802]; serine-type endopeptidase activity [GO:0004252] | PF00716; | 3.20.16.10; | Herpesviridae capsid scaffolding protein family | PTM: Capsid scaffolding protein is cleaved by assemblin after formation of the spherical procapsid. As a result, the capsid obtains its mature, icosahedral shape. Cleavages occur at two or more sites: release and tail site. {ECO:0000255|HAMAP-Rule:MF_04008}. | SUBCELLULAR LOCATION: [Capsid scaffolding protein]: Host cytoplasm {ECO:0000255|HAMAP-Rule:MF_04008}.; SUBCELLULAR LOCATION: [Assemblin]: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04008}.; SUBCELLULAR LOCATION: [Assembly protein]: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04008}. | CATALYTIC ACTIVITY: Reaction=Cleaves -Ala-|-Ser- and -Ala-|-Ala- bonds in the scaffold protein.; EC=3.4.21.97; Evidence={ECO:0000255|HAMAP-Rule:MF_04008}; | null | null | null | null | FUNCTION: [Capsid scaffolding protein]: Acts as a scaffold protein by binding major capsid protein in the cytoplasm, inducing the nuclear localization of both proteins. Multimerizes in the nucleus such as major capsid protein forms the icosahedral T=16 capsid. Autocatalytic cleavage releases the assembly protein, and s... | Simian cytomegalovirus (strain Colburn) |
P16047 | TGFB3_CHICK | MKMYAQRALVLLSLLSFATVSLALSSCTTLDLEHIKKKRVEAIRGQILSKLRLTSPPESVGPAHVPYQILALYNSTRELLEEMEEEKEESCSQENTESEYYAKEIHKFDMIQGLPEHNELGICPKGVTSNVFRFNVSSAEKNSTNLFRAEFRVLRVPNPSSKRSEQRIELFQILRPDEHIAKQRYLSGRNVQTRGSPEWLSFDVTDTVREWLLHRESNLGLEISIHCPCHTFQPNGDILENLHEVLEIKFKGIDSEDDYGRGDLGRLKKQKDLHNPHLILMMLPPHRLESPTLGGQRKKRALDTNYCFRNLEENCCVRPL... | null | null | cardiac epithelial to mesenchymal transition [GO:0060317]; cell activation [GO:0001775]; cell-cell junction organization [GO:0045216]; detection of hypoxia [GO:0070483]; embryonic digestive tract development [GO:0048566]; epithelial to mesenchymal transition involved in endocardial cushion formation [GO:0003198]; face ... | extracellular matrix [GO:0031012]; extracellular space [GO:0005615] | cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; identical protein binding [GO:0042802]; transforming growth factor beta binding [GO:0050431]; type I transforming growth factor beta receptor binding [GO:0034713]; type II transforming growth factor beta receptor binding [GO:0005114]; type III transfo... | PF00019;PF00688; | 2.60.120.970;2.10.90.10; | TGF-beta family | PTM: Transforming growth factor beta-3 proprotein: The precursor proprotein is cleaved in the Golgi apparatus to form Transforming growth factor beta-3 (TGF-beta-3) and Latency-associated peptide (LAP) chains, which remain non-covalently linked, rendering TGF-beta-3 inactive. {ECO:0000250|UniProtKB:P01137}. | SUBCELLULAR LOCATION: [Latency-associated peptide]: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P01137}.; SUBCELLULAR LOCATION: [Transforming growth factor beta-3]: Secreted {ECO:0000250|UniProtKB:P01137}. | null | null | null | null | null | FUNCTION: Transforming growth factor beta-3 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-3 (TGF-beta-3) chains, which constitute the regulatory and active subunit of TGF-beta-3, respectively. {ECO:0000250|UniProtKB:P01137, ECO:0000250|UniProtKB:P04202}.; FUNCTION: [L... | Gallus gallus (Chicken) |
P16050 | LOX15_HUMAN | MGLYRIRVSTGASLYAGSNNQVQLWLVGQHGEAALGKRLWPARGKETELKVEVPEYLGPLLFVKLRKRHLLKDDAWFCNWISVQGPGAGDEVRFPCYRWVEGNGVLSLPEGTGRTVGEDPQGLFQKHREEELEERRKLYRWGNWKDGLILNMAGAKLYDLPVDERFLEDKRVDFEVSLAKGLADLAIKDSLNVLTCWKDLDDFNRIFWCGQSKLAERVRDSWKEDALFGYQFLNGANPVVLRRSAHLPARLVFPPGMEELQAQLEKELEGGTLFEADFSLLDGIKANVILCSQQHLAAPLVMLKLQPDGKLLPMVIQLQL... | 1.13.11.-; 1.13.11.12; 1.13.11.31; 1.13.11.33 | COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250|UniProtKB:P16469, ECO:0000255|PROSITE-ProRule:PRU00726}; Note=Binds 1 Fe cation per subunit. {ECO:0000250|UniProtKB:P16469, ECO:0000255|PROSITE-ProRule:PRU00726}; | apoptotic cell clearance [GO:0043277]; arachidonic acid metabolic process [GO:0019369]; bone mineralization [GO:0030282]; cellular response to calcium ion [GO:0071277]; cellular response to interleukin-13 [GO:0035963]; fatty acid oxidation [GO:0019395]; hepoxilin biosynthetic process [GO:0051122]; inflammatory response... | cytoplasmic side of plasma membrane [GO:0009898]; cytosol [GO:0005829]; lipid droplet [GO:0005811]; membrane [GO:0016020]; plasma membrane [GO:0005886] | arachidonate 12(S)-lipoxygenase activity [GO:0004052]; arachidonate 15-lipoxygenase activity [GO:0050473]; iron ion binding [GO:0005506]; linoleate 13S-lipoxygenase activity [GO:0016165]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546] | PF00305;PF01477; | 3.10.450.60;2.60.60.20; | Lipoxygenase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:17052953, ECO:0000269|PubMed:21831839}. Cell membrane {ECO:0000269|PubMed:21831839}; Peripheral membrane protein {ECO:0000269|PubMed:17052953}. Lipid droplet {ECO:0000269|PubMed:19528634}. Note=Predominantly cytosolic; becomes enriched at membranes upon calci... | CATALYTIC ACTIVITY: Reaction=(5Z,8Z,11Z,14Z)-eicosatetraenoate + O2 = (12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate; Xref=Rhea:RHEA:10428, ChEBI:CHEBI:15379, ChEBI:CHEBI:32395, ChEBI:CHEBI:57444; EC=1.13.11.31; Evidence={ECO:0000269|PubMed:1944593}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10429; Evid... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3 uM for (9Z,12Z)-octadecadienoate {ECO:0000269|PubMed:8334154}; KM=12 uM for (5Z,8Z,11Z,14Z)-eicosatetraenoate {ECO:0000269|PubMed:8334154}; KM=3.8 uM for (9Z,12Z)-octadecadienoate {ECO:0000269|PubMed:24282679}; Vmax=10.6 umol/min/mg enzyme toward (9Z,12Z)-octadec... | PATHWAY: Lipid metabolism; hydroperoxy eicosatetraenoic acid biosynthesis. {ECO:0000269|PubMed:1944593}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7 with (9Z,12Z)-octadecadienoate as substrate. {ECO:0000269|PubMed:8334154}; | null | FUNCTION: Non-heme iron-containing dioxygenase that catalyzes the stereo-specific peroxidation of free and esterified polyunsaturated fatty acids generating a spectrum of bioactive lipid mediators (PubMed:17052953, PubMed:1944593, PubMed:24282679, PubMed:25293588, PubMed:32404334, PubMed:8334154). It inserts peroxyl gr... | Homo sapiens (Human) |
P16051 | GPA2_DICDI | MGICASSMEGEKTNTDINLSIEKERKKKHNEVKLLLLGAGESGKSTISKQMKIIHQSGYSNEERKEFKPIITRNILDNMRVLLDGMGRLGMTIDPSNSDAAVMIKELTSLQASIVTDCWGELNEDQGKKIKALWTDPGVKQAMRRANEFSTLPDSAPYFFDSIDRMTSPVYIPTDQDILHTRVMTRGVHETNFEIGKIKFRLVDVGGQRSERKKWLSCFDDVTAVVFCVALSEYDLLLYEDNSTNRMLESLRVFSDVCNSWFVNTPIILFLNKSDLFREKIKHVDLSETFPEYKGGRDYERASNYIKERFWQINKTEQKA... | null | null | actin filament polymerization [GO:0030041]; adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; adenylate cyclase-modulating G protein-coupled receptor signaling pathway [GO:0007188]; aggregation involved in sorocarp development [GO:0031152]; chemotaxis [GO:0006935]; phagocytosis [GO... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; heterotrimeric G-protein complex [GO:0005834]; plasma membrane [GO:0005886] | G protein activity [GO:0003925]; G protein-coupled receptor binding [GO:0001664]; G-protein beta-subunit binding [GO:0031681]; G-protein beta/gamma-subunit complex binding [GO:0031683]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; GTPase regulator activity [GO:0030695]; guanyl-nucleotide exchange factor adap... | PF00503; | 1.10.400.10;3.40.50.300; | G-alpha family | PTM: Ser-113 is transiently phosphorylated following stimulation with extracellular cAMP. {ECO:0000269|PubMed:8063709}. | null | null | null | null | null | null | FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. G alpha-2 is required for the early aggregation process and most of the known cAMP receptor-mediated responses (PubMed:2539262). Interacts with downstream effector gflB, a Rap... | Dictyostelium discoideum (Social amoeba) |
P16054 | KPCE_MOUSE | MVVFNGLLKIKICEAVSLKPTAWSLRHAVGPRPQTFLLDPYIALNVDDSRIGQTATKQKTNSPAWHDEFVTDVCNGRKIELAVFHDAPIGYDDFVANCTIQFEELLQNGSRHFEDWIDLEPEGKVYVIIDLSGSSGEAPKDNEERVFRERMRPRKRQGAVRRRVHQVNGHKFMATYLRQPTYCSHCRDFIWGVIGKQGYQCQVCTCVVHKRCHELIITKCAGLKKQETPDEVGSQRFSVNMPHKFGIHNYKVPTFCDHCGSLLWGLLRQGLQCKVCKMNVHRRCETNVAPNCGVDARGIAKVLADLGVTPDKITNSGQRR... | 2.7.11.13 | null | cell cycle [GO:0007049]; cell division [GO:0051301]; cell-substrate adhesion [GO:0031589]; cellular response to ethanol [GO:0071361]; cellular response to hypoxia [GO:0071456]; cellular response to platelet-derived growth factor stimulus [GO:0036120]; cellular response to prostaglandin E stimulus [GO:0071380]; chemosen... | cell periphery [GO:0071944]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; glutamatergic synapse [GO:0098978]; Golgi membrane [GO:0000139]; intermediate filament cytoskeleton [GO:0045111]; membrane [GO:0016020]; mitochondrion [GO:0005739]; neuromuscular junction [GO:0031594]; nucleus... | 14-3-3 protein binding [GO:0071889]; actin monomer binding [GO:0003785]; ATP binding [GO:0005524]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; diacylglycerol-dependent, calcium-independent serine/threonine kinase activity [GO:0004699]; enzyme activator activity [GO:0008047]; ethanol binding ... | PF00130;PF00168;PF00069;PF00433; | 3.30.60.20;2.60.40.150;1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, PKC subfamily | PTM: Phosphorylation on Thr-566 by PDPK1 triggers autophosphorylation on Ser-729 (By similarity). Phosphorylation in the hinge domain at Ser-350 by MAPK11 or MAPK14, Ser-346 by GSK3B and Ser-368 by autophosphorylation is required for interaction with YWHAB. {ECO:0000250, ECO:0000269|PubMed:17611075, ECO:0000269|PubMed:... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q02156}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q02156}. Cell membrane {ECO:0000250|UniProtKB:Q02156}. Cytoplasm, perinuclear region {ECO:0000269|PubMed:17611075}. Nucleus {ECO:0000269|PubMed:17611075}. Note=Translocated to plasma membrane in epithelial cel... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[p... | null | null | null | null | FUNCTION: Calcium-independent, phospholipid- and diacylglycerol (DAG)-dependent serine/threonine-protein kinase that plays essential roles in the regulation of multiple cellular processes linked to cytoskeletal proteins, such as cell adhesion, motility, migration and cell cycle, functions in neuron growth and ion chann... | Mus musculus (Mouse) |
P16056 | MET_MOUSE | MKAPTVLAPGILVLLLSLVQRSHGECKEALVKSEMNVNMKYQLPNFTAETPIQNVVLHGHHIYLGATNYIYVLNDKDLQKVSEFKTGPVLEHPDCLPCRDCSSKANSSGGVWKDNINMALLVDTYYDDQLISCGSVNRGTCQRHVLPPDNSADIQSEVHCMFSPEEESGQCPDCVVSALGAKVLLSEKDRFINFFVGNTINSSYPPGYSLHSISVRRLKETQDGFKFLTDQSYIDVLPEFLDSYPIKYIHAFESNHFIYFLTVQKETLDAQTFHTRIIRFCSVDSGLHSYMEMPLECILTEKRRKRSTREEVFNILQAAY... | 2.7.10.1 | null | adult behavior [GO:0030534]; brain development [GO:0007420]; cardiac muscle cell development [GO:0055013]; cardiac muscle contraction [GO:0060048]; cell migration [GO:0016477]; chemical synaptic transmission [GO:0007268]; establishment of localization in cell [GO:0051649]; excitatory postsynaptic potential [GO:0060079]... | basal plasma membrane [GO:0009925]; dendrite [GO:0030425]; excitatory synapse [GO:0060076]; extracellular space [GO:0005615]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; postsynaptic membrane [GO:0045211]; receptor complex [GO:0043235]; semaphorin receptor complex [GO:0002116]; sperm flagellum [GO:0036126] | ATP binding [GO:0005524]; beta-catenin binding [GO:0008013]; hepatocyte growth factor receptor activity [GO:0005008]; phosphatidylinositol 3-kinase binding [GO:0043548]; phospholipase binding [GO:0043274]; protein kinase activity [GO:0004672]; protein tyrosine kinase activity [GO:0004713]; protein-containing complex bi... | PF07714;PF01437;PF01403;PF01833; | 2.60.40.10;1.10.510.10;2.130.10.10; | Protein kinase superfamily, Tyr protein kinase family | PTM: Autophosphorylated in response to ligand binding on Tyr-1232 and Tyr-1233 in the kinase domain leading to further phosphorylation of Tyr-1347 and Tyr-1354 in the C-terminal multifunctional docking site. Dephosphorylated by PTPRJ at Tyr-1347 and Tyr-1363 (By similarity). Dephosphorylated by PTPN1 and PTPN2 (By simi... | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Receptor tyrosine kinase that transduces signals from the extracellular matrix into the cytoplasm by binding to hepatocyte growth factor/HGF ligand. Regulates many physiological processes including proliferation, scattering, morphogenesis and survival. Ligand binding at the cell surface induces autophosphoryl... | Mus musculus (Mouse) |
P16058 | ESR1_ONCMY | MLVRQSHTQISKPLGAPLRSRTTLESHVISPPKLSPQQPTTPNSNMYPEETRGGGGAAAFNYLDGGYDYTAPAQGPAPLYYSTTPQDAHGPPSDGSMQSLGSSPTGPLVFVSSSPQLSPQLSPFLHPPSHHGLPSQSYYLETSSTPLYRSSVVTNQLSASEEKLCIASDRQQSYSAAGSGVRVFEMANETRYCAVCSDFASGYHYGVWSCEGCKAFFKRSIQGHNDYMCPATNQCTMDRNRRKSCQACRLRKCYEVGMVKGGLRKDRGGRVLRKDKRYCGPAGDREKPYGDLEHRTAPPQDGGRNSSSSLNGGGGWRGPR... | null | null | cellular response to estrogen stimulus [GO:0071391]; intracellular estrogen receptor signaling pathway [GO:0030520]; response to cadmium ion [GO:0046686]; response to estradiol [GO:0032355]; response to testosterone [GO:0033574] | nucleus [GO:0005634] | androgen binding [GO:0005497]; DNA binding [GO:0003677]; estradiol binding [GO:1903924]; estrogen response element binding [GO:0034056]; nuclear estrogen receptor activity [GO:0030284]; nuclear estrogen receptor binding [GO:0030331]; nuclear receptor activity [GO:0004879]; protein homodimerization activity [GO:0042803]... | PF00104;PF02159;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR3 subfamily | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: The steroid hormones and their receptors are involved in the regulation of eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. | Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri) |
P16066 | ANPRA_HUMAN | MPGPRRPAGSRLRLLLLLLLPPLLLLLRGSHAGNLTVAVVLPLANTSYPWSWARVGPAVELALAQVKARPDLLPGWTVRTVLGSSENALGVCSDTAAPLAAVDLKWEHNPAVFLGPGCVYAAAPVGRFTAHWRVPLLTAGAPALGFGVKDEYALTTRAGPSYAKLGDFVAALHRRLGWERQALMLYAYRPGDEEHCFFLVEGLFMRVRDRLNITVDHLEFAEDDLSHYTRLLRTMPRKGRVIYICSSPDAFRTLMLLALEAGLCGEDYVFFHLDIFGQSLQGGQGPAPRRPWERGDGQDVSARQAFQAAKIITYKDPDNP... | 4.6.1.2 | null | blood vessel diameter maintenance [GO:0097746]; body fluid secretion [GO:0007589]; cell surface receptor signaling pathway [GO:0007166]; cGMP biosynthetic process [GO:0006182]; cGMP-mediated signaling [GO:0019934]; dopamine metabolic process [GO:0042417]; negative regulation of angiogenesis [GO:0016525]; negative regul... | ANPR-A receptor complex [GO:1990620]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]; G protein-coupled peptide receptor activity [GO:0008528]; GTP binding [GO:0005525]; guanylate cyclase activity [GO:0004383]; hormone binding [GO:0042562]; natriuretic peptide receptor activity [GO:0016941]; peptide hormone binding [GO:0017046]; peptide ... | PF01094;PF00211;PF07714; | 3.40.50.2300;3.30.70.1230;1.10.510.10; | Adenylyl cyclase class-4/guanylyl cyclase family | PTM: Phosphorylation of the protein kinase-like domain is required for full activation by ANP. {ECO:0000250}. | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | CATALYTIC ACTIVITY: Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2; Evidence={ECO:0000269|PubMed:1672777}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13666; Evidence={ECO:0000305|PubMed:1672777}; | null | null | null | null | FUNCTION: Receptor for the atrial natriuretic peptide NPPA/ANP and the brain natriuretic peptide NPPB/BNP which are potent vasoactive hormones playing a key role in cardiovascular homeostasis. Has guanylate cyclase activity upon binding of the ligand. {ECO:0000269|PubMed:1672777}. | Homo sapiens (Human) |
P16067 | ANPRB_RAT | MALPSLLLVVAALAGGVRPPGARNLTLAVVLPEHNLSYAWAWPRVGPAVALAVEALGRALPVDLRFVSSELDGACSEYLAPLRAVDLKLYHDPDLLLGPGCVYPAASVARFASHWHLPLLTAGAVASGFAAKNEHYRTLVRTGPSAPKLGEFVVTLHGHFNWTARAALLYLDARTDDRPHYFTIEGVFEALQGSNLSVQHQVYTREPGGPEQATHFIRANGRIVYICGPLEMLHEILLQAQRENLTNGDYVFFYLDVFGESLRAGPTRATGRPWQDNRTQEQAQALREAFQTVLVITYREPPNPEYQEFQNRLLIRARED... | 4.6.1.2 | null | activation of meiosis involved in egg activation [GO:0060466]; axonogenesis [GO:0007409]; axonogenesis involved in innervation [GO:0060385]; blood circulation [GO:0008015]; blood vessel development [GO:0001568]; blood vessel remodeling [GO:0001974]; bone development [GO:0060348]; bone growth [GO:0098868]; c-di-GMP sign... | cilium [GO:0005929]; cytoplasm [GO:0005737]; neuron projection [GO:0043005]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; synapse [GO:0045202] | adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]; GTP binding [GO:0005525]; guanylate cyclase activity [GO:0004383]; hormone binding [GO:0042562]; identical protein binding [GO:0042802]; natriuretic peptide receptor activity [GO:0016941]; peptide hormone binding [GO:0017046]; protein kinase activity [G... | PF01094;PF00211;PF07714; | 3.40.50.2300;3.30.70.1230;1.10.510.10; | Adenylyl cyclase class-4/guanylyl cyclase family | PTM: Phosphorylated. Phosphorylation of the protein kinase-like domain is required for full activation by CNP. {ECO:0000269|PubMed:20977274, ECO:0000269|PubMed:9624142}.; PTM: Glycosylated. {ECO:0000250|UniProtKB:P20594}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P20594}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:P20594}. | CATALYTIC ACTIVITY: Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2; Evidence={ECO:0000250|UniProtKB:P20594}; | null | null | null | null | FUNCTION: Receptor for the C-type natriuretic peptide NPPC/CNP hormone. Has guanylate cyclase activity upon binding of its ligand. May play a role in the regulation of skeletal growth. {ECO:0000250|UniProtKB:P20594}. | Rattus norvegicus (Rat) |
P16068 | GCYB1_BOVIN | MYGFVNHALELLVIRNYGPEVWEDIKKEAQLDEEGQFLVRIIYDDSKTYDLVAAASKVLNLNAGEILQMFGKMFFVFCQESGYDTILRVLGSNVREFLQNLDALHDHLATIYPGMRAPSFRCTDADKGKGLILHYYSEREGLQDIVIGIIKTVAQQIHGTEIDMKVIQQRNEECDHTQFLIEEKESKEEDFYEDLDRFEENGTQESRISPYTFCKAFPFHIIFDRDLVVTQCGNAIYRVLPQLQPGNCSLLSVFSLVRPHIDISFHGILSHINTVFVLRSKEGLLDVEKSECEDELTGTEISCLRLKGQMIYLPEADSIL... | 4.6.1.2 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000269|PubMed:7908439, ECO:0000269|PubMed:9521770}; Note=Binds 1 or 2 heme groups per heterodimer. Heme is required for responding to nitric oxide, but not for catalytic activity. {ECO:0000269|PubMed:7908439, ECO:0000269|PubMed:9521770}; | cellular response to nitric oxide [GO:0071732]; cGMP biosynthetic process [GO:0006182]; cGMP-mediated signaling [GO:0019934]; nitric oxide-cGMP-mediated signaling pathway [GO:0038060]; response to oxygen levels [GO:0070482] | cytoplasm [GO:0005737]; guanylate cyclase complex, soluble [GO:0008074] | GTP binding [GO:0005525]; guanylate cyclase activity [GO:0004383]; heme binding [GO:0020037]; metal ion binding [GO:0046872] | PF00211;PF07700;PF07701; | 6.10.250.780;3.90.1520.10;3.30.450.260;3.30.70.1230; | Adenylyl cyclase class-4/guanylyl cyclase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:7908439}. | CATALYTIC ACTIVITY: Reaction=GTP = 3',5'-cyclic GMP + diphosphate; Xref=Rhea:RHEA:13665, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:57746; EC=4.6.1.2; Evidence={ECO:0000269|PubMed:7908439}; | null | null | null | null | FUNCTION: Mediates responses to nitric oxide (NO) by catalyzing the biosynthesis of the signaling molecule cGMP. {ECO:0000269|PubMed:7908439}. | Bos taurus (Bovine) |
