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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P18067 | RAB7A_CANLF | MTSRKKVLLKVIILGDSGVGKTSLMNQYVNKKFSNQYKATIGADFLTKEVMVDDRLVTMQIWDTAGQERFQSLGVAFYRGADCCVLVFDVTAPNTFKTLDSWRDEFLIQASPRDPENFPFVVLGNKIDLENRQVATKRAQAWCYSKNNIPYFETSAKEAINVEQAFQTIARNALKQETEVELYNEFPEPIKLDKNDRAKTSAESCSC | 3.6.5.2 | null | early endosome to late endosome transport [GO:0045022]; endosome to lysosome transport [GO:0008333]; endosome to plasma membrane protein transport [GO:0099638]; epidermal growth factor catabolic process [GO:0007174]; lipid catabolic process [GO:0016042]; lipophagy [GO:0061724]; phagosome acidification [GO:0090383]; pha... | autophagosome membrane [GO:0000421]; cytosol [GO:0005829]; exocytic vesicle [GO:0070382]; late endosome [GO:0005770]; late endosome membrane [GO:0031902]; lipid droplet [GO:0005811]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; melanosome membrane [GO:0033162]; mitochondrial membrane [GO:0031966]; mitochondr... | G protein activity [GO:0003925]; GTP binding [GO:0005525] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Rab family | PTM: Deubiquitination at Lys-191 and Lys-194 by USP32. {ECO:0000250|UniProtKB:P51149}. | SUBCELLULAR LOCATION: Cytoplasmic vesicle, phagosome membrane {ECO:0000250|UniProtKB:P51149}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Late endosome membrane {ECO:0000250|UniProtKB:P51149}; Peripheral membrane protein {ECO:0000305}; Cytoplasmic side {ECO:0000305}. Lysosome membrane {EC... | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P51149}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|Uni... | null | null | null | null | FUNCTION: Small GTPase which cycles between active GTP-bound and inactive GDP-bound states. In its active state, binds to a variety of effector proteins playing a key role in the regulation of endo-lysosomal trafficking. Governs early-to-late endosomal maturation, microtubule minus-end as well as plus-end directed endo... | Canis lupus familiaris (Dog) (Canis familiaris) |
P18074 | ERCC2_HUMAN | MKLNVDGLLVYFPYDYIYPEQFSYMRELKRTLDAKGHGVLEMPSGTGKTVSLLALIMAYQRAYPLEVTKLIYCSRTVPEIEKVIEELRKLLNFYEKQEGEKLPFLGLALSSRKNLCIHPEVTPLRFGKDVDGKCHSLTASYVRAQYQHDTSLPHCRFYEEFDAHGREVPLPAGIYNLDDLKALGRRQGWCPYFLARYSILHANVVVYSYHYLLDPKIADLVSKELARKAVVVFDEAHNIDNVCIDSMSVNLTRRTLDRCQGNLETLQKTVLRIKETDEQRLRDEYRRLVEGLREASAARETDAHLANPVLPDEVLQEAVP... | 3.6.4.12 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:22678361}; COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000269|PubMed:22678361}; Note=Binds 1 [4Fe-4S] cluster. {ECO:0000269|PubMed:22678361}; | apoptotic process [GO:0006915]; bone mineralization [GO:0030282]; central nervous system myelin formation [GO:0032289]; chromosome segregation [GO:0007059]; determination of adult lifespan [GO:0008340]; embryonic cleavage [GO:0040016]; embryonic organ development [GO:0048568]; erythrocyte maturation [GO:0043249]; extra... | CAK-ERCC2 complex [GO:0070516]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; MMXD complex [GO:0071817]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle [GO:0005819]; transcription factor TFIID complex [GO:0005669]; transcription factor TFIIH core complex [GO:0000439]; transcription factor TFIIH holo complex [G... | 4 iron, 4 sulfur cluster binding [GO:0051539]; 5'-3' DNA helicase activity [GO:0043139]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; damaged DNA binding [GO:0003684]; DNA helicase activity [GO:0003678]; metal ion binding [GO:0046872]; protein-macromolecule adaptor activity [GO:0030674] | PF06733;PF06777;PF13307; | 3.40.50.300; | Helicase family, RAD3/XPD subfamily | PTM: ISGylated. {ECO:0000305|PubMed:16884686}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20797633, ECO:0000269|PubMed:23585563}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:20797633}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; | null | null | null | null | FUNCTION: ATP-dependent 5'-3' DNA helicase, component of the general transcription and DNA repair factor IIH (TFIIH) core complex, which is involved in general and transcription-coupled nucleotide excision repair (NER) of damaged DNA and, when complexed to CAK, in RNA transcription by RNA polymerase II. In NER, TFIIH a... | Homo sapiens (Human) |
P18075 | BMP7_HUMAN | MHVRSLRAAAPHSFVALWAPLFLLRSALADFSLDNEVHSSFIHRRLRSQERREMQREILSILGLPHRPRPHLQGKHNSAPMFMLDLYNAMAVEEGGGPGGQGFSYPYKAVFSTQGPPLASLQDSHFLTDADMVMSFVNLVEHDKEFFHPRYHHREFRFDLSKIPEGEAVTAAEFRIYKDYIRERFDNETFRISVYQVLQEHLGRESDLFLLDSRTLWASEEGWLVFDITATSNHWVVNPRHNLGLQLSVETLDGQSINPKLAGLIGRHGPQNKQPFMVAFFKATEVHFRSIRSTGSKQRSQNRSKTPKNQEALRMANVAE... | null | null | allantois development [GO:1905069]; ameloblast differentiation [GO:0036305]; axon guidance [GO:0007411]; BMP signaling pathway [GO:0030509]; branching involved in salivary gland morphogenesis [GO:0060445]; branching morphogenesis of an epithelial tube [GO:0048754]; cardiac muscle tissue development [GO:0048738]; cardia... | collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; vesicle [GO:0031982] | BMP receptor binding [GO:0070700]; cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; heparin binding [GO:0008201] | PF00019;PF00688; | 2.60.120.970;2.10.90.10; | TGF-beta family | PTM: Several N-termini starting at positions 293, 300, 315 and 316 have been identified by direct sequencing resulting in secretion of different mature forms. {ECO:0000269|PubMed:17977014}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Growth factor of the TGF-beta superfamily that plays important role in various biological processes, including embryogenesis, hematopoiesis, neurogenesis and skeletal morphogenesis (PubMed:31208997). Initiates the canonical BMP signaling cascade by associating with type I receptor ACVR1 and type II receptor A... | Homo sapiens (Human) |
P18077 | RL35A_HUMAN | MSGRLWSKAIFAGYKRGLRNQREHTALLKIEGVYARDETEFYLGKRCAYVYKAKNNTVTPGGKPNKTRVIWGKVTRAHGNSGMVRAKFRSNLPAKAIGHRIRVMLYPSRI | null | null | cytoplasmic translation [GO:0002181]; ribosomal large subunit biogenesis [GO:0042273]; rRNA processing [GO:0006364]; translation [GO:0006412] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; cytosolic ribosome [GO:0022626]; extracellular exosome [GO:0070062]; membrane [GO:0016020] | RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735]; tRNA binding [GO:0000049] | PF01247; | 2.40.10.190; | Eukaryotic ribosomal protein eL33 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399}. | null | null | null | null | null | FUNCTION: Component of the large ribosomal subunit (PubMed:23636399, PubMed:32669547). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:23636399, PubMed:32669547). Required for the proliferation and viability of hematopoietic cells (PubMed:18535205). {ECO:0... | Homo sapiens (Human) |
P18084 | ITB5_HUMAN | MPRAPAPLYACLLGLCALLPRLAGLNICTSGSATSCEECLLIHPKCAWCSKEDFGSPRSITSRCDLRANLVKNGCGGEIESPASSFHVLRSLPLSSKGSGSAGWDVIQMTPQEIAVNLRPGDKTTFQLQVRQVEDYPVDLYYLMDLSLSMKDDLDNIRSLGTKLAEEMRKLTSNFRLGFGSFVDKDISPFSYTAPRYQTNPCIGYKLFPNCVPSFGFRHLLPLTDRVDSFNEEVRKQRVSRNRDAPEGGFDAVLQAAVCKEKIGWRKDALHLLVFTTDDVPHIALDGKLGGLVQPHDGQCHLNEANEYTASNQMDYPSLA... | null | null | cell adhesion mediated by integrin [GO:0033627]; cell migration [GO:0016477]; cell-cell adhesion [GO:0098609]; cell-matrix adhesion [GO:0007160]; endodermal cell differentiation [GO:0035987]; epithelial cell-cell adhesion [GO:0090136]; integrin-mediated signaling pathway [GO:0007229]; stress fiber assembly [GO:0043149]... | cell surface [GO:0009986]; extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; integrin alphav-beta5 complex [GO:0034684]; integrin complex [GO:0008305]; phagocytic vesicle [GO:0045335]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | integrin binding [GO:0005178]; metal ion binding [GO:0046872]; virus receptor activity [GO:0001618] | PF18372;PF08725;PF07965;PF00362;PF17205; | 4.10.1240.30;1.20.5.100;2.10.25.10;3.30.1680.10;2.60.40.1510;3.40.50.410; | Integrin beta chain family | null | SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Integrin alpha-V/beta-5 (ITGAV:ITGB5) is a receptor for fibronectin. It recognizes the sequence R-G-D in its ligand.; FUNCTION: (Microbial infection) Integrin ITGAV:ITGB5 acts as a receptor for adenovirus type C. {ECO:0000269|PubMed:20615244}. | Homo sapiens (Human) |
P18085 | ARF4_HUMAN | MGLTISSLFSRLFGKKQMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEYKNICFTVWDVGGQDRIRPLWKHYFQNTQGLIFVVDSNDRERIQEVADELQKMLLVDELRDAVLLLFANKQDLPNAMAISEMTDKLGLQSLRNRTWYVQATCATQGTGLYEGLDWLSNELSKR | null | null | apical protein localization [GO:0045176]; cell migration [GO:0016477]; cilium assembly [GO:0060271]; dendritic spine development [GO:0060996]; endoplasmic reticulum to Golgi vesicle-mediated transport [GO:0006888]; establishment or maintenance of epithelial cell apical/basal polarity [GO:0045197]; intracellular protein... | cytosol [GO:0005829]; dendritic spine [GO:0043197]; extracellular exosome [GO:0070062]; glutamatergic synapse [GO:0098978]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; plasma membrane [GO:0005886]; ruffle membrane [GO:0032587] | epidermal growth factor receptor binding [GO:0005154]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; guanyl-nucleotide exchange factor activity [GO:0005085]; NAD+-protein-arginine ADP-ribosyltransferase activity [GO:0106274]; phospholipase D activator activity [GO:1990583] | PF00025; | 3.40.50.300; | Small GTPase superfamily, Arf family | null | SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000269|PubMed:25673879}. Membrane {ECO:0000305}; Lipid-anchor {ECO:0000305}. | null | null | null | null | null | FUNCTION: GTP-binding protein that functions as an allosteric activator of the cholera toxin catalytic subunit, an ADP-ribosyltransferase. Involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus. Part of the ciliary targeting complex containing Rab11, ASAP1, Rabin8/RAB3IP,... | Homo sapiens (Human) |
P18088 | DCE1_RAT | MASSTPSPATSSNAGADPNTTNLRPTTYDTWCGVAHGCTRKLGLKICGFLQRTNSLEEKSRLVSAFRERQASKNLLSCENSDPGARFRRTETDFSNLFAQDLLPAKNGEEQTVQFLLEVVDILLNYVRKTFDRSTKVLDFHHPHQLLEGMEGFNLELSDHPESLEQILVDCRDTLKYGVRTGHPRFFNQLSTGLDIIGLAGEWLTSTANTNMFTYEIAPVFVLMEQITLKKMREIIGWSNKDGDGIFSPGGAISNMYSIMAARYKYFPEVKTKGMAAVPKLVLFTSEHSHYSIKKAGAALGFGTDNVILIKCNERGKIIP... | 4.1.1.15 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000250|UniProtKB:Q99259}; | cellular response to hypoxia [GO:0071456]; gamma-aminobutyric acid biosynthetic process [GO:0009449]; glutamate catabolic process [GO:0006538]; locomotory exploration behavior [GO:0035641]; response to auditory stimulus [GO:0010996]; response to caloric restriction [GO:0061771]; response to cocaine [GO:0042220]; respon... | axon [GO:0030424]; axon terminus [GO:0043679]; cell cortex [GO:0005938]; cytoplasm [GO:0005737]; GABA-ergic synapse [GO:0098982]; inhibitory synapse [GO:0060077]; neuron projection terminus [GO:0044306]; neuronal cell body [GO:0043025]; presynapse [GO:0098793]; presynaptic active zone [GO:0048786]; synapse [GO:0045202] | glutamate binding [GO:0016595]; glutamate decarboxylase activity [GO:0004351]; identical protein binding [GO:0042802]; protein-containing complex binding [GO:0044877]; pyridoxal phosphate binding [GO:0030170] | PF00282; | 3.90.1150.170;3.40.640.10; | Group II decarboxylase family | null | null | CATALYTIC ACTIVITY: Reaction=H(+) + L-glutamate = 4-aminobutanoate + CO2; Xref=Rhea:RHEA:17785, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:29985, ChEBI:CHEBI:59888; EC=4.1.1.15; Evidence={ECO:0000269|PubMed:1924335}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17786; Evidence={ECO:0000305|PubMed:1924335... | null | null | null | null | FUNCTION: Catalyzes the synthesis of the inhibitory neurotransmitter gamma-aminobutyric acid (GABA) with pyridoxal 5'-phosphate as cofactor. {ECO:0000269|PubMed:1924335}. | Rattus norvegicus (Rat) |
P18089 | ADA2B_HUMAN | MDHQDPYSVQATAAIAAAITFLILFTIFGNALVILAVLTSRSLRAPQNLFLVSLAAADILVATLIIPFSLANELLGYWYFRRTWCEVYLALDVLFCTSSIVHLCAISLDRYWAVSRALEYNSKRTPRRIKCIILTVWLIAAVISLPPLIYKGDQGPQPRGRPQCKLNQEAWYILASSIGSFFAPCLIMILVYLRIYLIAKRSNRRGPRAKGGPGQGESKQPRPDHGGALASAKLPALASVASAREVNGHSKSTGEKEEGETPEDTGTRALPPSWAALPNSGQGQKEGVCGASPEDEAEEEEEEEEEEEECEPQAVPVSPA... | null | null | activation of protein kinase B activity [GO:0032148]; adenylate cyclase-activating adrenergic receptor signaling pathway [GO:0071880]; adrenergic receptor signaling pathway [GO:0071875]; angiogenesis [GO:0001525]; cell-cell signaling [GO:0007267]; female pregnancy [GO:0007565]; G protein-coupled receptor signaling path... | cell surface [GO:0009986]; cytosol [GO:0005829]; intracellular membrane-bounded organelle [GO:0043231]; plasma membrane [GO:0005886] | alpha2-adrenergic receptor activity [GO:0004938]; epinephrine binding [GO:0051379] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family, Adrenergic receptor subfamily, ADRA2B sub-subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23105096, ECO:0000269|PubMed:26811329, ECO:0000269|PubMed:27901063}; Multi-pass membrane protein {ECO:0000269|PubMed:23105096}. Note=Interaction with RAB26, GGA1, GGA2 and GGA3 mediates transport from the Golgi to the cell membrane. {ECO:0000269|PubMed:23105096, E... | null | null | null | null | null | FUNCTION: Alpha-2 adrenergic receptors mediate the catecholamine-induced inhibition of adenylate cyclase through the action of G proteins. The rank order of potency for agonists of this receptor is clonidine > norepinephrine > epinephrine = oxymetazoline > dopamine > p-tyramine = phenylephrine > serotonin > p-synephrin... | Homo sapiens (Human) |
P18090 | ADRB1_RAT | MGAGALALGASEPCNLSSAAPLPDGAATAARLLVLASPPASLLPPASEGSAPLSQQWTAGMGLLLALIVLLIVVGNVLVIVAIAKTPRLQTLTNLFIMSLASADLVMGLLVVPFGATIVVWGRWEYGSFFCELWTSVDVLCVTASIETLCVIALDRYLAITLPFRYQSLLTRARARALVCTVWAISALVSFLPILMHWWRAESDEARRCYNDPKCCDFVTNRAYAIASSVVSFYVPLCIMAFVYLRVFREAQKQVKKIDSCERRFLTGPPRPPSPAPSPSPGPPRPADSLANGRSSKRRPSRLVALREQKALKTLGIIMG... | null | null | adenylate cyclase-activating adrenergic receptor signaling pathway [GO:0071880]; adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; brown fat cell differentiation [GO:0050873]; diet induced thermogenesis [GO:0002024]; fear response [GO:0042596]; G protein-coupled receptor signaling ... | early endosome [GO:0005769]; membrane [GO:0016020]; neuronal dense core vesicle [GO:0098992]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]; Schaffer collateral - CA1 synapse [GO:0098685] | alpha-2A adrenergic receptor binding [GO:0031694]; amine binding [GO:0043176]; beta1-adrenergic receptor activity [GO:0004940]; G protein-coupled neurotransmitter receptor activity involved in regulation of postsynaptic membrane potential [GO:0099579]; PDZ domain binding [GO:0030165]; protein heterodimerization activit... | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family, Adrenergic receptor subfamily, ADRB1 sub-subfamily | PTM: Homologous desensitization of the receptor is mediated by its phosphorylation by beta-adrenergic receptor kinase. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12391161}; Multi-pass membrane protein {ECO:0000269|PubMed:12391161}. Early endosome {ECO:0000250}. Note=Localized at the plasma membrane. Found in the Golgi upon GOPC overexpression (By similarity). Colocalizes with RAPGEF2 at the plasma membrane. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Beta-adrenergic receptors mediate the catecholamine-induced activation of adenylate cyclase through the action of G proteins. This receptor binds epinephrine and norepinephrine with approximately equal affinity. Mediates Ras activation through G(s)-alpha- and cAMP-mediated signaling (By similarity). Involved ... | Rattus norvegicus (Rat) |
P18091 | ACTN_DROME | MMMENGLSMEYGDGYMEQEEEWEREGLLDPAWEKQQKKTFTAWCNSHLRKAGTAIDNIEEDFRNGLKLMLLLEVISGETLPKPDRGKMRFHKIANVNKALDFIASKGVHLVSIGAEEIVDGNLKMTLGMIWTIILRFAIQDISVEEMTAKEGLLLWCQRKTAPYKNVNVQNFHLSFKDGLAFCALIHRHRPDLIDYAKLSKDNPLENLNTAFDVAEKYLDIPRMLDPDDLINTPKPDERAIMTYVSCYYHAFQGAQQVGNNTALPDERAVMTYVSSYYHCFSGAQKAETAANRICKVLKVNQENERLMEEYERLASDLLE... | null | null | actin cytoskeleton organization [GO:0030036]; actin filament bundle assembly [GO:0051017]; muscle cell development [GO:0055001]; sarcomere organization [GO:0045214] | cell junction [GO:0030054]; cell projection [GO:0042995]; cortical actin cytoskeleton [GO:0030864]; focal adhesion [GO:0005925]; plasma membrane [GO:0005886]; Z disc [GO:0030018] | actin binding [GO:0003779]; actin filament binding [GO:0051015]; calcium ion binding [GO:0005509] | PF00307;PF13405;PF08726;PF00435; | 1.20.58.60;1.10.418.10;1.10.238.10; | Alpha-actinin family | null | SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:17353360}. Note=Colocalizes with Smn at the Z-line of indirect flight muscles. | null | null | null | null | null | FUNCTION: F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. This is a bundling protein. {ECO:0000269|PubMed:1734023, ECO:0000269|PubMed:2112549}. | Drosophila melanogaster (Fruit fly) |