P16070 | CD44_HUMAN | MDKFWWHAAWGLCLVPLSLAQIDLNITCRFAGVFHVEKNGRYSISRTEAADLCKAFNSTLPTMAQMEKALSIGFETCRYGFIEGHVVIPRIHPNSICAANNTGVYILTSNTSQYDTYCFNASAPPEEDCTSVTDLPNAFDGPITITIVNRDGTRYVQKGEYRTNPEDIYPSNPTDDDVSSGSSSERSSTSGGYIFYTFSTVHPIPDEDSPWITDSTDRIPATTLMSTSATATETATKRQETWDWFSWLFLPSESKNHLHTTTQMAGTSSNTISAGWEPNEENEDERDRHLSFSGSGIDDDEDFISSTISTTPRAFDHTKQ... | null | null | cartilage development [GO:0051216]; cell adhesion [GO:0007155]; cell migration [GO:0016477]; cell-cell adhesion [GO:0098609]; cell-matrix adhesion [GO:0007160]; cellular response to fibroblast growth factor stimulus [GO:0044344]; hyaluronan catabolic process [GO:0030214]; inflammatory response [GO:0006954]; monocyte ag... | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; cell projection [GO:0042995]; cell surface [GO:0009986]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; Golgi apparatus [GO:0005794]; lamellipodium membrane [GO:0031258]; macrophage migration inhibitor... | collagen binding [GO:0005518]; cytokine receptor activity [GO:0004896]; hyaluronic acid binding [GO:0005540]; transmembrane signaling receptor activity [GO:0004888] | PF00193; | 3.10.100.10; | null | PTM: Proteolytically cleaved in the extracellular matrix by specific proteinases (possibly MMPs) in several cell lines and tumors. {ECO:0000269|PubMed:12883358}.; PTM: N-glycosylated. {ECO:0000269|PubMed:12883358, ECO:0000269|PubMed:16335952, ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:22171320}.; PTM: O-glycosylat... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22726066, ECO:0000269|PubMed:23589287}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, microvillus {ECO:0000250|UniProtKB:P15379}. Secreted {ECO:0000269|PubMed:25326458, ECO:0000269|PubMed:36213313, ECO:0000269|PubMed:37453717}. Note=Colocaliz... | null | null | null | null | null | FUNCTION: Cell-surface receptor that plays a role in cell-cell interactions, cell adhesion and migration, helping them to sense and respond to changes in the tissue microenvironment (PubMed:16541107, PubMed:19703720, PubMed:22726066). Participates thereby in a wide variety of cellular functions including the activation... | Homo sapiens (Human) |
P16075 | MYOD1_CHICK | MDLLGPMEMTEGSLCSFTAADDFYDDPCFNTSDMHFFEDLDPRLVHVGGLLKPEEHPHTRAPPREPTEEEHVRAPSGHHQAGRCLLWACKACKRKTTNADRRKAATMRERRRLSKVNEAFETLKRCTSTNPNQRLPKVEILRNAIRYIESLQALLREQEDAYYPVLEHYSGESDASSPRSNCSDGMMEYSGPPCSSRRRNSYDSSYYTESPNDPKHGKSSVVSSLDCLSSIVERISTDNSTCPILPPAEAVAEGSPCSPQEGGNLSDSGAQIPSPTNCTPLPQESSSSSSSNPIYQVL | null | null | cellular response to estradiol stimulus [GO:0071392]; muscle cell fate commitment [GO:0042693]; muscle organ development [GO:0007517]; positive regulation of myoblast differentiation [GO:0045663]; positive regulation of skeletal muscle fiber development [GO:0048743]; positive regulation of snRNA transcription by RNA po... | nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | bHLH transcription factor binding [GO:0043425]; DNA-binding transcription activator activity [GO:0001216]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; E-box binding [GO:0070888]; identical protein binding [GO:0042802]; promoter-specific chromatin binding [GO:1990841]; protein dim... | PF01586;PF00010;PF12232; | 4.10.280.10; | null | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Acts as a transcriptional activator that promotes transcription of muscle-specific target genes and plays a role in muscle differentiation. Induces fibroblasts to differentiate into myoblasts. Interacts with and is inhibited by the twist protein. This interaction probably involves the basic domains of both pr... | Gallus gallus (Chicken) |
P16083 | NQO2_HUMAN | MAGKKVLIVYAHQEPKSFNGSLKNVAVDELSRQGCTVTVSDLYAMNLEPRATDKDITGTLSNPEVFNYGVETHEAYKQRSLASDITDEQKKVREADLVIFQFPLYWFSVPAILKGWMDRVLCQGFAFDIPGFYDSGLLQGKLALLSVTTGGTAEMYTKTGVNGDSRYFLWPLQHGTLHFCGFKVLAPQISFAPEIASEEERKGMVAAWSQRLQTIWKEEPIPCTAHWHFGQ | 1.10.5.1 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Note=Binds 1 zinc ion per subunit.; COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; | quinone catabolic process [GO:1901662] | cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654] | chloride ion binding [GO:0031404]; dihydronicotinamide riboside quinone reductase activity [GO:0001512]; electron transfer activity [GO:0009055]; FAD binding [GO:0071949]; melatonin binding [GO:1904408]; NAD(P)H dehydrogenase (quinone) activity [GO:0003955]; oxidoreductase activity [GO:0016491]; oxidoreductase activity... | PF02525; | 3.40.50.360; | NAD(P)H dehydrogenase (quinone) family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=1-(beta-D-ribofuranosyl)-1,4-dihydronicotinamide + a quinone + H(+) = a quinol + beta-nicotinamide D-riboside; Xref=Rhea:RHEA:12364, ChEBI:CHEBI:15378, ChEBI:CHEBI:15927, ChEBI:CHEBI:24646, ChEBI:CHEBI:55458, ChEBI:CHEBI:132124; EC=1.10.5.1; Evidence={ECO:0000269|PubMed:18579530}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=28 uM for NRH {ECO:0000269|PubMed:15078100, ECO:0000269|PubMed:9367528}; KM=11.6 uM for menadione {ECO:0000269|PubMed:15078100, ECO:0000269|PubMed:9367528}; KM=252 uM for NADH {ECO:0000269|PubMed:15078100, ECO:0000269|PubMed:9367528}; | null | null | null | FUNCTION: The enzyme apparently serves as a quinone reductase in connection with conjugation reactions of hydroquinones involved in detoxification pathways as well as in biosynthetic processes such as the vitamin K-dependent gamma-carboxylation of glutamate residues in prothrombin synthesis. {ECO:0000269|PubMed:1825472... | Homo sapiens (Human) |
P16086 | SPTN1_RAT | MDPSGVKVLETAEDIQERRQQVLDRYHRFKELSTLRRQKLEDSYRFQFFQRDAEELEKWIQEKLQVASDENYKDPTNLQGKLQKHQAFEAEVQANSGAIVKLDETGNLMISEGHFASETIRTRLMELHRQWELLLEKMREKGIKLLQAQKLVQYLRECEDVMDWINDKEAIVTSEELGQDLEHVEVLQKKFEEFQTDLAAHEERVNEVNQFAAKLIQEQHPEEELIKTKQEEVNAAWQRLKGLALQRQGKLFGAAEVQRFNRDVDETIGWIKEKEQLMASDDFGRDLASVQALLRKHEGLERDLAALEDKVKALCAEADR... | null | null | actin cytoskeleton organization [GO:0030036]; actin filament capping [GO:0051693] | cell junction [GO:0030054]; cell projection [GO:0042995]; cortical actin cytoskeleton [GO:0030864]; cortical cytoskeleton [GO:0030863]; cuticular plate [GO:0032437]; cytosol [GO:0005829]; fascia adherens [GO:0005916]; glutamatergic synapse [GO:0098978]; lateral plasma membrane [GO:0016328]; membrane [GO:0016020]; paran... | actin filament binding [GO:0051015]; calcium ion binding [GO:0005509]; calmodulin binding [GO:0005516]; protein-containing complex binding [GO:0044877]; spectrin binding [GO:0030507] | PF13499;PF08726;PF00018;PF00435; | 1.20.5.170;1.20.58.60;1.10.238.10;2.30.30.40; | Spectrin family | PTM: Phosphorylation of Tyr-1176 decreases sensitivity to cleavage by calpain in vitro. {ECO:0000269|PubMed:11971983}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000269|PubMed:15994232}. Note=Expressed along the cell membrane in podocytes and presumptive tubule cells during glomerulogenesis and is expressed along lateral cell margins in tubule cells. | null | null | null | null | null | FUNCTION: Fodrin, which seems to be involved in secretion, interacts with calmodulin in a calcium-dependent manner and is thus candidate for the calcium-dependent movement of the cytoskeleton at the membrane. {ECO:0000250}. | Rattus norvegicus (Rat) |
P16088 | POL_FIVPE | KEFGKLEGGASCSPSESNAASSNAICTSNGGETIGFVNYNKVGTTTTLEKRPEILIFVNGYPIKFLLDTGADITILNRRDFQVKNSIENGRQNMIGVGGGKRGTNYINVHLEIRDENYKTQCIFGNVCVLEDNSLIQPLLGRDNMIKFNIRLVMAQISDKIPVVKVKMKDPNKGPQIKQWPLTNEKIEALTEIVERLEKEGKVKRADSNNPWNTPVFAIKKKSGKWRMLIDFRELNKLTEKGAEVQLGLPHPAGLQIKKQVTVLDIGDAYFTIPLDPDYAPYTAFTLPRKNNAGPGRRFVWCSLPQGWILSPLIYQSTLD... | 2.7.7.-; 2.7.7.49; 3.1.-.-; 3.1.13.2; 3.1.26.13; 3.4.23.-; 3.6.1.23 | null | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; dUMP biosynthetic process [GO:0006226]; dUTP catabolic process [GO:0046081]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; viral genome integration into host DNA [GO:0044826] | null | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; dUTP diphosphatase activity [GO:0004170]; exoribonuclease H activity [GO:0004533]; magnesium ion binding [GO:0000287]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity [GO:0004523]; zinc ion binding [GO:0... | PF00692;PF00552;PF00075;PF00665;PF00077;PF00078;PF06815;PF06817; | 1.10.10.200;2.70.40.10;3.30.70.270;2.40.70.10;3.10.10.10;2.30.30.10;3.30.420.10; | Retroviral Pol polyprotein family | PTM: Cleavage sites that yield the mature proteins remain to be determined. | null | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end... | null | null | null | null | FUNCTION: During replicative cycle of retroviruses, the reverse-transcribed viral DNA is integrated into the host chromosome by the viral integrase enzyme. RNase H activity is associated with the reverse transcriptase. | Feline immunodeficiency virus (isolate Petaluma) (FIV) |
P16092 | FGFR1_MOUSE | MWGWKCLLFWAVLVTATLCTARPAPTLPEQAQPWGVPVEVESLLVHPGDLLQLRCRLRDDVQSINWLRDGVQLVESNRTRITGEEVEVRDSIPADSGLYACVTSSPSGSDTTYFSVNVSDALPSSEDDDDDDDSSSEEKETDNTKPNRRPVAPYWTSPEKMEKKLHAVPAAKTVKFKCPSSGTPNPTLRWLKNGKEFKPDHRIGGYKVRYATWSIIMDSVVPSDKGNYTCIVENEYGSINHTYQLDVVERSPHRPILQAGLPANKTVALGSNVEFMCKVYSDPQPHIQWLKHIEVNGSKIGPDNLPYVQILKTAGVNTTD... | 2.7.10.1 | null | angiogenesis [GO:0001525]; auditory receptor cell development [GO:0060117]; blood vessel morphogenesis [GO:0048514]; brain development [GO:0007420]; branching involved in salivary gland morphogenesis [GO:0060445]; calcium ion homeostasis [GO:0055074]; cardiac muscle cell proliferation [GO:0060038]; cell maturation [GO:... | cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; cell adhesion molecule binding [GO:0050839]; fibroblast growth factor binding [GO:0017134]; fibroblast growth factor receptor activity [GO:0005007]; heparin binding [GO:0008201]; protein homodimerization activity [GO:0042803]; protein-containing complex binding [GO:0044877]; receptor-receptor ... | PF07679;PF00047;PF07714; | 2.60.40.10;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, Fibroblast growth factor receptor subfamily | PTM: Autophosphorylated. Binding of FGF family members together with heparan sulfate proteoglycan or heparin promotes receptor dimerization and autophosphorylation on tyrosine residues. Autophosphorylation occurs in trans between the two FGFR molecules present in the dimer and proceeds in a highly ordered manner. Initi... | SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Nucleus. Cytoplasm, cytosol. Cytoplasmic vesicle. Note=After ligand binding, both receptor and ligand are rapidly internalized. Can translocate to the nucleus after internalization, or by translocation from the endoplasmic reticulum or Golgi appa... | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor for fibroblast growth factors and plays an essential role in the regulation of embryonic development, cell proliferation, differentiation and migration. Required for normal mesoderm patterning and correct axial organization during embryonic developm... | Mus musculus (Mouse) |
P16100 | IDH_AZOVI | MSTPKIIYTLTDEAPALATYSLLPIIKAFTGSSGIAVETRDISLAGRLIATFPEYLTDTQKISDDLAELGKLATTPDANIIKLPNISASVPQLKAAIKELQQQGYKLPDYPEEPKTDTEKDVKARYDKIKGSAVNPVLREGNSDRRAPLSVKNYARKHPHKMGAWSADSKSHVAHMDNGDFYGSEKAALIGAPGSVKIELIAKDGSSTVLKAKTSVQAGEIIDSSVMSKNALRNFIAAEIEDAKKQGVLLSVHLKATMMKVSDPIMFGQIVSEFYKDALTKHAEVLKQIGFDVNNGIGDLYARIKTLPEAKQKEIEADIQ... | 1.1.1.42 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit.; | glyoxylate cycle [GO:0006097]; tricarboxylic acid cycle [GO:0006099] | cytoplasm [GO:0005737] | isocitrate dehydrogenase (NADP+) activity [GO:0004450]; metal ion binding [GO:0046872] | PF03971; | 3.40.718.10; | Monomeric-type IDH family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=D-threo-isocitrate + NADP(+) = 2-oxoglutarate + CO2 + NADPH; Xref=Rhea:RHEA:19629, ChEBI:CHEBI:15562, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.42; | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is above 40 degrees Celsius.; | null | Azotobacter vinelandii |
P16104 | H2AX_HUMAN | MSGRGKTGGKARAKAKSRSSRAGLQFPVGRVHRLLRKGHYAERVGAGAPVYLAAVLEYLTAEILELAGNAARDNKKTRIIPRHLQLAIRNDEELNKLLGGVTIAQGGVLPNIQAVLLPKKTSATVGPKAPSGGKKATQASQEY | null | null | cellular response to gamma radiation [GO:0071480]; cellular senescence [GO:0090398]; cerebral cortex development [GO:0021987]; DNA damage checkpoint signaling [GO:0000077]; DNA damage response [GO:0006974]; double-strand break repair [GO:0006302]; double-strand break repair via homologous recombination [GO:0000724]; he... | centrosome [GO:0005813]; condensed nuclear chromosome [GO:0000794]; extracellular exosome [GO:0070062]; male germ cell nucleus [GO:0001673]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleosome [GO:0000786]; nucleus [GO:0005634]; replication fork [GO:0005657]; site of DNA damage [GO:0090734]; site of double... | damaged DNA binding [GO:0003684]; DNA binding [GO:0003677]; enzyme binding [GO:0019899]; histone binding [GO:0042393]; nucleosomal DNA binding [GO:0031492]; protein heterodimerization activity [GO:0046982]; structural constituent of chromatin [GO:0030527] | PF00125;PF16211; | 1.10.20.10; | Histone H2A family | PTM: Phosphorylated by VRK1 (PubMed:31527692). Phosphorylated on Ser-140 (to form gamma-H2AX or H2AX139ph) in response to DNA double strand breaks (DSBs) generated by exogenous genotoxic agents and by stalled replication forks, and may also occur during meiotic recombination events and immunoglobulin class switching in... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12419185, ECO:0000269|PubMed:12660252, ECO:0000269|PubMed:12697768, ECO:0000269|PubMed:15613478, ECO:0000269|PubMed:24429368}. Chromosome {ECO:0000269|PubMed:10959836, ECO:0000269|PubMed:11673449, ECO:0000269|PubMed:12607005, ECO:0000269|PubMed:12660252, ECO:0000269|Pub... | null | null | null | null | null | FUNCTION: Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication... | Homo sapiens (Human) |
P16109 | LYAM3_HUMAN | MANCQIAILYQRFQRVVFGISQLLCFSALISELTNQKEVAAWTYHYSTKAYSWNISRKYCQNRYTDLVAIQNKNEIDYLNKVLPYYSSYYWIGIRKNNKTWTWVGTKKALTNEAENWADNEPNNKRNNEDCVEIYIKSPSAPGKWNDEHCLKKKHALCYTASCQDMSCSKQGECLETIGNYTCSCYPGFYGPECEYVRECGELELPQHVLMNCSHPLGNFSFNSQCSFHCTDGYQVNGPSKLECLASGIWTNKPPQCLAAQCPPLKIPERGNMTCLHSAKAFQHQSSCSFSCEEGFALVGPEVVQCTASGVWTAPAPVCK... | null | null | calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0016339]; calcium-mediated signaling using intracellular calcium source [GO:0035584]; cell adhesion [GO:0007155]; cell-cell adhesion [GO:0098609]; defense response to Gram-negative bacterium [GO:0050829]; heterophilic cell-cell adhesio... | external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; platelet alpha granule membrane [GO:0031092]; platelet dense granule membrane [GO:0031088] | calcium ion binding [GO:0005509]; calcium-dependent protein binding [GO:0048306]; fucose binding [GO:0042806]; glycosphingolipid binding [GO:0043208]; heparin binding [GO:0008201]; integrin binding [GO:0005178]; lipopolysaccharide binding [GO:0001530]; oligosaccharide binding [GO:0070492]; sialic acid binding [GO:00336... | PF00059;PF00084; | 2.10.70.10;2.10.25.10;3.10.100.10; | Selectin/LECAM family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28011641}; Single-pass type I membrane protein {ECO:0000305|PubMed:28011641}. | null | null | null | null | null | FUNCTION: Ca(2+)-dependent receptor for myeloid cells that binds to carbohydrates on neutrophils and monocytes. Mediates the interaction of activated endothelial cells or platelets with leukocytes. The ligand recognized is sialyl-Lewis X. Mediates rapid rolling of leukocyte rolling over vascular surfaces during the ini... | Homo sapiens (Human) |
P16110 | LEG3_MOUSE | MADSFSLNDALAGSGNPNPQGYPGAWGNQPGAGGYPGAAYPGAYPGQAPPGAYPGQAPPGAYPGQAPPSAYPGPTAPGAYPGPTAPGAYPGQPAPGAFPGQPGAPGAYPQCSGGYPAAGPYGVPAGPLTVPYDLPLPGGVMPRMLITIMGTVKPNANRIVLDFRRGNDVAFHFNPRFNENNRRVIVCNTKQDNNWGKEERQSAFPFESGKPFKIQVLVEADHFKVAVNDAHLLQYNHRMKNLREISQLGISGDITLTSANHAMI | null | null | cell differentiation [GO:0030154]; eosinophil chemotaxis [GO:0048245]; extracellular matrix organization [GO:0030198]; innate immune response [GO:0045087]; macrophage chemotaxis [GO:0048246]; monocyte chemotaxis [GO:0002548]; mRNA processing [GO:0006397]; negative regulation of apoptotic process [GO:0043066]; negative ... | cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; cornified envelope [GO:0001533]; cytoplasm [GO:0005737]; external side of plasma membrane [GO:0009897]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; glial cell projection [GO:0097... | advanced glycation end-product receptor activity [GO:0050785]; disaccharide binding [GO:0048030]; Fc-gamma receptor I complex binding [GO:0034988]; IgE binding [GO:0019863]; laminin binding [GO:0043236]; monosaccharide binding [GO:0048029] | PF00337; | 2.60.120.200; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P17931}. Nucleus {ECO:0000250|UniProtKB:P17931}. Secreted {ECO:0000250|UniProtKB:P17931}. Note=Secreted by a non-classical secretory pathway and associates with the cell surface. Can be secreted; the secretion is dependent on protein unfolding and facilitated by th... | null | null | null | null | null | FUNCTION: Galactose-specific lectin which binds IgE. May mediate with the alpha-3, beta-1 integrin the stimulation by CSPG4 of endothelial cells migration. Together with DMBT1, required for terminal differentiation of columnar epithelial cells during early embryogenesis. In the nucleus: acts as a pre-mRNA splicing fact... | Mus musculus (Mouse) |
P16112 | PGCA_HUMAN | MTTLLWVFVTLRVITAAVTVETSDHDNSLSVSIPQPSPLRVLLGTSLTIPCYFIDPMHPVTTAPSTAPLAPRIKWSRVSKEKEVVLLVATEGRVRVNSAYQDKVSLPNYPAIPSDATLEVQSLRSNDSGVYRCEVMHGIEDSEATLEVVVKGIVFHYRAISTRYTLDFDRAQRACLQNSAIIATPEQLQAAYEDGFHQCDAGWLADQTVRYPIHTPREGCYGDKDEFPGVRTYGIRDTNETYDVYCFAEEMEGEVFYATSPEKFTFQEAANECRRLGARLATTGQLYLAWQAGMDMCSAGWLADRSVRYPISKARPNCGG... | null | null | cell adhesion [GO:0007155]; central nervous system development [GO:0007417]; glial cell differentiation [GO:0010001]; positive regulation of neuroblast proliferation [GO:0002052]; proteolysis [GO:0006508]; skeletal system development [GO:0001501] | collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi lumen [GO:0005796]; lysosomal lumen [GO:0043202]; perineuronal net [GO:0072534]; synapse [GO:0045202] | carbohydrate binding [GO:0030246]; extracellular matrix structural constituent [GO:0005201]; hyaluronic acid binding [GO:0005540]; metal ion binding [GO:0046872] | PF00059;PF00084;PF07686;PF00193; | 2.10.70.10;2.60.40.10;2.10.25.10;3.10.100.10; | Aggrecan/versican proteoglycan family | PTM: Contains mostly chondroitin sulfate, but also keratan sulfate chains, N-linked and O-linked oligosaccharides. The release of aggrecan fragments from articular cartilage into the synovial fluid at all stages of human osteoarthritis is the result of cleavage by aggrecanase. {ECO:0000269|PubMed:1569188, ECO:0000269|P... | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000250}. | null | null | null | null | null | FUNCTION: This proteoglycan is a major component of extracellular matrix of cartilagenous tissues. A major function of this protein is to resist compression in cartilage. It binds avidly to hyaluronic acid via an N-terminal globular region. | Homo sapiens (Human) |
P16115 | LDH_THEMA | MKIGIVGLGRVGSSTAFALLMKGFAREMVLIDVDKKRAEGDALDLIHGTPFTRRANIYAGDYADLKGSDVVIVAAGVPQKPGETRLQLLGRNARVMKEIARNVSKYAPDSIVIVVTNPVDVLTYFFLKESGMDPRKVFGSGTVLDTARLRTLIAQHCGFSPRSVHVYVIGEHGDSEVPVWSGAMIGGIPLQNMCQICQKCDSKILENFAEKTKRAAYEIIERKGATHYAIALAVADIVESIFFDEKRVLTLSVYLEDYLGVKDLCISVPVTLGKHGVERILELNLNEEELEAFRKSASILKNAINEITAEENKHQNTSG | 1.1.1.27 | null | glycolytic process [GO:0006096]; lactate metabolic process [GO:0006089]; pyruvate metabolic process [GO:0006090] | cytoplasm [GO:0005737] | L-lactate dehydrogenase activity [GO:0004459] | PF02866;PF00056; | 3.90.110.10;3.40.50.720; | LDH/MDH superfamily, LDH family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00488}. | 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:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:2318202}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=30 uM for NADH (at 55 degrees Celsius and in the absence of fructose 1,6-bisphosphate (FBP)) {ECO:0000269|PubMed:2318202}; KM=60 uM for pyruvate (at 55 degrees Celsius and in the presence of fructose 1,6-bisphosphate (FBP)) {ECO:0000269|PubMed:2318202}; KM=90 uM fo... | PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00488}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. {ECO:0000269|PubMed:2318202}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Long-term stability up to 80 degrees Celsius. Fructose 1,6-bisphosphate (FBP) increases the thermal stability at 90 degrees Celsius (pH 6.0). {ECO:0000269|PubMed:2318202}; | FUNCTION: Catalyzes the conversion of lactate to pyruvate. It is stereospecific for L(+)-lactate. {ECO:0000255|HAMAP-Rule:MF_00488, ECO:0000269|PubMed:2318202}. | Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8) |
P16116 | ALDR_BOVIN | AHNIVLYTGAKMPILGLGTWKSPPGKVTEAVKVAIDLGYRHIDCAHVYQNENEVGLALQAKLQEKVVKREDLFIVSKLWCTYHDKDLVKGACQKTLSDLKLDYLDLYLIHWPTGFKPGKDFFPLDEDGNVIPSEKDFVDTWTAMEELVDEGLVKAIGVSNFNHLQVEKILNKPGLKYKPAVNQIECHPYLTQEKLIQYCNSKGIVVTAYSPLGSPDRPWAKPEDPSILEDPRIKAIADKYNKTTAQVLIRFPIQRNLIVIPKSVTPERIAENFQVFDFELDKEDMNTLLSYNRDWRACALVSCASHRDYPFHEEF | 1.1.1.21; 1.1.1.300; 1.1.1.372; 1.1.1.54 | null | retinoid metabolic process [GO:0001523] | cytosol [GO:0005829] | alditol:NADP+ 1-oxidoreductase activity [GO:0004032]; allyl-alcohol dehydrogenase activity [GO:0047655]; glycerol dehydrogenase [NADP+] activity [GO:0047956]; NADP-retinol dehydrogenase activity [GO:0052650]; prostaglandin H2 endoperoxidase reductase activity [GO:0036130]; retinal dehydrogenase activity [GO:0001758] | PF00248; | 3.20.20.100; | Aldo/keto reductase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=an alditol + NADP(+) = an aldose + H(+) + NADPH; Xref=Rhea:RHEA:12789, Rhea:RHEA-COMP:9554, Rhea:RHEA-COMP:9555, ChEBI:CHEBI:15378, ChEBI:CHEBI:15693, ChEBI:CHEBI:17522, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.21; Evidence={ECO:0000250|UniProtKB:P15121}; CATALYTIC ACTIVITY: Reaction=... | null | null | null | null | FUNCTION: Catalyzes the NADPH-dependent reduction of a wide variety of carbonyl-containing compounds to their corresponding alcohols. Displays enzymatic activity towards endogenous metabolites such as aromatic and aliphatic aldehydes, ketones, monosacharides, bile acids and xenobiotics substrates. Key enzyme in the pol... | Bos taurus (Bovine) |
P16118 | F261_HUMAN | MSPEMGELTQTRLQKIWIPHSSGSSRLQRRRGSSIPQFTNSPTMVIMVGLPARGKTYISTKLTRYLNWIGTPTKVFNLGQYRREAVSYKNYEFFLPDNMEALQIRKQCALAALKDVHNYLSHEEGHVAVFDATNTTRERRSLILQFAKEHGYKVFFIESICNDPGIIAENIRQVKLGSPDYIDCDREKVLEDFLKRIECYEVNYQPLDEELDSHLSYIKIFDVGTRYMVNRVQDHIQSRTVYYLMNIHVTPRSIYLCRHGESELNIRGRIGGDSGLSVRGKQYAYALANFIQSQGISSLKVWTSHMKRTIQTAEALGVPY... | 2.7.1.105; 3.1.3.46 | null | animal organ regeneration [GO:0031100]; fructose 2,6-bisphosphate metabolic process [GO:0006003]; fructose metabolic process [GO:0006000]; gluconeogenesis [GO:0006094]; glycolytic process [GO:0006096]; negative regulation of glycolytic process through fructose-6-phosphate [GO:1904539]; response to cAMP [GO:0051591]; re... | 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase complex [GO:0043540]; cytosol [GO:0005829] | 6-phosphofructo-2-kinase activity [GO:0003873]; ATP binding [GO:0005524]; fructose-2,6-bisphosphate 2-phosphatase activity [GO:0004331]; fructose-6-phosphate binding [GO:0070095]; identical protein binding [GO:0042802]; kinase binding [GO:0019900] | PF01591;PF00300; | 3.40.50.300;3.40.50.1240; | Phosphoglycerate mutase family | null | null | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 2,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate; Xref=Rhea:RHEA:17289, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634, ChEBI:CHEBI:58579; EC=3.1.3.46; Evidence={ECO:0000269|PubMed:2837207}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17290;... | null | null | null | null | FUNCTION: Synthesis and degradation of fructose 2,6-bisphosphate. {ECO:0000269|PubMed:2837207}. | Homo sapiens (Human) |
P16125 | LDHB_MOUSE | MATLKEKLIASVADDEAAVPNNKITVVGVGQVGMACAISILGKSLADELALVDVLEDKLKGEMMDLQHGSLFLQTPKIVADKDYSVTANSKIVVVTAGVRQQEGESRLNLVQRNVNVFKFIIPQIVKYSPDCTIIVVSNPVDILTYVTWKLSGLPKHRVIGSGCNLDSARFRYLMAEKLGIHPSSCHGWILGEHGDSSVAVWSGVNVAGVSLQELNPEMGTDNDSENWKEVHKMVVDSAYEVIKLKGYTNWAIGLSVADLIESMLKNLSRIHPVSTMVKGMYGIENEVFLSLPCILNARGLTSVINQKLKDDEVAQLRKS... | 1.1.1.27 | null | lactate biosynthetic process from pyruvate [GO:0019244]; lactate metabolic process [GO:0006089]; NAD metabolic process [GO:0019674]; pyruvate metabolic process [GO:0006090] | cytosol [GO:0005829]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739]; myelin sheath [GO:0043209] | identical protein binding [GO:0042802]; kinase binding [GO:0019900]; L-lactate dehydrogenase activity [GO:0004459]; lactate dehydrogenase activity [GO:0004457]; 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:0000250|UniProtKB:P07195}; 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:0000250|UniProtKB:P07195}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23445; Evidence={ECO... | null | PATHWAY: Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1. {ECO:0000250|UniProtKB:P07195}. | null | null | FUNCTION: Interconverts simultaneously and stereospecifically pyruvate and lactate with concomitant interconversion of NADH and NAD(+). {ECO:0000250|UniProtKB:P07195}. | Mus musculus (Mouse) |
P16127 | CHLI1_ARATH | MASLLGTSSSAIWASPSLSSPSSKPSSSPICFRPGKLFGSKLNAGIQIRPKKNRSRYHVSVMNVATEINSTEQVVGKFDSKKSARPVYPFAAIVGQDEMKLCLLLNVIDPKIGGVMIMGDRGTGKSTTVRSLVDLLPEINVVAGDPYNSDPIDPEFMGVEVRERVEKGEQVPVIATKINMVDLPLGATEDRVCGTIDIEKALTEGVKAFEPGLLAKANRGILYVDEVNLLDDHLVDVLLDSAASGWNTVEREGISISHPARFILIGSGNPEEGELRPQLLDRFGMHAQVGTVRDADLRVKIVEERARFDSNPKDFRDTYK... | 6.6.1.1 | null | chlorophyll biosynthetic process [GO:0015995]; photosynthesis [GO:0015979] | chloroplast [GO:0009507]; chloroplast stroma [GO:0009570]; cytosol [GO:0005829]; magnesium chelatase complex [GO:0010007]; plant-type cell wall [GO:0009505] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; magnesium chelatase activity [GO:0016851] | PF17863;PF01078; | 1.10.8.80;3.40.50.300; | Mg-chelatase subunits D/I family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + Mg(2+) + protoporphyrin IX = ADP + 3 H(+) + Mg-protoporphyrin IX + phosphate; Xref=Rhea:RHEA:13961, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:18420, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57306, ChEBI:CHEBI:60492, ChEBI:CHEBI:456216; EC=6.6.1.1; Evidence={ECO:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=460 uM for ATP {ECO:0000269|PubMed:17472958}; Vmax=55 nmol/min/mg enzyme toward ATP {ECO:0000269|PubMed:17472958}; | PATHWAY: Porphyrin-containing compound metabolism; chlorophyll biosynthesis. | null | null | FUNCTION: Involved in chlorophyll biosynthesis. Catalyzes the insertion of magnesium ion into protoporphyrin IX to yield Mg-protoporphyrin IX. The magnesium-chelatase is a complex of three subunits, CHLI, CHLD and CHLH. The reaction takes place in two steps, with an ATP-dependent activation followed by an ATP-dependent... | Arabidopsis thaliana (Mouse-ear cress) |
P16140 | VATB_YEAST | MVLSDKELFAINKKAVEQGFNVKPRLNYNTVSGVNGPLVILEKVKFPRYNEIVNLTLPDGTVRQGQVLEIRGDRAIVQVFEGTSGIDVKKTTVEFTGESLRIPVSEDMLGRIFDGSGRPIDNGPKVFAEDYLDINGSPINPYARIYPEEMISTGVSAIDTMNSIARGQKIPIFSASGLPHNEIAAQICRQAGLVRPTKDVHDGHEENFSIVFAAMGVNLETARFFKQDFEENGSLERTSLFLNLANDPTIERIITPRLALTTAEYLAYQTERHVLTILTDMSSYADALREVSAAREEVPGRRGYPGYMYTDLSTIYERAG... | null | null | ATP metabolic process [GO:0046034]; endosomal lumen acidification [GO:0048388]; Golgi lumen acidification [GO:0061795]; intracellular calcium ion homeostasis [GO:0006874]; pexophagy [GO:0000425]; proteasome storage granule assembly [GO:1902906]; proton transmembrane transport [GO:1902600]; transmembrane transport [GO:0... | cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; fungal-type vacuole membrane [GO:0000329]; Golgi membrane [GO:0000139]; proton-transporting V-type ATPase complex [GO:0033176]; vacuolar proton-transporting V-type ATPase complex [GO:0016471]; vacuolar proton-transporting V-type ATPase, V1 domain [GO:0000... | ATP binding [GO:0005524]; proton-transporting ATPase activity, rotational mechanism [GO:0046961] | PF00006;PF02874; | 3.40.50.12240; | ATPase alpha/beta chains family | null | SUBCELLULAR LOCATION: Vacuole membrane {ECO:0000269|PubMed:2141385}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. | null | null | null | null | null | FUNCTION: Non-catalytic subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:2141385). V-ATPase is responsible for acidifying and maintaining the pH of intracell... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P16143 | PO2F1_XENLA | MKLHSSSKIQNHAWLSDARMNNPSETSKSPESGDGNTGTQTNGLDFQKQAVPIGAITSAQAQALLGHLHQVQLAGTSLQAAAHSLNVQTKFKEEPGEPMQVVQPSQQPSLQAAIPQTQLMVAGGQIAGLTLTPAQQQMLLQQAQAQLLAAAVQHSASQQHNAAGATISASAATPMTQIPLSQPIQIAQDLQQLQQLQQQNLNLQQYVLVHPTTNLQSAQFIISQTPQGQQGLLQAQNLLTQLPQQSQANLLQSQPSITLTSQPATPTRTIAATPVQQLPQSQTTPKRIDTPSLEEPSDLEELEQFAKTFKQRRIKLGFTQ... | null | null | Notch signaling pathway [GO:0007219]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; radial glial cell differentiation [GO:0060019]; regulation of apoptotic process [GO:0042981] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565] | PF00046;PF00157;PF19536; | 1.10.10.60;1.10.260.40; | POU transcription factor family, Class-2 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:2017364}. Nucleus {ECO:0000269|PubMed:2017364, ECO:0000269|PubMed:7542467}. Note=Retained in the cytoplasm during early development, then gradually translocates to the nucleus around the mid-blastula transition (MBT). | null | null | null | null | null | FUNCTION: Transcription factor that binds to the octamer motif (5'-ATTTGCAT-3') and activates the promoters of the genes of some small nuclear RNAs (snRNA) and histone H2B (PubMed:2017364). In vitro does not bind to variant octamer sequences, such as the H2B octamer 5'-GTTTGCAT-3', although binding has been observed in... | Xenopus laevis (African clawed frog) |
P16144 | ITB4_HUMAN | MAGPRPSPWARLLLAALISVSLSGTLANRCKKAPVKSCTECVRVDKDCAYCTDEMFRDRRCNTQAELLAAGCQRESIVVMESSFQITEETQIDTTLRRSQMSPQGLRVRLRPGEERHFELEVFEPLESPVDLYILMDFSNSMSDDLDNLKKMGQNLARVLSQLTSDYTIGFGKFVDKVSVPQTDMRPEKLKEPWPNSDPPFSFKNVISLTEDVDEFRNKLQGERISGNLDAPEGGFDAILQTAVCTRDIGWRPDSTHLLVFSTESAFHYEADGANVLAGIMSRNDERCHLDTTGTYTQYRTQDYPSVPTLVRLLAKHNII... | null | null | autophagy [GO:0006914]; cell adhesion [GO:0007155]; cell adhesion mediated by integrin [GO:0033627]; cell motility [GO:0048870]; cell-cell adhesion [GO:0098609]; cell-matrix adhesion [GO:0007160]; filopodium assembly [GO:0046847]; hemidesmosome assembly [GO:0031581]; integrin-mediated signaling pathway [GO:0007229]; me... | basal plasma membrane [GO:0009925]; basement membrane [GO:0005604]; cell junction [GO:0030054]; cell leading edge [GO:0031252]; cell surface [GO:0009986]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; hemidesmosome [GO:0030056]; integrin complex [GO:0008305]; nuclear membrane [GO:0031965]; nucleolus ... | G protein-coupled receptor binding [GO:0001664]; integrin binding [GO:0005178]; metal ion binding [GO:0046872] | PF03160;PF07974;PF00041;PF18372;PF07965;PF00362;PF17205; | 2.60.40.2030;4.10.1240.30;2.60.40.10;2.10.25.10;3.30.1680.10;2.60.40.1510;3.40.50.410; | Integrin beta chain family | PTM: Palmitoylated by DHHC3 at several cysteines of the membrane-proximal region, enhancing stability and cell surface expression. Palmitoylation also promotes secondary association with tertaspanins. {ECO:0000269|PubMed:15611341, ECO:0000269|PubMed:22314500}. | SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Cell membrane; Lipid-anchor. Cell junction, hemidesmosome. Note=Colocalizes with DST at the leading edge of migrating keratinocytes. | null | null | null | null | null | FUNCTION: Integrin alpha-6/beta-4 is a receptor for laminin. Plays a critical structural role in the hemidesmosome of epithelial cells. Is required for the regulation of keratinocyte polarity and motility. ITGA6:ITGB4 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling (PubMed:20682778)... | Homo sapiens (Human) |
P16150 | LEUK_HUMAN | MATLLLLLGVLVVSPDALGSTTAVQTPTSGEPLVSTSEPLSSKMYTTSITSDPKADSTGDQTSALPPSTSINEGSPLWTSIGASTGSPLPEPTTYQEVSIKMSSVPQETPHATSHPAVPITANSLGSHTVTGGTITTNSPETSSRTSGAPVTTAASSLETSRGTSGPPLTMATVSLETSKGTSGPPVTMATDSLETSTGTTGPPVTMTTGSLEPSSGASGPQVSSVKLSTMMSPTTSTNASTVPFRNPDENSRGMLPVAVLVALLAVIVLVALLLLWRRRQKRRTGALVLSRGGKRNGVVDAWAGPAQVPEEGAVTVTVG... | null | null | apoptotic signaling pathway [GO:0097190]; cell surface receptor signaling pathway [GO:0007166]; cellular defense response [GO:0006968]; chemotaxis [GO:0006935]; defense response to bacterium [GO:0042742]; establishment or maintenance of cell polarity [GO:0007163]; immune response [GO:0006955]; leukocyte tethering or ro... | basement membrane [GO:0005604]; cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; membrane [GO:0016020]; microvillus [GO:0005902]; plasma membrane [GO:0005886]; PML body [GO:0016605]; uropod [GO:0001931] | heat shock protein binding [GO:0031072]; Hsp70 protein binding [GO:0030544]; transmembrane signaling receptor activity [GO:0004888] | null | null | null | PTM: Glycosylated; has a high content of sialic acid and O-linked carbohydrate structures. {ECO:0000269|PubMed:1731338}.; PTM: Phosphorylation at Ser-355 is regulated by chemokines, requires its association with ERM proteins (EZR, RDX and MSN) and is essential for its function in the regulation of T-cell trafficking to... | SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}. Cell projection, microvillus {ECO:0000250|UniProtKB:P13838}. Cell projection, uropodium {ECO:0000250|UniProtKB:P15702}. Note=Localizes to the uropodium and microvilli via its interaction with ERM proteins (EZR, RDX and MSN)... | null | null | null | null | null | FUNCTION: Predominant cell surface sialoprotein of leukocytes which regulates multiple T-cell functions, including T-cell activation, proliferation, differentiation, trafficking and migration. Positively regulates T-cell trafficking to lymph-nodes via its association with ERM proteins (EZR, RDX and MSN) (By similarity)... | Homo sapiens (Human) |
P16152 | CBR1_HUMAN | MSSGIHVALVTGGNKGIGLAIVRDLCRLFSGDVVLTARDVTRGQAAVQQLQAEGLSPRFHQLDIDDLQSIRALRDFLRKEYGGLDVLVNNAGIAFKVADPTPFHIQAEVTMKTNFFGTRDVCTELLPLIKPQGRVVNVSSIMSVRALKSCSPELQQKFRSETITEEELVGLMNKFVEDTKKGVHQKEGWPSSAYGVTKIGVTVLSRIHARKLSEQRKGDKILLNACCPGWVRTDMAGPKATKSPEEGAETPVYLALLPPDAEGPHGQFVSEKRVEQW | 1.1.1.184; 1.1.1.189; 1.1.1.196; 1.1.1.197; 1.1.1.71 | null | cyclooxygenase pathway [GO:0019371]; epithelial cell differentiation [GO:0030855]; glucocorticoid metabolic process [GO:0008211]; positive regulation of reactive oxygen species metabolic process [GO:2000379]; vitamin K metabolic process [GO:0042373]; xenobiotic metabolic process [GO:0006805] | cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular vesicle [GO:1903561] | 15-hydroxyprostaglandin dehydrogenase (NADP+) activity [GO:0047021]; 15-hydroxyprostaglandin-D dehydrogenase (NADP+) activity [GO:0047020]; alcohol dehydrogenase (NADP+) activity [GO:0008106]; carbonyl reductase (NADPH) activity [GO:0004090]; oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as ac... | PF00106; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a secondary alcohol + NADP(+) = a ketone + H(+) + NADPH; Xref=Rhea:RHEA:19257, ChEBI:CHEBI:15378, ChEBI:CHEBI:17087, ChEBI:CHEBI:35681, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.184; Evidence={ECO:0000269|PubMed:17344335, ECO:0000269|PubMed:1921984, ECO:0000269|PubMed:7005231}; CATALYT... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=30 uM for S-nitrosoglutathione {ECO:0000269|PubMed:18826943}; KM=22 uM for menadione {ECO:0000269|PubMed:17344335, ECO:0000269|PubMed:18826943}; KM=309 uM for prostaglandin E2 {ECO:0000269|PubMed:17344335, ECO:0000269|PubMed:18826943}; KM=450 uM for prostaglandin E... | null | null | null | FUNCTION: NADPH-dependent reductase with broad substrate specificity. Catalyzes the reduction of a wide variety of carbonyl compounds including quinones, prostaglandins, menadione, plus various xenobiotics. Catalyzes the reduction of the antitumor anthracyclines doxorubicin and daunorubicin to the cardiotoxic compounds... | Homo sapiens (Human) |
P16154 | TCDA_CLODI | MSLISKEELIKLAYSIRPRENEYKTILTNLDEYNKLTTNNNENKYLQLKKLNESIDVFMNKYKTSSRNRALSNLKKDILKEVILIKNSNTSPVEKNLHFVWIGGEVSDIALEYIKQWADINAEYNIKLWYDSEAFLVNTLKKAIVESSTTEALQLLEEEIQNPQFDNMKFYKKRMEFIYDRQKRFINYYKSQINKPTVPTIDDIIKSHLVSEYNRDETVLESYRTNSLRKINSNHGIDIRANSLFTEQELLNIYSQELLNRGNLAAASDIVRLLALKNFGGVYLDVDMLPGIHSDLFKTISRPSSIGLDRWEMIKLEAIM... | 2.4.1.-; 3.4.22.- | COFACTOR: [Toxin A]: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:27571750}; Note=Binds 1 Zn(2+) ion per subunit (PubMed:27571750). Zn(2+) is required for autocatalytic cleavage (PubMed:27571750). {ECO:0000269|PubMed:27571750}; COFACTOR: [Glucosyltransferase TcdA]: Name=Mn(2+); Xref=ChEBI:CHEBI:290... | proteolysis [GO:0006508] | extracellular region [GO:0005576]; host cell cytosol [GO:0044164]; host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020] | cysteine-type peptidase activity [GO:0008234]; glycosyltransferase activity [GO:0016757]; lipid binding [GO:0008289]; metal ion binding [GO:0046872]; toxin activity [GO:0090729] | PF01473;PF19127;PF11713;PF12919;PF12920;PF12918; | 1.10.10.1780;1.10.274.80;1.10.3730.30;1.20.58.1190;3.40.50.11050;2.10.270.10; | Clostridial glucosylating toxin (LCGT) family | PTM: [Toxin A]: Undergoes autocatalytic cleavage to release the N-terminal part (Glucosyltransferase TcdA), which constitutes the active part of the toxin, in the host cytosol (PubMed:17334356, PubMed:19553670, PubMed:22267739, PubMed:27571750). 1D-myo-inositol hexakisphosphate-binding (InsP6) activates the peptidase C... | SUBCELLULAR LOCATION: [Toxin A]: Secreted {ECO:0000269|PubMed:22685398}. Host endosome membrane {ECO:0000250|UniProtKB:P18177}. Note=Secreted from C.difficile cell into the extracellular environment via help of holin-like protein TcdE/UtxA (PubMed:22685398). Binds to the cell surface receptors via the receptor-binding ... | CATALYTIC ACTIVITY: [Glucosyltransferase TcdA]: Reaction=L-threonyl-[protein] + UDP-alpha-D-glucose = 3-O-(alpha-D-glucosyl)-L-threonyl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:64684, Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:16656, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013, ChEBI:CHEBI:58223, ChEBI:CHEBI:58885, ChEBI:CHEBI:156085... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=43.9 uM for UDP-alpha-D-glucose (in presence of K(+)) {ECO:0000269|PubMed:22747490}; KM=36.3 uM for UDP-alpha-D-glucose (in presence of NH4(+)) {ECO:0000269|PubMed:22747490}; KM=51.1 uM for UDP-alpha-D-glucose (in presence of Na(+)) {ECO:0000269|PubMed:22747490}; V... | null | null | null | FUNCTION: [Toxin A]: Precursor of a cytotoxin that targets and disrupts the colonic epithelium, inducing the host inflammatory and innate immune responses and resulting in diarrhea and pseudomembranous colitis (PubMed:20844489). TcdA and TcdB constitute the main toxins that mediate the pathology of C.difficile infectio... | Clostridioides difficile (Peptoclostridium difficile) |
P16157 | ANK1_HUMAN | MPYSVGFREADAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYGTKGKVRLPALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETKTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDC... | null | null | cytoskeleton organization [GO:0007010]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; exocytosis [GO:0006887]; maintenance of epithelial cell apical/basal polarity [GO:0045199]; positive regulation of organelle organization [GO:0010638]; protein localization to plasma membrane [GO:0072659]; si... | ankyrin-1 complex [GO:0170014]; axolemma [GO:0030673]; basolateral plasma membrane [GO:0016323]; cytoplasmic side of plasma membrane [GO:0009898]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; M band [GO:0031430]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; sarco... | ATPase binding [GO:0051117]; cytoskeletal anchor activity [GO:0008093]; enzyme binding [GO:0019899]; protein phosphatase binding [GO:0019903]; spectrin binding [GO:0030507]; structural constituent of cytoskeleton [GO:0005200]; structural molecule activity [GO:0005198]; transmembrane transporter binding [GO:0044325] | PF00023;PF12796;PF13606;PF13637;PF00531;PF17809;PF00791; | 2.60.220.30;2.60.40.2660;1.25.40.20;1.10.533.10; | null | PTM: Regulated by phosphorylation.; PTM: Palmitoylated.; PTM: Hydroxylated by HIF1AN at several asparagine and 1 aspartate residue within ANK repeat region. Hydroxylation seems to increase the conformational stability of this region and may also modulate protein-protein interactions mediated by the ANK repeat region. {... | SUBCELLULAR LOCATION: [Isoform Er1]: Cytoplasm, cytoskeleton. Note=Probably the other erythrocyte (Er) isoforms, are located near the surface of erythrocytic plasma membrane.; SUBCELLULAR LOCATION: [Isoform Mu17]: Membrane. Cytoplasm, myofibril, sarcomere, M line. Note=Colocalizes with OBSCN isoform 3/obscurin at the M... | null | null | null | null | null | FUNCTION: Component of the ankyrin-1 complex, a multiprotein complex involved in the stability and shape of the erythrocyte membrane (PubMed:35835865). Attaches integral membrane proteins to cytoskeletal elements; binds to the erythrocyte membrane protein band 4.2, to Na-K ATPase, to the lymphocyte membrane protein GP8... | Homo sapiens (Human) |