P18094 | ENV_HV2BE | MEPGRNQLFVVILLTSACLVYCSQYVTVFYGIPAWKNASIPLFCATKNRDTWGTIQCLPDNDDYQEIILNVTEAFDAWNNTVTEQAVEDVWHLFETSIKPCVKLTPLCVAMNCSRVQGNTTTPNPRTSSSTTSRPPTSAASIINETSNCIENNTCAGLGYEEMMQCEFNMKGLEQDKKRRYKDTWYLEDVVCDNTTAGTCYMRHCNTSIIKESCDKHYWDAMRFRYCAPPGFALLRCNDTNYSGFEPKCTKVVAASCTRMMETQTSTWFGFNGTRAENRTYIYWHGRDNRTIISLNKYYNLTMRCKRPGNKTVLPITLMS... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; suppression by virus of host tetherin activity [GO:0039587]; virion attachment to host cell [GO:0019062] | host cell endosome membrane [GO:0044175]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | structural molecule activity [GO:0005198] | PF00516;PF00517; | 1.10.287.210;2.170.40.20; | null | PTM: Specific enzymatic cleavages in vivo yield mature proteins. Envelope glycoproteins are synthesized as an inactive precursor that is heavily N-glycosylated and processed likely by host cell furin in the Golgi to yield the mature SU and TM proteins. The cleavage site between SU and TM requires the minimal sequence [... | SUBCELLULAR LOCATION: [Transmembrane protein gp41]: Virion membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Host endosome membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=It is p... | null | null | null | null | null | FUNCTION: The surface protein gp120 (SU) attaches the virus to the host lymphoid cell by binding to the primary receptor CD4. This interaction induces a structural rearrangement creating a high affinity binding site for a chemokine coreceptor like CXCR4 and/or CCR5. This peculiar 2 stage receptor-interaction strategy a... | Human immunodeficiency virus type 2 subtype A (isolate BEN) (HIV-2) |
P18095 | GAG_HV2BE | MGARNSVLRGKKADELEKVRLRPGGKKKYRLKHIVWAANELDKFGLAESLLESKEGCQKILRVLDPLVPTGSENLKSLFNTVCVIWCLHAEEKVKDTEEAKKLAQRHLVAETGTAEKMPNTSRPTAPPSGKRGNYPVQQAGGNYVHVPLSPRTLNAWVKLVEEKKFGAEVVPGFQALSEGCTPYDINQMLNCVGDHQAAMQIIREIINEEAADWDSQHPIPGPLPAGQLRDPRGSDIAGTTSTVDEQIQWMYRPQNPVPVGNIYRRWIQIGLQKCVRKYNPTNILDIKQGPKEPFQSYVDRFYKSLRAEQTDPAVKNWMT... | null | null | viral budding via host ESCRT complex [GO:0039702] | host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | RNA binding [GO:0003723]; structural molecule activity [GO:0005198]; zinc ion binding [GO:0008270] | PF00540;PF00607;PF19317;PF00098; | 1.10.1200.30;1.10.375.10;1.10.150.90;1.20.5.760;4.10.60.10; | Primate lentivirus group gag polyprotein family | PTM: Gag-Pol polyprotein: Specific enzymatic cleavages by the viral protease yield mature proteins. {ECO:0000250|UniProtKB:P12493}.; PTM: [Matrix protein p17]: Tyrosine phosphorylated presumably in the virion by a host kinase. Phosphorylation is apparently not a major regulator of membrane association. {ECO:0000250|Uni... | SUBCELLULAR LOCATION: [Gag polyprotein]: Host cell membrane {ECO:0000250|UniProtKB:P12493}; Lipid-anchor {ECO:0000250|UniProtKB:P12493}. Host endosome, host multivesicular body {ECO:0000250|UniProtKB:P12493}. Note=These locations are probably linked to virus assembly sites. The main location is the cell membrane, but u... | null | null | null | null | null | FUNCTION: [Gag polyprotein]: Mediates, with Gag-Pol polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 2 subtype A (isolate BEN) (HIV-2) |
P18096 | POL_HV2BE | MGARNSVLRGKKADELEKVRLRPGGKKKYRLKHIVWAANELDKFGLAESLLESKEGCQKILRVLDPLVPTGSENLKSLFNTVCVIWCLHAEEKVKDTEEAKKLAQRHLVAETGTAEKMPNTSRPTAPPSGKRGNYPVQQAGGNYVHVPLSPRTLNAWVKLVEEKKFGAEVVPGFQALSEGCTPYDINQMLNCVGDHQAAMQIIREIINEEAADWDSQHPIPGPLPAGQLRDPRGSDIAGTTSTVDEQIQWMYRPQNPVPVGNIYRRWIQIGLQKCVRKYNPTNILDIKQGPKEPFQSYVDRFYKSLRAEQTDPAVKNWMT... | 2.7.7.-; 2.7.7.49; 2.7.7.7; 3.1.-.-; 3.1.13.2; 3.1.26.13; 3.4.23.47 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for reverse transcriptase polymerase activity. {ECO:0000250}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; Note=Binds 2 magnesium ions for ribonuclease H (RNase H) activity. Substrate-binding is ... | DNA integration [GO:0015074]; DNA recombination [GO:0006310]; establishment of integrated proviral latency [GO:0075713]; proteolysis [GO:0006508]; symbiont entry into host cell [GO:0046718]; symbiont-mediated suppression of host gene expression [GO:0039657]; viral genome integration into host DNA [GO:0044826]; viral pe... | host cell [GO:0043657]; host cell nucleus [GO:0042025]; host cell plasma membrane [GO:0020002]; host multivesicular body [GO:0072494]; membrane [GO:0016020]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | aspartic-type endopeptidase activity [GO:0004190]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; exoribonuclease H activity [GO:0004533]; lipid binding [GO:0008289]; RNA stem-loop binding [GO:0035613]; RNA-directed DNA polymerase activity [GO:0003964]; RNA-DNA hybrid ribonuclease activity... | PF00540;PF00607;PF19317;PF00552;PF02022;PF00075;PF00665;PF00077;PF00078;PF06815;PF06817;PF00098; | 1.10.10.200;1.10.1200.30;3.30.70.270;2.40.70.10;3.10.10.10;1.10.375.10;1.10.150.90;2.30.30.10;3.30.420.10;1.20.5.760;4.10.60.10; | null | PTM: [Gag-Pol polyprotein]: Specific enzymatic cleavages by the viral protease yield mature proteins. The protease is released by autocatalytic cleavage. The polyprotein is cleaved during and after budding, this process is termed maturation. Proteolytic cleavage of p66 RT removes the RNase H domain to yield the p51 RT ... | SUBCELLULAR LOCATION: [Gag-Pol polyprotein]: Host cell membrane; Lipid-anchor. Host endosome, host multivesicular body. Note=These locations are linked to virus assembly sites. The main location is the cell membrane, but under some circumstances, late endosomal compartments can serve as productive sites for virion asse... | CATALYTIC ACTIVITY: Reaction=Endopeptidase for which the P1 residue is preferably hydrophobic.; EC=3.4.23.47; Evidence={ECO:0000255|PROSITE-ProRule:PRU00275}; CATALYTIC ACTIVITY: Reaction=Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immun... | null | null | null | null | FUNCTION: [Gag-Pol polyprotein]: Mediates, with Gag polyprotein, the essential events in virion assembly, including binding the plasma membrane, making the protein-protein interactions necessary to create spherical particles, recruiting the viral Env proteins, and packaging the genomic RNA via direct interactions with ... | Human immunodeficiency virus type 2 subtype A (isolate BEN) (HIV-2) |
P18101 | RL40_DROME | MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGIIEPSLRILAQKYNCDKMICRKCYARLHPRATNCRKKKCGHTNNLRPKKKLK | null | null | cytoplasmic translation [GO:0002181]; modification-dependent protein catabolic process [GO:0019941]; protein modification process [GO:0036211]; protein ubiquitination [GO:0016567]; translation [GO:0006412]; ubiquitin-dependent protein catabolic process [GO:0006511] | cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; cytosolic small ribosomal subunit [GO:0022627]; nucleus [GO:0005634] | protein tag activity [GO:0031386]; RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735]; ubiquitin protein ligase binding [GO:0031625] | PF01020;PF00240; | 4.10.1060.50; | Ubiquitin family; Eukaryotic ribosomal protein eL40 family | null | SUBCELLULAR LOCATION: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.; SUBCELLULAR LOCATION: [Large ribosomal subunit protein eL40]: Cytoplasm {ECO:0000250}. | null | null | null | null | null | FUNCTION: [Ubiquitin]: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polyme... | Drosophila melanogaster (Fruit fly) |
P18102 | TLL_DROME | MQSSEGSPDMMDQKYNSVRLSPAASSRILYHVPCKVCRDHSSGKHYGIYACDGCAGFFKRSIRRSRQYVCKSQKQGLCVVDKTHRNQCRACRLRKCFEVGMNKDAVQHERGPRNSTLRRHMAMYKDAMMGAGEMPQIPAEILMNTAALTGFPGVPMPMPGLPQRAGHHPAHMAAFQPPPSAAAVLDLSVPRVPHHPVHQGHHGFFSPTAAYMNALATRALPPTPPLMAAEHIKETAAEHLFKNVNWIKSVRAFTELPMPDQLLLLEESWKEFFILAMAQYLMPMNFAQLLFVYESENANREIMGMVTREVHAFQEVLNQL... | null | null | Bolwig's organ morphogenesis [GO:0001746]; cell differentiation [GO:0030154]; cell fate commitment [GO:0045165]; cell fate specification [GO:0001708]; insect visual primordium development [GO:0001748]; inter-male aggressive behavior [GO:0002121]; mushroom body development [GO:0016319]; negative regulation of transcript... | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; nuclear receptor activity [GO:0004879]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; transcription corepressor binding [GO:0001222]; zinc ion binding [GO:0008270] | 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: Orphan receptor that binds DNA as a monomer to hormone response elements (HRE) containing an extended core motif half-site sequence 5'-AAGTCA-3' in which the 5' flanking nucleotides participate in determining receptor specificity. This receptor binds to the consensus sequence [AG][AG]AAGTCAA. Plays a key role... | Drosophila melanogaster (Fruit fly) |
P18105 | NOD_DROME | MEGAKLSAVRIAVREAPYRQFLGRREPSVVQFPPWSDGKSLIVDQNEFHFDHAFPATISQDEMYQALILPLVDKLLEGFQCTALAYGQTGTGKSYSMGMTPPGEILPEHLGILPRALGDIFERVTARQENNKDAIQVYASFIEIYNEKPFDLLGSTPHMPMVAARCQRCTCLPLHSQADLHHILELGTRNRRVRPTNMNSNSSRSHAIVTIHVKSKTHHSRMNIVDLAGSEGVRRTGHEGVARQEGVNINLGLLSINKVVMSMAAGHTVIPYRDSVLTTVLQASLTAQSYLTFLACISPHQCDLSETLSTLRFGTSAKKL... | null | null | distributive segregation [GO:0032837]; establishment of meiotic spindle orientation [GO:0051296]; female meiotic nuclear division [GO:0007143]; meiotic chromosome segregation [GO:0045132]; microtubule-based movement [GO:0007018]; positive regulation of microtubule polymerization [GO:0031116]; spindle assembly involved ... | cytoplasm [GO:0005737]; kinesin complex [GO:0005871]; microtubule [GO:0005874] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; microtubule binding [GO:0008017]; microtubule motor activity [GO:0003777]; microtubule plus-end binding [GO:0051010] | PF00225; | 1.10.150.280;3.40.850.10; | TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. | null | null | null | null | null | FUNCTION: Required for the distributive chromosome segregation of non-exchange chromosomes during meiosis. May be a microtubule motor required to hold distributively 'paired' chromosomes at the metaphase plate until anaphase. | Drosophila melanogaster (Fruit fly) |
P18106 | FER_DROME | MGFSSALQSRAAHEALIVRQDAELRLMETMKRSIQMKAKCDKEYAISLTAVAQQGLKIDRADEMQGSLISKSWRSYMDELDHQAKQFKFNAEQLEVVCDKLTHLSQDKRKARKAYQEEHAKIAARLNHLTDEVVRKKSEYQKHLEGYKALRTRFEENYIKAPSRSGRKLDDVRDKYQKACRKLHLTHNEYVLSITEAIEVEKDFRNVLLPGLLEHQQSVQESFILLWRNILQEAAQYGDLTADKYKEIQKRIDTVIGSINPTEEYGEFTEKYKTSPTTPLLFQFDETLIQDIPGKLQSSTLTVDNLTVDWLRNRLQELEG... | 2.7.10.2 | null | actin filament bundle assembly [GO:0051017]; axon guidance [GO:0007411]; cell adhesion [GO:0007155]; chemotaxis [GO:0006935]; dorsal closure [GO:0007391]; dorsal closure, amnioserosa morphology change [GO:0046664]; dorsal closure, elongation of leading edge cells [GO:0007394]; phosphorylation [GO:0016310]; regulation o... | adherens junction [GO:0005912]; extrinsic component of cytoplasmic side of plasma membrane [GO:0031234] | ATP binding [GO:0005524]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; phospholipid binding [GO:0005543]; protein tyrosine kinase activity [GO:0004713] | PF00611;PF07714;PF00017; | 1.20.1270.60;3.30.505.10;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, Fes/fps subfamily | null | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:9038371}; Peripheral membrane protein {ECO:0000269|PubMed:9038371}. Cell junction, adherens junction {ECO:0000269|PubMed:9038371}. Note=At stages 11-12 of embryogenesis, localizes to adherens junctions in epidermal cells. At stages 13-14, is no longer detected in the 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=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Tyrosine-protein kinase which is required during embryogenesis for formation of the actin cable in leading edge cells of the dorsal epidermis and for the timely progression of dorsal closure. May play a role in regulation of adherens junctions and cell adhesion through phosphorylation of the beta-catenin arm.... | Drosophila melanogaster (Fruit fly) |
P18111 | CDX1_MOUSE | MYVGYVLDKDSPVYPGPARPSSLGLGPPTYAPPGPAPAPPQYPDFAGYTHVEPAPAPPPTWAAPFPAPKDDWAAAYGPGPTASAASPAPLAFGPPPDFSPVPAPPGPGPGILAQSLGAPGAPSSPGAPRRTPYEWMRRSVAAAGGGGSGKTRTKDKYRVVYTDHQRLELEKEFHYSRYITIRRKSELAANLGLTERQVKIWFQNRRAKERKVNKKKQQQQQPLPPTQLPLPLDGTPTPSGPPLGSLCPTNAGLLGTPSPVPVKEEFLP | null | null | animal organ morphogenesis [GO:0009887]; anterior/posterior axis specification [GO:0009948]; anterior/posterior pattern specification [GO:0009952]; bone morphogenesis [GO:0060349]; cell differentiation [GO:0030154]; embryo development [GO:0009790]; pattern specification process [GO:0007389]; positive regulation of tran... | nucleus [GO:0005634] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; methyl-CpG binding [GO:0008327]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; RNA polymerase II transcription regulatory region sequence-s... | PF04731;PF00046; | 1.10.10.60; | Caudal homeobox family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Plays a role in transcriptional regulation. Involved in activated KRAS-mediated transcriptional activation of PRKD1 in colorectal cancer (CRC) cells. Binds to the PRKD1 promoter in colorectal cancer (CRC) cells. Could play a role in the terminal differentiation of the intestine. Binds preferentially to methyl... | Mus musculus (Mouse) |
P18113 | THB_RAT | MTPNSMTENRLPAWDKQKPHPDRGQDWKLVGMSEACLHRKSHVERRGALKNEQTSSHLIQATWASSIFHLDPDDVNDQSVSSAQTFQTEEKKCKGYIPSYLDKDELCVVCGDKATGYHYRCITCEGCKGFFRRTIQKSLHPSYSCKYEGKCIIDKVTRNQCQECRFKKCIYVGMATDLVLDDSKRLAKRKLIEENREKRRREELQKSIGHKPEPTDEEWELIKTVTEAHVATNAQGSHWKQKRKFLPEDIGQAPIVNAPEGGQVDLEAFSHFTKIITPAITRVVDFAKKLPMFCELPCEDQIILLKGCCMEIMSLRAAVR... | null | null | animal organ morphogenesis [GO:0009887]; cell differentiation [GO:0030154]; cellular response to thyroid hormone stimulus [GO:0097067]; embryonic organ development [GO:0048568]; female courtship behavior [GO:0008050]; mRNA transcription by RNA polymerase II [GO:0042789]; negative regulation of DNA-templated transcripti... | nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575] | chromatin binding [GO:0003682]; chromatin DNA binding [GO:0031490]; double-stranded DNA binding [GO:0003690]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; nuclear receptor activity [GO:0004879]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific... | PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR1 subfamily | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Nuclear hormone receptor that can act as a repressor or activator of transcription. High affinity receptor for thyroid hormones, including triiodothyronine and thyroxine. | Rattus norvegicus (Rat) |
P18115 | THAB_XENLA | MDQNLSGLDCLSEPDEKRWPDGKRKRKNSQCMGKSGMSGDSLVSLPPAGYIPSYLDKDEPCVVCSDKATGYHYRCITCEGCKGFFRRTIQKNLHPSYSCKYDGCCIIDKITRNQCQLCRFKKCIAVGMAMDLVLDDSKRVAKRKLIEENRVRRRKEEMIKTLQQRPEPSSEEWELIRIVTEAHRSTNAQGSHWKQRRKFLPEDIGQSPMASMPDGDKVDLEAFSEFTKIITPAITRVVDFAKKLPMFSELTCEDQIILLKGCCMEIMSLRAAVRYDPDSETLTLSGEMAVKREQLKNGGLGVVSDAIFDLGRSLAAFNLD... | null | null | cell differentiation [GO:0030154]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; retinoic acid receptor signaling pathway [GO:0048384]; thyroid hormone media... | nucleus [GO:0005634] | nuclear receptor activity [GO:0004879]; nuclear retinoid X receptor binding [GO:0046965]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; thyr... | PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR1 subfamily | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: High affinity receptor for triiodothyronine (T3). {ECO:0000269|PubMed:2402492, ECO:0000269|PubMed:8969201}. | Xenopus laevis (African clawed frog) |
P18117 | THBA_XENLA | MPSSMSGYIPSYLDKDELCVVCGDKATGYHYRCITCEGCKGFFRRTIQKNLHPSYSCKYEGKCVIDKVTRNQCQECRFKKCIAVGMATDLVLDDNKRLAKRKLIEENREKRRKDEIQKSLVQKPEPTQEEWELIQVVTEAHVATNAQGSHWKQKRKFLPEDIGQAPIVNAPEGGKVDLEAFSQFTKIITPAITRVVDFAKKLPMFCELPCEDQIILLKGCCMEIMSLRAAVRYDPESETLTLNGEMAVTRGQLKNGGLGVVSDAIFDLGVSLSSFSLDDTEVALLQAVLLMSSDRPGLASVERIEKCQEGFLLAFEHYIN... | null | null | cell differentiation [GO:0030154]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of transcription by RNA polymerase II [GO:0045944]; retinoic ac... | nucleus [GO:0005634] | nuclear receptor activity [GO:0004879]; protein heterodimerization activity [GO:0046982]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565]; thyroid hormone binding [GO:0070324]; zinc ion binding [GO:0008270] | PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR1 subfamily | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: High affinity receptor for triiodothyronine (T3). {ECO:0000269|PubMed:12553426, ECO:0000269|PubMed:15590892, ECO:0000269|PubMed:16627555}. | Xenopus laevis (African clawed frog) |
P18122 | CATA1_MAIZE | MDPYKHRPSSGSNSSFWTTNSGAPVWNNNSALTVGQRGPILLEDYHLIEKLAQFDRERIPERVVHARGASAKGFFEVTHDVSHLTCADFLRAPGVQTPVIVRFSTVVHERGSPETLRDPRGFAVKFYTREGNFDLVGNNMPVFFIRDGMKFPDMVHAFKPNPKTNLQENWRIVDFFSHHPESLHMFTFLFDDVGIPLNYRHMEGFGVNTYSLINRDGKPHLVKFHWKPTCGVKCLLDNEAVTVGGTCHSHATKDLYDSIAAGNYPEWKLYIQTIDLDHEDKFDFDPLDVTKTWPEDIIPLQPVGRMVLNKNVDNFFAENE... | 1.11.1.6 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; | circadian rhythm [GO:0007623]; cold acclimation [GO:0009631]; hydrogen peroxide catabolic process [GO:0042744]; regulation of cellular response to heat [GO:1900034]; response to abscisic acid [GO:0009737]; response to absence of light [GO:0009646]; response to auxin [GO:0009733]; response to cadmium ion [GO:0046686]; r... | cytoplasm [GO:0005737]; peroxisome [GO:0005777]; plasma membrane [GO:0005886] | catalase activity [GO:0004096]; heme binding [GO:0020037]; metal ion binding [GO:0046872] | PF00199;PF06628; | 2.40.180.10; | Catalase family | null | SUBCELLULAR LOCATION: Peroxisome. | CATALYTIC ACTIVITY: Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU10013}; | null | null | null | null | FUNCTION: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. | Zea mays (Maize) |
P18123 | CATA3_MAIZE | MTMDPTKFRPSSSHDTTVTTTNAGAPVWNDNEALTVGPRGPILLEDYHLIEKVAHFARERIPERVVHARGASAKGFFECTHDVTSLTCADFLRAPGVRTPVIVRFSTVIHERGSPETIRDPRGFAVKFYTREGNWDLLGNNFPVFFIRDGIKFPDVIHAFKPNPRSHVQEYWRVFDFLSHLPESLHTFFFLFDDVGVPSDYRHMEGFGVNTYTFVSAAGKAQYVKFHWKPTCGVRCILTDEEAALVGGRNHSHATQDLYDSIAAGSFPEWTLYVQVMDPDTEEQYDFDPLDDTKTWPEDLLPLRPVGRLVLDRNVDNFFN... | 1.11.1.6 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; | circadian rhythm [GO:0007623]; cold acclimation [GO:0009631]; hydrogen peroxide catabolic process [GO:0042744]; response to auxin [GO:0009733]; response to hydrogen peroxide [GO:0042542]; response to oxidative stress [GO:0006979]; response to reactive oxygen species [GO:0000302]; response to xenobiotic stimulus [GO:000... | cytoplasm [GO:0005737]; mitochondrion [GO:0005739]; peroxisome [GO:0005777]; plasma membrane [GO:0005886] | catalase activity [GO:0004096]; heme binding [GO:0020037]; metal ion binding [GO:0046872] | PF00199;PF06628; | 2.40.180.10; | Catalase family | null | SUBCELLULAR LOCATION: Mitochondrion. | CATALYTIC ACTIVITY: Reaction=2 H2O2 = 2 H2O + O2; Xref=Rhea:RHEA:20309, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240; EC=1.11.1.6; Evidence={ECO:0000255|PROSITE-ProRule:PRU10013}; | null | null | null | null | FUNCTION: Occurs in almost all aerobically respiring organisms and serves to protect cells from the toxic effects of hydrogen peroxide. Its levels are highest in the light period and are lowest in the dark period, hence it may be important for scavenging hydrogen peroxide at night, rather than during the day. | Zea mays (Maize) |
P18124 | RL7_HUMAN | MEGVEEKKKEVPAVPETLKKKRRNFAELKIKRLRKKFAQKMLRKARRKLIYEKAKHYHKEYRQMYRTEIRMARMARKAGNFYVPAEPKLAFVIRIRGINGVSPKVRKVLQLLRLRQIFNGTFVKLNKASINMLRIVEPYIAWGYPNLKSVNELIYKRGYGKINKKRIALTDNALIARSLGKYGIICMEDLIHEIYTVGKRFKEANNFLWPFKLSSPRGGMKKKTTHFVEGGDAGNREDQINRLIRRMN | null | null | cytoplasmic translation [GO:0002181]; maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000463]; ribosomal large subunit biogenesis [GO:0042273]; rRNA processing [GO:0006364]; translation [GO:0006412] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic large ribosomal subunit [GO:0022625]; cytosolic ribosome [GO:0022626]; focal adhesion [GO:0005925]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleus [GO:0005634]; postsynaptic density [GO:0014069]; ribonucleoprotein complex [GO:1990904] | DNA binding [GO:0003677]; identical protein binding [GO:0042802]; mRNA binding [GO:0003729]; RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735] | PF00327;PF08079; | 3.30.1390.20; | Universal ribosomal protein uL30 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23636399}. | null | null | null | null | null | FUNCTION: Component of the large ribosomal subunit (PubMed:12962325, PubMed:23636399, PubMed:32669547). The ribosome is a large ribonucleoprotein complex responsible for the synthesis of proteins in the cell (PubMed:12962325, PubMed:23636399, PubMed:32669547). Binds to G-rich structures in 28S rRNA and in mRNAs (PubMed... | Homo sapiens (Human) |
P18125 | CP7A1_RAT | MMTISLIWGIAVLVSCCIWFIVGIRRRKAGEPPLENGLIPYLGCALKFGSNPLEFLRANQRKHGHVFTCKLMGKYVHFITNSLSYHKVLCHGKYFDWKKFHYTTSAKAFGHRSIDPNDGNTTENINNTFTKTLQGDALCSLSEAMMQNLQSVMRPPGLPKSKSNAWVTEGMYAFCYRVMFEAGYLTLFGRDISKTDTQKALILNNLDNFKQFDQVFPALVAGLPIHLFKTAHKAREKLAEGLKHKNLCVRDQVSELIRLRMFLNDTLSTFDDMEKAKTHLAILWASQANTIPATFWSLFQMIRSPEAMKAASEEVSGALQ... | 1.14.14.23; 1.14.14.26 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P22680}; | bile acid and bile salt transport [GO:0015721]; bile acid biosynthetic process [GO:0006699]; bile acid signaling pathway [GO:0038183]; cellular response to cholesterol [GO:0071397]; cellular response to glucose stimulus [GO:0071333]; cholesterol catabolic process [GO:0006707]; cholesterol homeostasis [GO:0042632]; nega... | endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231] | 24-hydroxycholesterol 7alpha-hydroxylase activity [GO:0033782]; cholesterol 7-alpha-monooxygenase activity [GO:0008123]; heme binding [GO:0020037]; iron ion binding [GO:0005506] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305|PubMed:1694852}; Single-pass membrane protein {ECO:0000305}. Microsome membrane {ECO:0000305|PubMed:1694852}; Single-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=cholesterol + O2 + reduced [NADPH--hemoprotein reductase] = 7alpha-hydroxycholesterol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:21812, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16113, ChEBI:C... | null | PATHWAY: Lipid metabolism; bile acid biosynthesis. {ECO:0000305|PubMed:1694852, ECO:0000305|PubMed:2335522}.; PATHWAY: Steroid metabolism; cholesterol degradation. {ECO:0000305|PubMed:1694852, ECO:0000305|PubMed:2335522}. | null | null | FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of endogenous cholesterol and its oxygenated derivatives (oxysterols) (PubMed:1694852, PubMed:2335522). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electron... | Rattus norvegicus (Rat) |
P18130 | ADA1A_BOVIN | MVFLSGNASDSSNCTHPPPPVNISKAILLGVILGGLILFGVLGNILVILSVACHRHLHSVTHYYIVNLAVADLLLTSTVLPFSAIFEILGYWAFGRVFCNVWAAVDVLCCTASIMGLCIISIDRYIGVSYPLRYPTIVTQKRGLMALLCVWALSLVISIGPLFGWRQPAPEDETICQINEEPGYVLFSALGSFYVPLTIILVMYCRVYVVAKRESRGLKSGLKTDKSDSEQVTLRIHRKNAQVGGSGVTSAKNKTHFSVRLLKFSREKKAAKTLGIVVGCFVLCWLPFFLVMPIGSFFPDFRPSETVFKIAFWLGYLNSC... | null | null | adenylate cyclase-activating adrenergic receptor signaling pathway [GO:0071880]; cell-cell signaling [GO:0007267]; phospholipase C-activating G protein-coupled receptor signaling pathway [GO:0007200]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; positive regulation of heart rate by epinephri... | caveola [GO:0005901]; cytoplasm [GO:0005737]; nuclear membrane [GO:0031965]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | alpha1-adrenergic receptor activity [GO:0004937]; protein heterodimerization activity [GO:0046982] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family, Adrenergic receptor subfamily, ADRA1A sub-subfamily | null | SUBCELLULAR LOCATION: Nucleus membrane; Multi-pass membrane protein. Cell membrane {ECO:0000250|UniProtKB:P35348}; Multi-pass membrane protein {ECO:0000255}. Cytoplasm {ECO:0000250|UniProtKB:P35348}. Membrane, caveola {ECO:0000250|UniProtKB:P35348}. Note=Location at the nuclear membrane facilitates heterooligomerizatio... | null | null | null | null | null | FUNCTION: This alpha-adrenergic receptor mediates its action by association with G proteins that activate a phosphatidylinositol-calcium second messenger system. Its effect is mediated by G(q) and G(11) proteins. Nuclear ADRA1A-ADRA1B heterooligomers regulate phenylephrine (PE)-stimulated ERK signaling in cardiac myocy... | Bos taurus (Bovine) |
P18141 | GLYC_TACVF | MGQFISFMQEIPIFLQEALNIALVAVSLICIVKGLVNLYRCGLFQLMVFLVLAGRSCSEETFKIGMHTKFQEVSLSLSALLTNQSHELPMLCLANKTHLYLKSGRSSFKINIDSVTVLTRSEVNLTSINLTRSIDVFVHSPKLGSCFESDEEWVVAWWIEAIGHRWDQDPGLLCRNKTKTEGKLIQINISRADGNVHYGWRLKNGLDHIYRGREEPCFEGEQCLIKIQPEDWPTDCKADHTNTFRFLSRSQKSIAVGRTLKAFFSWSLTDPLGNEAPGGYCLEKWMLVASELKCFGNTAIAKCNQNHDSEFCDMLRLFDY... | null | null | fusion of virus membrane with host endosome membrane [GO:0039654]; receptor-mediated endocytosis of virus by host cell [GO:0019065]; virion attachment to host cell [GO:0019062] | host cell endoplasmic reticulum membrane [GO:0044167]; host cell Golgi membrane [GO:0044178]; host cell plasma membrane [GO:0020002]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | metal ion binding [GO:0046872] | PF00798; | 6.10.140.1590;2.20.28.180; | Arenaviridae GPC protein family | PTM: [Pre-glycoprotein polyprotein GP complex]: Specific enzymatic cleavages in vivo yield mature proteins. GP-C polyprotein is cleaved in the endoplasmic reticulum by the host protease MBTPS1. Only cleaved glycoprotein is incorporated into virions. The SSP remains stably associated with the GP complex following cleava... | SUBCELLULAR LOCATION: [Stable signal peptide]: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host endoplasmic reticulum membrane {ECO:0000255|HAMAP-Rule:MF_04084}; Single-pass type II membrane protein {ECO:0000255|HAMAP-Rule:MF_04084}. Host Go... | null | null | null | null | null | FUNCTION: [Stable signal peptide]: Functions as a cleaved signal peptide that is retained as the third component of the GP complex (GP-C). Helps to stabilize the spike complex in its native conformation. The SSP is required for efficient glycoprotein expression, post-translational maturation cleavage of G1 and G2, glyc... | Tacaribe virus (strain Franze-Fernandez) (TCRV) |
P18146 | EGR1_HUMAN | MAAAKAEMQLMSPLQISDPFGSFPHSPTMDNYPKLEEMMLLSNGAPQFLGAAGAPEGSGSNSSSSSSGGGGGGGGGSNSSSSSSTFNPQADTGEQPYEHLTAESFPDISLNNEKVLVETSYPSQTTRLPPITYTGRFSLEPAPNSGNTLWPEPLFSLVSGLVSMTNPPASSSSAPSPAASSASASQSPPLSCAVPSNDSSPIYSAAPTFPTPNTDIFPEPQSQAFPGSAGTALQYPPPAYPAAKGGFQVPMIPDYLFPQQQGDLGLGTPDQKPFQGLESRTQQPSLTPLSTIKAFATQSGSQDLKALNTSYQSQLIKPSR... | null | null | BMP signaling pathway [GO:0030509]; cellular response to gamma radiation [GO:0071480]; cellular response to heparin [GO:0071504]; cellular response to interleukin-8 [GO:0098759]; cellular response to mycophenolic acid [GO:0071506]; circadian regulation of gene expression [GO:0032922]; circadian temperature homeostasis ... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; double-stranded methylated DNA binding [GO:0010385]; hemi-methylate... | PF11914;PF11928;PF00096; | 3.30.160.60; | EGR C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20363028}. Cytoplasm {ECO:0000269|PubMed:20363028}. | null | null | null | null | null | FUNCTION: Transcriptional regulator (PubMed:20121949). Recognizes and binds to the DNA sequence 5'-GCG(T/G)GGGCG-3'(EGR-site) in the promoter region of target genes (By similarity). Binds double-stranded target DNA, irrespective of the cytosine methylation status (PubMed:25258363, PubMed:25999311). Regulates the transc... | Homo sapiens (Human) |
P18153 | D7L1_AEDAE | MKLPLLLAIVTTFSVVASTGPFDPEEMLFTFTRCMEDNLEDGPNRLPMLAKWKEWINEPVDSPATQCFGKCVLVRTGLYDPVAQKFDASVIQEQFKAYPSLGEKSKVEAYANAVQQLPSTNNDCAAVFKAYDPVHKAHKDTSKNLFHGNKELTKGLYEKLGKDIRQKKQSYFEFCENKYYPAGSDKRQQLCKIRQYTVLDDALFKEHTDCVMKGIRYITKNNELDAEEVKRDFMQVNKDTKALEKVLNDCKSKEPSNAGEKSWHYYKCLVESSVKDDFKEAFDYREVRSQIYAFNLPKKQVYSKPAVQSQVMEIDGKQCP... | null | null | regulation of defense response to virus [GO:0050688]; vasodilation [GO:0042311] | extracellular region [GO:0005576] | odorant binding [GO:0005549]; toxin activity [GO:0090729] | PF01395; | 1.10.238.20; | PBP/GOBP family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2052024, ECO:0000269|PubMed:27632170}. | null | null | null | null | null | FUNCTION: Modulates blood feeding of female mosquitoes on vertebrate species by binding and sequestering different mediators involved in the host response, such as biogenic amines and eicosanoids (PubMed:32799410, PubMed:37909749). Binds serotonin, histamine, leukotriene B4, leukotriene C4, leukotriene D4, leukotriene ... | Aedes aegypti (Yellowfever mosquito) (Culex aegypti) |
P18155 | MTDC_MOUSE | MASVSLLSALAVRLLRPTHGCHPRLQPFHLAAVRNEAVVISGRKLAQQIKQEVQQEVEEWVASGNKRPHLSVILVGDNPASHSYVLNKTRAAAEVGINSETIVKPASVSEEELLNSIRKLNNDENVDGLLVQLPLPEHIDERKVCNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVVAGRSKNVGMPIAMLLHTDGAHERPGGDATVTISHRYTPKEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINRVQDPVTAKPKLVGDVDFEGVKKKAGYITPVPGGVGPMTVAML... | 1.5.1.15; 3.5.4.9 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:3487546}; | tetrahydrofolate interconversion [GO:0035999] | mitochondrion [GO:0005739] | magnesium ion binding [GO:0000287]; methenyltetrahydrofolate cyclohydrolase activity [GO:0004477]; methylenetetrahydrofolate dehydrogenase (NAD+) activity [GO:0004487]; methylenetetrahydrofolate dehydrogenase (NADP+) activity [GO:0004488]; phosphate ion binding [GO:0042301] | PF00763;PF02882; | 3.40.50.10860;3.40.50.720; | Tetrahydrofolate dehydrogenase/cyclohydrolase family | null | SUBCELLULAR LOCATION: Mitochondrion. | CATALYTIC ACTIVITY: Reaction=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NAD(+) = (6R)-5,10-methenyltetrahydrofolate + NADH; Xref=Rhea:RHEA:22892, ChEBI:CHEBI:15636, ChEBI:CHEBI:57455, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.5.1.15; Evidence={ECO:0000269|PubMed:2647744, ECO:0000269|PubMed:3487546}; CATALYTIC ACTI... | null | null | null | null | FUNCTION: Although its dehydrogenase activity is NAD-specific, it can also utilize NADP at a reduced efficiency. {ECO:0000250|UniProtKB:P13995}. | Mus musculus (Mouse) |
P18160 | SPLA_DICDI | MNSKNDLFIGFFFFFYNYYYYYNNNNNNNNNNNNNNNNNNNNNNNNNNNNNNIYIIVIIGLDPQQNHPSLKIPPPPSPTSPYVRRHARQHSRSNSSNSPGELTGGVEIIQQQNSINTQTSPPTSTSPNTVPPPPPTNTTTSSTTITRNSNNINNSNGGIINSSSGSNINNSSSSGVINTNINNSGGNISPTSNSLPSSNNNILYTSSGSNSGNNNNNNNTINISSGSSGINNSSNSNINNNNNNNSSSSSGIHASGSLTAIPTNTNSNSSIFHSSNSVNRINKSNYSADSLVLPPNRISQVPQSQTQPQLQISPSTSFSS... | 2.7.10.2 | null | anatomical structure morphogenesis [GO:0009653]; phosphorylation [GO:0016310]; signal transduction [GO:0007165]; sorocarp development [GO:0030587]; sporulation resulting in formation of a cellular spore [GO:0030435] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein kinase activity [GO:0004672]; protein serine/threonine/tyrosine kinase activity [GO:0004712]; protein tyrosine kinase activity [GO:0004713] | PF07714;PF07647;PF00622; | 2.60.120.920;1.10.150.50;1.10.510.10; | Protein kinase superfamily, TKL Tyr protein kinase family | PTM: Tyrosine kinase domain is capable of autophosphorylation, in vitro; however it is also autophosphorylated on serine and threonine residues. | null | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Essential for spore differentiation. | Dictyostelium discoideum (Social amoeba) |
P18161 | SPLB_DICDI | MGITSSKPVSGSNTTTNSPTNQKAISEKKQKPKRTNKRNLSTDSKSSTCSSPTNNYLADELVVDLNSMEIEGADSIQYSGHSHSSSMTNSMTNSMRNSANEKQLQQKQQQPQQQPQQQQPQPHQSHDDLNSSALDQDDGEFNNNFENESEVESISSSSINNNNTNNNSNNNNNNNNNNNNNNNNNNNIPSISNISNNNINNNINNNNNNNSCKQKNSKNKKNKNKNNNNKNSSSSNERPYSISYDNEGSTTKSNSTLSLYSNISNLHSITSHSIQDASIVCENCNHHMTKPIHLLSLSLEPTSAASLDIHRNGNFSITLA... | 2.7.10.2 | null | hyperosmotic response [GO:0006972]; positive regulation of gene expression [GO:0010628]; positive regulation of protein import into nucleus [GO:0042307]; positive regulation of receptor signaling pathway via STAT [GO:1904894]; protein autophosphorylation [GO:0046777]; receptor signaling pathway via STAT [GO:0097696]; r... | cytoplasm [GO:0005737]; cytosol [GO:0005829] | ATP binding [GO:0005524]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; protein kinase activity [GO:0004672]; protein tyrosine kinase activity [GO:0004713]; STAT family protein binding [GO:0097677] | PF07714; | 1.10.510.10; | Protein kinase superfamily, TKL Tyr protein kinase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | null | Dictyostelium discoideum (Social amoeba) |