P16163 | URIC_DROME | MFATPLRQPAAANHQTPKNSAGMDEHGKPYQYEITDHGYGKDAVKVLHVSRNGPVHAIQEFEVGTHLKLYSKKDYYQGNNSDIVATDSQKNTVYLLAKKHGIESPEKFALLLARHFINKYSHVEEAHVHVEAYPWQRVCQEETRTNVNGKCENGVQGNCDFSSIDNRSLHNHAFIFTPTALHYCDVVIRRTDPKQTVITGIKGLRVLKTTQSSFVNFVNDEFRSLPDQYDRIFSTVVDCSWEYSDTENLDFLRAWQTVKNIIIRNFAGDPQVGVSSPSVQHTLYLSERQVLDVLPQVSVISMTMPNKHYFNFDTKPFQKI... | 1.7.3.3 | null | allantoin biosynthetic process [GO:0019428]; purine nucleobase catabolic process [GO:0006145]; urate catabolic process [GO:0019628] | peroxisome [GO:0005777] | urate oxidase activity [GO:0004846] | PF01014; | 3.10.270.10; | Uricase family | null | SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:2118989}. | CATALYTIC ACTIVITY: Reaction=H2O + O2 + urate = 5-hydroxyisourate + H2O2; Xref=Rhea:RHEA:21368, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:17775, ChEBI:CHEBI:18072; EC=1.7.3.3; | null | PATHWAY: Purine metabolism; urate degradation; (S)-allantoin from urate: step 1/3. | null | null | FUNCTION: Catalyzes the oxidation of uric acid to 5-hydroxyisourate, which is further processed to form (S)-allantoin. {ECO:0000269|PubMed:2118989}. | Drosophila melanogaster (Fruit fly) |
P16177 | NK3R_RAT | MASVPRGENWTDGTVEVGTHTGNLSSALGVTEWLALQAGNFSSALGLPATTQAPSQVRANLTNQFVQPSWRIALWSLAYGLVVAVAVFGNLIVIWIILAHKRMRTVTNYFLVNLAFSDASVAAFNTLINFIYGLHSEWYFGANYCRFQNFFPITAVFASIYSMTAIAVDRYMAIIDPLKPRLSATATKIVIGSIWILAFLLAFPQCLYSKIKVMPGRTLCYVQWPEGPKQHFTYHIIVIILVYCFPLLIMGVTYTIVGITLWGGEIPGDTCDKYHEQLKAKRKVVKMMIIVVVTFAICWLPYHVYFILTAIYQQLNRWKY... | null | null | positive regulation of blood pressure [GO:0045777]; positive regulation of flagellated sperm motility [GO:1902093]; positive regulation of heart rate [GO:0010460]; positive regulation of uterine smooth muscle contraction [GO:0070474]; regulation of dopamine metabolic process [GO:0042053]; regulation of feeding behavior... | dendrite membrane [GO:0032590]; neuronal cell body membrane [GO:0032809]; plasma membrane [GO:0005886]; sperm midpiece [GO:0097225] | tachykinin receptor activity [GO:0004995] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | PTM: The anchoring of this receptor to the plasma membrane is probably mediated by the palmitoylation of a cysteine residue. | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: This is a receptor for the tachykinin neuropeptide neuromedin-K (neurokinin B). It is associated with G proteins that activate a phosphatidylinositol-calcium second messenger system. The rank order of affinity of this receptor to tachykinins is: neuromedin-K > substance K > substance P. | Rattus norvegicus (Rat) |
P16180 | RR17_ARATH | MITSSLTSSLQALKLSSPFAHGSTPLSSLSKPNSFPNHRMPALVPVIRAMKTMQGRVVCATSDKTVAVEVVRLAPHPKYKRRVRMKKKYQAHDPDNQFKVGDVVRLEKSRPISKTKSFVALPVIARAARKAEAGGDELLGLPLESQQPA | null | null | plastid translation [GO:0032544] | chloroplast [GO:0009507]; chloroplast envelope [GO:0009941]; chloroplast stroma [GO:0009570]; chloroplast thylakoid [GO:0009534]; mitochondrion [GO:0005739]; plastid small ribosomal subunit [GO:0000312] | mRNA binding [GO:0003729]; rRNA binding [GO:0019843]; structural constituent of ribosome [GO:0003735] | PF00366; | 2.40.50.140; | Universal ribosomal protein uS17 family | null | SUBCELLULAR LOCATION: Plastid, chloroplast {ECO:0000305}. | null | null | null | null | null | FUNCTION: One of the primary rRNA binding proteins, it binds specifically to the 5'-end of 16S ribosomal RNA (By similarity). Required for optimal plastid performance in terms of photosynthesis and growth. Required for the translation of plastid mRNAs. Plays a critical role in biosynthesis of thylakoid membrane protein... | Arabidopsis thaliana (Mouse-ear cress) |
P16209 | 1A01_PANTR | MAVMPPRTLLLLLSGALALTQTWAGSHSMRYFFTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQRMEPRAPWIEQEGPEYWDEETRSAKAHSQTDRVDLGTLRGYYNQSEDGSHTIQIMYGCDVGSDGRFLRGYRQDAYDGKDYIALNEDLRSWTAADMAAQITKRKWEAAHAAEQRRAYLEGTCVEWLRRYLENGKETLQRTDPPKTHMTHHPISDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWEPSSQPTIPIVGIIAGLVLLGA... | null | null | antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib [GO:0002476]; immune response [GO:0006955]; positive regulation of T cell mediated cytotoxicity [GO:0001916] | early endosome membrane [GO:0031901]; ER to Golgi transport vesicle membrane [GO:0012507]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; MHC class I protein complex [GO:0042612]; phagocytic vesicle membrane [GO:0030670]; rec... | peptide antigen binding [GO:0042605]; signaling receptor binding [GO:0005102] | PF07654;PF00129;PF06623; | 2.60.40.10;3.30.500.10; | MHC class I family | null | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Involved in the presentation of foreign antigens to the immune system. | Pan troglodytes (Chimpanzee) |
P16210 | 1A02_PANTR | MQVTAPRTVLLLLSAALALTETWAGSHSMKYFYTAVSRPGRGEPRFISVGYVDDTQFVWFDSDAASPREEPRAPWIEQEGPEYWDRETQISKTNAQTYRESLRNLRGYYNQSEAGSHIIQRMYGCDMGPDGRLLRGYEQYAYDGKDYIALNQDLSSWTAADTAAQITQRKWEAARWAEQLRAYLEGTCVEWLRRYLENGKETLQRADPPKTHVTHHPISDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDRTFQKWAAVVVPSGEEQRYTCHVQHEGLPKPLTLRWEPSSQSTIPIVGIVAGLAVLAV... | null | null | antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib [GO:0002476]; immune response [GO:0006955]; positive regulation of T cell mediated cytotoxicity [GO:0001916] | early endosome membrane [GO:0031901]; ER to Golgi transport vesicle membrane [GO:0012507]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; MHC class I protein complex [GO:0042612]; phagocytic vesicle membrane [GO:0030670]; rec... | peptide antigen binding [GO:0042605]; signaling receptor binding [GO:0005102] | PF07654;PF00129;PF06623; | 2.60.40.10;3.30.500.10; | MHC class I family | null | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Involved in the presentation of foreign antigens to the immune system. | Pan troglodytes (Chimpanzee) |
P16211 | 1A01_PONPY | MAIMAPRTLLLLLSGALALTQTWAGSHSMRYFSTSVSRPGRGEPRFIAVGYVDDTQFVRFDSDAASQRMEPRTPWMEQEGPEYWDRETRSVKAHAQTNRVDLGTLRGYYNQSDGGSHTIQRMFGCDVGPDGRFLRGYEQHAYDGKDYIALNEDLRSWTAADMAAQITQRKWEAAGAAEQDRAYLEGLCVESLRRYLENGKETLQRTDAPKTHMTHHPVSDHEATLRCWALGFYPAEITLTWQRDGEDQTQDTELVETRPAGDGTFQKWAAVVVPSGKEQRYTCHVQHEGLPEPLTLRWELSSQPTIPIVGIIAGLVLLGA... | null | null | antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib [GO:0002476]; immune response [GO:0006955]; positive regulation of T cell mediated cytotoxicity [GO:0001916] | early endosome membrane [GO:0031901]; ER to Golgi transport vesicle membrane [GO:0012507]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; MHC class I protein complex [GO:0042612]; phagocytic vesicle membrane [GO:0030670]; rec... | peptide antigen binding [GO:0042605]; signaling receptor binding [GO:0005102] | PF07654;PF00129;PF06623; | 2.60.40.10;3.30.500.10; | MHC class I family | null | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Involved in the presentation of foreign antigens to the immune system. | Pongo pygmaeus (Bornean orangutan) |
P16212 | HLAE_PONPY | GTLLLLLSEALALTETWAGSHSLKYFHTSVSRPGRGEPRFISVGYVDDTQFVRFDNDAASPRMVPRAQWMEQEGPEYWDRETRSARDTAQTFRVNLRTLRGYYNQTEAGSHTLQWMHGCDLGPDGRFLRGYEQFAYDGKDYLTLNEDLRSWTAVDTAAQISERKSNDACEAEHQRAYLEDTCVEWLRKYLEKGKETLLHLDPPKTHVTHHRISDHEATLRCWALGFYPAEITLTWQRDGEDQNQYTELVETRPAGDGTFQKWAAVVVPSGEEQRYTCHVQHEGLPEPLTLRWEPASQTTIPIVGIFAGLVLLGAVVTGAT... | null | null | antigen processing and presentation of endogenous peptide antigen via MHC class I via ER pathway, TAP-independent [GO:0002486]; antigen processing and presentation of endogenous peptide antigen via MHC class Ib [GO:0002476]; immune response [GO:0006955]; positive regulation of T cell mediated cytotoxicity [GO:0001916] | early endosome membrane [GO:0031901]; ER to Golgi transport vesicle membrane [GO:0012507]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; MHC class I protein complex [GO:0042612]; phagocytic vesicle membrane [GO:0030670]; rec... | peptide antigen binding [GO:0042605]; signaling receptor binding [GO:0005102] | PF07654;PF00129;PF06623; | 2.60.40.10;3.30.500.10; | MHC class I family | null | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Involved in the presentation of foreign antigens to the immune system. | Pongo pygmaeus (Bornean orangutan) |
P16219 | ACADS_HUMAN | MAAALLARASGPARRALCPRAWRQLHTIYQSVELPETHQMLLQTCRDFAEKELFPIAAQVDKEHLFPAAQVKKMGGLGLLAMDVPEELGGAGLDYLAYAIAMEEISRGCASTGVIMSVNNSLYLGPILKFGSKEQKQAWVTPFTSGDKIGCFALSEPGNGSDAGAASTTARAEGDSWVLNGTKAWITNAWEASAAVVFASTDRALQNKGISAFLVPMPTPGLTLGKKEDKLGIRGSSTANLIFEDCRIPKDSILGEPGMGFKIAMQTLDMGRIGIASQALGIAQTALDCAVNYAENRMAFGAPLTKLQVIQFKLADMALA... | 1.3.8.1 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|Ref.10}; Note=Binds 1 FAD per subunit. {ECO:0000269|Ref.10}; | butyrate catabolic process [GO:0046359]; fatty acid beta-oxidation [GO:0006635]; fatty acid beta-oxidation using acyl-CoA dehydrogenase [GO:0033539] | centrosome [GO:0005813]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | acyl-CoA dehydrogenase activity [GO:0003995]; butyryl-CoA dehydrogenase activity [GO:0004085]; flavin adenine dinucleotide binding [GO:0050660] | PF00441;PF02770;PF02771; | 1.10.540.10;2.40.110.10;1.20.140.10; | Acyl-CoA dehydrogenase family | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:Q3ZBF6}. | CATALYTIC ACTIVITY: Reaction=a short-chain 2,3-saturated fatty acyl-CoA + H(+) + oxidized [electron-transfer flavoprotein] = a short-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]; Xref=Rhea:RHEA:47196, Rhea:RHEA-COMP:10685, Rhea:RHEA-COMP:10686, ChEBI:CHEBI:15378, ChEBI:CHEBI:57692, ChEBI:CHEBI:58307,... | null | PATHWAY: Lipid metabolism; mitochondrial fatty acid beta-oxidation. {ECO:0000305|PubMed:11134486}. | null | null | FUNCTION: Short-chain specific acyl-CoA dehydrogenase is one of the acyl-CoA dehydrogenases that catalyze the first step of mitochondrial fatty acid beta-oxidation, an aerobic process breaking down fatty acids into acetyl-CoA and allowing the production of energy from fats (By similarity). The first step of fatty acid ... | Homo sapiens (Human) |
P16220 | CREB1_HUMAN | MTMESGAENQQSGDAAVTEAENQQMTVQAQPQIATLAQVSMPAAHATSSAPTVTLVQLPNGQTVQVHGVIQAAQPSVIQSPQVQTVQISTIAESEDSQESVDSVTDSQKRREILSRRPSYRKILNDLSSDAPGVPRIEEEKSEEETSAPAITTVTVPTPIYQTSSGQYIAITQGGAIQLANNGTDGVQGLQTLTMTNAAATQPGTTILQYAQTTDGQQILVPSNQVVVQAASGDVQTYQIRTAPTSTIAPGVVMASSPALPTQPAEEAARKREVRLMKNREAARECRRKKKEYVKCLENRVAVLENQNKTLIEELKALKD... | null | null | axonogenesis [GO:0007409]; cAMP-mediated signaling [GO:0019933]; cellular response to forskolin [GO:1904322]; cellular response to hepatocyte growth factor stimulus [GO:0035729]; cellular response to leukemia inhibitory factor [GO:1990830]; cellular response to retinoic acid [GO:0071300]; cellular response to zinc ion ... | ATF4-CREB1 transcription factor complex [GO:1990589]; chromatin [GO:0000785]; euchromatin [GO:0000791]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575] | cAMP response element binding [GO:0035497]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; enzyme binding [GO:0019899]; identical protein bi... | PF00170;PF02173; | 1.20.5.170; | BZIP family | PTM: Stimulated by phosphorylation. Phosphorylation of both Ser-119 and Ser-128 in the SCN regulates the activity of CREB and participates in circadian rhythm generation. Phosphorylation of Ser-119 allows CREBBP binding. In liver, phosphorylation is induced by fasting or glucagon in a circadian fashion (By similarity).... | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00312, ECO:0000255|PROSITE-ProRule:PRU00978, ECO:0000269|PubMed:12552083}. | null | null | null | null | null | FUNCTION: Phosphorylation-dependent transcription factor that stimulates transcription upon binding to the DNA cAMP response element (CRE), a sequence present in many viral and cellular promoters (By similarity). Transcription activation is enhanced by the TORC coactivators which act independently of Ser-119 phosphoryl... | Homo sapiens (Human) |
P16225 | SPAI_PIG | MRSRSFLVLVAVFLICETLVAQRLDRIRGPKGQGQDPVEGQDQDEGPGPVKVEILDIGQDPVKGQDPVKGQDPVKGQDPVKGQDLVKSQDPVKAELPDIGQDVVKGHEPVEGQDPVNAQLPDKVQDPVKAQPAVPGRFLLSKRGHCPRILFRCPLSNPSNKCWRDYDCPGVKKCCEGFCGKDCLYPK | null | null | antibacterial humoral response [GO:0019731]; copulation [GO:0007620]; innate immune response [GO:0045087] | extracellular space [GO:0005615] | serine-type endopeptidase inhibitor activity [GO:0004867] | PF10511;PF00095; | 4.10.75.10; | null | PTM: The short form (AA 127-187) may be an artifact due to the strongly acidic conditions of the duodenum. The pro-SPAI form may be the native form. | null | null | null | null | null | null | FUNCTION: Inhibits Na(+),K(+) ATPase by the competitive mode against Na(+). | Sus scrofa (Pig) |
P16228 | CATE_RAT | MKPLFVLLLLLLLLDLAQAQGVLHRVPLRRHQSLRKKLRAQGQLSDFWRSHNLDMIEFSESCNVDKGINEPLINYLDMEYFGTVSIGSPSQNFTVIFDTGSSNLWVPSVYCTSPACKAHPVFHPSQSSTYMEVGNHFSIQYGTGSLTGIIGADQVSVEGLTVEGQQFGESVKEPGQTFVNAEFDGILGLGYPSLAVGGVTPVFDNMMAQNLVALPMFSVYLSSDPQGGSGSELTFGGYDPSHFSGSLNWIPVTKQGYWQIALDGIQVGDTVMFCSEGCQAIVDTGTSLITGPPKKIKQLQEAIGATPMDGEYAVDCATLN... | 3.4.23.34 | null | antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; protein autoprocessing [GO:0016540]; proteolysis [GO:0006508] | endosome [GO:0005768] | aspartic-type endopeptidase activity [GO:0004190]; identical protein binding [GO:0042802]; peptidase activity [GO:0008233] | PF07966;PF00026; | 6.10.140.60;2.40.70.10; | Peptidase A1 family | PTM: Glycosylated. The nature of the carbohydrate chain varies between cell types. In brain microglia, the proenzyme contains a high mannose-type oligosaccharide, while the mature enzyme contains a complex-type oligosaccharide. In stomach and spleen, the mature enzyme contains a high mannose-type oligosaccharide. In er... | SUBCELLULAR LOCATION: Endosome {ECO:0000269|PubMed:8491674, ECO:0000269|PubMed:9572291}. Note=The proenzyme is localized to the endoplasmic reticulum and Golgi apparatus, while the mature enzyme is localized to the endosome. | CATALYTIC ACTIVITY: Reaction=Similar to cathepsin D, but slightly broader specificity.; EC=3.4.23.34; Evidence={ECO:0000269|PubMed:8157122}; | null | null | null | null | FUNCTION: May have a role in immune function. Probably involved in the processing of antigenic peptides during MHC class II-mediated antigen presentation. May play a role in activation-induced lymphocyte depletion in the thymus, and in neuronal degeneration and glial cell activation in the brain (By similarity). {ECO:0... | Rattus norvegicus (Rat) |
P16232 | DHI1_RAT | MKKYLLPVLVLCLGYYYSTNEEFRPEMLQGKKVIVTGASKGIGREMAYHLSKMGAHVVLTARSEEGLQKVVSRCLELGAASAHYIAGTMEDMAFAERFVVEAGKLLGGLDMLILNHITQTTMSLFHDDIHSVRRSMEVNFLSYVVLSTAALPMLKQSNGSIAIISSMAGKMTQPLIASYSASKFALDGFFSTIRKEHLMTKVNVSITLCVLGFIDTETALKETSGIILSQAAPKEECALEIIKGTVLRKDEVYYDKSSWTPLLLGNPGRRIMEFLSLRSYNRDLFVSN | 1.1.1.146; 1.1.1.201 | null | cellular response to estradiol stimulus [GO:0071392]; glucocorticoid biosynthetic process [GO:0006704]; glucocorticoid catabolic process [GO:0006713]; lung development [GO:0030324]; mineralocorticoid metabolic process [GO:0008212]; regulation of pentose-phosphate shunt [GO:0043456]; response to nutrient levels [GO:0031... | apical part of cell [GO:0045177]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]; nuclear membrane [GO:0031965] | 11-beta-hydroxysteroid dehydrogenase (NADP+) activity [GO:0070524]; 7-beta-hydroxysteroid dehydrogenase (NADP+) activity [GO:0047022]; cortisol dehydrogenase activity [GO:0102196]; NADP binding [GO:0050661]; protein homodimerization activity [GO:0042803]; steroid binding [GO:0005496] | PF00106; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | PTM: Glycosylated. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. | CATALYTIC ACTIVITY: Reaction=an 11beta-hydroxysteroid + NADP(+) = an 11-oxosteroid + H(+) + NADPH; Xref=Rhea:RHEA:11388, ChEBI:CHEBI:15378, ChEBI:CHEBI:35346, ChEBI:CHEBI:47787, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.146; Evidence={ECO:0000269|PubMed:12460758, ECO:0000269|PubMed:14973125, ECO:0000269|PubMed:280... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=367 nM for corticosterone {ECO:0000269|PubMed:14973125}; KM=681 nM for 11-dehydrocorticosterone {ECO:0000269|PubMed:14973125}; KM=776 nM for 7-oxocholesterol {ECO:0000269|PubMed:14973125}; KM=3.1 uM for 11-dehydrocorticosterone {ECO:0000269|PubMed:12460758}; KM=2.5... | null | null | null | FUNCTION: Controls the reversible conversion of biologically active glucocorticoids such as 11-dehydrocorticosterone to corticosterone using NADP(H) (PubMed:12460758, PubMed:14973125, PubMed:8613810). Participates in the corticosteroid receptor-mediated anti-inflammatory response, as well as metabolic and homeostatic p... | Rattus norvegicus (Rat) |
P16233 | LIPP_HUMAN | MLPLWTLSLLLGAVAGKEVCYERLGCFSDDSPWSGITERPLHILPWSPKDVNTRFLLYTNENPNNFQEVAADSSSISGSNFKTNRKTRFIIHGFIDKGEENWLANVCKNLFKVESVNCICVDWKGGSRTGYTQASQNIRIVGAEVAYFVEFLQSAFGYSPSNVHVIGHSLGAHAAGEAGRRTNGTIGRITGLDPAEPCFQGTPELVRLDPSDAKFVDVIHTDGAPIVPNLGFGMSQVVGHLDFFPNGGVEMPGCKKNILSQIVDIDGIWEGTRDFAACNHLRSYKYYTDSIVNPDGFAGFPCASYNVFTANKCFPCPSGG... | 3.1.1.3 | null | intestinal cholesterol absorption [GO:0030299]; lipid catabolic process [GO:0016042]; lipid metabolic process [GO:0006629]; positive regulation of triglyceride lipase activity [GO:0061365] | extracellular region [GO:0005576]; extracellular space [GO:0005615] | all-trans-retinyl-palmitate hydrolase, all-trans-retinol forming activity [GO:0047376]; lipase activity [GO:0016298]; metal ion binding [GO:0046872]; triglyceride lipase activity [GO:0004806] | PF00151;PF01477; | 3.40.50.1820;2.60.60.20; | AB hydrolase superfamily, Lipase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:25862608}. | 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:10769148}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:120... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7. {ECO:0000269|PubMed:17401110}; | null | FUNCTION: Plays an important role in fat metabolism. It preferentially splits the esters of long-chain fatty acids at positions 1 and 3, producing mainly 2-monoacylglycerol and free fatty acids, and shows considerably higher activity against insoluble emulsified substrates than against soluble ones. {ECO:0000269|PubMed... | Homo sapiens (Human) |
P16234 | PGFRA_HUMAN | MGTSHPAFLVLGCLLTGLSLILCQLSLPSILPNENEKVVQLNSSFSLRCFGESEVSWQYPMSEEESSDVEIRNEENNSGLFVTVLEVSSASAAHTGLYTCYYNHTQTEENELEGRHIYIYVPDPDVAFVPLGMTDYLVIVEDDDSAIIPCRTTDPETPVTLHNSEGVVPASYDSRQGFNGTFTVGPYICEATVKGKKFQTIPFNVYALKATSELDLEMEALKTVYKSGETIVVTCAVFNNEVVDLQWTYPGEVKGKGITMLEEIKVPSIKLVYTLTVPEATVKDSGDYECAARQATREVKEMKKVTISVHEKGFIEIKPT... | 2.7.10.1 | null | adrenal gland development [GO:0030325]; cardiac myofibril assembly [GO:0055003]; cell activation [GO:0001775]; cell chemotaxis [GO:0060326]; cellular response to amino acid stimulus [GO:0071230]; cellular response to reactive oxygen species [GO:0034614]; embryonic cranial skeleton morphogenesis [GO:0048701]; embryonic ... | cell junction [GO:0030054]; cilium [GO:0005929]; cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; external side of plasma membrane [GO:0009897]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; microvillus [GO:0005902]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]... | ATP binding [GO:0005524]; platelet-derived growth factor alpha-receptor activity [GO:0005018]; platelet-derived growth factor binding [GO:0048407]; platelet-derived growth factor receptor binding [GO:0005161]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; protein-containing compl... | PF07679;PF07714; | 2.60.40.10;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, CSF-1/PDGF receptor subfamily | PTM: N-glycosylated.; PTM: Ubiquitinated, leading to its internalization and degradation. {ECO:0000305|PubMed:21596750}.; PTM: Autophosphorylated on tyrosine residues upon ligand binding. Autophosphorylation occurs in trans, i.e. one subunit of the dimeric receptor phosphorylates tyrosine residues on the other subunit.... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14644164, ECO:0000269|PubMed:2554309, ECO:0000269|PubMed:8188664}; Single-pass type I membrane protein {ECO:0000269|PubMed:14644164, ECO:0000269|PubMed:2554309, ECO:0000269|PubMed:8188664}. Cell projection, cilium {ECO:0000250|UniProtKB:P26618}. Golgi apparatus {E... | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Tyrosine-protein kinase that acts as a cell-surface receptor for PDGFA, PDGFB and PDGFC and plays an essential role in the regulation of embryonic development, cell proliferation, survival and chemotaxis. Depending on the context, promotes or inhibits cell proliferation and cell migration. Plays an important ... | Homo sapiens (Human) |