P18163 | ACSL1_RAT | MEVHELFRYFRMPELIDIRQYVRTLPTNTLMGFGAFAALTTFWYATRPKALKPPCDLSMQSVEVTGTTEGVRRSAVLEDDKLLLYYYDDVRTMYDGFQRGIQVSNDGPCLGSRKPNQPYEWISYKQVAEMAECIGSALIQKGFKPCSEQFIGIFSQNRPEWVTIEQGCFTYSMVVVPLYDTLGTDAITYIVNKAELSVIFADKPEKAKLLLEGVENKLTPCLKIIVIMDSYDNDLVERGQKCGVEIIGLKALEDLGRVNRTKPKPPEPEDLAIICFTSGTTGNPKGAMVTHQNIMNDCSGFIKATESAFIASPEDVLISF... | 6.2.1.15; 6.2.1.24; 6.2.1.3 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; | adiponectin-activated signaling pathway [GO:0033211]; fatty acid metabolic process [GO:0006631]; fatty acid transport [GO:0015908]; lipid biosynthetic process [GO:0008610]; long-chain fatty acid import into cell [GO:0044539]; long-chain fatty acid metabolic process [GO:0001676]; long-chain fatty-acyl-CoA biosynthetic p... | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; peroxisomal membrane [GO:0005778] | acetate-CoA ligase activity [GO:0003987]; arachidonate-CoA ligase activity [GO:0047676]; ATP binding [GO:0005524]; long-chain fatty acid-CoA ligase activity [GO:0004467]; oleoyl-CoA ligase activity [GO:0090434]; phytanate-CoA ligase activity [GO:0050197]; pristanate-CoA ligase activity [GO:0070251]; protein serine/thre... | PF00501; | 3.40.50.12780; | ATP-dependent AMP-binding enzyme family | null | SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Peroxisome membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Microsome membrane {ECO:0000250}; Single-pass type III membrane protein {ECO:0000250}. Endoplasmic reticulum memb... | CATALYTIC ACTIVITY: Reaction=a long-chain fatty acid + ATP + CoA = a long-chain fatty acyl-CoA + AMP + diphosphate; Xref=Rhea:RHEA:15421, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57560, ChEBI:CHEBI:83139, ChEBI:CHEBI:456215; EC=6.2.1.3; Evidence={ECO:0000269|PubMed:28209804}; PhysiologicalDi... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=649 uM for ATP {ECO:0000269|PubMed:15683247}; KM=6.4 uM for CoA {ECO:0000269|PubMed:15683247}; KM=5 uM for palmitate {ECO:0000269|PubMed:15683247}; KM=2.7 uM for palmitate (when expressed in bacteria) {ECO:0000269|PubMed:28209804}; KM=6.6 uM for stearate (when expr... | null | null | null | FUNCTION: Catalyzes the conversion of long-chain fatty acids to their active form acyl-CoAs for both synthesis of cellular lipids, and degradation via beta-oxidation (PubMed:10198260, PubMed:10749848, PubMed:28209804, PubMed:8978480). Preferentially uses palmitoleate, oleate and linoleate (By similarity). Preferentiall... | Rattus norvegicus (Rat) |
P18168 | SERR_DROME | MFRKHFRRKPATSSSLESTIESADSLGMSKKTATKRQRPRHRVPKIATLPSTIRDCRSLKSACNLIALILILLVHKISAAGNFELEILEISNTNSHLLNGYCCGMPAELRATKTIGCSPCTTAFRLCLKEYQTTEQGASISTGCSFGNATTKILGGSSFVLSDPGVGAIVLPFTFRWTKSFTLILQALDMYNTSYPDAERLIEETSYSGVILPSPEWKTLDHIGRNARITYRVRVQCAVTYYNTTCTTFCRPRDDQFGHYACGSEGQKLCLNGWQGVNCEEAICKAGCDPVHGKCDRPGECECRPGWRGPLCNECMVYPG... | null | null | compound eye development [GO:0048749]; crystal cell differentiation [GO:0042688]; cuticle pattern formation [GO:0035017]; eye-antennal disc development [GO:0035214]; germ-line stem cell population maintenance [GO:0030718]; glial cell proliferation [GO:0014009]; imaginal disc-derived leg morphogenesis [GO:0007480]; imag... | apical cortex [GO:0045179]; apical plasma membrane [GO:0016324]; axolemma [GO:0030673]; cell surface [GO:0009986]; plasma membrane [GO:0005886] | calcium ion binding [GO:0005509]; glycosphingolipid binding [GO:0043208]; Notch binding [GO:0005112]; receptor ligand activity [GO:0048018] | PF21700;PF01414;PF00008;PF07645;PF12661;PF07657; | 2.10.25.140;2.60.40.3510;2.10.25.10; | null | PTM: Ubiquitinated by mind-bomb, leading to its endocytosis and subsequent degradation. {ECO:0000305}. | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Acts as a ligand for Notch (N) receptor. Essential for proper ectodermal development. Serrate represents an element in a network of interacting molecules operating at the cell surface during the differentiation of certain tissues. | Drosophila melanogaster (Fruit fly) |
P18169 | DEC11_DROME | MRLFSLLPLLALLVVQAAGQSEVTSDDPATDAGSTTNSTTDTKPRIPSQDEILGQMPSINPIRTGNPQMDAFYMMFPALGSLLKWGSLFPAYSILGAIPDNLQPTAAASKVVLVLADDATAKTRVARQNPPPNPLGQLMNWPALPQDFQLPSMDLGPQVGSFLAQLPAMPTVPGLLGAAAPVPAPAPAPAAAPPPAPAPAADPPAAPVPDAPQPAILGQAALQNAFTFFNPANFDASSLLGQSVPTFAPPNLDFVAQMQRQFFPGMTPAQPAAAGTDAQASDISEVRVRPEDPYSQEAQMKIKSALEMEQERQQQAQVKD... | null | null | chorion-containing eggshell formation [GO:0007304]; egg chorion assembly [GO:0007306]; response to starvation [GO:0042594] | egg chorion [GO:0042600]; extracellular region [GO:0005576]; nucleus [GO:0005634] | cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; structural constituent of egg chorion [GO:0005213] | PF04624;PF04626;PF04625; | null | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3378704}. | null | null | null | null | null | FUNCTION: Required for proper assembly of the eggshell. {ECO:0000269|PubMed:3378704}. | Drosophila melanogaster (Fruit fly) |
P18170 | DEC12_DROME | MRLFSLLPLLALLVVQAAGQSEVTSDDPATDAGSTTNSTTDTKPRIPSQDEILGQMPSINPIRTGNPQMDAFYMMFPALGSLLKWGSLFPAYSILGAIPDNLQPTAAASKVVLVLADDATAKTRVARQNPPPNPLGQLMNWPALPQDFQLPSMDLGPQVGSFLAQLPAMPTVPGLLGAAAPVPAPAPAPAAAPPPAPAPAADPPAAPVPDAPQPAILGQAALQNAFTFFNPANFDASSLLGQSVPTFAPPNLDFVAQMQRQFFPGMTPAQPAAAGTDAQASDISEVRVRPEDPYSQEAQMKIKSALEMEQERQQQAQVKD... | null | null | chorion-containing eggshell formation [GO:0007304]; egg chorion assembly [GO:0007306]; response to starvation [GO:0042594] | egg chorion [GO:0042600]; extracellular region [GO:0005576]; nucleus [GO:0005634] | cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; structural constituent of egg chorion [GO:0005213] | PF04624;PF04626;PF04625; | null | null | PTM: Proteolytic cleavage of isoform FC106 generates 2 further products, S80 and S60. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3378704}. | null | null | null | null | null | FUNCTION: Required for proper assembly of the eggshell. {ECO:0000269|PubMed:3378704}. | Drosophila melanogaster (Fruit fly) |
P18171 | DEC13_DROME | MRLFSLLPLLALLVVQAAGQSEVTSDDPATDAGSTTNSTTDTKPRIPSQDEILGQMPSINPIRTGNPQMDAFYMMFPALGSLLKWGSLFPAYSILGAIPDNLQPTAAASKVVLVLADDATAKTRVARQNPPPNPLGQLMNWPALPQDFQLPSMDLGPQVGSFLAQLPAMPTVPGLLGAAAPVPAPAPAPAAAPPPAPAPAADPPAAPVPDAPQPAILGQAALQNAFTFFNPANFDASSLLGQSVPTFAPPNLDFVAQMQRQFFPGMTPAQPAAAGTDAQASDISEVRVRPEDPYSQEAQMKIKSALEMEQERQQQAQVKD... | null | null | chorion-containing eggshell formation [GO:0007304]; egg chorion assembly [GO:0007306]; response to starvation [GO:0042594] | egg chorion [GO:0042600]; extracellular region [GO:0005576]; nucleus [GO:0005634] | cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; structural constituent of egg chorion [GO:0005213] | PF04624;PF04626;PF04625; | null | null | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:3378704}. | null | null | null | null | null | FUNCTION: Required for proper assembly of the eggshell. {ECO:0000269|PubMed:3378704}. | Drosophila melanogaster (Fruit fly) |
P18177 | TCDB_CLODI | MSLVNRKQLEKMANVRFRTQEDEYVAILDALEEYHNMSENTVVEKYLKLKDINSLTDIYIDTYKKSGRNKALKKFKEYLVTEVLELKNNNLTPVEKNLHFVWIGGQINDTAINYINQWKDVNSDYNVNVFYDSNAFLINTLKKTVVESAINDTLESFRENLNDPRFDYNKFFRKRMEIIYDKQKNFINYYKAQREENPELIIDDIVKTYLSNEYSKEIDELNTYIEESLNKITQNSGNDVRNFEEFKNGESFNLYEQELVERWNLAAASDILRISALKEIGGMYLDVDMLPGIQPDLFESIEKPSSVTVDFWEMTKLEAI... | 2.4.1.-; 3.4.22.- | COFACTOR: [Toxin B]: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:27571750, ECO:0000269|PubMed:31308519}; Note=Binds 1 Zn(2+) ion per subunit (PubMed:27571750, PubMed:31308519). Zn(2+) is required for autocatalytic cleavage (PubMed:27571750). {ECO:0000269|PubMed:27571750, ECO:0000269|PubMed:3130851... | 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]; glucosyltransferase activity [GO:0046527]; lipid binding [GO:0008289]; metal ion binding [GO:0046872]; toxin activity [GO:0090729] | PF01473;PF19127;PF11647;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 B]: Undergoes autocatalytic cleavage to release the N-terminal part (Glucosyltransferase TcdB), which constitutes the active part of the toxin, in the host cytosol (PubMed:12941936, PubMed:17334356, PubMed:27571750). 1D-myo-inositol hexakisphosphate-binding (InsP6) activates the peptidase C80 domain and pro... | SUBCELLULAR LOCATION: [Toxin B]: Secreted {ECO:0000269|PubMed:22685398}. Host endosome membrane {ECO:0000269|PubMed:11152463, ECO:0000305|PubMed:12941936}. 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 recepto... | CATALYTIC ACTIVITY: [Glucosyltransferase TcdB]: 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=6 uM for UDP-alpha-D-glucose {ECO:0000269|PubMed:16157585}; KM=4.3 uM for UDP-alpha-D-glucose {ECO:0000269|PubMed:17901056}; KM=960 uM for UDP-N-acetyl-alpha-D-glucosamine {ECO:0000269|PubMed:16157585}; Note=kcat is 2120 h(-1) with UDP-alpha-D-glucose as substrate ... | null | null | null | FUNCTION: [Toxin B]: 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, PubMed:24919149). TcdB constitutes the main toxin that mediates the pathology of C.difficile... | Clostridioides difficile (Peptoclostridium difficile) |
P18181 | CD48_MOUSE | MCFIKQGWCLVLELLLLPLGTGFQGHSIPDINATTGSNVTLKIHKDPLGPYKRITWLHTKNQKILEYNYNSTKTIFESEFKGRVYLEENNGALHISNVRKEDKGTYYMRVLRETENELKITLEVFDPVPKPSIEINKTEASTDSCHLRLSCEVKDQHVDYTWYESSGPFPKKSPGYVLDLIVTPQNKSTFYTCQVSNPVSSKNDTVYFTLPCDLARSSGVCWTATWLVVTTLIIHRILLT | null | null | mast cell activation [GO:0045576]; natural killer cell activation involved in immune response [GO:0002323]; signal transduction [GO:0007165]; T cell activation [GO:0042110] | external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; protein-containing complex [GO:0032991] | MHC class I protein binding [GO:0042288] | PF13895;PF07686; | 2.60.40.10; | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1383383}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:1693656}. Secreted {ECO:0000250|UniProtKB:P09326}. | null | null | null | null | null | FUNCTION: Glycosylphosphatidylinositol (GPI)-anchored cell surface glycoprotein that interacts via its N-terminal immunoglobulin domain with cell surface receptors including 2B4/CD244 or CD2 to regulate immune cell function and activation (PubMed:21278219, PubMed:9881969). Participates in T-cell signaling transduction ... | Mus musculus (Mouse) |
P18187 | PHNS_SOLFR | MNFSVGLGRDDAEKRLVQNGVSRRDFMKFCATVAAAMGMGPAFAPKVAEALTAKHRPSVVWLHNAECTGCTEAAIRTIKPYIDALILDTISLDYQETIMAAAGEAAEAALHQALEGKDGYYLVVEGGLPTIDGGQWGMVAGHPMIETTKKAAAKAKGIICIGTCSAYGGVQKAKPNPSQAKGVSEALGVKTINIPGCPPNPINFVGAVVHVLTKGIPDLDENGRPKLFYGELVHDNCPRLPHFEASEFAPSFDSEEAKKGFCLYELGCKGPVTYNNCPKVLFNQVNWPVQAGHPCLGCSEPDFWDTMTPFYEQG | 1.12.2.1 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Note=Binds 2 [4Fe-4S] clusters per subunit.; COFACTOR: Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; Note=Binds 1 [3Fe-4S] cluster per subunit.; | anaerobic respiration [GO:0009061] | [Ni-Fe] hydrogenase complex [GO:0044569]; ferredoxin hydrogenase complex [GO:0009375]; membrane [GO:0016020]; periplasmic space [GO:0042597] | 3 iron, 4 sulfur cluster binding [GO:0051538]; 4 iron, 4 sulfur cluster binding [GO:0051539]; cytochrome-c3 hydrogenase activity [GO:0047806]; electron transfer activity [GO:0009055]; ferredoxin hydrogenase activity [GO:0008901]; metal ion binding [GO:0046872] | PF14720;PF01058; | 4.10.480.10;3.40.50.700; | [NiFe]/[NiFeSe] hydrogenase small subunit family | PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has been experimentally proven. | SUBCELLULAR LOCATION: Periplasm. | CATALYTIC ACTIVITY: Reaction=2 Fe(III)-[cytochrome c3] + H2 = 2 Fe(II)-[cytochrome c3] + 2 H(+); Xref=Rhea:RHEA:20625, Rhea:RHEA-COMP:11576, Rhea:RHEA-COMP:11577, ChEBI:CHEBI:15378, ChEBI:CHEBI:18276, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.12.2.1; | null | null | null | null | FUNCTION: Involved in hydrogen uptake for the anaerobic reduction of sulfate to hydrogen sulfide in an electron transport chain. Cytochrome c3 is the physiological electron acceptor. | Solidesulfovibrio fructosivorans (Desulfovibrio fructosivorans) |
P18190 | MBHS_AZOCH | MSQLETXYDVMRRQGITRRSFLKYCSLTGRPCLGPTFAPQIAHAMETRPPTPVVWLHGLECTCCSESFIRSGDPLVKDVVLSMISLDYDDTLMPPRHQGTVEETMRKYKGEYILAVEGNPPLNEDGMFCIVGGKPFLDQLKHAAKDAKAVIAWGSCASWGCVQAAKPNPTQAVPIHKVITDKPMIKVPGCPPIAEVMTGVITYMLTFGKLPELDRQGRPKMFYGQRIHDKSYRRPHFDAGQFVEHWDDEGARKGYCLYKVGCKGPTSYNACSTVRWNEGTSFPIQAGHGCIGCSEDGFWDKGSFYERLTTIPQFGIEKNA... | 1.12.99.6 | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250|UniProtKB:P21853}; Note=Binds 2 [4Fe-4S] clusters. {ECO:0000250|UniProtKB:P21853}; COFACTOR: Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; Evidence={ECO:0000250|UniProtKB:P21853}; Note=Binds 1 [3Fe-4S] cluster. {ECO:0000250|UniProtKB:P21853... | anaerobic respiration [GO:0009061] | [Ni-Fe] hydrogenase complex [GO:0044569]; ferredoxin hydrogenase complex [GO:0009375]; plasma membrane [GO:0005886] | 3 iron, 4 sulfur cluster binding [GO:0051538]; 4 iron, 4 sulfur cluster binding [GO:0051539]; electron transfer activity [GO:0009055]; ferredoxin hydrogenase activity [GO:0008901]; hydrogenase (acceptor) activity [GO:0033748]; metal ion binding [GO:0046872] | PF14720;PF01058; | 4.10.480.10;3.40.50.700; | [NiFe]/[NiFeSe] hydrogenase small subunit family | PTM: Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven. | SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=A + H2 = AH2; Xref=Rhea:RHEA:12116, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499, ChEBI:CHEBI:18276; EC=1.12.99.6; | null | null | null | null | FUNCTION: This enzyme recycles the H(2) produced by nitrogenase to increase the production of ATP and to protect nitrogenase against inhibition or damage by O(2) under carbon- or phosphate-limited conditions. | Azotobacter chroococcum mcd 1 |
P18196 | MINC_ECOLI | MSNTPIELKGSSFTLSVVHLHEAEPKVIHQALEDKIAQAPAFLKHAPVVLNVSALEDPVNWSAMHKAVSATGLRVIGVSGCKDAQLKAEIEKMGLPILTEGKEKAPRPAPTPQAPAQNTTPVTKTRLIDTPVRSGQRIYAPQCDLIVTSHVSAGAELIADGNIHVYGMMRGRALAGASGDRETQIFCTNLMAELVSIAGEYWLSDQIPAEFYGKAARLQLVENALTVQPLN | null | null | cell division [GO:0051301]; cell morphogenesis [GO:0000902]; division septum assembly [GO:0000917]; regulation of cell division [GO:0051302]; regulation of division septum assembly [GO:0032955] | cell pole [GO:0060187]; cytosol [GO:0005829] | identical protein binding [GO:0042802] | PF03775;PF05209; | 2.160.20.70;3.30.70.260; | MinC family | null | null | null | null | null | null | null | FUNCTION: Cell division inhibitor that blocks the formation of polar Z ring septums. Rapidly oscillates between the poles of the cell to destabilize FtsZ filaments that have formed before they mature into polar Z rings. Prevents FtsZ polymerization. {ECO:0000269|PubMed:22380631}. | Escherichia coli (strain K12) |
P18200 | PGPA_ECOLI | MTILPRHKDVAKSRLKMSNPWHLLAVGFGSGLSPIVPGTMGSLAAIPFWYLMTFLPWQLYSLVVMLGICIGVYLCHQTAKDMGVHDHGSIVWDEFIGMWITLMALPTNDWQWVAAGFVIFRILDMWKPWPIRWFDRNVHGGMGIMIDDIVAGVISAGILYFIGHHWPLGILS | 3.1.3.27 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:21148555}; | glycerophospholipid biosynthetic process [GO:0046474]; phosphatidylglycerol biosynthetic process [GO:0006655]; phospholipid catabolic process [GO:0009395]; phospholipid dephosphorylation [GO:0046839]; response to magnesium ion [GO:0032026] | plasma membrane [GO:0005886] | lipid phosphatase activity [GO:0042577]; metal ion binding [GO:0046872]; phosphatidylglycerophosphatase activity [GO:0008962] | PF04608; | null | null | null | SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:21148555}; Multi-pass membrane protein {ECO:0000269|PubMed:21148555}. | CATALYTIC ACTIVITY: Reaction=1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + H2O = 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) + phosphate; Xref=Rhea:RHEA:33751, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:60110, ChEBI:CHEBI:64716; EC=3.1.3.27; Evidence={ECO:0000269|PubMed:20485265, ECO:000026... | null | PATHWAY: Phospholipid metabolism; phosphatidylglycerol biosynthesis; phosphatidylglycerol from CDP-diacylglycerol: step 2/2. | null | null | FUNCTION: Lipid phosphatase which dephosphorylates phosphatidylglycerophosphate (PGP) to phosphatidylglycerol (PG). {ECO:0000269|PubMed:20485265, ECO:0000269|PubMed:21148555, ECO:0000269|PubMed:2846510, ECO:0000269|PubMed:6296050}. | Escherichia coli (strain K12) |
P18203 | FKB1A_BOVIN | MGVQVETISPGDGRTFPKRGQTCVVHYTGMLEDGKKFDSSRDRNKPFKFVLGKQEVIRGWEEGVAQMSVGQRAKLTISPDYAYGATGHPGIIPPNATLIFDVELLKLE | 5.2.1.8 | null | amyloid fibril formation [GO:1990000]; cytokine-mediated signaling pathway [GO:0019221]; heart morphogenesis [GO:0003007]; heart trabecula formation [GO:0060347]; muscle contraction [GO:0006936]; negative regulation of phosphoprotein phosphatase activity [GO:0032515]; negative regulation of protein phosphorylation [GO:... | cytoplasm [GO:0005737]; cytoplasmic side of membrane [GO:0098562]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; ryanodine receptor complex [GO:1990425]; sarcoplasmic reticulum [GO:0016529]; sarcoplasmic reticulum membrane [GO:0033017]; Z disc [GO:0030018] | activin binding [GO:0048185]; calcium channel inhibitor activity [GO:0019855]; FK506 binding [GO:0005528]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755]; protein homodimerization activity [GO:0042803]; SMAD binding [GO:0046332]; transmembrane transporter binding [GO:0044325] | PF00254; | 3.10.50.40; | FKBP-type PPIase family, FKBP1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P62942}. Sarcoplasmic reticulum membrane {ECO:0000250|UniProtKB:P62943}; Peripheral membrane protein {ECO:0000250|UniProtKB:P62943}; Cytoplasmic side {ECO:0000250|UniProtKB:P62943}. | CATALYTIC ACTIVITY: Reaction=[protein]-peptidylproline (omega=180) = [protein]-peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833, ChEBI:CHEBI:83834; EC=5.2.1.8; Evidence={ECO:0000250|UniProtKB:P62942}; | null | null | null | null | FUNCTION: Keeps in an inactive conformation TGFBR1, the TGF-beta type I serine/threonine kinase receptor, preventing TGF-beta receptor activation in absence of ligand. May modulate the RYR1 calcium channel activity. PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic p... | Bos taurus (Bovine) |
P18206 | VINC_HUMAN | MPVFHTRTIESILEPVAQQISHLVIMHEEGEVDGKAIPDLTAPVAAVQAAVSNLVRVGKETVQTTEDQILKRDMPPAFIKVENACTKLVQAAQMLQSDPYSVPARDYLIDGSRGILSGTSDLLLTFDEAEVRKIIRVCKGILEYLTVAEVVETMEDLVTYTKNLGPGMTKMAKMIDERQQELTHQEHRVMLVNSMNTVKELLPVLISAMKIFVTTKNSKNQGIEEALKNRNFTVEKMSAEINEIIRVLQLTSWDEDAWASKDTEAMKRALASIDSKLNQAKGWLRDPSASPGDAGEQAIRQILDEAGKVGELCAGKERRE... | null | null | adherens junction assembly [GO:0034333]; apical junction assembly [GO:0043297]; axon extension [GO:0048675]; cell adhesion [GO:0007155]; cell-matrix adhesion [GO:0007160]; epithelial cell-cell adhesion [GO:0090136]; lamellipodium assembly [GO:0030032]; maintenance of blood-brain barrier [GO:0035633]; morphogenesis of a... | adherens junction [GO:0005912]; brush border [GO:0005903]; cell projection [GO:0042995]; cell-cell contact zone [GO:0044291]; cell-cell junction [GO:0005911]; cell-substrate junction [GO:0030055]; costamere [GO:0043034]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; extracellular exosome [GO:... | actin binding [GO:0003779]; alpha-catenin binding [GO:0045294]; beta-catenin binding [GO:0008013]; cadherin binding [GO:0045296]; dystroglycan binding [GO:0002162]; molecular adaptor activity [GO:0060090]; structural molecule activity [GO:0005198]; ubiquitin protein ligase binding [GO:0031625] | PF01044; | 1.20.120.230;1.20.120.810; | Vinculin/alpha-catenin family | PTM: Phosphorylated; on serines, threonines and tyrosines. Phosphorylation on Tyr-1133 in activated platelets affects head-tail interactions and cell spreading but has no effect on actin binding nor on localization to focal adhesion plaques (By similarity). {ECO:0000250|UniProtKB:P12003}.; PTM: Acetylated; mainly by my... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P12003}; Peripheral membrane protein {ECO:0000250|UniProtKB:P12003}; Cytoplasmic side {ECO:0000250|UniProtKB:P12003}. Cell junction, adherens junction {ECO:0000250|UniProtKB:P12003}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:P12003}. Cytoplasm, cytos... | null | null | null | null | null | FUNCTION: Actin filament (F-actin)-binding protein involved in cell-matrix adhesion and cell-cell adhesion. Regulates cell-surface E-cadherin expression and potentiates mechanosensing by the E-cadherin complex. May also play important roles in cell morphology and locomotion. {ECO:0000269|PubMed:20484056}. | Homo sapiens (Human) |
P18211 | HB2D_RAT | MVWLARDSCVAAVILLLTVLSPPVALVRDPTPRFLEQVKGECHFYNGTQRVRFLARYIYNREEYTRFDSDVGEFRAVTELGRPSAEYYNKQKEYMEQLRATVDTACKHDYEISESFLVPRTVEPKVTVYPSKTQPLEHHNLLVCSVSDFYPGSVEVRWFRNGEEEKDGLVSTGLIRNGDWTFQLLVMLETVPQGGEVYTCQVEHPSLPSPVRVEWKAQSTSAQNKKMSGVGGIVLGLLFLGAGLFVYFRNQKGQSGLQPTGLLN | null | null | antigen processing and presentation of endogenous peptide antigen via MHC class II [GO:0002491]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; humoral immune response [GO:0006959]; immune response [GO:0006955]; inflammatory response to antigenic stimulus [GO:0002437]; m... | cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; immunological synapse [GO:0001772]; late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; MHC class II protein complex [GO:0042613] | CD4 receptor binding [GO:0042609]; MHC class II protein complex binding [GO:0023026]; MHC class II receptor activity [GO:0032395]; peptide antigen binding [GO:0042605]; polysaccharide binding [GO:0030247]; T cell receptor binding [GO:0042608] | PF07654;PF00969; | 2.60.40.10; | MHC class II family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Involved in the presentation of foreign antigens to the immune system. | Rattus norvegicus (Rat) |
P18238 | ADT3_YEAST | MSSDAKQQETNFAINFLMGGVSAAIAKTAASPIERVKILIQNQDEMIKQGTLDKKYSGIVDCFKRTAKQEGLISFWRGNTANVIRYFPTQALNFAFKDKIKLMFGFKKEEGYGKWFAGNLASGGAAGALSLLFVYSLDFARTRLAADAKSSKKGGARQFNGLTDVYKKTLKSDGIAGLYRGFMPSVVGIVVYRGLYFGMFDSLKPLVLTGSLDGSFLASFLLGWVVTTGASTCSYPLDTVRRRMMMTSGQAVKYNGAIDCLKKIVASEGVGSLFKGCGANILRSVAGAGVISMYDQLQMILFGKKFK | null | null | anaerobic respiration [GO:0009061]; heme transport [GO:0015886]; mitochondrial ADP transmembrane transport [GO:0140021]; mitochondrial ATP transmembrane transport [GO:1990544]; negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway [GO:1901029]; transmembrane transp... | mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739] | ATP:ADP antiporter activity [GO:0005471]; identical protein binding [GO:0042802] | PF00153; | 1.50.40.10; | Mitochondrial carrier (TC 2.A.29) family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P18239}; Multi-pass membrane protein {ECO:0000269|PubMed:24474793}. | CATALYTIC ACTIVITY: Reaction=ADP(in) + ATP(out) = ADP(out) + ATP(in); Xref=Rhea:RHEA:34999, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; Evidence={ECO:0000305|PubMed:2165073}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35000; Evidence={ECO:0000305|PubMed:2165073}; | null | null | null | null | FUNCTION: ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell (PubMed:2165073). Cycles between the cytoplasmic-open state (c-state) and the matrix-open state (m-state): operates by the alternating access mechanism with a single substrate... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P18239 | ADT2_YEAST | MSSNAQVKTPLPPAPAPKKESNFLIDFLMGGVSAAVAKTAASPIERVKLLIQNQDEMLKQGTLDRKYAGILDCFKRTATQEGVISFWRGNTANVIRYFPTQALNFAFKDKIKAMFGFKKEEGYAKWFAGNLASGGAAGALSLLFVYSLDYARTRLAADSKSSKKGGARQFNGLIDVYKKTLKSDGVAGLYRGFLPSVVGIVVYRGLYFGMYDSLKPLLLTGSLEGSFLASFLLGWVVTTGASTCSYPLDTVRRRMMMTSGQAVKYDGAFDCLRKIVAAEGVGSLFKGCGANILRGVAGAGVISMYDQLQMILFGKKFK | null | null | ADP transport [GO:0015866]; aerobic respiration [GO:0009060]; anaerobic respiration [GO:0009061]; apoptotic process [GO:0006915]; ATP transport [GO:0015867]; heme transport [GO:0015886]; mitochondrial ADP transmembrane transport [GO:0140021]; mitochondrial ATP transmembrane transport [GO:1990544]; mitochondrial transpo... | membrane [GO:0016020]; mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739] | ATP:ADP antiporter activity [GO:0005471] | PF00153; | 1.50.40.10; | Mitochondrial carrier (TC 2.A.29) family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000269|PubMed:795470}; Multi-pass membrane protein {ECO:0000269|PubMed:24474793}. | CATALYTIC ACTIVITY: Reaction=ADP(in) + ATP(out) = ADP(out) + ATP(in); Xref=Rhea:RHEA:34999, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:24474793}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:35000; Evidence={ECO:0000269|PubMed:24474793}; | null | null | null | null | FUNCTION: ADP:ATP antiporter that mediates import of ADP into the mitochondrial matrix for ATP synthesis, and export of ATP out to fuel the cell (PubMed:24474793). Cycles between the cytoplasmic-open state (c-state) and the matrix-open state (m-state): operates by the alternating access mechanism with a single substrat... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P18242 | CATD_MOUSE | MKTPGVLLLILGLLASSSFAIIRIPLRKFTSIRRTMTEVGGSVEDLILKGPITKYSMQSSPKTTEPVSELLKNYLDAQYYGDIGIGTPPQCFTVVFDTGSSNLWVPSIHCKILDIACWVHHKYNSDKSSTYVKNGTSFDIHYGSGSLSGYLSQDTVSVPCKSDQSKARGIKVEKQIFGEATKQPGIVFVAAKFDGILGMGYPHISVNNVLPVFDNLMQQKLVDKNIFSFYLNRDPEGQPGGELMLGGTDSKYYHGELSYLNVTRKAYWQVHMDQLEVGNELTLCKGGCEAIVDTGTSLLVGPVEEVKELQKAIGAVPLIQ... | 3.4.23.5 | null | autophagosome assembly [GO:0000045]; insulin catabolic process [GO:1901143]; insulin receptor recycling [GO:0038020]; lipoprotein catabolic process [GO:0042159]; positive regulation of apoptotic process [GO:0043065]; protein catabolic process [GO:0030163]; proteolysis [GO:0006508]; regulation of establishment of protei... | collagen-containing extracellular matrix [GO:0062023]; endosome lumen [GO:0031904]; endosome membrane [GO:0010008]; extracellular space [GO:0005615]; GABA-ergic synapse [GO:0098982]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; melanosome [GO:0042470]; membrane raft [GO:0045121]; mitochondrion [GO:0005739]; ... | aspartic-type endopeptidase activity [GO:0004190]; aspartic-type peptidase activity [GO:0070001]; endopeptidase activity [GO:0004175]; hydrolase activity [GO:0016787]; peptidase activity [GO:0008233]; peptide binding [GO:0042277] | PF07966;PF00026; | 2.40.70.10; | Peptidase A1 family | PTM: N- and O-glycosylated. {ECO:0000250|UniProtKB:P07339, ECO:0000269|PubMed:16170054}.; PTM: Undergoes proteolytic cleavage and activation by ADAM30. {ECO:0000250|UniProtKB:P07339}. | SUBCELLULAR LOCATION: Lysosome. Melanosome {ECO:0000250}. Secreted, extracellular space {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=Specificity similar to, but narrower than, that of pepsin A. Does not cleave the 4-Gln-|-His-5 bond in B chain of insulin.; EC=3.4.23.5; | null | null | null | null | FUNCTION: Acid protease active in intracellular protein breakdown. Plays a role in APP processing following cleavage and activation by ADAM30 which leads to APP degradation. {ECO:0000250|UniProtKB:P07339}. | Mus musculus (Mouse) |
P18246 | CXA1_BOVIN | MGDWSALGKLLDKVQAYSTAGGKVWLSVLFIFRILLLGTAVESAWGDEQSAFRCNTQQPGCENVCYDKSFPISHVRFWVLQIIFVSVPTLLYLAHVFYVMRKEEKLNKKEEELKVVAQTDGANVDMHLKQIEIKKFKYGIEEHGKVKMRGGLLRTYIISILFKSVFEVAFLLIQWYIYGFSLSAVYTCKRDPCPHQVDCFLSRPTEKTIFIIFMLVVSLVSLALNIIELFYVFFKGVKDRVKGKSDPYHTTTGPLSPSKDCGSPKYAYFNGCSSPTAPLSPMSPPGYKLVTGDRNNSSCRNYNKQASEQNWANYSAEQNR... | null | null | adult heart development [GO:0007512]; ATP transport [GO:0015867]; blood vessel morphogenesis [GO:0048514]; bone development [GO:0060348]; bone remodeling [GO:0046849]; cell communication [GO:0007154]; cell communication by electrical coupling [GO:0010644]; cell-cell signaling [GO:0007267]; embryonic heart tube developm... | apical plasma membrane [GO:0016324]; cell junction [GO:0030054]; connexin complex [GO:0005922]; cytoplasm [GO:0005737]; early endosome [GO:0005769]; endoplasmic reticulum [GO:0005783]; fascia adherens [GO:0005916]; gap junction [GO:0005921]; intercalated disc [GO:0014704]; late endosome [GO:0005770]; lysosome [GO:00057... | gap junction channel activity [GO:0005243]; gap junction hemi-channel activity [GO:0055077]; PDZ domain binding [GO:0030165]; SH3 domain binding [GO:0017124]; tubulin binding [GO:0015631] | PF00029;PF03508; | 1.20.5.1130;1.20.1440.80; | Connexin family, Alpha-type (group II) subfamily | PTM: Phosphorylation at Ser-326, Ser-329 and Ser-331 by CK1 modulates gap junction assembly. Phosphorylated at Ser-369 by PRKCG; phosphorylation induces disassembly of gap junction plaques and inhibition of gap junction activity. Phosphorylation at Ser-369 by PRKCD triggers its internalization into small vesicles leadi... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P17302}; Multi-pass membrane protein {ECO:0000255}. Cell junction, gap junction {ECO:0000250|UniProtKB:P17302}. Endoplasmic reticulum {ECO:0000250|UniProtKB:P23242}. Note=Localizes at the intercalated disk (ICD) in cardiomyocytes and proper localization at ICD ... | null | null | null | null | null | FUNCTION: Gap junction protein that acts as a regulator of bladder capacity. A gap junction consists of a cluster of closely packed pairs of transmembrane channels, the connexons, through which materials of low MW diffuse from one cell to a neighboring cell. May play a critical role in the physiology of hearing by part... | Bos taurus (Bovine) |
P18247 | POLG_PVYN | MATYMSTICFGSFECKLPYSPASCEHIVKEREVPASVDPFADLETQLSARLLKQKYATVRVLKNGTFTYRYKTDAQIMRIQKKLERKDREEYHFQMAAPSIVSKITIAGGDPPSKSEPQAPRGIIHTTPRMRKVKTRPIIKLTEGQMNHLIKQIKQIMSEKRGSVHLISKKTTHVQYKKILGAYSAAVRTAHMMGLRRRVDFRCDMWTVGLLQRLARTDKWSNQVRTINIRRGDSGVILNTKSLKGHFGRSSGGLFIVRGSHEGKLYDARSRVTQSILNSMIQFSNADNFWKGLDGNWARMRYPSDHTCVAGLPVEDCGR... | 2.7.7.48; 3.4.-.-; 3.4.22.44; 3.4.22.45; 3.6.4.- | null | DNA-templated transcription [GO:0006351]; proteolysis [GO:0006508]; viral RNA genome replication [GO:0039694]; virus-mediated perturbation of host defense response [GO:0019049] | helical viral capsid [GO:0019029]; host cell cytoplasmic vesicle [GO:0044161]; host cell nucleus [GO:0042025] | ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; helicase activity [GO:0004386]; hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides [GO:0016818]; RNA binding [GO:0003723]; RNA-dependent RNA polymerase activity [GO:0003968]; serine-type peptidase activity [GO:0... | PF00270;PF00271;PF00863;PF00851;PF01577;PF00767;PF08440;PF13608;PF00680; | 3.30.70.270;3.90.70.150;3.40.50.300;2.40.10.10; | Potyviridae genome polyprotein family | PTM: [Viral genome-linked protein]: VPg is uridylylated by the polymerase and is covalently attached to the 5'-end of the genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase (By similarity). {ECO:0000250|UniProtKB:P09814}.; PTM: [Genome polyprotein]: Potyviral RNA is expressed as ... | SUBCELLULAR LOCATION: [6 kDa protein 1]: Host cytoplasmic vesicle. Note=Probably colocalizes with 6K2-induced vesicles associated with host chloroplasts. {ECO:0000250|UniProtKB:P13529}.; SUBCELLULAR LOCATION: [6 kDa protein 2]: Host cytoplasmic vesicle {ECO:0000250|UniProtKB:P09814}. Note=6K-induced vesicles associate ... | 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=Hydrolyz... | null | null | null | null | FUNCTION: [Helper component proteinase]: Required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus. Interacts with virions and aphid stylets. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a m... | Potato virus Y (strain N) (PVY) |
P18254 | IGF1_CHICK | MEKINSLSTQLVKCCFCDFLKVKMHTVSYIHFFYLGLCLLTLTSSAAAGPETLCGAELVDALQFVCGDRGFYFSKPTGYGSSSRRLHHKGIVDECCFQSCDLRRLEMYCAPIKPPKSARSVRAQRHTDMPKAQKEVHLKNTSRGNTGNRNYRM | null | null | cell population proliferation [GO:0008283]; cochlea morphogenesis [GO:0090103]; cranial ganglion formation [GO:0061560]; gene expression [GO:0010467]; insulin-like growth factor receptor signaling pathway [GO:0048009]; negative regulation of apoptotic process [GO:0043066]; negative regulation of insulin secretion [GO:0... | extracellular space [GO:0005615] | growth factor activity [GO:0008083]; hormone activity [GO:0005179]; insulin-like growth factor receptor binding [GO:0005159] | PF00049; | 1.10.100.10; | Insulin family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: The insulin-like growth factors, isolated from plasma, are structurally and functionally related to insulin but have a much higher growth-promoting activity. Acts as a ligand for IGF1R. Binds to the alpha subunit of IGF1R, leading to the activation of the intrinsic tyrosine kinase activity which autophosphory... | Gallus gallus (Chicken) |