P16235 | LSHR_RAT | MGRRVPALRQLLVLAVLLLKPSQLQSRELSGSRCPEPCDCAPDGALRCPGPRAGLARLSLTYLPVKVIPSQAFRGLNEVVKIEISQSDSLERIEANAFDNLLNLSELLIQNTKNLLYIEPGAFTNLPRLKYLSICNTGIRTLPDVTKISSSEFNFILEICDNLHITTIPGNAFQGMNNESVTLKLYGNGFEEVQSHAFNGTTLISLELKENIYLEKMHSGAFQGATGPSILDISSTKLQALPSHGLESIQTLIALSSYSLKTLPSKEKFTSLLVATLTYPSHCCAFRNLPKKEQNFSFSIFENFSKQCESTVRKADNETL... | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; adenylate cyclase-modulating G protein-coupled receptor signaling pathway [GO:0007188]; arachidonic acid secretion [GO:0050482]; cellular response to gonadotropin stimulus [GO:0071371]; cellular response to luteinizing hormone stimu... | centriolar satellite [GO:0034451]; endosome [GO:0005768]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | ATPase binding [GO:0051117]; choriogonadotropin hormone binding [GO:0038106]; choriogonadotropin hormone receptor activity [GO:0035472]; G protein-coupled peptide receptor activity [GO:0008528]; identical protein binding [GO:0042802]; luteinizing hormone receptor activity [GO:0004964]; peptide hormone binding [GO:00170... | PF00001;PF13306; | 1.20.1070.10;3.80.10.10; | G-protein coupled receptor 1 family, FSH/LSH/TSH subfamily | PTM: Sulfated. {ECO:0000250|UniProtKB:P22888}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P22888}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P22888}. Secreted. Note=Some isoforms may be secreted. | null | null | null | null | null | FUNCTION: Receptor for lutropin-choriogonadotropic hormone. The activity of this receptor is mediated by G proteins which activate adenylate cyclase. {ECO:0000250|UniProtKB:P22888}. | Rattus norvegicus (Rat) |
P16236 | REL_CHICK | MAGISEPYIEIFEQPRQRGMRFRYKCEGRSAGSIPGEHSTDNNKTFPSIQILNYFGKVKIRTTLVTKNEPYKPHPHDLVGKDCRDGYYEAEFGPERRVLSFQNLGIQCVKKKDLKESISLRISKKINPFNVPEEQLHNIDEYDLNVVRLCFQAFLPDEHGNYTLALPPLISNPIYDNRAPNTAELRICRVNKNCGSVKGGDEIFILCDKVQKDDIEVRFVLDNWEAKGSFSQADVHRQVAIVFRTPPFLRDITEPITVKMQLRRPSDQEVSEPMDFRYLPDEKDPYGNKAKRQRSTLAWQKLIQDCGSAVTERPKAAPIP... | null | null | apoptotic DNA fragmentation [GO:0006309]; canonical NF-kappaB signal transduction [GO:0007249]; cellular response to stress [GO:0033554]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; non-canonical NF-kappaB signal transduction [GO:0038061]; positive regulation of transcription by RNA polymer... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF16179;PF00554; | 2.60.40.10;2.60.40.340; | null | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Proto-oncogene that may play a role in differentiation and lymphopoiesis. NF-kappa-B is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processed such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-... | Gallus gallus (Chicken) |
P16241 | CF1A_DROME | MAATSYMTPPSGDLDMALGGGGYHTSSPRSAADAGEMKYMQHHHHHHAAAAAAAHHQLPSSPSPNGQGNGGGLGLGSGSGLGSWSALHPDPWMQTHHTHHLPAAAAVASAADTVKQEMSHLSQQTRIQQGMASPHAAWHAPHAGHYAPTGGSPLQYHHAMNGMLHHPAHAVAAAHHQSVAPLHHTLRGESPQLHIHHHMGGGDRDAISGGEEDTPTSDDLEAFAKQFKQRRIKLGFTQADVGLALGTLYGNVFSQTTICRFEALQLSFKNMCKLKPLLQKWLEEADSTTGSPTSIDKIAAQGRKRKKRTSIEVSVKGALE... | null | null | brain development [GO:0007420]; brain segmentation [GO:0035284]; dendrite morphogenesis [GO:0048813]; motor neuron axon guidance [GO:0008045]; peripheral nervous system development [GO:0007422]; positive regulation of antimicrobial peptide biosynthetic process [GO:0002807]; positive regulation of transcription by RNA p... | nucleus [GO:0005634] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-specif... | PF00046;PF00157; | 1.10.10.60;1.10.260.40; | POU transcription factor family, Class-3 subfamily | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Binds to a DNA sequence element required for the expression of the dopa decarboxylase gene (Ddc) in specific dopaminergic neurons. Could also play an early role in specific ectodermal cells, and a subsequent role in the embryonic nervous system. {ECO:0000269|PubMed:1680380, ECO:0000269|PubMed:1967821}. | Drosophila melanogaster (Fruit fly) |
P16243 | MAOC_MAIZE | MLSTRTAAVAASASPASPWKLGGRSEGGASCDGCRTYRNTLRRRAAPAKVRALPPRRVDAVAMVSNAETETEKEQEEAAAASEELPVMPWATSVASGYTLLRDPHHNKGLAFTEEERDGHYLRGLLPPAVLSQELQIKKFMNTLRQYQTPLQRYIAMMNLQETDERLFYKLLIDNVVELLPFVYTPTVGEACQKYGSIFGRPQGLYVSLKDKGKVLEVLRNWPHRNIQVICVTDGERILGLGDLGCQGMGIPVGKLALYTALGGVDPSVCLPITIDVGTNNEFLLNDEFYIGLRQKRATGEEYDELIEEFMSAVKQFYGE... | 1.1.1.40 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; Note=Divalent metal cations. Prefers magnesium or manganese. {ECO:0000250}; | malate metabolic process [GO:0006108]; pyruvate metabolic process [GO:0006090] | chloroplast [GO:0009507] | malate dehydrogenase (decarboxylating) (NADP+) activity [GO:0004473]; metal ion binding [GO:0046872]; NAD binding [GO:0051287]; oxaloacetate decarboxylase activity [GO:0008948] | PF00390;PF03949; | 3.40.50.10380;3.40.50.720; | Malic enzymes family | null | SUBCELLULAR LOCATION: Plastid, chloroplast. | CATALYTIC ACTIVITY: Reaction=(S)-malate + NADP(+) = CO2 + NADPH + pyruvate; Xref=Rhea:RHEA:18253, ChEBI:CHEBI:15361, ChEBI:CHEBI:15589, ChEBI:CHEBI:16526, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.40; Evidence={ECO:0000269|PubMed:31235877}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18254; Evidence={ECO:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.23 mM for malate {ECO:0000269|PubMed:31235877}; KM=14.9 uM for NADP {ECO:0000269|PubMed:31235877}; Note=kcat is 28.1 sec(-1) with malate as substrate. {ECO:0000269|PubMed:31235877}; | PATHWAY: Photosynthesis; C4 acid pathway. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5-8.0. {ECO:0000269|PubMed:31235877}; | null | FUNCTION: The chloroplastic ME isoform decarboxylates malate shuttled from neighboring mesophyll cells. The CO(2) released is then refixed by ribulose-bisphosphate carboxylase. This pathway eliminates the photorespiratory loss of CO(2) that occurs in most plants. {ECO:0000269|PubMed:31235877}. | Zea mays (Maize) |
P16250 | HIS4_STRCO | MSKLELLPAVDVRDGQAVRLVHGESGTETSYGSPLEAALAWQRSGAEWLHLVDLDAAFGTGDNRALIAEVAQAMDIKVELSGGIRDDDTLAAALATGCTRVNLGTAALETPEWVAKVIAEHGDKIAVGLDVRGTTLRGRGWTRDGGDLYETLDRLNKEGCARYVVTDIAKDGTLQGPNLELLKNVCAATDRPVVASGGVSSLDDLRAIAGLVPAGVEGAIVGKALYAKAFTLEEALEATS | 5.3.1.16; 5.3.1.24 | null | histidine biosynthetic process [GO:0000105]; tryptophan biosynthetic process [GO:0000162] | cytoplasm [GO:0005737] | 1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity [GO:0003949]; phosphoribosylanthranilate isomerase activity [GO:0004640] | PF00977; | 3.20.20.70; | HisA/HisF family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide = 5-[(5-phospho-1-deoxy-D-ribulos-1-ylimino)methylamino]-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide; Xref=Rhea:RHEA:15469, ChEBI:CHEBI:58435, ChEBI:CHEBI:58525; EC=5.3.1.16; Evid... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=28 uM for ProFAR {ECO:0000269|PubMed:15654319}; KM=4 uM for PRA {ECO:0000269|PubMed:15654319}; | PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9.; PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L-tryptophan from chorismate: step 3/5. | null | null | FUNCTION: Catalyzes the isomerization of the aminoaldose moiety of ProFAR to the aminoketose of PRFAR in the biosynthesis pathway for histidine and the isomerization of the aminoaldose PRA to the aminoketose CdRP in the biosynthsis pathway for tryptophan. | Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) |
P16257 | TSPO_RAT | MSQSWVPAVGLTLVPSLGGFMGAYFVRGEGLRWYASLQKPSWHPPRWTLAPIWGTLYSAMGYGSYIIWKELGGFTEEAMVPLGLYTGQLALNWAWPPIFFGARQMGWALVDLMLVSGVATATTLAWHRVSPPAARLLYPYLAWLAFATMLNYYVWRDNSGRRGGSRLTE | null | null | adrenal gland development [GO:0030325]; behavioral response to pain [GO:0048266]; cellular hypotonic response [GO:0071476]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to zinc ion [GO:0071294]; chloride transport [GO:0006821]; cholesterol homeostasis [GO:0042632]; contact inhibition [GO:0060... | cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739] | androgen binding [GO:0005497]; benzodiazepine receptor activity [GO:0008503]; cholesterol binding [GO:0015485]; transmembrane transporter binding [GO:0044325] | PF03073; | 1.20.1260.100; | TspO/BZRP family | PTM: The N-terminus is blocked. | SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Membrane {ECO:0000269|PubMed:2555358}; Multi-pass membrane protein {ECO:0000269|PubMed:2555358}. | null | null | null | null | null | FUNCTION: Promotes the transport of cholesterol across mitochondrial membranes and may play a role in lipid metabolism, but its precise physiological role is controversial. It is apparently not required for steroid hormone biosynthesis (By similarity). Can bind protoporphyrin IX and may play a role in the transport of ... | Rattus norvegicus (Rat) |
P16258 | OSBP1_RABIT | MAATELRGVVGPGPAAIAAPGGGGAGPPVVGGGGGGRGDAGPGSGAASGTVAAAAAGGQGPGAGGVAAAAGPAPTPPAGGSGSSGTGGSGSAREGWLFKWTNYIKGYQRRWFVLSNGLLSYYRSKAEMRHTCRGTINLATANITVEDSCNFIISNGGAQTYHLKASSEVERQRWVTALELAKAKAVKMLAESDESGDEESVSQTDKTELQNTLRTLSSKVEDLSTCNDLIAKHGTALQRSLSELESLKLPAESNEKIKQVNERATLFRITSNAMINACRDFLVLAQTHSKKWQKSLQYERDQRIRLEETLEQLAKQHNHL... | null | null | intracellular cholesterol transport [GO:0032367]; sterol transport [GO:0015918] | cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139]; perinuclear endoplasmic reticulum [GO:0097038]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; trans-Golgi network [GO:0005802] | cholesterol binding [GO:0015485]; phosphatidylinositol-4-phosphate binding [GO:0070273]; sterol transfer activity [GO:0120015] | PF01237;PF00169; | 2.40.160.120;2.30.29.30; | OSBP family | PTM: The N-terminus is blocked. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P22059}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P22059}. Golgi apparatus membrane {ECO:0000250|UniProtKB:P22059}; Peripheral membrane protein {ECO:0000250|UniProtKB:P22059}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P22059}; Perip... | null | null | null | null | null | FUNCTION: Lipid transporter involved in lipid countertransport between the Golgi complex and membranes of the endoplasmic reticulum: specifically exchanges sterol with phosphatidylinositol 4-phosphate (PI4P), delivering sterol to the Golgi in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatase in the en... | Oryctolagus cuniculus (Rabbit) |
P16259 | CAN3_RAT | MPTVISPTVAPRTGAEPRSPGPVPHPAQGKTTEAGGGHPGGIYSAIISRNFPIIGVKEKTFEQLHKKCLEKKVLYLDPEFPPDETSLFYSQKFPIQFVWKRPPEICENPRFIIGGANRTDICQGDLGDCWLLAAIACLTLNERLLFRVIPHDQSFTENYAGIFHFQFWRYGDWVDVVIDDCLPTYNNQLVFTKSNHRNEFWSALLEKAYAKLHGSYEALKGGNTTEAMEDFTGGVTEFFEIKDAPSDMYKIMRKAIERGSLMGCSIDDGTNMTYGTSPSGLNMGELIARMVRNMDNSLLRDSDLDPRASDDRPSRTIVPV... | 3.4.22.54 | null | calcium-dependent self proteolysis [GO:1990092]; cellular response to calcium ion [GO:0071277]; cellular response to salt stress [GO:0071472]; G1 to G0 transition involved in cell differentiation [GO:0070315]; muscle structure development [GO:0061061]; myofibril assembly [GO:0030239]; negative regulation of apoptotic p... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; myofibril [GO:0030016]; nucleolus [GO:0005730]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991]; T-tubule [GO:0030315]; Z disc [GO:0030018] | calcium ion binding [GO:0005509]; calcium-dependent cysteine-type endopeptidase activity [GO:0004198]; catalytic activity [GO:0003824]; enzyme binding [GO:0019899]; ligase regulator activity [GO:0055103]; molecular adaptor activity [GO:0060090]; peptidase activity [GO:0008233]; signaling receptor binding [GO:0005102]; ... | PF01067;PF16648;PF13405;PF13833;PF00648; | 2.60.120.380;3.90.70.10;1.10.238.10; | Peptidase C2 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P20807}. Nucleus, nucleolus {ECO:0000250|UniProtKB:P20807}. | CATALYTIC ACTIVITY: Reaction=Broad endopeptidase activity.; EC=3.4.22.54; | null | null | null | null | FUNCTION: Calcium-regulated non-lysosomal thiol-protease. Proteolytically cleaves CTBP1 at 'His-399'. Mediates, with UTP25, the proteasome-independent degradation of p53/TP53. {ECO:0000250|UniProtKB:P20807}. | Rattus norvegicus (Rat) |
P16262 | COX1_BACP3 | MSTIARKKGVGAVLWDYLTTVDHKKIAHLYLISGGFFFLLGGLEALFIRIQLAKPNNDFLVGGLYNEVLTMHGTTMIFLAAMPLVFAFMNAVVPLQIGARDVAFPFLNALGFWMFFFGGLFLNCSWFLGGAPDAGWTSYASLSLDSKAHHGIDFYTLGLQISGFGTIMGAINFLVTIINMRAPGMTFMRMPMFTWATFVTSALILFAFPPLTVGLIFMMMDRLFGGNFFNPAAGGNTIIWEHLFWVFGHPEVYILVLPAFGIFSEIFATFSRKRLFGYSSMVFATVLIAFLGFMVWAHHMFTVGMGPIANAIFAVATMTI... | 7.1.1.9 | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Note=Binds 1 copper B ion per subunit.; COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Note=Binds 2 heme groups per subunit.; | electron transport coupled proton transport [GO:0015990]; oxidative phosphorylation [GO:0006119]; respiratory electron transport chain [GO:0022904] | plasma membrane [GO:0005886]; respirasome [GO:0070469] | cytochrome-c oxidase activity [GO:0004129]; heme binding [GO:0020037]; metal ion binding [GO:0046872] | PF00115; | 1.10.287.70;1.20.210.10; | Heme-copper respiratory oxidase family | null | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. | CATALYTIC ACTIVITY: Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-[cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436, Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=7.1.1.9; | null | PATHWAY: Energy metabolism; oxidative phosphorylation. | null | null | FUNCTION: Cytochrome c oxidase is the component of the respiratory chain that catalyzes the reduction of oxygen to water. Subunits 1-3 form the functional core of the enzyme complex. Co I is the catalytic subunit of the enzyme. Electrons originating in cytochrome c are transferred via the copper A center of subunit 2 a... | Bacillus sp. (strain PS3) |
P16275 | IFEB_HELPO | TSKISTTYEEEGRQSKIQPRAFVITRSGPTSRSSSYSARQSYGSRSSITPGVYQQLSSSGITDFRGTREKEKREMQNLNERLAGYIEKVHFLDAQVKKLEAENEALRNRKSESLQPIRDAYENELAQARKVIDELSSTKGVSEAKVAGLQDEIASLRELIGTYENQSKDYRKKIESLGNQIGEYEGELHTLRIRCGSLEDENAKVRELLDKIQDQNRRLRADLDTETSAHIEADCLAQTKTEECEFYKDLLDQLELLKPEPMQIKGMDYAEFWKSELSKCVRDIQSAYDEKIDIIQQDIEAKYSSQINSLRSGNVKDGMQ... | null | null | heterochromatin formation [GO:0031507]; nuclear envelope organization [GO:0006998]; nuclear migration [GO:0007097]; nuclear pore localization [GO:0051664]; protein localization to nuclear envelope [GO:0090435] | cytoplasm [GO:0005737]; intermediate filament [GO:0005882]; nuclear envelope [GO:0005635]; nuclear lamina [GO:0005652] | structural constituent of cytoskeleton [GO:0005200] | PF00038; | 1.20.5.170;1.20.5.1160; | Intermediate filament family | null | SUBCELLULAR LOCATION: Cytoplasm. | null | null | null | null | null | FUNCTION: Epithelial intermediate filament protein. | Helix pomatia (Roman snail) (Edible snail) |
P16276 | ACON_PIG | MAPYSLLVTRLQKALGVRQYHVASVLCQRAKVAMSHFEPHEYIRYDLLEKNIDIVRKRLNRPLTLSEKIVYGHLDDPANQEIERGKTYLRLRPDRVAMQDATAQMAMLQFISSGLPKVAVPSTIHCDHLIEAQLGGEKDLRRAKDINQEVYNFLATAGAKYGVGFWRPGSGIIHQIILENYAYPGVLLIGTDSHTPNGGGLGGICIGVGGADAVDVMAGIPWELKCPKVIGVKLTGSLSGWTSPKDVILKVAGILTVKGGTGAIVEYHGPGVDSISCTGMATICNMGAEIGATTSVFPYNHRMKKYLSKTGRADIANLAD... | 4.2.1.3 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000269|PubMed:10631981, ECO:0000269|PubMed:2726740, ECO:0000269|PubMed:27818104}; Note=Binds 1 [4Fe-4S] cluster per subunit. Binding of a [3Fe-4S] cluster leads to an inactive enzyme. {ECO:0000269|PubMed:10631981, ECO:0000269|PubMed:2726740}; | tricarboxylic acid cycle [GO:0006099] | cytosol [GO:0005829]; mitochondrion [GO:0005739] | 4 iron, 4 sulfur cluster binding [GO:0051539]; aconitate hydratase activity [GO:0003994]; metal ion binding [GO:0046872] | PF00330;PF00694; | 3.40.1060.10;3.30.499.10;3.20.19.10; | Aconitase/IPM isomerase family | PTM: Forms covalent cross-links mediated by transglutaminase TGM2, between a glutamine and the epsilon-amino group of a lysine residue, forming homopolymers and heteropolymers. {ECO:0000250|UniProtKB:Q9ER34}. | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:2303429}. | CATALYTIC ACTIVITY: Reaction=citrate = D-threo-isocitrate; Xref=Rhea:RHEA:10336, ChEBI:CHEBI:15562, ChEBI:CHEBI:16947; EC=4.2.1.3; Evidence={ECO:0000269|PubMed:10631981}; | null | PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 2/2. | null | null | FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-aconitate. {ECO:0000269|PubMed:10631981}. | Sus scrofa (Pig) |
P16277 | BLK_MOUSE | MGLLSSKRQVSEKGKGWSPVKIRTQDKAPPPLPPLVVFNHLAPPSPNQDPDEEERFVVALFDYAAVNDRDLQVLKGEKLQVLRSTGDWWLARSLVTGREGYVPSNFVAPVETLEVEKWFFRTISRKDAERQLLAPMNKAGSFLIRESESNKGAFSLSVKDITTQGEVVKHYKIRSLDNGGYYISPRITFPTLQALVQHYSKKGDGLCQKLTLPCVNLAPKNLWAQDEWEIPRQSLKLVRKLGSGQFGEVWMGYYKNNMKVAIKTLKEGTMSPEAFLGEANVMKTLQHERLVRLYAVVTREPIYIVTEYMARGCLLDFLKT... | 2.7.10.2 | null | B cell receptor signaling pathway [GO:0050853]; cell differentiation [GO:0030154]; innate immune response [GO:0045087]; peptidyl-tyrosine phosphorylation [GO:0018108]; positive regulation of insulin secretion [GO:0032024]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169] | cytosol [GO:0005829]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234] | ATP binding [GO:0005524]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein tyrosine kinase activity [GO:0004713]; signaling receptor binding [GO:0005102] | PF07714;PF00017;PF00018; | 3.30.505.10;2.30.30.40;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, SRC subfamily | PTM: Phosphorylated on tyrosine residues after antibody-mediated surface engagement of the B-cell antigen receptor (BCR).; PTM: Ubiquitination of activated BLK by the UBE3A ubiquitin protein ligase leads to its degradation by the ubiquitin-proteasome pathway. {ECO:0000269|PubMed:10449731}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Note=Present and active in lipid rafts (By similarity). Membrane location is required for the phosphorylation of CD79A and CD79B. {ECO:0000250, ECO:0000269|PubMed:7592958}. | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; | null | null | null | null | FUNCTION: Non-receptor tyrosine kinase involved in B-lymphocyte development, differentiation and signaling. B-cell receptor (BCR) signaling requires a tight regulation of several protein tyrosine kinases and phosphatases, and associated coreceptors (PubMed:12563261, PubMed:14662906, PubMed:2404338, PubMed:7608542, PubM... | Mus musculus (Mouse) |