P18258 | TBA1_PARLI | MRECISIHVGQAGVQMGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVVDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTVGKELIDIVLDRIRKLADQCTGLQGFLIFHSFGGGTGSGFSSLLMERLSVDYGKKSKLEFAVYPAPQISTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLATYAPVISAEKAYHEQLTVSEITNACFEPANQMVKCDPRHGKYMACCLLYR... | 3.6.5.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363}; | microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278]; nuclear division [GO:0000280]; nuclear migration by microtubule mediated pushing forces [GO:0098863] | cytoplasm [GO:0005737]; microtubule [GO:0005874]; nucleus [GO:0005634]; spindle [GO:0005819] | GTP binding [GO:0005525]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; structural constituent of cytoskeleton [GO:0005200] | PF00091;PF03953; | 1.10.287.600;3.30.1330.20;3.40.50.1440; | Tubulin family | PTM: Undergoes a tyrosination/detyrosination cycle, the cyclic removal and re-addition of a C-terminal tyrosine residue by the enzymes tubulin tyrosine carboxypeptidase (TTCP) and tubulin tyrosine ligase (TTL), respectively. {ECO:0000250}.; PTM: Acetylation of alpha chains at Lys-40 stabilizes microtubules and affects ... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P68363}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P6836... | null | null | null | null | FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers a... | Paracentrotus lividus (Common sea urchin) |
P18265 | GSK3A_RAT | MSGGGPSGGGPGGSGRARTSSFAEPGGGGGGGGGGPGGSASGPGGTGGGKASVGAMGGGVGASSSGGGPSGSGGGGSGGPGAGTSFPPPGVKLGRDSGKVTTVVATLGQGPERSQEVAYTDIKVIGNGSFGVVYQARLAETRELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDELYLNLVLEYVPETVYRVARHFTKAKLIIPIIYVKVYMYQLFRSLAYIHSQGVCHRDIKPQNLLVDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDVWSAGCVLAELLLGQPIF... | 2.7.11.1; 2.7.11.26 | null | autosome genomic imprinting [GO:0141068]; cardiac left ventricle morphogenesis [GO:0003214]; cell differentiation [GO:0030154]; cell migration [GO:0016477]; cellular response to glucocorticoid stimulus [GO:0071385]; cellular response to insulin stimulus [GO:0032869]; cellular response to interleukin-3 [GO:0036016]; cel... | axon [GO:0030424]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; microtubule [GO:0005874]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | ATP binding [GO:0005524]; protein kinase A catalytic subunit binding [GO:0034236]; protein kinase activity [GO:0004672]; protein kinase binding [GO:0019901]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine kinase binding [GO:0120283]; signalin... | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, GSK-3 subfamily | PTM: Phosphorylated by AKT1 at Ser-21: upon insulin-mediated signaling, the activated PKB/AKT1 protein kinase phosphorylates and deactivates GSK3A, resulting in the dephosphorylation and activation of GYS1. Activated by phosphorylation at Tyr-279 (By similarity). {ECO:0000250}. | null | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[tau protein] = ADP + H(+) + O-phospho-L-seryl-[tau protein]; Xref=Rhea:RHEA:12801, Rhea:RHEA-COMP:13701, Rhea:RHEA-COMP:13702, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.26; CATALYTIC ACTIVITY: Reaction=ATP + L-th... | null | null | null | null | FUNCTION: Constitutively active protein kinase that acts as a negative regulator in the hormonal control of glucose homeostasis, Wnt signaling and regulation of transcription factors and microtubules, by phosphorylating and inactivating glycogen synthase (GYS1 or GYS2), CTNNB1/beta-catenin, APC and AXIN1. Requires prim... | Rattus norvegicus (Rat) |
P18266 | GSK3B_RAT | MSGRPRTTSFAESCKPVQQPSAFGSMKVSRDKDGSKVTTVVATPGQGPDRPQEVSYTDTKVIGNGSFGVVYQAKLCDSGELVAIKKVLQDKRFKNRELQIMRKLDHCNIVRLRYFFYSSGEKKDEVYLNLVLDYVPETVYRVARHYSRAKQTLPVIYVKLYMYQLFRSLAYIHSFGICHRDIKPQNLLLDPDTAVLKLCDFGSAKQLVRGEPNVSYICSRYYRAPELIFGATDYTSSIDMWSAGCVLAELLLGQPIFPGDSGVDQLVEIIKVLGTPTREQIREMNPNYTEFKFPQIKAHPWTKVFRPRTPPEAIALCSRL... | 2.7.11.1; 2.7.11.26 | null | animal organ morphogenesis [GO:0009887]; autosome genomic imprinting [GO:0141068]; axon extension [GO:0048675]; axonogenesis [GO:0007409]; beta-catenin destruction complex disassembly [GO:1904886]; bone remodeling [GO:0046849]; canonical Wnt signaling pathway [GO:0060070]; cell differentiation [GO:0030154]; cell growth... | axon [GO:0030424]; beta-catenin destruction complex [GO:0030877]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; dendritic shaft [GO:0043198]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; growth cone [GO:0030426]; meiotic spindle [GO:0072687]; membrane... | ATP binding [GO:0005524]; beta-catenin binding [GO:0008013]; dynactin binding [GO:0034452]; dynein complex binding [GO:0070840]; integrin binding [GO:0005178]; ionotropic glutamate receptor binding [GO:0035255]; kinase activity [GO:0016301]; NF-kappaB binding [GO:0051059]; p53 binding [GO:0002039]; protease binding [GO... | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, GSK-3 subfamily | PTM: Phosphorylated by AKT1 and ILK1. Upon insulin-mediated signaling, the activated PKB/AKT1 and RPS6KA3 protein kinases phosphorylate and deactivate GSK3B, resulting in the dephosphorylation and activation of GYS1. Activated by phosphorylation at Tyr-216 (By similarity). Inactivated by phosphorylation at Ser-9 (By si... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P49841}. Nucleus {ECO:0000250|UniProtKB:P49841}. Membrane {ECO:0000269|PubMed:16815997}. Cell membrane {ECO:0000250|UniProtKB:P49841}. Note=The phosphorylated form shows localization to cytoplasm and cell membrane. The MEMO1-RHOA-DIAPH1 signaling pathway controls l... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[tau protein] = ADP + H(+) + O-phospho-L-seryl-[tau protein]; Xref=Rhea:RHEA:12801, Rhea:RHEA-COMP:13701, Rhea:RHEA-COMP:13702, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.26; Evidence={ECO:0000250|UniProtKB:P49841}... | null | null | null | null | FUNCTION: Constitutively active protein kinase that acts as a negative regulator in the hormonal control of glucose homeostasis, Wnt signaling and regulation of transcription factors and microtubules, by phosphorylating and inactivating glycogen synthase (GYS1 or GYS2), EIF2B, CTNNB1/beta-catenin, APC, AXIN1, DPYSL2/CR... | Rattus norvegicus (Rat) |
P18272 | NCAP_EBOZM | MDSRPQKIWMAPSLTESDMDYHKILTAGLSVQQGIVRQRVIPVYQVNNLEEICQLIIQAFEAGVDFQESADSFLLMLCLHHAYQGDYKLFLESGAVKYLEGHGFRFEVKKRDGVKRLEELLPAVSSGKNIKRTLAAMPEEETTEANAGQFLSFASLFLPKLVVGEKACLEKVQRQIQVHAEQGLIQYPTAWQSVGHMMVIFRLMRTNFLIKFLLIHQGMHMVAGHDANDAVISNSVAQARFSGLLIVKTVLDHILQKTERGVRLHPLARTAKVKNEVNSFKAALSSLAKHGEYAPFARLLNLSGVNNLEHGLFPQLSAIA... | null | null | viral RNA genome packaging [GO:0019074] | helical viral capsid [GO:0019029]; host cell cytoplasm [GO:0030430]; ribonucleoprotein complex [GO:1990904]; viral nucleocapsid [GO:0019013] | RNA binding [GO:0003723] | PF05505; | 1.20.120.1160; | Filoviruses nucleoprotein family | PTM: Phosphorylated by host. {ECO:0000269|PubMed:16571791}.; PTM: O-glycosylated by host. {ECO:0000269|PubMed:16571791}.; PTM: Acetylated by host EP300 in vitro. {ECO:0000269|PubMed:30205953}. | SUBCELLULAR LOCATION: Virion {ECO:0000269|PubMed:16719918}. Host cytoplasm {ECO:0000269|PubMed:28794491, ECO:0000269|PubMed:29290611, ECO:0000269|PubMed:32528005}. | null | null | null | null | null | FUNCTION: Oligomerizes into helical capsid to encapsidate the viral genome, protecting it from nucleases and the cellular innate immune response (PubMed:16719918, PubMed:25865894, PubMed:26119732, PubMed:30333622). VP35 binds to and stabilizes monomeric NP, keeping it soluble (PubMed:25865894, PubMed:26119732). Upon vi... | Zaire ebolavirus (strain Mayinga-76) (ZEBOV) (Zaire Ebola virus) |
P18278 | ADHA_ACEAC | MTRPASAKRRSLLGILAAGTICAAALPYAAVPARADGQGNTGEAIIHADDHPENWLSYGRTYSEQRYSPLDQINRSNVGDLKLLGYYTLDTNRGQEATPLVVDGIMYATTNWSKMEALDAATGKLLWQYDPKVPGNIADKGCCDTVNRGAGYWNGKVFWGTFDGRLVAADAKTGKKVWAVNTIPADASLGKQRSYTVDGAVRVAKGLVLIGNGGAEFGARGFVSAFDAETGKLKWRFYTVPNNKNEPDHAASDNILMNKAYKTWGPKGAWVRQGGGGTVWDSLVYDPVSDLIYLAVGNGSPWNYKYRSEGIGSNLFLGSI... | 1.1.5.5 | COFACTOR: Name=pyrroloquinoline quinone; Xref=ChEBI:CHEBI:58442; Evidence={ECO:0000250|UniProtKB:O05542}; Note=Binds 1 PQQ group per subunit. {ECO:0000250|UniProtKB:O05542}; COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:O05542}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtK... | null | outer membrane-bounded periplasmic space [GO:0030288]; plasma membrane [GO:0005886]; respirasome [GO:0070469] | calcium ion binding [GO:0005509]; electron transfer activity [GO:0009055]; heme binding [GO:0020037]; oxidoreductase activity, acting on CH-OH group of donors [GO:0016614] | PF13442;PF13360; | 1.10.760.10;2.140.10.10; | Bacterial PQQ dehydrogenase family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Peripheral membrane protein {ECO:0000305}; Periplasmic side {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a ubiquinone + ethanol = a ubiquinol + acetaldehyde; Xref=Rhea:RHEA:26442, Rhea:RHEA-COMP:9565, Rhea:RHEA-COMP:9566, ChEBI:CHEBI:15343, ChEBI:CHEBI:16236, ChEBI:CHEBI:16389, ChEBI:CHEBI:17976; EC=1.1.5.5; Evidence={ECO:0000250|UniProtKB:O05542}; | null | null | null | null | FUNCTION: Dehydrogenase component of the alcohol dehydrogenase multicomponent enzyme system which is involved in the production of acetic acid and in the ethanol oxidase respiratory chain. Quinohemoprotein alcohol dehydrogenase (ADH) catalyzes the oxidation of ethanol to acetaldehyde by transferring electrons to the ub... | Acetobacter aceti |
P18280 | NTF3_RAT | MSILFYVIFLAYLRGIQGNNMDQRSLPEDSLNSLIIKLIQADILKNKLSKQMVDVKENYQSTLPKAEAPREPEQGEATRSEFQPMIATDTELLRQQRRYNSPRVLLSDSTPLEPPPLYLMEDYVGNPVVTNRTSPRRKRYAEHKSHRGEYSVCDSESLWVTDKSSAIDIRGHQVTVLGEIKTGNSPVKQYFYETRCKEARPVKNGCRGIDDKHWNSQCKTSQTYVRALTSENNKLVGWRWIRIDTSCVCALSRKIGRT | null | null | axon guidance [GO:0007411]; brain development [GO:0007420]; enteric nervous system development [GO:0048484]; epidermis development [GO:0008544]; generation of neurons [GO:0048699]; glial cell fate determination [GO:0007403]; induction of positive chemotaxis [GO:0050930]; mechanoreceptor differentiation [GO:0042490]; me... | axon [GO:0030424]; cytoplasmic vesicle [GO:0031410]; dendrite [GO:0030425]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; synaptic vesicle [GO:0008021] | chemoattractant activity [GO:0042056]; growth factor activity [GO:0008083]; nerve growth factor binding [GO:0048406]; nerve growth factor receptor binding [GO:0005163] | PF00243;PF19338; | 2.10.90.10; | NGF-beta family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Seems to promote the survival of visceral and proprioceptive sensory neurons. | Rattus norvegicus (Rat) |
P18283 | GPX2_HUMAN | MAFIAKSFYDLSAISLDGEKVDFNTFRGRAVLIENVASLUGTTTRDFTQLNELQCRFPRRLVVLGFPCNQFGHQENCQNEEILNSLKYVRPGGGYQPTFTLVQKCEVNGQNEHPVFAYLKDKLPYPYDDPFSLMTDPKLIIWSPVRRSDVAWNFEKFLIGPEGEPFRRYSRTFPTINIEPDIKRLLKVAI | 1.11.1.12; 1.11.1.9 | null | response to oxidative stress [GO:0006979] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; intercellular bridge [GO:0045171]; mitotic spindle [GO:0072686] | electron transfer activity [GO:0009055]; glutathione peroxidase activity [GO:0004602]; phospholipid-hydroperoxide glutathione peroxidase activity [GO:0047066] | PF00255; | 3.40.30.10; | Glutathione peroxidase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:8428933}. | CATALYTIC ACTIVITY: Reaction=2 glutathione + H2O2 = glutathione disulfide + 2 H2O; Xref=Rhea:RHEA:16833, ChEBI:CHEBI:15377, ChEBI:CHEBI:16240, ChEBI:CHEBI:57925, ChEBI:CHEBI:58297; EC=1.11.1.9; Evidence={ECO:0000269|PubMed:36608588, ECO:0000269|PubMed:8428933}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16834... | null | null | null | null | FUNCTION: Catalyzes the reduction of hydroperoxides in a glutathione-dependent manner thus regulating cellular redox homeostasis (PubMed:36608588, PubMed:8428933). Can reduce small soluble hydroperoxides such as H2O2, cumene hydroperoxide and tert-butyl hydroperoxide, as well as several fatty acid-derived hydroperoxide... | Homo sapiens (Human) |
P18287 | APOE_RABIT | MKVWWAVLAAAILAGCRAQTEQEVEVPEQARWKAGQPWELALGRFWDYLRWVQSLSDQVQEELLSSQVTQELTMLMEETMKEVKAYKSELEEQLSPMAQEHRARLSKELQVAGALEADMEDVCNRLAQYRGEAQAMLGQSTEELARAFSSHLRKLRKRLLRDAEDLQKRMAVYGAGAREGAERGVSAVRERLGSRLERGRLRVATVGTLAGRPLRERAQAWGERLRGHLEEVGSRARDRLNEVREQVEEVRVKVEEQAPQMRLQAEAFQARLKSWFEPLVEDMQRQWAGLVEKLQAAMPSKAPAAAPIENQ | null | null | cholesterol catabolic process [GO:0006707]; cholesterol efflux [GO:0033344]; chylomicron remnant clearance [GO:0034382]; high-density lipoprotein particle assembly [GO:0034380]; intermediate-density lipoprotein particle clearance [GO:0071831]; lipoprotein biosynthetic process [GO:0042158]; lipoprotein catabolic process... | chylomicron [GO:0042627]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; high-density lipoprotein particle [GO:0034364]; intermediate-density lipoprotein particle [GO:0034363]; low-density lipoprotein particle [GO:0034362]; multivesicular body, internal vesicle [GO:0097487]; very-low-density lip... | amyloid-beta binding [GO:0001540]; heparan sulfate proteoglycan binding [GO:0043395]; heparin binding [GO:0008201]; identical protein binding [GO:0042802]; lipid binding [GO:0008289]; low-density lipoprotein particle receptor binding [GO:0050750]; peptide binding [GO:0042277]; protein homodimerization activity [GO:0042... | PF01442; | 1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: APOE exists as multiple glycosylated and sialylated glycoforms within cells and in plasma. The extent of glycosylation and sialylation are tissue and context specific. {ECO:0000250|UniProtKB:P02649}.; PTM: Glycated in plasma VLDL. {ECO:0000250|UniProtKB:P02649}.; PTM: Phosphorylated by FAM20C in the extracellular ... | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space {ECO:0000250|UniProtKB:P02649}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P02649}. Extracellular vesicle {ECO:0000250|UniProtKB:P02649}. Endosome, multivesicular body {ECO:0000250|UniProtKB:P026... | null | null | null | null | null | FUNCTION: APOE is an apolipoprotein, a protein associating with lipid particles, that mainly functions in lipoprotein-mediated lipid transport between organs via the plasma and interstitial fluids. APOE is a core component of plasma lipoproteins and is involved in their production, conversion and clearance. Apolipoprot... | Oryctolagus cuniculus (Rabbit) |
P18288 | TBAT_ONCMY | MRECISIHVGQAGVQIGNACWELYCLEHGIQPDGQMPSDKTIGGGDDSFNTFFSETGAGKHVPRAVFVDLEPTVVDEVRTGTYRQLFHPEQLITGKEDAANNYARGHYTIGKEIVDLVLDRVRKLSDQCTGLQGFLIFHSFGGGTGSGFASLLMERLSVDYGKKSKLEFAIYPAPQVSTAVVEPYNSILTTHTTLEHSDCAFMVDNEAIYDICRRNLDIERPTYTNLNRLIGQIVSSITASLRFDGALNVDLTEFQTNLVPYPRIHFPLVTYAPVISAEKAYHEMLSVAEITNACFEPANQMVKCDPRHGKYMACCMLYR... | 3.6.5.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363}; | microtubule cytoskeleton organization [GO:0000226]; mitotic cell cycle [GO:0000278] | cytoplasm [GO:0005737]; microtubule [GO:0005874] | GTP binding [GO:0005525]; hydrolase activity [GO:0016787]; metal ion binding [GO:0046872]; structural constituent of cytoskeleton [GO:0005200] | PF00091;PF03953; | 1.10.287.600;3.30.1330.20;3.40.50.1440; | Tubulin family | PTM: Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Bo... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; Evidence={ECO:0000250|UniProtKB:P68363}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670; Evidence={ECO:0000250|UniProtKB:P6836... | null | null | null | null | FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers a... | Oncorhynchus mykiss (Rainbow trout) (Salmo gairdneri) |
P18289 | JRA_DROME | MKTPVSAAANLSIQNAGSSGATAIQIIPKTEPVGEEGPMSLDFQSPNLNTSTPNPNKRPGSLDLNSKSAKNKRIFAPLVINSPDLSSKTVNTPDLEKILLSNNLMQTPQPGKVFPTKAGPVTVEQLDFGRGFEEALHNLHTNSQAFPSANSAANSAANNTTAAAMTAVNNGISGGTFTYTNMTEGFSVIKDEPVNQASSPTVNPIDMEAQEKIKLERKRQRNRVAASKCRKRKLERISKLEDRVKVLKGENVDLASIVKNLKDHVAQLKQQVMEHIAAGCTVPPNSTDQ | null | null | chorion micropyle formation [GO:0046844]; defense response to Gram-negative bacterium [GO:0050829]; dorsal appendage formation [GO:0046843]; dorsal closure [GO:0007391]; imaginal disc fusion, thorax closure [GO:0046529]; JNK cascade [GO:0007254]; modulation by host of viral genome replication [GO:0044827]; negative reg... | cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; transcription factor AP-1 complex [GO:0035976]; transcription regulator complex [GO:0005667] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein heterodimerization activity [GO:0046982]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00170;PF03957; | 1.20.5.170; | BZIP family, Jun subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9224723}. | null | null | null | null | null | FUNCTION: Transcription factor that recognizes and binds to the enhancer heptamer motif 5'-TGA[CG]TCA-3' (PubMed:1696724, PubMed:2116361). Plays a role in dorsal closure (PubMed:9224723). {ECO:0000269|PubMed:1696724, ECO:0000269|PubMed:2116361, ECO:0000269|PubMed:9224723}. | Drosophila melanogaster (Fruit fly) |