P16278 | BGAL_HUMAN | MPGFLVRILPLLLVLLLLGPTRGLRNATQRMFEIDYSRDSFLKDGQPFRYISGSIHYSRVPRFYWKDRLLKMKMAGLNAIQTYVPWNFHEPWPGQYQFSEDHDVEYFLRLAHELGLLVILRPGPYICAEWEMGGLPAWLLEKESILLRSSDPDYLAAVDKWLGVLLPKMKPLLYQNGGPVITVQVENEYGSYFACDFDYLRFLQKRFRHHLGDDVVLFTTDGAHKTFLKCGALQGLYTTVDFGTGSNITDAFLSQRKCEPKGPLINSEFYTGWLDHWGQPHSTIKTEAVASSLYDILARGASVNLYMFIGGTNFAYWNGA... | 3.2.1.23 | null | carbohydrate metabolic process [GO:0005975]; galactose catabolic process [GO:0019388]; glycosphingolipid catabolic process [GO:0046479]; heparan sulfate proteoglycan catabolic process [GO:0030200]; keratan sulfate catabolic process [GO:0042340]; response to cortisone [GO:0051413]; response to Thyroglobulin triiodothyro... | azurophil granule lumen [GO:0035578]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; ficolin-1-rich granule lumen [GO:1904813]; Golgi apparatus [GO:0005794]; intracellular membrane-bounded organelle [GO:0043231]; lysosomal lumen [GO:0043202]; perinuclear region of cytopla... | beta-galactosidase activity [GO:0004565]; galactoside binding [GO:0016936]; protein homodimerization activity [GO:0042803] | PF21317;PF21467;PF01301; | 2.60.120.260;3.20.20.80; | Glycosyl hydrolase 35 family | null | SUBCELLULAR LOCATION: [Isoform 1]: Lysosome {ECO:0000269|PubMed:2511208, ECO:0000269|PubMed:3084261}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, perinuclear region {ECO:0000269|PubMed:2511208}. Note=Localized to the perinuclear area of the cytoplasm but not to lysosomes. {ECO:0000269|PubMed:2511208}. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.; EC=3.2.1.23; Evidence={ECO:0000269|PubMed:15714521, ECO:0000269|PubMed:19472408, ECO:0000269|PubMed:24737316, ECO:0000269|PubMed:2511208, ECO:0000269|PubMed:25936995, ECO:0000269|PubMed:3143362, ECO:00002... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5-5.5.; | null | FUNCTION: [Isoform 1]: Cleaves beta-linked terminal galactosyl residues from gangliosides, glycoproteins, and glycosaminoglycans. {ECO:0000269|PubMed:15714521, ECO:0000269|PubMed:19472408, ECO:0000269|PubMed:2511208, ECO:0000269|PubMed:25936995, ECO:0000269|PubMed:8200356}.; FUNCTION: [Isoform 2]: Has no beta-galactosi... | Homo sapiens (Human) |
P16283 | B3A3_MOUSE | MANGVIPPPGGASPLPQVRVPLEEPPLGPDVEEEDDDLGKTLAVSRFGDLISKTPAWDPEKPSRSYSERDFEFHRHTSHHTHHPLSARLPPPHKLRRPPPTSARHTRRKRKKEKTSAPPSEGTPPIQEEGGAGAEEEEEEEEEEEGESEAEPVEPLPPGPPQKAKFSIGSDEDDSPGLPVKAPCAKALPSVGLQSDQSPQRSGSSPSPRARASRISTEKSRPWSPSASYDLRERLCPGSALGNPGPEQRVPTDEAEAQMLGSADLDDMKSHRLEDNPGVRRHLVKKPSRIQGGRGSPSGLAPILRRKKKKKKLDRRPHEV... | null | null | bicarbonate transport [GO:0015701]; cardiac conduction [GO:0061337]; pH reduction [GO:0045851]; regulation of cardiac muscle cell action potential [GO:0098901]; regulation of intracellular pH [GO:0051453]; transmembrane transport [GO:0055085] | external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886] | chloride:bicarbonate antiporter activity [GO:0140900]; enzyme binding [GO:0019899]; transmembrane transporter activity [GO:0022857] | PF07565;PF00955; | 1.10.287.570; | Anion exchanger (TC 2.A.31) family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2686841}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=chloride(out) + hydrogencarbonate(in) = chloride(in) + hydrogencarbonate(out); Xref=Rhea:RHEA:72363, ChEBI:CHEBI:17544, ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:2686841}; | null | null | null | null | FUNCTION: Sodium-independent anion exchanger which mediates the electroneutral exchange of chloride for bicarbonate ions across the cell membrane. May be involved in the regulation of intracellular pH, and the modulation of cardiac action potential (By similarity). {ECO:0000250|UniProtKB:P48751, ECO:0000269|PubMed:2686... | Mus musculus (Mouse) |
P16284 | PECA1_HUMAN | MQPRWAQGATMWLGVLLTLLLCSSLEGQENSFTINSVDMKSLPDWTVQNGKNLTLQCFADVSTTSHVKPQHQMLFYKDDVLFYNISSMKSTESYFIPEVRIYDSGTYKCTVIVNNKEKTTAEYQVLVEGVPSPRVTLDKKEAIQGGIVRVNCSVPEEKAPIHFTIEKLELNEKMVKLKREKNSRDQNFVILEFPVEEQDRVLSFRCQARIISGIHMQTSESTKSELVTVTESFSTPKFHISPTGMIMEGAQLHIKCTIQVTHLAQEFPEIIIQKDKAIVAHNRHGNKAVYSVMAMVEHSGNYTCKVESSRISKVSSIVVN... | null | null | bicellular tight junction assembly [GO:0070830]; cell recognition [GO:0008037]; cell surface receptor signaling pathway [GO:0007166]; cell-cell adhesion [GO:0098609]; cell-cell adhesion via plasma-membrane adhesion molecules [GO:0098742]; diapedesis [GO:0050904]; establishment of endothelial barrier [GO:0061028]; glome... | cell-cell junction [GO:0005911]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]; platelet alpha granule membrane [GO:0031092]; protein-containing complex [GO:0032991]; secretory granule membran... | protein homodimerization activity [GO:0042803]; transmembrane signaling receptor activity [GO:0004888] | PF13895;PF13927;PF17736; | 2.60.40.10; | null | PTM: Phosphorylated on Ser and Tyr residues after cellular activation by src kinases (PubMed:18710921, PubMed:19342684, PubMed:21464369, PubMed:9298995). Upon activation, phosphorylated on Ser-729 which probably initiates the dissociation of the membrane-interaction segment (residues 709-729) from the cell membrane all... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17580308}; Single-pass type I membrane protein {ECO:0000305}. Note=Cell surface expression on neutrophils is down-regulated upon fMLP or CXCL8/IL8-mediated stimulation. {ECO:0000269|PubMed:17580308}.; SUBCELLULAR LOCATION: [Isoform Long]: Cell membrane {ECO:000026... | null | null | null | null | null | FUNCTION: Cell adhesion molecule which is required for leukocyte transendothelial migration (TEM) under most inflammatory conditions (PubMed:17580308, PubMed:19342684). Tyr-690 plays a critical role in TEM and is required for efficient trafficking of PECAM1 to and from the lateral border recycling compartment (LBRC) an... | Homo sapiens (Human) |
P16286 | PHOSP_RABVS | MSKIFVNPSAIRAGLADLEMAEETVDLINRNIEDNQAHLQGEPIEVDNLPEDMGRLHLDDGKSPNHGEIAKVGEGKYREDFQMDEGEDPSFLFQSYLENVGVQIVRQMRSGERFLKIWSQTVEEIISYVAVNFPNPPGKSSEDKSTQTTGRELKKETTPTPSQRESQSSKARMAAQIASGPPALEWSATNEEDDLSVEAEIAHQIAESFSKKYKFPSRSSGILLYNFEQLKMNLDDIVKEAKNVPGVTRLAHDGSKLPLRCVLGWVALANSKKFQLLVESDKLSKIMQDDLNRYTSC | null | null | microtubule-dependent intracellular transport of viral material towards nucleus [GO:0075521]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of TBK1 activity [GO:0039723]; symbiont-mediated suppression of host J... | host cell [GO:0043657]; host cell cytoplasm [GO:0030430]; host cell nucleus [GO:0042025]; virion component [GO:0044423] | RNA-dependent RNA polymerase activity [GO:0003968] | PF03012; | 6.10.140.1560;1.20.120.820; | Lyssavirus protein P family | PTM: Phosphorylated by host PKC and by an unknown kinase. {ECO:0000250}. | SUBCELLULAR LOCATION: [Phosphoprotein]: Virion. Host cytoplasm {ECO:0000269|PubMed:36640307}.; SUBCELLULAR LOCATION: [Isoform P2]: Host cytoplasm {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform P3]: Host nucleus {ECO:0000250}.; SUBCELLULAR LOCATION: [Isoform P5]: Host nucleus {ECO:0000250}. | null | null | null | null | null | FUNCTION: Non catalytic polymerase cofactor and regulatory protein that plays a role in viral transcription and replication. Stabilizes the RNA polymerase L to the N-RNA template and binds the soluble protein N, preventing it from encapsidating non-genomic RNA. Also inhibits host IFN-alpha and IFN-beta signaling by bin... | Rabies virus (strain SAD B19) (RABV) |
P16287 | MATRX_RABVS | MNLLRKIVKNRRDEDTQKSSPASAPLDDDDLWLPPPEYVPLKELTGKKNMRNFCINGRVKVCSPNGYSFRILRHILKSFDEIYSGNHRMIGLVKVVIGLALSGSPVPEGLNWVYKLRRTFIFQWADSRGPLEGEELEYSQEITWDDDTEFVGLQIRVIAKQCHIQGRVWCINMNPRACQLWSDMSLQTQRSEEDKDSSLLLE | null | null | negative regulation of viral transcription [GO:0032897]; viral budding via host ESCRT complex [GO:0039702] | host cell cytoplasm [GO:0030430]; host cell endomembrane system [GO:0033645]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | structural constituent of virion [GO:0039660] | PF04785; | 3.10.460.20; | Lyssavirus matrix protein family | null | SUBCELLULAR LOCATION: Virion membrane; Peripheral membrane protein. Host endomembrane system; Peripheral membrane protein. Host cytoplasm {ECO:0000269|PubMed:33208464}. | null | null | null | null | null | FUNCTION: Plays a major role in assembly, budding and uncoating of virion after membrane fusion (PubMed:33208464). Completely covers the ribonucleoprotein coil and keep it in condensed bullet-shaped form. Inhibits viral transcription and stimulates replication. Plays a major role in early induction of TRAIL-mediated ap... | Rabies virus (strain SAD B19) (RABV) |
P16289 | L_RABVS | MLDPGEVYDDPIDPIELEAEPRGTPIVPNILRNSDYNLNSPLIEDPARLMLEWLKTGNRPYRMTLTDNCSRSFRVLKDYFKKVDLGSLKVGGMAAQSMISLWLYGAHSESNRSRRCITDLAHFYSKSSPIEKLLNLTLGNRGLRIPPEGVLSCLERVDYDNAFGRYLANTYSSYLFFHVITLYMNALDWDEEKTILALWKDLTSVDIGKDLVKFKDQIWGLLIVTKDFVYSQSSNCLFDRNYTLMLKDLFLSRFNSLMVLLSPPEPRYSDDLISQLCQLYIAGDQVLSMCGNSGYEVIKILEPYVVNSLVQRAEKFRPLI... | 2.1.1.375; 2.7.7.48; 2.7.7.88; 3.6.1.- | null | negative stranded viral RNA replication [GO:0039689] | host cell cytoplasm [GO:0030430]; virion component [GO:0044423] | ATP binding [GO:0005524]; GTPase activity [GO:0003924]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; RNA-dependent RNA polymerase activity [GO:0003968] | PF21080;PF14314;PF21081;PF14318;PF00946; | null | Rhabdoviruses protein L family | null | SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P03523}. Host cytoplasm {ECO:0000250|UniProtKB:P03523}. Note=L and P are packaged asymmetrically towards the blunt end of the virus. {ECO:0000250|UniProtKB:P03523}. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=a 5'-end... | null | null | null | null | FUNCTION: RNA-directed RNA polymerase that catalyzes the transcription of viral mRNAs, their capping and polyadenylation. The template is composed of the viral RNA tightly encapsidated by the nucleoprotein (N). The viral polymerase binds to the genomic RNA at the 3' leader promoter, and transcribes subsequently all vir... | Rabies virus (strain SAD B19) (RABV) |
P16290 | PGAM2_RAT | MATHRLVMVRHGESSWNQENRFCGWFDAELSEKGAEEAKRGATAIKDAKIEFDICYTSVLKRAIRTLWTILDVTDQMWVPVVRTWRLNERHYGGLTGLNKAETAAKHGEEQVKIWRRSFDTPPPPMDEKHNYYASISKDRRYAGLKPEELPTCESLKDTIARALPFWNEEIAPKIKAGKRVLIAAHGNSLRGIVKHLEGMSDQAIMELNLPTGIPIVYELNQELKPTKPMRFLGDEETVRKAMEAVAAQGKAK | 5.4.2.11; 5.4.2.4 | null | canonical glycolysis [GO:0061621]; gluconeogenesis [GO:0006094]; glycolytic process [GO:0006096]; Notch signaling pathway [GO:0007219]; response to inorganic substance [GO:0010035]; response to mercury ion [GO:0046689]; spermatogenesis [GO:0007283]; striated muscle contraction [GO:0006941] | cytosol [GO:0005829] | 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity [GO:0046538]; bisphosphoglycerate mutase activity [GO:0004082]; hydrolase activity [GO:0016787]; identical protein binding [GO:0042802]; phosphoglycerate mutase activity [GO:0004619] | PF00300; | 3.40.50.1240; | Phosphoglycerate mutase family, BPG-dependent PGAM subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate; Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289; EC=5.4.2.11; Evidence={ECO:0000250|UniProtKB:P18669}; CATALYTIC ACTIVITY: Reaction=(2R)-3-phospho-glyceroyl phosphate = (2R)-2,3-bisphosphoglycerate + H(+); Xref=Rhea:RHEA:17765, C... | null | null | null | null | FUNCTION: Interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase), but with a reduced activity. | Rattus norvegicus (Rat) |
P16293 | FA9_PIG | YNSGKLEESFVRGNLERECIEEKCSFEEAREVFENTEKTNEFWKQYVDGDQCEPNPCLNGGLCKDDINSYECWCQVGFEGKNCELDATCNIKNGRCKQFCKTGADSKVLCSCTTGYRLAPDQKSCKPAVPFPCGRVSVSHSPTTLTRAEIIFSNMDYENSTEVEPILDSLTESNQSSDDFIRIVGGENAKPGQFPWQVLLNGKIDAFCGGSIINEKWVVTAAHCIEPGVKITVVAGEYNTEETEPTEQRRNVIRAIPHHSYNATVNKYSHDIALLELDEPLTLNSYVTPICIADKEYTNIFLKFGSGYVSGWGRVFNRGR... | 3.4.21.22 | null | blood coagulation [GO:0007596]; proteolysis [GO:0006508]; zymogen activation [GO:0031638] | extracellular space [GO:0005615] | calcium ion binding [GO:0005509]; endopeptidase activity [GO:0004175]; serine-type endopeptidase activity [GO:0004252] | PF00008;PF14670;PF00594;PF00089; | 4.10.740.10;2.10.25.10;2.40.10.10; | Peptidase S1 family | PTM: Activated by factor XIa, which excises the activation peptide. The propeptide can also be removed by snake venom protease. {ECO:0000250|UniProtKB:P00740}.; PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000250|UniProtKB:P00740}... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P00740}. | CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa.; EC=3.4.21.22; Evidence={ECO:0000250|UniProtKB:P00740}; | null | null | null | null | FUNCTION: Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholipids, and factor VIIIa. {ECO:0000250|UniProtKB:P00740}. | Sus scrofa (Pig) |
P16294 | FA9_MOUSE | MKHLNTVMAESPALITIFLLGYLLSTECAVFLDRENATKILTRPKRYNSGKLEEFVRGNLERECIEERCSFEEAREVFENTEKTTEFWKQYVDGDQCESNPCLNGGICKDDISSYECWCQVGFEGRNCELDATCNIKNGRCKQFCKNSPDNKVICSCTEGYQLAEDQKSCEPTVPFPCGRASISYSSKKITRAETVFSNMDYENSTEAVFIQDDITDGAILNNVTESSESLNDFTRVVGGENAKPGQIPWQVILNGEIEAFCGGAIINEKWIVTAAHCLKPGDKIEVVAGEYNIDKKEDTEQRRNVIRTIPHHQYNATIN... | 3.4.21.22 | null | blood coagulation [GO:0007596]; zymogen activation [GO:0031638] | extracellular space [GO:0005615] | calcium ion binding [GO:0005509]; endopeptidase activity [GO:0004175]; peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252] | PF00008;PF14670;PF00594;PF00089; | 4.10.740.10;2.10.25.10;2.40.10.10; | Peptidase S1 family | PTM: Activated by factor XIa, which excises the activation peptide. The propeptide can also be removed by snake venom protease. {ECO:0000250|UniProtKB:P00740}.; PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000250|UniProtKB:P00740}... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P00740}. | CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa.; EC=3.4.21.22; Evidence={ECO:0000250|UniProtKB:P00740}; | null | null | null | null | FUNCTION: Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholipids, and factor VIIIa. {ECO:0000250|UniProtKB:P00740}. | Mus musculus (Mouse) |
P16296 | FA9_RAT | MADAPGLIPIFLLGYLLSTECAVFLDRENATKILTRPKRYNSGKLEEFVQGNLERECIEERCSFEEAREVFENTEKTTEFWKQYVDGDQCESNPCLNGGICKDDINSYECWCQAGFEGRNCELDATCSIKNGRCKQFCKNSPDNKIICSCTEGYQLAEDQKSCEPAVPFPCGRVSVAYNSKKITRAETVFSNTDYGNSTELILDDITNSTILDNLTENSEPINDFTRVVGGENAKPGQIPWQVILNGEIEAFCGGAIINEKWIVTAAHCLKPGDKIEVVAGEHNIDEKEDTEQRRNVIRTIPHHQYNATINKYSHDIALL... | 3.4.21.22 | null | blood coagulation [GO:0007596]; proteolysis [GO:0006508]; zymogen activation [GO:0031638] | extracellular space [GO:0005615] | calcium ion binding [GO:0005509]; endopeptidase activity [GO:0004175]; metal ion binding [GO:0046872]; peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252] | PF00008;PF14670;PF00594;PF00089; | 4.10.740.10;2.10.25.10;2.40.10.10; | Peptidase S1 family | PTM: Activated by factor XIa, which excises the activation peptide. The propeptide can also be removed by snake venom protease. {ECO:0000250|UniProtKB:P00740}.; PTM: The iron and 2-oxoglutarate dependent 3-hydroxylation of aspartate and asparagine is (R) stereospecific within EGF domains. {ECO:0000250|UniProtKB:P00740}... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P00740}. | CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa.; EC=3.4.21.22; Evidence={ECO:0000250|UniProtKB:P00740}; | null | null | null | null | FUNCTION: Factor IX is a vitamin K-dependent plasma protein that participates in the intrinsic pathway of blood coagulation by converting factor X to its active form in the presence of Ca(2+) ions, phospholipids, and factor VIIIa. {ECO:0000250|UniProtKB:P00740}. | Rattus norvegicus (Rat) |
P16297 | IL2RB_MOUSE | MATIALPWSLSLYVFLLLLATPWASAAVKNCSHLECFYNSRANVSCMWSHEEALNVTTCHVHAKSNLRHWNKTCELTLVRQASWACNLILGSFPESQSLTSVDLLDINVVCWEEKGWRRVKTCDFHPFDNLRLVAPHSLQVLHIDTQRCNISWKVSQVSHYIEPYLEFEARRRLLGHSWEDASVLSLKQRQQWLFLEMLIPSTSYEVQVRVKAQRNNTGTWSPWSQPLTFRTRPADPMKEILPMSWLRYLLLVLGCFSGFFSCVYILVKCRYLGPWLKTVLKCHIPDPSEFFSQLSSQHGGDLQKWLSSPVPLSFFSPSG... | null | null | cytokine-mediated signaling pathway [GO:0019221]; immunoglobulin mediated immune response [GO:0016064]; interleukin-15-mediated signaling pathway [GO:0035723]; interleukin-2-mediated signaling pathway [GO:0038110]; negative regulation of apoptotic process [GO:0043066]; positive regulation of phagocytosis [GO:0050766] | cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886] | coreceptor activity [GO:0015026]; cytokine receptor activity [GO:0004896]; interleukin-15 receptor activity [GO:0042010]; interleukin-2 binding [GO:0019976]; interleukin-2 receptor activity [GO:0004911] | PF18707; | 2.60.40.10; | Type I cytokine receptor family, Type 4 subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P14784}; Single-pass type I membrane protein {ECO:0000255}. Cell surface {ECO:0000250|UniProtKB:P14784}. | null | null | null | null | null | FUNCTION: Receptor for interleukin-2. This beta subunit is involved in receptor mediated endocytosis and transduces the mitogenic signals of IL2. Probably in association with IL15RA, involved in the stimulation of neutrophil phagocytosis by IL15 (By similarity). {ECO:0000250|UniProtKB:P14784}. | Mus musculus (Mouse) |
P16298 | PP2BB_HUMAN | MAAPEPARAAPPPPPPPPPPPGADRVVKAVPFPPTHRLTSEEVFDLDGIPRVDVLKNHLVKEGRVDEEIALRIINEGAAILRREKTMIEVEAPITVCGDIHGQFFDLMKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWVLKILYPSTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYEACMEAFDSLPLAALLNQQFLCVHGGLSPEIHTLDDIRRLDRFKEPPAFGPMCDLLWSDPSEDFGNEKSQEHFSHNTVRGCSYFYNYPAVCEFLQNNNLLSIIRAHEAQDAGYRMYRKSQTTGFPSLITIFSAPNY... | 3.1.3.16 | COFACTOR: Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence={ECO:0000269|PubMed:26794871}; Note=Binds 1 Fe(3+) ion per subunit. {ECO:0000269|PubMed:26794871}; COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:26794871}; Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:26794871}; | axon extension [GO:0048675]; calcineurin-mediated signaling [GO:0097720]; calcineurin-NFAT signaling cascade [GO:0033173]; calcium-ion regulated exocytosis [GO:0017156]; dephosphorylation [GO:0016311]; heart development [GO:0007507]; learning [GO:0007612]; locomotion involved in locomotory behavior [GO:0031987]; lympha... | calcineurin complex [GO:0005955]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; glutamatergic synapse [GO:0098978]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; protein serine/threonine phosphatase complex [GO:0008287]; T-tubule [GO:0030315]; Z disc [GO:0030018] | calcium ion binding [GO:0005509]; calmodulin binding [GO:0005516]; calmodulin-dependent protein phosphatase activity [GO:0033192]; enzyme binding [GO:0019899]; myosin phosphatase activity [GO:0017018]; protein dimerization activity [GO:0046983]; protein phosphatase 2B binding [GO:0030346]; protein serine/threonine phos... | PF00149; | 3.60.21.10; | PPP phosphatase family, PP-2B subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19154138}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000269|PubMed:19154138, ECO:0000269|PubMed:25720963, EC... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.69 uM for NFATC1 {ECO:0000269|PubMed:19154138}; KM=0.7 uM for DARPP32 {ECO:0000269|PubMed:19154138}; | null | null | null | FUNCTION: Calcium-dependent, calmodulin-stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca(2+)-mediated signals (PubMed:19154138, PubMed:25720963, PubMed:26794871, PubMed:32753672). Dephosphorylates TFEB in response to lysosomal Ca(2+) release, resulting in TFEB nuclear... | Homo sapiens (Human) |
P16301 | LCAT_MOUSE | MGLPGSPWQRVLLLLGLLLPPATPFWLLNVLFPPHTTPKAELSNHTRPVILVPGCLGNRLEAKLDKPDVVNWMCYRKTEDFFTIWLDFNLFLPLGVDCWIDNTRIVYNHSSGRVSNAPGVQIRVPGFGKTESVEYVDDNKLAGYLHTLVQNLVNNGYVRDETVRAAPYDWRLAPHQQDEYYKKLAGLVEEMYAAYGKPVFLIGHSLGCLHVLHFLLRQPQSWKDHFIDGFISLGAPWGGSIKAMRILASGDNQGIPILSNIKLKEEQRITTTSPWMLPAPHVWPEDHVFISTPNFNYTVQDFERFFTDLHFEEGWHMFLQ... | 2.3.1.43; 3.1.1.47 | null | cholesterol homeostasis [GO:0042632]; cholesterol metabolic process [GO:0008203]; cholesterol transport [GO:0030301]; high-density lipoprotein particle remodeling [GO:0034375]; lipid metabolic process [GO:0006629]; lipoprotein biosynthetic process [GO:0042158]; lipoprotein metabolic process [GO:0042157]; phosphatidylch... | extracellular space [GO:0005615]; high-density lipoprotein particle [GO:0034364] | 1-alkyl-2-acetylglycerophosphocholine esterase activity [GO:0003847]; apolipoprotein A-I binding [GO:0034186]; phosphatidylcholine-sterol O-acyltransferase activity [GO:0004607]; phospholipase A2 activity [GO:0004623]; platelet-activating factor acetyltransferase activity [GO:0047179]; sterol esterase activity [GO:0004... | PF02450; | 3.40.50.1820; | AB hydrolase superfamily, Lipase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:19065001, ECO:0000269|PubMed:8820107}. Note=Secreted into blood plasma (PubMed:8820107). Produced in astrocytes and secreted into cerebral spinal fluid (CSF) (By similarity). {ECO:0000250|UniProtKB:P04180, ECO:0000269|PubMed:8820107}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + a sterol = a 1-acyl-sn-glycero-3-phosphocholine + a sterol ester; Xref=Rhea:RHEA:21204, ChEBI:CHEBI:15889, ChEBI:CHEBI:35915, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=2.3.1.43; Evidence={ECO:0000255|PROSITE-ProRule:PRU10037, ECO:0000269|PubMed:1565... | null | null | null | null | FUNCTION: Central enzyme in the extracellular metabolism of plasma lipoproteins. Synthesized mainly in the liver and secreted into plasma where it converts cholesterol and phosphatidylcholines (lecithins) to cholesteryl esters and lysophosphatidylcholines on the surface of high and low density lipoproteins (HDLs and LD... | Mus musculus (Mouse) |