P18291 | GRAB_RAT | MKLLLLLLSFSLAPKTEAGEIIGGHEAKPHSRPYMAYLQIMDEYSGSKKCGGFLIREDFVLTAAHCSGSKINVTLGAHNIKEQEKMQQIIPVVKIIPHPAYNSKTISNDIMLLKLKSKAKRSSAVKPLNLPRRNVKVKPGDVCYVAGWGKLGPMGKYSDTLQEVELTVQEDQKCESYLKNYFDKANEICAGDPKIKRASFRGDSGGPLVCKKVAAGIVSYGQNDGSTPRAFTKVSTFLSWIKKTMKKS | 3.4.21.79 | null | defense response to bacterium [GO:0042742]; granzyme-mediated programmed cell death signaling pathway [GO:0140507]; killing of cells of another organism [GO:0031640]; natural killer cell mediated cytotoxicity [GO:0042267]; negative regulation of translation [GO:0017148]; neuron apoptotic process [GO:0051402]; positive ... | cytolytic granule [GO:0044194]; cytoplasm [GO:0005737]; early endosome [GO:0005769]; extracellular space [GO:0005615]; intracellular membrane-bounded organelle [GO:0043231] | serine-type endopeptidase activity [GO:0004252]; serine-type peptidase activity [GO:0008236] | PF00089; | 2.40.10.10; | Peptidase S1 family, Granzyme subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:9765264}. Cytolytic granule {ECO:0000250|UniProtKB:P10144}. Note=Delivered into the target cell by perforin. {ECO:0000250|UniProtKB:P10144}. | CATALYTIC ACTIVITY: Reaction=Preferential cleavage: -Asp-|-Xaa- >> -Asn-|-Xaa- > -Met-|-Xaa-, -Ser-|-Xaa-.; EC=3.4.21.79; Evidence={ECO:0000269|PubMed:9765264}; | null | null | null | null | FUNCTION: Abundant protease in the cytosolic granules of cytotoxic T-cells and NK-cells which activates caspase-independent pyroptosis when delivered into the target cell through the immunological synapse (By similarity). It cleaves after Asp (PubMed:9765264). Once delivered into the target cell, acts by catalyzing cle... | Rattus norvegicus (Rat) |
P18292 | THRB_RAT | MLHVRGLGLPGCLALAALASLVHSQHVFLAPQQALSLLQRVRRANSGFLEELRKGNLERECVEEQCSYEEAFEALESPQDTDVFWAKYTVCDSVRKPRETFMDCLEGRCAMDLGLNYHGNVSVTHTGIECQLWRSRYPHRPDINSTTHPGADLKENFCRNPDSSTSGPWCYTTDPTVRREECSIPVCGQEGRTTVKMTPRSRGSKENLSPPLGECLLERGRLYQGNLAVTTLGSPCLAWDSLPTKTLSKYQNFDPEVKLVQNFCRNPDRDEEGAWCFVAQQPGFEYCSLNYCDEAVGEENHDGDESIAGRTTDAEFHTFF... | 3.4.21.5 | null | acute-phase response [GO:0006953]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; cell surface receptor signaling pathway [GO:0007166]; cellular response to mechanical stimulus [GO:0071260]; fibrinolysis [GO:0042730]; G protein-coupled receptor signaling pathway [GO:0007186]; liga... | collagen-containing extracellular matrix [GO:0062023]; extracellular space [GO:0005615] | calcium ion binding [GO:0005509]; endopeptidase activity [GO:0004175]; heparin binding [GO:0008201]; lipopolysaccharide binding [GO:0001530]; peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252]; signaling receptor binding [GO:0005102]; thrombospondin receptor activity [GO:0070053] | PF00594;PF00051;PF09396;PF00089; | 2.40.20.10;4.10.140.10;2.40.10.10; | Peptidase S1 family | PTM: The gamma-carboxyglutamyl residues, which bind calcium ions, result from the carboxylation of glutamyl residues by a microsomal enzyme, the vitamin K-dependent carboxylase. The modified residues are necessary for the calcium-dependent interaction with a negatively charged phospholipid surface, which is essential f... | null | CATALYTIC ACTIVITY: Reaction=Selective cleavage of Arg-|-Gly bonds in fibrinogen to form fibrin and release fibrinopeptides A and B.; EC=3.4.21.5; | null | null | null | null | FUNCTION: Thrombin, which cleaves bonds after Arg and Lys, converts fibrinogen to fibrin and activates factors V, VII, VIII, XIII, and, in complex with thrombomodulin, protein C. Functions in blood homeostasis, inflammation and wound healing. | Rattus norvegicus (Rat) |
P18293 | ANPRA_MOUSE | MPGSRRVRPRLRALLLLPPLLLLRSGHASDLTVAVVLPLTNTSYPWSWARVGPAVELALGRVKARPDLLPGWTVRMVLGSSENAAGVCSDTAAPLAAVDLKWEHSPAVFLGPGCVYSAAPVGRFTAHWRVPLLTAGAPALGIGVKDEYALTTRTGPSHVKLGDFVTALHRRLGWEHQALVLYADRLGDDRPCFFIVEGLYMRVRERLNITVNHQEFVEGDPDHYTKLLRTVQRKGRVIYICSSPDAFRNLMLLALDAGLTGEDYVFFHLDVFGQSLQGAQGPVPRKPWERDDGQDRRARQAFQAAKIITYKEPDNPEYLE... | 4.6.1.2 | null | blood vessel diameter maintenance [GO:0097746]; cell surface receptor signaling pathway [GO:0007166]; cGMP biosynthetic process [GO:0006182]; cGMP-mediated signaling [GO:0019934]; dopamine metabolic process [GO:0042417]; intracellular signal transduction [GO:0035556]; negative regulation of smooth muscle cell prolifera... | ANPR-A receptor complex [GO:1990620]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | adenylate cyclase activity [GO:0004016]; ATP binding [GO:0005524]; GTP binding [GO:0005525]; guanylate cyclase activity [GO:0004383]; natriuretic peptide receptor activity [GO:0016941]; peptide hormone binding [GO:0017046]; peptide receptor activity [GO:0001653]; protein kinase activity [GO:0004672] | 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; | 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. | Mus musculus (Mouse) |
P18296 | CUT1_SCHPO | MSTRSIVTSKVSWTPEKFISALSYPEHCSITLVKRLKASVKLKDLKQNISRDAPSWTFEHLFVAFKCAVSNLAKQWAELSTTDKEKTRRMFCTPSRLNTAHRPEVFYLLECCTYILEQMQVVTKNTSHLYDCIRSGVSICNRLLDMEIFEPAISLLMKTHKNLIILLTYRDHDAIPTATLLNPTLDVSEIQLESCLFVPMVPASYFLNIGTIVVTFQLNVLRCLSLSQINGLSLNTINNLQSEDGPFQWIERSFPSQVQLANSRREILARLLTRFSMIQNNALQSFKLLILSIALWLNILSSQRADDKEFDVNQLETRIL... | 3.4.22.49 | null | cell division [GO:0051301]; DNA damage response [GO:0006974]; meiotic chromosome separation [GO:0051307]; meiotic nuclear division [GO:0140013]; mitotic sister chromatid separation [GO:0051306]; proteolysis [GO:0006508] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitotic spindle [GO:0072686]; mitotic spindle midzone [GO:1990023]; mitotic spindle pole body [GO:0044732]; nucleus [GO:0005634]; separase-securin complex [GO:1990520] | cysteine-type endopeptidase activity [GO:0004197]; endopeptidase activity [GO:0004175] | PF03568; | null | null | null | SUBCELLULAR LOCATION: Cytoplasm. Nucleus. | CATALYTIC ACTIVITY: Reaction=All bonds known to be hydrolyzed by this endopeptidase have arginine in P1 and an acidic residue in P4. P6 is often occupied by an acidic residue or by a hydroxy-amino-acid residue, the phosphorylation of which enhances cleavage.; EC=3.4.22.49; | null | null | null | null | FUNCTION: Caspase-like protease, which plays a central role in the chromosome segregation by cleaving the rad21 subunit of the cohesin complex at the onset of anaphase. During most of the cell cycle, it is inactivated by securin/cut2 protein. It is also required for pointed nuclear formation. {ECO:0000269|PubMed:123902... | Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) |
P18297 | SPRE_RAT | MEGGRLGCAVCVLTGASRGFGRALAPQLAGLLSPGSVLLLSARSDSMLRQLKEELCTQQPGLQVVLAAADLGTESGVQQLLSAVRELPRPERLQRLLLINNAGTLGDVSKGFLNINDLAEVNNYWALNLTSMLCLTTGTLNAFSNSPGLSKTVVNISSLCALQPFKGWGLYCAGKAARDMLYQVLAVEEPSVRVLSYAPGPLDTNMQQLARETSMDPELRSRLQKLNSEGELVDCGTSAQKLLSLLQRDTFQSGAHVDFYDI | 1.1.1.153 | null | cell morphogenesis involved in neuron differentiation [GO:0048667]; dopamine metabolic process [GO:0042417]; L-phenylalanine metabolic process [GO:0006558]; nitric oxide biosynthetic process [GO:0006809]; norepinephrine metabolic process [GO:0042415]; pteridine metabolic process [GO:0019889]; regulation of multicellula... | cytoplasm [GO:0005737] | protein homodimerization activity [GO:0042803]; sepiapterin reductase activity [GO:0004757] | PF00106; | 3.40.50.720; | Sepiapterin reductase family | PTM: In vitro phosphorylation of Ser-46, Ser-196 and Ser-214 by CaMK2 does not change kinetic parameters. {ECO:0000269|PubMed:11825621}. | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=L-erythro-7,8-dihydrobiopterin + NADP(+) = H(+) + NADPH + sepiapterin; Xref=Rhea:RHEA:18953, ChEBI:CHEBI:15378, ChEBI:CHEBI:16095, ChEBI:CHEBI:43029, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.1.1.153; Evidence={ECO:0000269|PubMed:10350607}; PhysiologicalDirection=right-to-left; Xref=Rhea:R... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=12.6 uM for sepiapterin {ECO:0000269|PubMed:10350607, ECO:0000269|PubMed:11825621}; KM=2.8 uM for NADPH {ECO:0000269|PubMed:10350607, ECO:0000269|PubMed:11825621}; Note=kcat is 9.7 sec(-1) with sepiapterin as substrate (PubMed:10350607). kcat is 11.1 sec(-1) with N... | null | null | null | FUNCTION: Catalyzes the final one or two reductions in tetra-hydrobiopterin biosynthesis to form 5,6,7,8-tetrahydrobiopterin. | Rattus norvegicus (Rat) |
P18298 | METK2_RAT | MNGQLNGFHEAFIEEGTFLFTSESVGEGHPDKICDQINDAVLDAHLQQDPDAKVACETVAKTGMILLAGEITSRAAIDYQKVVREAIKHIGYDDSSKGFDYKTCNVLVALEQQSPDIAQGVHLDRNEEDIGAGDQGLMFGYATDETEECMPLTIVLAHKLNAKLAELRRNGTLPWLRPDSKTQVTVQYMQDRGAVIPIRVHTIVISVQHDEEVCLDEMRDALKEKLIKAVVPAKYLDEDTIYHLQPSGRFVIGGPQGDAGLTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARWVAKSLVKGGLCRRVLVQVSY... | 2.5.1.6 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P0A817}; Note=Binds 2 magnesium ions per subunit. The magnesium ions interact primarily with the substrate. {ECO:0000250|UniProtKB:P31153}; COFACTOR: Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250|UniProtKB:P0A817}; Note=Binds 1 po... | cellular response to leukemia inhibitory factor [GO:1990830]; circadian rhythm [GO:0007623]; one-carbon metabolic process [GO:0006730]; protein heterooligomerization [GO:0051291]; protein hexamerization [GO:0034214]; response to cAMP [GO:0051591]; response to hormone [GO:0009725]; response to light stimulus [GO:0009416... | cytosol [GO:0005829]; methionine adenosyltransferase complex [GO:0048269] | amino acid binding [GO:0016597]; ATP binding [GO:0005524]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; methionine adenosyltransferase activity [GO:0004478]; small molecule binding [GO:0036094] | PF02773;PF02772;PF00438; | 3.30.300.10; | AdoMet synthase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-methionine = diphosphate + phosphate + S-adenosyl-L-methionine; Xref=Rhea:RHEA:21080, ChEBI:CHEBI:15377, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:43474, ChEBI:CHEBI:57844, ChEBI:CHEBI:59789; EC=2.5.1.6; Evidence={ECO:0000250|UniProtKB:P31153}; | null | PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. {ECO:0000250|UniProtKB:P31153}. | null | null | FUNCTION: Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate. {ECO:0000250|UniProtKB:P31153}. | Rattus norvegicus (Rat) |
P18314 | URE1_KLEAE | MSNISRQAYADMFGPTVGDKVRLADTELWIEVEDDLTTYGEEVKFGGGKVIRDGMGQGQMLAADCVDLVLTNALIVDHWGIVKADIGVKDGRIFAIGKAGNPDIQPNVTIPIGAATEVIAAEGKIVTAGGIDTHIHWICPQQAEEALVSGVTTMVGGGTGPAAGTHATTCTPGPWYISRMLQAADSLPVNIGLLGKGNVSQPDALREQVAAGVIGLKIHEDWGATPAAIDCALTVADEMDIQVALHSDTLNESGFVEDTLAAIGGRTIHTFHTEGAGGGHAPDIITACAHPNILPSSTNPTLPYTLNTIDEHLDMLMVCH... | 3.5.1.5 | COFACTOR: Name=Ni cation; Xref=ChEBI:CHEBI:25516; Evidence={ECO:0000255|HAMAP-Rule:MF_01953, ECO:0000269|PubMed:1400317, ECO:0000269|PubMed:1624427, ECO:0000269|PubMed:8318888}; Note=Binds 2 nickel ions per subunit. {ECO:0000255|HAMAP-Rule:MF_01953, ECO:0000269|PubMed:1400317, ECO:0000269|PubMed:1624427, ECO:0000269|Pu... | urea catabolic process [GO:0043419] | cytoplasm [GO:0005737] | nickel cation binding [GO:0016151]; urease activity [GO:0009039] | PF01979;PF00449; | 3.20.20.140;2.30.40.10; | Metallo-dependent hydrolases superfamily, Urease alpha subunit family | PTM: Carboxylation allows a single lysine to coordinate two nickel ions. {ECO:0000255|HAMAP-Rule:MF_01953, ECO:0000269|PubMed:10913264, ECO:0000269|PubMed:7754395, ECO:0000269|PubMed:8702515, ECO:0000269|PubMed:8718850}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01953}. | CATALYTIC ACTIVITY: Reaction=2 H(+) + H2O + urea = CO2 + 2 NH4(+); Xref=Rhea:RHEA:20557, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16199, ChEBI:CHEBI:16526, ChEBI:CHEBI:28938; EC=3.5.1.5; Evidence={ECO:0000255|HAMAP-Rule:MF_01953, ECO:0000269|PubMed:10500143, ECO:0000269|PubMed:11015224, ECO:0000269|PubMed:1400... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.3 mM for urea {ECO:0000269|PubMed:10913264, ECO:0000269|PubMed:11594743, ECO:0000269|PubMed:1400317, ECO:0000269|PubMed:8318888}; Vmax=1.9 mmol/min/mg enzyme {ECO:0000269|PubMed:10913264, ECO:0000269|PubMed:11594743, ECO:0000269|PubMed:1400317, ECO:0000269|PubMed... | PATHWAY: Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_01953}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.75. {ECO:0000269|PubMed:10913264, ECO:0000269|PubMed:11594743, ECO:0000269|PubMed:1400317, ECO:0000269|PubMed:8318888}; | null | null | Klebsiella aerogenes (Enterobacter aerogenes) |
P18326 | CPXE_STRGO | MTDTATTPQTTDAPAFPSNRSCPYQLPDGYAQLRDTPGPLHRVTLYDGRQAWVVTKHEAARKLLGDPRLSSNRTDDNFPATSPRFEAVRESPQAFIGLDPPEHGTRRRMTISEFTVKRIKGMRPEVEEVVHGFLDEMLAAGPTADLVSQFALPVPSMVICRLLGVPYADHEFFQDASKRLVQSTDAQSALTARNDLAGYLDGLITQFQTEPGAGLVGALVADQLANGEIDREELISTAMLLLIAGHETTASMTSLSVITLLDHPEQYAALRADRSLVPGAVEELLRYLAIADIAGGRVATADIEVEGHLIRAGEGVIVVN... | 1.14.15.22 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000269|PubMed:15207715, ECO:0000269|PubMed:18314962, ECO:0000269|PubMed:18937506}; | cholesterol catabolic process [GO:0006707]; vitamin D3 metabolic process [GO:0070640] | cytoplasm [GO:0005737] | cholest-4-en-3-one 26-monooxygenase activity [GO:0036199]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, NAD(P)H as one donor, and incorporation of one atom of oxygen [GO:0016709]; steroid hydroxylase acti... | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15207715}. | CATALYTIC ACTIVITY: Reaction=calciol + 2 H(+) + O2 + 2 reduced [2Fe-2S]-[ferredoxin] = calcidiol + H2O + 2 oxidized [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:50696, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:17933, ChEBI:CHEBI:28940, ChEBI:CHEBI:33737, C... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.54 uM for vitamin D3 (at pH 7.4 and 30 degrees Celsius) {ECO:0000269|PubMed:15207715}; KM=0.59 uM for vitamin D2 (at pH 7.4 and 30 degrees Celsius) {ECO:0000269|PubMed:15207715}; KM=0.91 uM for 25-hydroxyvitamin D3 (1-alpha-hydroxylation)(at pH 7.4 and 30 degrees... | null | null | null | FUNCTION: Involved in the metabolism of vitamin D3 (calciol) and of a number of sulfonylurea herbicides. Catalyzes the two-step hydroxylation (25- and 1-alpha-hydroxylation) of vitamin D3 (VD3) to yield its active form 1-alpha,25-dihydroxyvitamin D3 (calcitriol). The first step is the hydroxylation of the C-25 position... | Streptomyces griseolus |
P18331 | INHBA_RAT | MPLLWLRGFLLASCWIIVRSSPTPGSEGHGAAPDCPSCALATLPKDGPNSQPEMVEAVKKHILNMLHLKKRPDVTQPVPKAALLNAIRKLHVGKVGENGYVEIEDDIGRRAEMNELMEQTSEIITFAESGTARKTLHFEISKEGSDLSVVERAEVWLFLKVPKANRTRTKVTIRLFQQQKHPQGSLDMGDEAEEMGLKGERSELLLSEKVVDARKSTWHIFPVSSSIQRLLDQGKSSLDVRIACEQCQESGASLVLLGKKKKKEVDGDGKKKDGSDGGLEEEKEQSHRPFLMLQARQSEDHPHRRRRRGLECDGKVNICC... | null | null | activin receptor signaling pathway [GO:0032924]; autophagy [GO:0006914]; cardiac fibroblast cell development [GO:0060936]; cellular response to angiotensin [GO:1904385]; cellular response to cholesterol [GO:0071397]; cellular response to follicle-stimulating hormone stimulus [GO:0071372]; cellular response to hypoxia [... | activin A complex [GO:0043509]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; inhibin A complex [GO:0043512]; perinuclear region of cytoplasm [GO:0048471] | cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; hormone activity [GO:0005179]; identical protein binding [GO:0042802]; peptide hormone binding [GO:0017046]; protein-containing complex binding [GO:0044877]; signaling receptor binding [GO:0005102]; type II activin receptor binding [GO:0070699] | PF00019;PF00688; | 2.60.120.970;2.10.90.10; | TGF-beta family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250}. | null | null | null | null | null | FUNCTION: Inhibins and activins inhibit and activate, respectively, the secretion of follitropin by the pituitary gland. Inhibins/activins are involved in regulating a number of diverse functions such as hypothalamic and pituitary hormone secretion, gonadal hormone secretion, germ cell development and maturation, eryth... | Rattus norvegicus (Rat) |
P18334 | CSK2A_CAEEL | MPPIPSRARVYAEVNPSRPREYWDYEAHMIEWGQIDDYQLVRKLGRGKYSEVFEGFKMSTDEKVVVKILKPVKKKKIKREIKILENLRGGTNIITLLDVVKDPISRTPALIFEHVNNSDFKQLYQTLSDYDIRYYLYELLKALDFCHSQGIMHRDVKPHNVMIDAEKRELRLIDWGLAEFYHPRQDYNVRVASRYFKGPELLVDYQCYDYSLDMWSLGCMLASMIFRKEPFFHGHDNYDQLVRIAKVLGTDELYEYIARYHIDLDPRFNDILGRHSRKRWERFIHAENQHLVTPEALDFLDKLLRYDHAERLTAQEAMGH... | 2.7.11.1 | null | DNA damage response [GO:0006974]; peptidyl-serine phosphorylation [GO:0018105]; regulation of cell cycle [GO:0051726]; regulation of transcription by RNA polymerase I [GO:0006356]; regulation of transcription by RNA polymerase III [GO:0006359]; response to hermaphrodite contact [GO:0034606]; vulval location [GO:0034608... | axon [GO:0030424]; cilium [GO:0005929]; cytosol [GO:0005829]; dendrite [GO:0030425]; neuronal cell body [GO:0043025]; non-motile cilium [GO:0097730]; nucleus [GO:0005634]; perikaryon [GO:0043204]; protein kinase CK2 complex [GO:0005956] | ATP binding [GO:0005524]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, CK2 subfamily | null | SUBCELLULAR LOCATION: Cell projection, axon {ECO:0000269|PubMed:16481400}. Cell projection, cilium {ECO:0000269|PubMed:16481400}. Cell projection, dendrite {ECO:0000269|PubMed:16481400}. Perikaryon {ECO:0000269|PubMed:16481400}. Note=Enriched in cilia in male sensory neurons. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Casein kinases are operationally defined by their preferential utilization of acidic proteins such as caseins as substrates. The alpha chain contains the catalytic site. May participate in Wnt signaling. Modulates two aspects of male mating behavior; response to hermaphrodite contact and vulval location, acti... | Caenorhabditis elegans |