P16303 | EST1D_RAT | MRLYPLVWLFLAACTAWGYPSSPPVVNTVKGKVLGKYVNLEGFAQPVAVFLGIPFAKPPLGSLRFAPPQPAEPWNFVKNTTSYPPMCSQDAVGGQVLSELFTNRKENIPLQFSEDCLYLNVYTPADLTKNSRLPVMVWIHGGGLVVGGASTYDGQVLSAHENVVVVTIQYRLGIWGFFSTGDEHSQGNWGHLDQVAALHWVQDNIANFGGNPGSVTIFGESAGGFSVSALVLSPLAKNLFHRAISESGVVLTSALITTDSKPIANLIATLSGCKTTTSAVMVHCLRQKTEDELLETSLKLNLFKLDLLGNPKESYPFLPT... | 3.1.1.1; 3.1.1.67 | null | acylglycerol catabolic process [GO:0046464]; cellular response to cholesterol [GO:0071397]; cellular response to cold [GO:0070417]; cellular response to low-density lipoprotein particle stimulus [GO:0071404]; cholesterol biosynthetic process [GO:0006695]; cholesterol homeostasis [GO:0042632]; cholesterol metabolic proc... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; intracellular membrane-bounded organelle [GO:0043231]; lipid droplet [GO:0005811] | all-trans-retinyl-palmitate hydrolase, all-trans-retinol forming activity [GO:0047376]; carboxylesterase activity [GO:0106435]; carboxylic ester hydrolase activity [GO:0052689]; fatty-acyl-ethyl-ester synthase activity [GO:0030339]; retinyl-palmitate esterase activity [GO:0050253]; sterol esterase activity [GO:0004771]... | PF00135; | 3.40.50.1820; | Type-B carboxylesterase/lipase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:Q8VCT4}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q8VCT4}. Lipid droplet {ECO:0000250|UniProtKB:Q8VCT4}. Microsome {ECO:0000269|PubMed:12230550}. | CATALYTIC ACTIVITY: Reaction=all-trans-retinyl hexadecanoate + H2O = all-trans-retinol + H(+) + hexadecanoate; Xref=Rhea:RHEA:13933, ChEBI:CHEBI:7896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17336, ChEBI:CHEBI:17616; Evidence={ECO:0000269|PubMed:12230550}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.71 M for oleic acid {ECO:0000269|PubMed:1429692}; KM=1.16 uM for retinyl palmitate {ECO:0000269|PubMed:12230550}; Vmax=1482 nmol/h/mg enzyme toward oleic acid {ECO:0000269|PubMed:1429692}; Note=kcat is 0.22 min(-1) with retinyl palmitate as substrate. {ECO:000026... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH for FAEE synthesis is 7.0. Optimum pH for PNPB-hydrolyzing activity is 6-8. {ECO:0000269|PubMed:1429692}; | null | FUNCTION: Major lipase in white adipose tissue (By similarity). Involved in the metabolism of xenobiotics and of natural substrates. Hydrolyzes triacylglycerols and monoacylglycerols, with a preference for monoacylglycerols. The susceptibility of the substrate increases with decreasing acyl chain length of the fatty ac... | Rattus norvegicus (Rat) |
P16304 | KAD_BACSU | MNLVLMGLPGAGKGTQGERIVEDYGIPHISTGDMFRAAMKEETPLGLEAKSYIDKGELVPDEVTIGIVKERLGKDDCERGFLLDGFPRTVAQAEALEEILEEYGKPIDYVINIEVDKDVLMERLTGRRICSVCGTTYHLVFNPPKTPGICDKDGGELYQRADDNEETVSKRLEVNMKQTQPLLDFYSEKGYLANVNGQQDIQDVYADVKDLLGGLKK | 2.7.4.3 | null | AMP salvage [GO:0044209]; CDP biosynthetic process [GO:0046705]; nucleoside diphosphate metabolic process [GO:0009132]; nucleoside monophosphate metabolic process [GO:0009123]; phosphorylation [GO:0016310]; UDP biosynthetic process [GO:0006225] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | adenylate kinase activity [GO:0004017]; ATP binding [GO:0005524]; cytidylate kinase activity [GO:0004127]; nucleoside diphosphate kinase activity [GO:0004550]; UMP kinase activity [GO:0033862]; zinc ion binding [GO:0008270] | PF00406;PF05191; | 3.40.50.300; | Adenylate kinase family | null | SUBCELLULAR LOCATION: Cytoplasm. | 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_00235}; | null | PATHWAY: Purine metabolism; AMP biosynthesis via salvage pathway; AMP from ADP: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00235}. | null | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 45 degrees Celsius. Thermal denaturation midpoint (Tm) is 47.6 degrees Celsius and is raised to 66.0 degrees Celsius when AK is complexed with the inhibitor Ap5A. {ECO:0000269|PubMed:15100224}; | 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. {ECO:0000255|HAMAP-Rule:MF_00235}. | Bacillus subtilis (strain 168) |
P16305 | GBRA6_MOUSE | MVLLLPWLFIILWLENAQAQLEDEGNFYSENVSRILDNLLEGYDNRLRPGFGGAVTEVKTDIYVTSFGPVSDVEMEYTMDVFFRQTWTDERLKFKGPAEILSLNNLMVSKIWTPDTFFRNGKKSIAHNMTTPNKLFRLMQNGTILYTMRLTINADCPMRLVNFPMDGHACPLKFGSYAYPKTEIIYTWKKGPLYSVEVPEESSSLLQYDLIGQTVSSETIKSNTGEYVIMTVYFHLQRKMGYFMIQIYTPCIMTVILSQVSFWINKESVPARTVFGITTVLTMTTLSISARHSLPKVSYATAMDWFIAVCFAFVFSALIE... | null | null | chloride transmembrane transport [GO:1902476]; gamma-aminobutyric acid signaling pathway [GO:0007214]; inhibitory synapse assembly [GO:1904862]; regulation of postsynaptic membrane potential [GO:0060078]; synaptic transmission, GABAergic [GO:0051932] | cerebellar Golgi cell to granule cell synapse [GO:0099192]; chloride channel complex [GO:0034707]; dendrite [GO:0030425]; dendrite membrane [GO:0032590]; GABA-A receptor complex [GO:1902711]; GABA-ergic synapse [GO:0098982]; hippocampal mossy fiber to CA3 synapse [GO:0098686]; neuron projection [GO:0043005]; neuronal c... | benzodiazepine receptor activity [GO:0008503]; diazepam binding [GO:0050809]; GABA-A receptor activity [GO:0004890]; GABA-gated chloride ion channel activity [GO:0022851]; heterocyclic compound binding [GO:1901363]; inhibitory extracellular ligand-gated monoatomic ion channel activity [GO:0005237]; protein-containing c... | PF02931;PF02932; | 2.70.170.10;1.20.58.390; | Ligand-gated ion channel (TC 1.A.9) family, Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily, GABRA6 sub-subfamily | null | SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250|UniProtKB:P30191}; Multi-pass membrane protein {ECO:0000255}. Cell membrane {ECO:0000250|UniProtKB:P30191}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:P08219}; | null | null | null | null | FUNCTION: Alpha subunit of the heteropentameric ligand-gated chloride channel gated by gamma-aminobutyric acid (GABA), a major inhibitory neurotransmitter in the brain (By similarity). GABA-gated chloride channels, also named GABA(A) receptors (GABAAR), consist of five subunits arranged around a central pore and contai... | Mus musculus (Mouse) |
P16310 | GHR_RAT | MDLWRVFLTLALAVSSDMFPGSGATPATLGKASPVLQRINPSLRESSSGKPRFTKCRSPELETFSCYWTEGDDHNLKVPGSIQLYYARRIAHEWTPEWKECPDYVSAGANSCYFNSSYTSIWIPYCIKLTTNGDLLDEKCFTVDEIVQPDPPIGLNWTLLNISLPGIRGDIQVSWQPPPSADVLKGWIILEYEIQYKEVNETKWKTMSPIWSTSVPLYSLRLDKEHEVRVRSRQRSFEKYSEFSEVLRVTFPQMDTLAACEEDFRFPWFLIIIFGIFGVAVMLFVVIFSKQQRIKMLILPPVPVPKIKGIDPDLLKEGKL... | null | null | cartilage development involved in endochondral bone morphogenesis [GO:0060351]; cellular response to hormone stimulus [GO:0032870]; cellular response to insulin stimulus [GO:0032869]; cytokine-mediated signaling pathway [GO:0019221]; endocytosis [GO:0006897]; growth hormone receptor signaling pathway [GO:0060396]; horm... | cell surface [GO:0009986]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytosol [GO:0005829]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; growth hormone receptor complex [GO:0070195]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; plasma membran... | cytokine binding [GO:0019955]; growth factor binding [GO:0019838]; growth hormone receptor activity [GO:0004903]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; peptide hormone binding [GO:0017046]; protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; protein phospha... | PF09067;PF12772; | 2.60.40.10; | Type I cytokine receptor family, Type 1 subfamily | PTM: On GH binding, phosphorylated on tyrosine residues in the cytoplasmic domain by JAK2. Phosphorylation on either (or all of) Tyr-534, Tyr-566 and/or Tyr-627 is required for STAT5 activation. Phosphorylation on Tyr-333 would seem necessary for JAK2 activation. {ECO:0000269|PubMed:7545168, ECO:0000269|PubMed:9231797}... | SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Note=On growth hormone binding, GHR is ubiquitinated, internalized, down-regulated and transported into a degradative or non-degradative pathway.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted. Membrane. Note=Mainly secreted. In adipose tissue, iso... | null | null | null | null | null | FUNCTION: Receptor for pituitary gland growth hormone involved in regulating postnatal body growth. On ligand binding, couples to, and activates the JAK2/STAT5 pathway.; FUNCTION: The soluble form (GHBP) acts as a reservoir of growth hormone in plasma and may be a modulator/inhibitor of GH signaling. | Rattus norvegicus (Rat) |
P16311 | PEPT1_DERFA | MKFVLAIASLLVLSTVYARPASIKTFEEFKKAFNKNYATVEEEEVARKNFLESLKYVEANKGAINHLSDLSLDEFKNRYLMSAEAFEQLKTQFDLNAETSACRINSVNVPSELDLRSLRTVTPIRMQGGCGSCWAFSGVAATESAYLAYRNTSLDLSEQELVDCASQHGCHGDTIPRGIEYIQQNGVVEERSYPYVAREQRCRRPNSQHYGISNYCQIYPPDVKQIREALTQTHTAIAVIIGIKDLRAFQHYDGRTIIQHDNGYQPNYHAVNIVGYGSTQGDDYWIVRNSWDTTWGDSGYGYFQAGNNLMMIEQYPYVVI... | 3.4.22.65 | null | proteolysis involved in protein catabolic process [GO:0051603] | extracellular space [GO:0005615]; lysosome [GO:0005764] | cysteine-type endopeptidase activity [GO:0004197] | PF08246;PF00112; | 3.90.70.10; | Peptidase C1 family | null | SUBCELLULAR LOCATION: Secreted. | CATALYTIC ACTIVITY: Reaction=Broad endopeptidase specificity.; EC=3.4.22.65; | null | null | null | null | FUNCTION: Thiol protease that hydrolyzes proteins, with a preference for Phe or basic residues. | Dermatophagoides farinae (American house dust mite) |
P16330 | CN37_MOUSE | MNTSFTRKSHTFLPKLFFRKMSSSGAKEKPELQFPFLQDEDTVATLHECKTLFILRGLPGSGKSTLARLILEKYHDGTKMVSADAYKIIPGSRADFSEAYKRLDEDLAGYCRRDIRVLVLDDTNHERERLDQLFEMADQYQYQVVLVEPKTAWRLDCAQLKEKNQWQLSADDLKKLKPGLEKDFLPLYFGWFLTKKSSETLRKAGQVFLEELGNHKAFKKELRHFISGDEPKEKLELVSYFGKRPPGVLHCTTKFCDYGKAAGAEEYAQQEVVKRSYGKAFKLSISALFVTPKTAGAQVVLTDQELQLWPSDLDKPSASE... | 3.1.4.37 | null | adult locomotory behavior [GO:0008344]; axonogenesis [GO:0007409]; cyclic nucleotide catabolic process [GO:0009214]; forebrain development [GO:0030900]; oligodendrocyte differentiation [GO:0048709]; regulation of mitochondrial membrane permeability [GO:0046902]; response to lipopolysaccharide [GO:0032496]; response to ... | cell projection [GO:0042995]; cytoplasm [GO:0005737]; extracellular space [GO:0005615]; melanosome [GO:0042470]; membrane [GO:0016020]; microvillus [GO:0005902]; mitochondrial inner membrane [GO:0005743]; mitochondrial outer membrane [GO:0005741]; myelin sheath [GO:0043209]; myelin sheath abaxonal region [GO:0035748]; ... | 2',3'-cyclic-nucleotide 3'-phosphodiesterase activity [GO:0004113]; cyclic nucleotide binding [GO:0030551]; RNA binding [GO:0003723] | PF13671;PF05881; | 3.90.1740.10;3.40.50.300; | 2H phosphoesterase superfamily, CNPase family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:18076147}; Lipid-anchor {ECO:0000269|PubMed:18076147}. Melanosome {ECO:0000250|UniProtKB:P09543}. Note=Firmly bound to membrane structures of brain white matter. | CATALYTIC ACTIVITY: Reaction=a nucleoside 2',3'-cyclic phosphate + H2O = a nucleoside 2'-phosphate + H(+); Xref=Rhea:RHEA:14489, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:66954, ChEBI:CHEBI:78552; EC=3.1.4.37; Evidence={ECO:0000250|UniProtKB:P06623}; | null | null | null | null | FUNCTION: Catalyzes the formation of 2'-nucleotide products from 2',3'-cyclic substrates (By similarity). May participate in RNA metabolism in the myelinating cell, CNP is the third most abundant protein in central nervous system myelin (PubMed:22393399). {ECO:0000250|UniProtKB:P06623, ECO:0000269|PubMed:22393399}. | Mus musculus (Mouse) |
P16331 | PH4H_MOUSE | MAAVVLENGVLSRKLSDFGQETSYIEDNSNQNGAVSLIFSLKEEVGALAKVLRLFEENEINLTHIESRPSRLNKDEYEFFTYLDKRSKPVLGSIIKSLRNDIGATVHELSRDKEKNTVPWFPRTIQELDRFANQILSYGAELDADHPGFKDPVYRARRKQFADIAYNYRHGQPIPRVEYTEEERKTWGTVFRTLKALYKTHACYEHNHIFPLLEKYCGFREDNIPQLEDVSQFLQTCTGFRLRPVAGLLSSRDFLGGLAFRVFHCTQYIRHGSKPMYTPEPDICHELLGHVPLFSDRSFAQFSQEIGLASLGAPDEYIEK... | 1.14.16.1 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250|UniProtKB:P04176}; | L-phenylalanine catabolic process [GO:0006559]; L-phenylalanine metabolic process [GO:0006558]; tyrosine biosynthetic process [GO:0006571]; tyrosine biosynthetic process, by oxidation of phenylalanine [GO:0019293] | null | amino acid binding [GO:0016597]; identical protein binding [GO:0042802]; iron ion binding [GO:0005506]; phenylalanine 4-monooxygenase activity [GO:0004505] | PF01842;PF00351; | 1.10.800.10; | Biopterin-dependent aromatic amino acid hydroxylase family | PTM: Phosphorylation at Ser-16 increases basal activity and facilitates activation by the substrate phenylalanine. {ECO:0000250|UniProtKB:P00439}. | null | CATALYTIC ACTIVITY: Reaction=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-phenylalanine + O2 = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + L-tyrosine; Xref=Rhea:RHEA:20273, ChEBI:CHEBI:15379, ChEBI:CHEBI:15642, ChEBI:CHEBI:58095, ChEBI:CHEBI:58315, ChEBI:CHEBI:59560; EC=1.14.16.1; Evidence={ECO:000025... | null | PATHWAY: Amino-acid degradation; L-phenylalanine degradation; acetoacetate and fumarate from L-phenylalanine: step 1/6. | null | null | FUNCTION: Catalyzes the hydroxylation of L-phenylalanine to L-tyrosine. {ECO:0000250|UniProtKB:P00439}. | Mus musculus (Mouse) |
P16332 | MUTA_MOUSE | MLRAKNQLFLLSPHYLKQLNIPSASRWKRLLHQQQPLHPEWAVLAKKQLKGKNPEDLIWHTPEGISIKPLYSRADTLDLPEELPGVKPFTRGPYPTMYTYRPWTIRQYAGFSTVEESNKFYKDNIKAGQQGLSVAFDLATHRGYDSDNPRVRGDVGMAGVAIDTVEDTKILFDGIPLEKMSVSMTMNGAVIPVLATFIVTGEEQGVPKEKLTGTIQNDILKEFMVRNTYIFPPEPSMKIIADIFQYTAQHMPKFNSISISGYHMQEAGADAILELAYTIADGLEYCRTGLQAGLTIDEFAPRLSFFWGIGMNFYMEIAKM... | 5.4.99.2 | COFACTOR: Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408; Evidence={ECO:0000269|PubMed:1978672}; | homocysteine metabolic process [GO:0050667]; post-embryonic development [GO:0009791]; propionate metabolic process, methylmalonyl pathway [GO:0019678]; succinyl-CoA biosynthetic process [GO:1901290] | cytoplasm [GO:0005737]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | cobalamin binding [GO:0031419]; GTPase activity [GO:0003924]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; methylmalonyl-CoA mutase activity [GO:0004494]; modified amino acid binding [GO:0072341]; protein homodimerization activity [GO:0042803] | PF02310;PF01642; | 3.40.50.280;3.20.20.240; | Methylmalonyl-CoA mutase family | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000250|UniProtKB:P22033}. Mitochondrion {ECO:0000250|UniProtKB:P22033}. Cytoplasm {ECO:0000250|UniProtKB:P22033}. | CATALYTIC ACTIVITY: Reaction=(R)-methylmalonyl-CoA = succinyl-CoA; Xref=Rhea:RHEA:22888, ChEBI:CHEBI:57292, ChEBI:CHEBI:57326; EC=5.4.99.2; Evidence={ECO:0000269|PubMed:1978672}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:22889; Evidence={ECO:0000305|PubMed:1978672}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.2 uM for adenosylcob(III)alamin {ECO:0000269|PubMed:1978672}; KM=0.27 mM for methylmalonyl-CoA {ECO:0000269|PubMed:1978672}; | null | null | null | FUNCTION: Catalyzes the reversible isomerization of methylmalonyl-CoA (MMCoA) (generated from branched-chain amino acid metabolism and degradation of dietary odd chain fatty acids and cholesterol) to succinyl-CoA (3-carboxypropionyl-CoA), a key intermediate of the tricarboxylic acid cycle. {ECO:0000269|PubMed:1978672}. | Mus musculus (Mouse) |
P16333 | NCK1_HUMAN | MAEEVVVVAKFDYVAQQEQELDIKKNERLWLLDDSKSWWRVRNSMNKTGFVPSNYVERKNSARKASIVKNLKDTLGIGKVKRKPSVPDSASPADDSFVDPGERLYDLNMPAYVKFNYMAEREDELSLIKGTKVIVMEKCSDGWWRGSYNGQVGWFPSNYVTEEGDSPLGDHVGSLSEKLAAVVNNLNTGQVLHVVQALYPFSSSNDEELNFEKGDVMDVIEKPENDPEWWKCRKINGMVGLVPKNYVTVMQNNPLTSGLEPSPPQCDYIRPSLTGKFAGNPWYYGKVTRHQAEMALNERGHEGDFLIRDSESSPNDFSVS... | null | null | actin filament organization [GO:0007015]; antiviral innate immune response [GO:0140374]; cell migration [GO:0016477]; ephrin receptor signaling pathway [GO:0048013]; lamellipodium assembly [GO:0030032]; negative regulation of endoplasmic reticulum stress-induced eIF2 alpha phosphorylation [GO:1903912]; negative regulat... | cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein phosphatase type 1 complex [GO:0000164]; ribosome [GO:0005840]; vesicle membrane [GO:0012506] | cadherin binding [GO:0045296]; cytoskeletal anchor activity [GO:0008093]; ephrin receptor binding [GO:0046875]; eukaryotic initiation factor eIF2 binding [GO:0071074]; molecular condensate scaffold activity [GO:0140693]; protein domain specific binding [GO:0019904]; protein kinase inhibitor activity [GO:0004860]; prote... | PF00017;PF00018; | 3.30.505.10;2.30.30.40; | null | PTM: Phosphorylated on Ser and Tyr residues. Phosphorylated in response to activation of EGFR and FcERI. Phosphorylated by activated PDGFRB. {ECO:0000269|PubMed:10026169, ECO:0000269|PubMed:1333046, ECO:0000269|PubMed:1448108, ECO:0000269|PubMed:18835251, ECO:0000269|PubMed:7692233}. | SUBCELLULAR LOCATION: Cytoplasm. Endoplasmic reticulum. Nucleus. Note=Mostly cytoplasmic, but shuttles between the cytoplasm and the nucleus. Import into the nucleus requires the interaction with SOCS7. Predominantly nuclear following genotoxic stresses, such as UV irradiation, hydroxyurea or mitomycin C treatments. | null | null | null | null | null | FUNCTION: Adapter protein which associates with tyrosine-phosphorylated growth factor receptors, such as KDR and PDGFRB, or their cellular substrates. Maintains low levels of EIF2S1 phosphorylation by promoting its dephosphorylation by PP1. Plays a role in the DNA damage response, not in the detection of the damage by ... | Homo sapiens (Human) |
P16340 | PUR2_DROPS | MSHSVLVIGSGGREHAICWKLSQSTLVKQIYALPGSFGIQQVEKCRNLDAKVLDPKDFEAIAKWSKKNEISLVVVGPEDPLALGLGDVLQKEGIPCFGPGKQGAQIEADKKWAKDFMLRHGIPTARYESFTDTNKAKAFIRSAPYQALVVKAAGLAAGKGVVVAANVDEACQAVDEILGDLKYGQAGATLVVEELLEGEEISVLAFTDGKSVRAMLPAQDHKRLGNGDTGPNTGGMGAYCPCPLISQPALELVQRAVLERAVQGLIKERITYQGVLYAGLMLTRDGPRVLEFNCRFGDPETQVILPLLETDLFEVMQACC... | 2.1.2.2; 6.3.3.1; 6.3.4.13 | null | 'de novo' IMP biosynthetic process [GO:0006189]; adenine biosynthetic process [GO:0046084] | cytosol [GO:0005829] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; phosphoribosylamine-glycine ligase activity [GO:0004637]; phosphoribosylformylglycinamidine cyclo-ligase activity [GO:0004641]; phosphoribosylglycinamide formyltransferase activity [GO:0004644] | PF00586;PF02769;PF00551;PF01071;PF02843;PF02844; | 3.40.50.20;3.30.1490.20;3.30.470.20;3.40.50.170;3.90.600.10;3.90.650.10;3.30.1330.10; | GARS family; AIR synthase family; GART family | null | null | CATALYTIC ACTIVITY: Reaction=5-phospho-beta-D-ribosylamine + ATP + glycine = ADP + H(+) + N(1)-(5-phospho-beta-D-ribosyl)glycinamide + phosphate; Xref=Rhea:RHEA:17453, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57305, ChEBI:CHEBI:58681, ChEBI:CHEBI:143788, ChEBI:CHEBI:456216; EC=6.3.4.13; Evid... | 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. {ECO:0000250|UniProtKB:P00967}.; PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-pho... | null | null | FUNCTION: Trifunctional enzyme required for de novo purine biosynthesis. {ECO:0000250|UniProtKB:P00967}. | Drosophila pseudoobscura pseudoobscura (Fruit fly) |
P16341 | KAX51_LEIHE | AFCNLRMCQLSCRSLGLLGKCIGDKCECVKH | null | null | null | extracellular region [GO:0005576] | ion channel inhibitor activity [GO:0008200]; potassium channel regulator activity [GO:0015459]; toxin activity [GO:0090729] | PF00451; | null | Short scorpion toxin superfamily, Potassium channel inhibitor family, Alpha-KTx 05 subfamily | PTM: Two disulfide bonds are the minimal requirement needed to produce a nativelike and bio-active conformation in this toxin. The third disulfide provides an additional contribution to structure stabilization and can modulate biological potency depending on its position and the structural regions involved in biologica... | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2839478}. | null | null | null | null | null | FUNCTION: Blocker for the small conductance calcium-activated potassium channels (PubMed:11527975, PubMed:2307683, PubMed:2839478). Shows the best affinity for KCa2.2/KCNN2 (Kd=0.2 nM), followed by KCa2.3/KCNN3 (Kd=1.1 nM) and KCa2.1/KCNN1 (Kd=325 nM) (PubMed:11527975). {ECO:0000269|PubMed:11527975, ECO:0000269|PubMed:... | Leiurus hebraeus (Deathstalker scorpion) (Leiurus quinquestriatus hebraeus) |
P16356 | RPB1_CAEEL | MALVGVDFQAPLRIVSRVQFGILGPEEIKRMSVAHVEFPEVYENGKPKLGGLMDPRQGVIDRRGRCMTCAGNLTDCPGHFGHLELAKPVFHIGFLTKTLKILRCVCFYCGRLLIDKSAPRVLEILKKTGTNSKKRLTMIYDLCKAKSVCEGAAEKEEGMPDDPDDPMNDGKKVAGGCGRYQPSYRRVGIDINAEWKKNVNEDTQERKIMLTAERVLEVFQQITDEDILVIGMDPQFARPEWMICTVLPVPPLAVRPAVVTFGSAKNQDDLTHKLSDIIKTNQQLQRNEANGAAAHVLTDDVRLLQFHVATLVDNCIPGLP... | 2.7.7.6 | null | DNA-templated transcription [GO:0006351]; embryo development ending in birth or egg hatching [GO:0009792]; gastrulation [GO:0007369]; mRNA transcription by RNA polymerase II [GO:0042789]; transcription by RNA polymerase II [GO:0006366] | chromosome [GO:0005694]; euchromatin [GO:0000791]; nuclear body [GO:0016604]; nucleus [GO:0005634]; RNA polymerase II, core complex [GO:0005665] | DNA binding [GO:0003677]; DNA-directed 5'-3' RNA polymerase activity [GO:0003899]; metal ion binding [GO:0046872]; RNA polymerase II activity [GO:0001055] | PF04997;PF00623;PF04983;PF05000;PF04998;PF04992;PF04990;PF05001; | 1.10.132.30;1.10.150.390;2.40.40.20;3.30.1360.140;6.10.250.2940;6.20.50.80;3.30.1490.180;4.10.860.120;1.10.274.100; | RNA polymerase beta' chain family | PTM: The tandem 7 residues repeats in the C-terminal domain (CTD) can be highly phosphorylated. The phosphorylation activates Pol II (By similarity). Phosphorylation occurs mainly at residues 'Ser-2' and 'Ser-5' of the heptapeptide repeat and starts at the 3- to 4-cell embryonic stage (PubMed:14726532, PubMed:17291483)... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14726532, ECO:0000269|PubMed:17291483, ECO:0000269|PubMed:23903194}. Chromosome {ECO:0000269|PubMed:27541139}. Note=Localizes to punctate nucleoplasmic structures in the nuclei of interphase somatic cells when phosphorylated at 'Ser-5' of the C-terminal heptapeptide rep... | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.6; | null | null | null | null | FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Largest and catalytic component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Forms the polymerase active center together with the s... | Caenorhabditis elegans |
P16368 | TIMP2_BOVIN | MGAAARSLPLAFCLLLLGTLLPRADACSCSPVHPQQAFCNADIVIRAKAVNKKEVDSGNDIYGNPIKRIQYEIKQIKMFKGPDQDIEFIYTAPAAAVCGVSLDIGGKKEYLIAGKAEGNGNMHITLCDFIVPWDTLSATQKKSLNHRYQMGCECKITRCPMIPCYISSPDECLWMDWVTEKNINGHQAKFFACIKRSDGSCAWYRGAAPPKQEFLDIEDP | null | null | negative regulation of membrane protein ectodomain proteolysis [GO:0051045]; response to cytokine [GO:0034097]; response to hormone [GO:0009725] | extracellular matrix [GO:0031012]; extracellular space [GO:0005615] | metal ion binding [GO:0046872]; metalloendopeptidase inhibitor activity [GO:0008191]; protease binding [GO:0002020] | PF00965; | 2.40.50.120;3.90.370.10; | Protease inhibitor I35 (TIMP) family | PTM: The activity of TIMP2 is dependent on the presence of disulfide bonds. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Complexes with metalloproteinases (such as collagenases) and irreversibly inactivates them by binding to their catalytic zinc cofactor. | Bos taurus (Bovine) |
P16370 | RPB3_YEAST | MSEEGPQVKIREASKDNVDFILSNVDLAMANSLRRVMIAEIPTLAIDSVEVETNTTVLADEFIAHRLGLIPLQSMDIEQLEYSRDCFCEDHCDKCSVVLTLQAFGESESTTNVYSKDLVIVSNLMGRNIGHPIIQDKEGNGVLICKLRKGQELKLTCVAKKGIAKEHAKWGPAAAIEFEYDPWNKLKHTDYWYEQDSAKEWPQSKNCEYEDPPNEGDPFDYKAQADTFYMNVESVGSIPVDQVVVRGIDTLQKKVASILLALTQMDQDKVNFASGDNNTASNMLGSNEDVMMTGAEQDPYSNASQMGNTGSGGYDNAW | null | null | RNA-templated transcription [GO:0001172]; termination of RNA polymerase II transcription [GO:0006369]; transcription by RNA polymerase II [GO:0006366]; transcription elongation by RNA polymerase II [GO:0006368]; transcription initiation at RNA polymerase II promoter [GO:0006367] | nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II, core complex [GO:0005665] | DNA binding [GO:0003677]; metal ion binding [GO:0046872]; protein dimerization activity [GO:0046983]; RNA polymerase II activity [GO:0001055] | PF01000;PF01193; | 2.170.120.12;3.30.1360.10; | Archaeal Rpo3/eukaryotic RPB3 RNA polymerase subunit family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates. Component of RNA polymerase II which synthesizes mRNA precursors and many functional non-coding RNAs. Pol II is the central component of the basal RNA polymerase II transcription... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P16371 | GROU_DROME | MYPSPVRHPAAGGPPPQGPIKFTIADTLERIKEEFNFLQAQYHSIKLECEKLSNEKTEMQRHYVMYYEMSYGLNVEMHKQTEIAKRLNTLINQLLPFLQADHQQQVLQAVERAKQVTMQELNLIIGHQQQHGIQQLLQQIHAQQVPGGPPQPMGALNPFGALGATMGLPHGPQGLLNKPPEHHRPDIKPTGLEGPAAAEERLRNSVSPADREKYRTRSPLDIENDSKRRKDEKLQEDEGEKSDQDLVVDVANEMESHSPRPNGEHVSMEVRDRESLNGERLEKPSSSGIKQERPPSRSGSSSSRSTPSLKTKDMEKPGTP... | null | null | cell differentiation [GO:0030154]; epidermal growth factor receptor signaling pathway [GO:0007173]; fibroblast growth factor receptor signaling pathway [GO:0008543]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation ... | nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991]; transcription regulator complex [GO:0005667] | CRD domain binding [GO:0071906]; DNA-binding transcription factor binding [GO:0140297]; HMG box domain binding [GO:0071837]; transcription corepressor activity [GO:0003714]; transcription factor binding [GO:0008134] | PF03920;PF00400; | 2.130.10.10; | WD repeat Groucho/TLE family | PTM: Ubiquitinated by XIAP/BIRC4. {ECO:0000269|PubMed:22304967}. | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Transcriptional corepressor that regulates transcription when recruited to specific target DNA by hairy-related bHLH proteins (PubMed:8001118, PubMed:8649374). Maternally required for neurogenesis; in the segregation of the neuroectoderm (PubMed:8001118). Directly or indirectly interacts with Notch and Delta ... | Drosophila melanogaster (Fruit fly) |
P16375 | 7UP1_DROME | MCASPSTAPGFFNPRPQSGAELSAFDIGLSRSMGLGVPPHSAWHEPPASLGGHLHAASAGPGTTTGSVATGGGGTTPSSVASQQSAVIKQDLSCPSLNQAGSGHHPGIKEDLSSSLPSANGGSAGGHHSGSGSGSGSGVNPGHGSDMLPLIKGHGQDMLTSIKGQPTGCGSTTPSSQANSSHSQSSNSGSQIDSKQNIECVVCGDKSSGKHYGQFTCEGCKSFFKRSVRRNLTYSCRGSRNCPIDQHHRNQCQYCRLKKCLKMGMRREAVQRGRVPPTQPGLAGMHGQYQIANGDPMGIAGFNGHSYLSSYISLLLRAEP... | null | null | cardioblast cell fate determination [GO:0007510]; cell differentiation [GO:0030154]; epithelial cell proliferation involved in Malpighian tubule morphogenesis [GO:0061331]; fat body development [GO:0007503]; glial cell development [GO:0021782]; heart development [GO:0007507]; neuroblast development [GO:0014019]; neuron... | cytoplasm [GO:0005737]; nucleus [GO:0005634]; synapse [GO:0045202] | DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; nuclear receptor activity [GO:0004879]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; zinc ion bi... | PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR2 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}. | null | null | null | null | null | FUNCTION: Receptor that is required in photoreceptors R1, R3, R4 and R6 during eye development; generation of the ganglion mother cell-2 (GMC-2) fate in the nb7-3 lineage, coinciding with the transition in the expression of HB to KR in the neuroblasts (NBs). {ECO:0000269|PubMed:15691762, ECO:0000269|PubMed:2105166}. | Drosophila melanogaster (Fruit fly) |
P16376 | 7UP2_DROME | MCASPSTAPGFFNPRPQSGAELSAFDIGLSRSMGLGVPPHSAWHEPPASLGGHLHAASAGPGTTTGSVATGGGGTTPSSVASQQSAVIKQDLSCPSLNQAGSGHHPGIKEDLSSSLPSANGGSAGGHHSGSGSGSGSGVNPGHGSDMLPLIKGHGQDMLTSIKGQPTGCGSTTPSSQANSSHSQSSNSGSQIDSKQNIECVVCGDKSSGKHYGQFTCEGCKSFFKRSVRRNLTYSCRGSRNCPIDQHHRNQCQYCRLKKCLKMGMRREAVQRGRVPPTQPGLAGMHGQYQIANGDPMGIAGFNGHSYLSSYISLLLRAEP... | null | null | cardioblast cell fate determination [GO:0007510]; cell differentiation [GO:0030154]; epithelial cell proliferation involved in Malpighian tubule morphogenesis [GO:0061331]; fat body development [GO:0007503]; glial cell development [GO:0021782]; glucose homeostasis [GO:0042593]; heart development [GO:0007507]; lipid hom... | cytoplasm [GO:0005737]; nucleus [GO:0005634]; synapse [GO:0045202] | DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; nuclear receptor activity [GO:0004879]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; zinc ion bi... | PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR2 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}. | null | null | null | null | null | FUNCTION: Receptor that is required in photoreceptors R1, R3, R4 and R6 during eye development; generation of the ganglion mother cell-2 (GMC-2) fate in the nb7-3 lineage, coinciding with the transition in the expression of HB to KR in the neuroblasts (NBs). {ECO:0000269|PubMed:15691762, ECO:0000269|PubMed:2105166}. | Drosophila melanogaster (Fruit fly) |
P16378 | GNAO_DROME | MGCAQSAEERAAAARSRLIERNLKEDGIQAAKDIKLLLLGAGESGKSTIVKQMKIIHESGFTAEDFKQYRPVVYSNTIQSLVAILRAMPTLSIQYSNNERESDAKMVFDVCQRMHDTEPFSEELLAAMKRLWQDAGVQECFSRSNEYQLNDSAKYFLDDLDRLGAKDYQPTEQDILRTRVKTTGIVEVHFSFKNLNFKLFDVGGQRSERKKWIHCFEDVTAIIFCVAMSEYDQVLHEDETTNRMQESLKLFDSICNNKWFTDTSIILFLNKKDLFEEKIRKSPLTICFPEYTGGQEYGEAAAYIQAQFEAKNKSTSKEIY... | null | null | adenylate cyclase-modulating G protein-coupled receptor signaling pathway [GO:0007188]; asymmetric cell division [GO:0008356]; axon ensheathment in central nervous system [GO:0032291]; behavioral response to starvation [GO:0042595]; calcium-mediated signaling [GO:0019722]; cell adhesion involved in heart morphogenesis ... | cytoplasm [GO:0005737]; heterotrimeric G-protein complex [GO:0005834]; plasma membrane [GO:0005886] | corticotropin-releasing hormone receptor 1 binding [GO:0051430]; G protein-coupled receptor binding [GO:0001664]; G protein-coupled serotonin receptor binding [GO:0031821]; G-protein beta/gamma-subunit complex binding [GO:0031683]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872]; ... | PF00503; | 1.10.400.10;3.40.50.300; | G-alpha family, G(i/o/t/z) subfamily | null | null | null | null | null | null | null | FUNCTION: Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Plays a role in glial cell differentiation during embryogenesis; loco, Galphai and the G-protein coupled receptor, moody, are required in the surface glia to achieve effective... | Drosophila melanogaster (Fruit fly) |
P16379 | L_VSNJO | MDFDLIEDSANWEDDESDFFLRDILSQEDQMSYLNTADYNLNSPLISDDMVYIIKRMNHEEVPPIWRSKEWDSPLDMLRGCQAQPMSHQEMHNWFGTWIQNIQHDSAQGFTFLKEVDKESEMTYDLVSTFLKGWVGKDYPFKSKNKEIDSMALVGPLCQKFLDLHKITLILNAVSLGETKELLATFKGKYRMSCENIPIARLRLPSLGPVFMCKGWTYIHKERVLMDRNFLLMCKDVIIGRMQTFLSMIGRSDNKFSPDQIYTLANVYRIGDKILEQCGNKAYDLIKMIEPICNLKMMELARLHRPKIPKFPHFEEHVKG... | 2.1.1.375; 2.7.7.48; 2.7.7.88; 3.6.1.- | null | negative stranded viral RNA replication [GO:0039689] | host cell cytoplasm [GO:0030430]; virion component [GO:0044423] | ATP binding [GO:0005524]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872]; mRNA 5'-cap (guanine-N7-)-methyltransferase activity [GO:0004482]; RNA-dependent RNA polymerase activity [GO:0003968] | PF21080;PF14314;PF21081;PF14318;PF00946; | 3.40.50.150; | Rhabdoviridae protein L family | null | SUBCELLULAR LOCATION: Virion {ECO:0000250|UniProtKB:P03523}. Host cytoplasm {ECO:0000250|UniProtKB:P03523}. Note=L and P are packaged asymmetrically towards the blunt end of the virus. {ECO:0000250|UniProtKB:P03523}. | CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + RNA(n) = diphosphate + RNA(n+1); Xref=Rhea:RHEA:21248, Rhea:RHEA-COMP:14527, Rhea:RHEA-COMP:17342, ChEBI:CHEBI:33019, ChEBI:CHEBI:61557, ChEBI:CHEBI:140395; EC=2.7.7.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU00539}; CATALYTIC ACTIVITY: Reaction=GTP + H2... | null | null | null | null | FUNCTION: Responsible for RNA synthesis (replicase and transcriptase), cap addition, and cap methylation (By similarity). Performs also the polyadenylation of subgenomic mRNAs by a stuttering mechanism at a slipery stop site present at the end of viral genes (By similarity). The template is composed of the viral RNA ti... | Vesicular stomatitis New Jersey virus (strain Ogden subtype Concan) (VSNJV) |
P16381 | DDX3L_MOUSE | MSHVAEEDELGLDQQLAGLDLTSRDSQSGGSTASKGRYIPPHLRNREAAKAFYDKDGSRWSKDKDAYSSFGSRSDTRAKSSFFSDRGGSGSRGRFDERGRSDYESVGSRGGRSGFGKFERGGNSRWCDKADEDDWSKPLPPSERLEQELFSGGNTGINFEKYDDIPVEATGNNCPPHIESFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYTDGPGEALRAMKENGKYGRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLLV... | 3.6.4.13 | null | cell differentiation [GO:0030154]; gamete generation [GO:0007276]; negative regulation of gene expression [GO:0010629]; spermatogenesis [GO:0007283] | nucleus [GO:0005634]; P granule [GO:0043186] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677]; mRNA binding [GO:0003729]; RNA helicase activity [GO:0003724] | PF00270;PF00271; | 3.40.50.300; | DEAD box helicase family, DDX3/DED1 subfamily | null | null | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; | null | null | null | null | FUNCTION: Putative ATP-dependent RNA helicase. Possible role in a key step of the spermatogenic process. | Mus musculus (Mouse) |
P16382 | IL4RA_MOUSE | MGRLCTKFLTSVGCLILLLVTGSGSIKVLGEPTCFSDYIRTSTCEWFLDSAVDCSSQLCLHYRLMFFEFSENLTCIPRNSASTVCVCHMEMNRPVQSDRYQMELWAEHRQLWQGSFSPSGNVKPLAPDNLTLHTNVSDEWLLTWNNLYPSNNLLYKDLISMVNISREDNPAEFIVYNVTYKEPRLSFPINILMSGVYYTARVRVRSQILTGTWSEWSPSITWYNHFQLPLIQRLPLGVTISCLCIPLFCLFCYFSITKIKKIWWDQIPTPARSPLVAIIIQDAQVPLWDKQTRSQESTKYPHWKTCLDKLLPCLLKHRVK... | null | null | cytokine-mediated signaling pathway [GO:0019221]; defense response to protozoan [GO:0042832]; immunoglobulin mediated immune response [GO:0016064]; negative regulation of T-helper 1 cell differentiation [GO:0045626]; positive regulation of chemokine production [GO:0032722]; positive regulation of cold-induced thermogen... | centriolar satellite [GO:0034451]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; nucleoplasm [GO:0005654]; receptor complex [GO:0043235] | cytokine receptor activity [GO:0004896]; interleukin-4 receptor activity [GO:0004913] | PF09238; | 2.60.40.10; | Type I cytokine receptor family, Type 4 subfamily | PTM: On IL4 binding, phosphorylated on C-terminal tyrosine residues. {ECO:0000250|UniProtKB:P24394}.; PTM: Soluble IL4R can also be produced by proteolytic cleavage at the cell surface (shedding). {ECO:0000269|PubMed:8757301}. | SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 2]: Secreted. | null | null | null | null | null | FUNCTION: Receptor for both interleukin 4 and interleukin 13. Couples to the JAK1/2/3-STAT6 pathway. The IL4 response is involved in promoting Th2 differentiation. The IL4/IL13 responses are involved in regulating IgE production and, chemokine and mucus production at sites of allergic inflammation. In certain cell type... | Mus musculus (Mouse) |
P16383 | GCFC2_HUMAN | MAHRPKRTFRQRAADSSDSDGAEESPAEPGAPRELPVPGSAEEEPPSGGGRAQVAGLPHRVRGPRGRGRVWASSRRATKAAPRADEGSESRTLDVSTDEEDKIHHSSESKDDQGLSSDSSSSLGEKELSSTVKIPDAAFIQAARRKRELARAQDDYISLDVQHTSSISGMKRESEDDPESEPDDHEKRIPFTLRPQTLRQRMAEESISRNEETSEESQEDEKQDTWEQQQMRKAVKIIEERDIDLSCGNGSSKVKKFDTSISFPPVNLEIIKKQLNTRLTLLQETHRSHLREYEKYVQDVKSSKSTIQNLESSSNQALNC... | null | null | mRNA splicing, via spliceosome [GO:0000398]; spliceosomal complex assembly [GO:0000245] | cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; U2-type post-mRNA release spliceosomal complex [GO:0071008] | DNA binding [GO:0003677] | PF07842; | null | GCF family | null | SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:24304693}. Nucleus, nucleolus {ECO:0000269|PubMed:24304693}. | null | null | null | null | null | FUNCTION: Involved in pre-mRNA splicing through regulating spliceosome C complex formation (PubMed:24304693). May play a role during late-stage splicing events and turnover of excised introns (PubMed:24304693). {ECO:0000269|PubMed:24304693}. | Homo sapiens (Human) |
P16384 | MIAA_ECOLI | MSDISKASLPKAIFLMGPTASGKTALAIELRKILPVELISVDSALIYKGMDIGTAKPNAEELLAAPHRLLDIRDPSQAYSAADFRRDALAEMADITAAGRIPLLVGGTMLYFKALLEGLSPLPSADPEVRARIEQQAAEQGWESLHRQLQEVDPVAAARIHPNDPQRLSRALEVFFISGKTLTELTQTSGDALPYQVHQFAIAPASRELLHQRIEQRFHQMLASGFEAEVRALFARGDLHTDLPSIRCVGYRQMWSYLEGEISYDEMVYRGVCATRQLAKRQITWLRGWEGVHWLDSEKPEQARDEVLQVVGAIAG | 2.5.1.75 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:9012675}; | cellular response to heat [GO:0034605]; regulation of cytoplasmic translation in response to stress [GO:1990497]; tRNA modification [GO:0006400] | null | AMP dimethylallyltransferase activity [GO:0009824]; ATP binding [GO:0005524]; tRNA dimethylallyltransferase activity [GO:0052381] | PF01715; | 1.10.20.140;1.10.287.890;3.40.50.300; | IPP transferase family | null | null | CATALYTIC ACTIVITY: Reaction=adenosine(37) in tRNA + dimethylallyl diphosphate = diphosphate + N(6)-dimethylallyladenosine(37) in tRNA; Xref=Rhea:RHEA:26482, Rhea:RHEA-COMP:10162, Rhea:RHEA-COMP:10375, ChEBI:CHEBI:33019, ChEBI:CHEBI:57623, ChEBI:CHEBI:74411, ChEBI:CHEBI:74415; EC=2.5.1.75; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=96 nM for tRNA(Phe) {ECO:0000269|PubMed:9012675, ECO:0000269|PubMed:9148919}; KM=3.2 uM for DMAPP {ECO:0000269|PubMed:9012675, ECO:0000269|PubMed:9148919}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 6.5-9. {ECO:0000269|PubMed:9012675, ECO:0000269|PubMed:9148919}; | null | FUNCTION: Catalyzes the transfer of a dimethylallyl group onto the adenine at position 37 in tRNAs that read codons beginning with uridine, leading to the formation of N6-(dimethylallyl)adenosine (i(6)A). {ECO:0000269|PubMed:9012675, ECO:0000269|PubMed:9148919}. | Escherichia coli (strain K12) |
P16386 | LIPS_BOVIN | MDLRTMTQSLVTLAEDNMAFFSSQGPGETARRLTGVFAGIREQALGLEPALGRLLSVAHLFDLDTETPANGYRSLVHTARCCLAHLLHKSRYVASNRRSIFFRTSHNLAELEAYLAALTQLRALAYYAQRLLTTNQPGRLFFEGDERVIADFLREYVTLHKGCFYGRCLGFQFTPAIRPFLQTISIGLVSFGEHYKRNETGISVTASSLFTDGRFAIDPELRGAEFERIIQNLDVHFWKAFWNITEIQVLSSLANMASTTVRVSRLLSLPPVAFEMPLTSDPELTVTISPPLAHTGPGPVLVRLISYDLREGQDSKELSS... | 3.1.1.23; 3.1.1.79 | null | cholesterol metabolic process [GO:0008203]; diacylglycerol catabolic process [GO:0046340]; ether lipid metabolic process [GO:0046485]; lipid catabolic process [GO:0016042]; termination of RNA polymerase I transcription [GO:0006363]; transcription initiation at RNA polymerase I promoter [GO:0006361]; triglyceride catabo... | caveola [GO:0005901]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; lipid droplet [GO:0005811]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | 1,2-diacylglycerol acylhydrolase activity [GO:0102259]; 1,3-diacylglycerol acylhydrolase activity [GO:0102258]; acylglycerol lipase activity [GO:0047372]; all-trans-retinyl-palmitate hydrolase, all-trans-retinol forming activity [GO:0047376]; hormone-sensitive lipase activity [GO:0033878]; retinyl-palmitate esterase ac... | PF07859;PF06350; | 3.40.50.1820; | 'GDXG' lipolytic enzyme family | PTM: Phosphorylation by AMPK reduces its translocation towards the lipid droplets. {ECO:0000250|UniProtKB:P54310}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q05469}. Membrane, caveola {ECO:0000250|UniProtKB:Q05469}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q05469}. Lipid droplet {ECO:0000250|UniProtKB:P54310}. Note=Found in the high-density caveolae. Translocates to the cytoplasm from the caveolae upon insulin sti... | CATALYTIC ACTIVITY: Reaction=a diacylglycerol + H2O = a fatty acid + a monoacylglycerol + H(+); Xref=Rhea:RHEA:32731, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17408, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.79; Evidence={ECO:0000250|UniProtKB:P15304}; CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O ... | null | PATHWAY: Glycerolipid metabolism; triacylglycerol degradation. | null | null | FUNCTION: Lipase with broad substrate specificity, catalyzing the hydrolysis of triacylglycerols (TAGs), diacylglycerols (DAGs), monoacylglycerols (MAGs), cholesteryl esters and retinyl esters (By similarity). Shows a preferential hydrolysis of DAGs over TAGs and MAGs (By similarity). Preferentially hydrolyzes fatty ac... | Bos taurus (Bovine) |
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