P18335 | ARGD_ECOLI | MAIEQTAITRATFDEVILPIYAPAEFIPVKGQGSRIWDQQGKEYVDFAGGIAVTALGHCHPALVNALKTQGETLWHISNVFTNEPALRLGRKLIEATFAERVVFMNSGTEANETAFKLARHYACVRHSPFKTKIIAFHNAFHGRSLFTVSVGGQPKYSDGFGPKPADIIHVPFNDLHAVKAVMDDHTCAVVVEPIQGEGGVTAATPEFLQGLRELCDQHQALLVFDEVQCGMGRTGDLFAYMHYGVTPDILTSAKALGGGFPISAMLTTAEIASAFHPGSHGSTYGGNPLACAVAGAAFDIINTPEVLEGIQAKRQRFVD... | 2.6.1.11; 2.6.1.17 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000255|HAMAP-Rule:MF_01107, ECO:0000305|PubMed:10074354}; Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000255|HAMAP-Rule:MF_01107, ECO:0000305|PubMed:10074354}; | arginine biosynthetic process via ornithine [GO:0042450]; lysine biosynthetic process via diaminopimelate and N-succinyl-2-amino-6-ketopimelate [GO:0033359] | cytoplasm [GO:0005737] | identical protein binding [GO:0042802]; N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity [GO:0003992]; pyridoxal phosphate binding [GO:0030170]; succinyldiaminopimelate transaminase activity [GO:0009016] | PF00202; | 3.90.1150.10;3.40.640.10; | Class-III pyridoxal-phosphate-dependent aminotransferase family, ArgD subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01107, ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=2-oxoglutarate + N(2)-acetyl-L-ornithine = L-glutamate + N-acetyl-L-glutamate 5-semialdehyde; Xref=Rhea:RHEA:18049, ChEBI:CHEBI:16810, ChEBI:CHEBI:29123, ChEBI:CHEBI:29985, ChEBI:CHEBI:57805; EC=2.6.1.11; Evidence={ECO:0000255|HAMAP-Rule:MF_01107, ECO:0000269|PubMed:10074354}; CATALYTIC ACT... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.15 mM for N-acetylornithine {ECO:0000269|PubMed:10074354}; KM=0.075 mM for N-succinyldiaminopimelate {ECO:0000269|PubMed:10074354}; | PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 4/4. {ECO:0000255|HAMAP-Rule:MF_01107, ECO:0000305|PubMed:10074354}.; PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase rou... | null | null | FUNCTION: Involved in both the arginine and lysine biosynthetic pathways. {ECO:0000255|HAMAP-Rule:MF_01107, ECO:0000269|PubMed:10074354}. | Escherichia coli (strain K12) |
P18337 | LYAM1_MOUSE | MVFPWRCEGTYWGSRNILKLWVWTLLCCDFLIHHGTHCWTYHYSEKPMNWENARKFCKQNYTDLVAIQNKREIEYLENTLPKSPYYYWIGIRKIGKMWTWVGTNKTLTKEAENWGAGEPNNKKSKEDCVEIYIKRERDSGKWNDDACHKRKAALCYTASCQPGSCNGRGECVETINNHTCICDAGYYGPQCQYVVQCEPLEAPELGTMDCIHPLGNFSFQSKCAFNCSEGRELLGTAETQCGASGNWSSPEPICQVVQCEPLEAPELGTMDCIHPLGNFSFQSKCAFNCSEGRELLGTAETQCGASGNWSSPEPICQETN... | null | null | calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0016339]; heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0007157]; leukocyte tethering or rolling [GO:0050901]; positive regulation of neutrophil chemotaxis [GO:0090023]; regulation of apoptotic process... | cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; plasma membrane [GO:0005886] | calcium ion binding [GO:0005509]; cell adhesion molecule binding [GO:0050839]; glycolipid binding [GO:0051861]; oligosaccharide binding [GO:0070492]; sialic acid binding [GO:0033691] | PF00059;PF00084; | 2.10.70.10;3.10.100.10; | Selectin/LECAM family | PTM: N-glycosylated. {ECO:0000250|UniProtKB:P14151}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1693096, ECO:0000269|PubMed:2646713}; Single-pass type I membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Calcium-dependent lectin that mediates cell adhesion by binding to glycoproteins on neighboring cells. Mediates the adherence of lymphocytes to endothelial cells of high endothelial venules in peripheral lymph nodes (PubMed:1693096). Promotes initial tethering and rolling of leukocytes in endothelia (By simil... | Mus musculus (Mouse) |
P18339 | RDRP_TMGMV | MAHIQSIISNALLESVSGKNTLVNDLARRRMYDTAVEEFNARDRRPKVNFSKTISEEQTLLVSNAYPEFQITFYNTQNAVHSLAGGLRALELEYLMLQVPYGSPTYDIGGNFAAHLFKGRDYVHCCMPNLDIRDIMRHEGQKDSIEMYLSRLSRSNKVIPEFQREAFNRYAEAPNEVCCSKTFQDCRIHPPENSGRRYAVALHSLYDIPVHEFGAALISKNIHVCYAASILAEALLLDQTEVTLNEIGATFKREGDDVSFFFADESTLNYSHKYKNILHYVVKSYFPASSRIVYFKEFLVTRVNTWFCKFTKVDTYILYK... | 2.1.1.-; 2.7.7.-; 2.7.7.48; 3.6.4.13 | null | DNA-templated transcription [GO:0006351]; RNA processing [GO:0006396]; viral RNA genome replication [GO:0039694]; virus-mediated perturbation of host defense response [GO:0019049] | null | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; mRNA methyltransferase activity [GO:0008174]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA-dependent RNA polymerase activity [GO:0003968] | PF00978;PF20896;PF01443;PF01660; | 3.30.450.420;3.40.50.300; | SsRNA positive-strand viruses RNA-directed RNA polymerase family | null | null | 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=ATP + H2... | null | null | null | null | FUNCTION: [Replicase large subunit]: Is an RNA-dependent RNA polymerase active in viral RNA replication.; FUNCTION: [Replicase small subunit]: Is a methyltransferase active in RNA capping and an RNA helicase. Methyltransferase displays a cytoplasmic capping enzyme activity. This function is necessary since all viral RN... | Tobacco mild green mosaic virus (TMGMV) (TMV strain U2) |
P18340 | CXCL9_MOUSE | MKSAVLFLLGIIFLEQCGVRGTLVIRNARCSCISTSRGTIHYKSLKDLKQFAPSPNCNKTEIIATLKNGDQTCLDPDSANVKKLMKEWEKKISQKKKQKRGKKHQKNMKNRKPKTPQSRRRSRKTT | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; antimicrobial humoral immune response mediated by antimicrobial peptide [GO:0061844]; cellular response to lipopolysaccharide [GO:0071222]; chemokine-mediated signaling pathway [GO:0070098]; chemotaxis [GO:0006935]; defense response... | external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615] | chemokine activity [GO:0008009]; CXCR chemokine receptor binding [GO:0045236]; CXCR3 chemokine receptor binding [GO:0048248] | PF00048; | 2.40.50.40; | Intercrine alpha (chemokine CxC) family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: May be a cytokine that affects the growth, movement, or activation state of cells that participate in immune and inflammatory response. | Mus musculus (Mouse) |
P18341 | TGFB1_BOVIN | MPPSGLRLLPLLLPLLWLLMLTPGRPVAGLSTCKTIDMELVKRKRIEAIRGQILSKLRLASPPSQGDVPPGPLPEAILALYNSTRDRVAGESAETEPEPEADYYAKEVTRVLMVEYGNKIYDKMKSSSHSIYMFFNTSELREAVPEPVLLSRADVRLLRLKLKVEQHVELYQKYSNNSWRYLSNRLLAPSDSPEWLSFDVTGVVRQWLTRREEIEGFRLSAHCSCDSKDNTLQVDINGFSSGRRGDLATIHGMNRPFLLLMATPLERAQHLHSSRHRRALDTNYCFSSTEKNCCVRQLYIDFRKDLGWKWIHEPKGYHAN... | null | null | ATP biosynthetic process [GO:0006754]; cell-cell junction organization [GO:0045216]; cellular response to transforming growth factor beta stimulus [GO:0071560]; chondrocyte differentiation [GO:0002062]; epithelial to mesenchymal transition [GO:0001837]; extracellular matrix assembly [GO:0085029]; extrinsic apoptotic si... | blood microparticle [GO:0072562]; cell surface [GO:0009986]; cytoplasm [GO:0005737]; extracellular matrix [GO:0031012]; extracellular space [GO:0005615]; nucleus [GO:0005634] | antigen binding [GO:0003823]; cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; type I transforming growth factor beta receptor binding [GO:0034713]; type II transforming growth factor beta receptor binding [GO:0005114]; type III transforming growth factor beta receptor binding [GO:0034714] | PF00019;PF00688; | 2.60.120.970;2.10.90.10; | TGF-beta family | PTM: Transforming growth factor beta-1 proprotein: The precursor proprotein is cleaved in the Golgi apparatus by FURIN to form Transforming growth factor beta-1 (TGF-beta-1) and Latency-associated peptide (LAP) chains, which remain non-covalently linked, rendering TGF-beta-1 inactive. {ECO:0000250|UniProtKB:P01137}.; P... | SUBCELLULAR LOCATION: [Latency-associated peptide]: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P01137}.; SUBCELLULAR LOCATION: [Transforming growth factor beta-1]: Secreted {ECO:0000250|UniProtKB:P01137}. | null | null | null | null | null | FUNCTION: Transforming growth factor beta-1 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-1 (TGF-beta-1) chains, which constitute the regulatory and active subunit of TGF-beta-1, respectively. {ECO:0000250|UniProtKB:P01137}.; FUNCTION: [Latency-associated peptide]: Re... | Bos taurus (Bovine) |
P18356 | POLG_DEN2U | SAGMIIMLIPTVMAFHLTTRNGEPHMIVSRQEKGKSLLFKTEDGVNMCTLMAMDLGELCEDTITYKCPLLRQNEPEDIDCWCNSTSTWVTYGTCTTTGEHRREKRSVALVPHVGMGLETRTETWMSSEGAWKHAQRIEIWILRHPGFTIMAAILAYTIGTTHFQRALIFILLTAVAPSMTMRCIGISNRDFVEGVSGGSWVDIVLEHGSCVTTMAKNKPTLDFELIKTEAKQPATLRKYCIEAKLTNTTTESRCPTQGEPSLNEEQDKRFVCKHSMVDRGWGNGCGLFGKGGIVTCAMFTCKKNMEGKVVQPENLEYTIV... | null | null | clathrin-dependent endocytosis of virus by host cell [GO:0075512]; fusion of virus membrane with host endosome membrane [GO:0039654]; virion attachment to host cell [GO:0019062]; virus-mediated perturbation of host defense response [GO:0019049] | extracellular region [GO:0005576]; host cell endoplasmic reticulum membrane [GO:0044167]; membrane [GO:0016020]; viral envelope [GO:0019031]; viral nucleocapsid [GO:0019013]; virion membrane [GO:0055036] | protein dimerization activity [GO:0046983] | PF21659;PF02832;PF00869;PF01004;PF01570; | 1.20.1280.260;2.60.40.350;1.10.8.970;2.60.260.50;2.60.98.10;3.30.67.10;3.30.387.10; | null | PTM: [Protein prM]: Cleaved in post-Golgi vesicles by a host furin, releasing the mature small envelope protein M, and peptide pr. This cleavage is incomplete as up to 30% of viral particles still carry uncleaved prM. {ECO:0000250|UniProtKB:P17763}.; PTM: [Envelope protein E]: N-glycosylated. {ECO:0000250|UniProtKB:P17... | SUBCELLULAR LOCATION: [Peptide pr]: Secreted {ECO:0000250|UniProtKB:P17763}.; SUBCELLULAR LOCATION: [Small envelope protein M]: Virion membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:0000255}. Host endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P17763}; Multi-pass membrane protein {ECO:... | null | null | null | null | null | FUNCTION: [Peptide pr]: Prevents premature fusion activity of envelope proteins in trans-Golgi by binding to envelope protein E at pH6.0. After virion release in extracellular space, gets dissociated from E dimers. {ECO:0000250|UniProtKB:P17763}.; FUNCTION: [Protein prM]: Acts as a chaperone for envelope protein E duri... | Dengue virus type 2 (strain Thailand/PUO-218/1980) (DENV-2) |
P18357 | BLAR_STAAU | MAKLLIMSIVSFCFIFLLLLFFRYILKRYFNYMLNYKVWYLTLLAGLIPFIPIKFSLFKFNNVNNQAPTVESKSHDLNHNINTTKPIQEFATDIHKFNWDSIDNISTVIWIVLVIILSFKFLKALLYLKYLKKQSLYLNENEKNKIDTILFNHQYKKNIVIRKAETIQSPITFWYGKYIILIPSSYFKSVIDKRLKYIILHEYAHAKNRDTLHLIIFNIFSIIMSYNPLVHIVKRKIIHDNEVEADRFVLNNINKNEFKTYAESIMDSVLNVPFFNKNILSHSFNGKKSLLKRRLINIKEANLKKQSKLILIFICIFTFL... | null | null | cell wall organization [GO:0071555] | plasma membrane [GO:0005886] | penicillin binding [GO:0008658] | PF05569;PF00905; | 3.40.710.10; | Peptidase M56 family | PTM: Carboxylation occurs on two lysine residues. Carboxylation at 'Lys-392' activates the active site serine residue for acylation (PubMed:12591921). On acylation, the lysine side chain experiences a spontaneous decarboxylation that entraps the sensor in its activated state (PubMed:15506754, PubMed:21775440). {ECO:000... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P12287}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P12287}. | null | null | null | null | null | FUNCTION: Integral membrane protein involved in sensing of the presence of beta-lactam antibiotics and transduction of the information to the cytoplasm. Mechanistically, activation of the signal transducer involves acylation of a serine in the C-terminal sensor domain upon binding of the beta-lactam antibiotic (PubMed:... | Staphylococcus aureus |
P18378 | PG041_VACCW | MLAFCYSLPNAGDVIKGRVYEKDYALYIYLFDYPHFEAILAESVKMHMDRYVEYRDKLVGKTVKVKVIRVDYTKGYIDVNYKRMCRHQ | null | null | symbiont-mediated suppression of host PKR/eIFalpha signaling [GO:0039580]; symbiont-mediated suppression of host type I interferon-mediated signaling pathway [GO:0039502]; virus-mediated perturbation of host defense response [GO:0019049] | cytoplasm [GO:0005737] | peptidase inhibitor activity [GO:0030414]; protein sequestering activity [GO:0140311]; protein serine/threonine kinase inhibitor activity [GO:0030291]; RNA binding [GO:0003723] | PF00575; | 2.40.50.140; | Poxviridae K3 protein family | null | null | null | null | null | null | null | FUNCTION: Viral mimic of EIF2S1/eIF-2alpha that acts as a pseudosubstrate for EIF2AK2/PKR kinase (PubMed:8099586, PubMed:9199350). Inhibits therefore EIF2S1/eIF-2alpha phosphorylation by host EIF2AK2/PKR kinase and prevents protein synthesis shutoff (PubMed:8099586, PubMed:9199350). Determinant of host species specific... | Vaccinia virus (strain Western Reserve) (VACV) (Vaccinia virus (strain WR)) |
P18405 | S5A1_HUMAN | MATATGVAEERLLAALAYLQCAVGCAVFARNRQTNSVYGRHALPSHRLRVPARAAWVVQELPSLALPLYQYASESAPRLRSAPNCILLAMFLVHYGHRCLIYPFLMRGGKPMPLLACTMAIMFCTCNGYLQSRYLSHCAVYADDWVTDPRFLIGFGLWLTGMLINIHSDHILRNLRKPGDTGYKIPRGGLFEYVTAANYFGEIMEWCGYALASWSVQGAAFAFFTFCFLSGRAKEHHEWYLRKFEEYPKFRKIIIPFLF | 1.3.1.22 | null | androgen biosynthetic process [GO:0006702]; androgen catabolic process [GO:0006710]; bone development [GO:0060348]; cell differentiation [GO:0030154]; cellular response to cAMP [GO:0071320]; cellular response to dexamethasone stimulus [GO:0071549]; cellular response to epinephrine stimulus [GO:0071872]; cellular respon... | cell body fiber [GO:0070852]; endoplasmic reticulum membrane [GO:0005789]; neuronal cell body [GO:0043025]; perinuclear region of cytoplasm [GO:0048471] | 3-oxo-5-alpha-steroid 4-dehydrogenase activity [GO:0003865]; 3-oxo-5alpha-steroid 4-dehydrogenase (NADP+) activity [GO:0047751]; amide binding [GO:0033218]; electron transfer activity [GO:0009055]; NADPH binding [GO:0070402] | PF02544; | 1.20.120.1630; | Steroid 5-alpha reductase family | null | SUBCELLULAR LOCATION: Microsome membrane; Multi-pass membrane protein. Endoplasmic reticulum membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a 3-oxo-5alpha-steroid + NADP(+) = a 3-oxo-Delta(4)-steroid + H(+) + NADPH; Xref=Rhea:RHEA:54384, ChEBI:CHEBI:13601, ChEBI:CHEBI:15378, ChEBI:CHEBI:47909, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.3.1.22; Evidence={ECO:0000269|PubMed:2339109}; CATALYTIC ACTIVITY: Reaction=androst-4-ene-3,1... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.6 uM for testosterone {ECO:0000269|PubMed:2339109}; KM=1.7 uM for androstenedione {ECO:0000269|PubMed:2339109}; KM=0.8 uM for progesterone {ECO:0000269|PubMed:2339109}; Vmax=3.6 nmol/min/mg enzyme toward testosterone {ECO:0000269|PubMed:2339109}; Vmax=5.3 nmol/mi... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimally active at alkaline pHs.; | null | FUNCTION: Converts testosterone into 5-alpha-dihydrotestosterone and progesterone or corticosterone into their corresponding 5-alpha-3-oxosteroids. It plays a central role in sexual differentiation and androgen physiology. {ECO:0000269|PubMed:2339109}. | Homo sapiens (Human) |
P18406 | CCN1_MOUSE | MSSSTFRTLAVAVTLLHLTRLALSTCPAACHCPLEAPKCAPGVGLVRDGCGCCKVCAKQLNEDCSKTQPCDHTKGLECNFGASSTALKGICRAQSEGRPCEYNSRIYQNGESFQPNCKHQCTCIDGAVGCIPLCPQELSLPNLGCPNPRLVKVSGQCCEEWVCDEDSIKDSLDDQDDLLGLDASEVELTRNNELIAIGKGSSLKRLPVFGTEPRVLFNPLHAHGQKCIVQTTSWSQCSKSCGTGISTRVTNDNPECRLVKETRICEVRPCGQPVYSSLKKGKKCSKTKKSPEPVRFTYAGCSSVKKYRPKYCGSCVDGRC... | null | null | apoptotic process [GO:0006915]; apoptotic process involved in heart morphogenesis [GO:0003278]; atrial septum morphogenesis [GO:0060413]; atrioventricular valve morphogenesis [GO:0003181]; cell adhesion [GO:0007155]; cell-cell adhesion [GO:0098609]; chemotaxis [GO:0006935]; chondroblast differentiation [GO:0060591]; ch... | collagen-containing extracellular matrix [GO:0062023]; cytosol [GO:0005829]; extracellular space [GO:0005615]; membrane [GO:0016020] | extracellular matrix binding [GO:0050840]; growth factor binding [GO:0019838]; heparin binding [GO:0008201]; integrin binding [GO:0005178] | PF00007;PF00219;PF19035;PF00093; | 2.10.70.10;2.20.100.10; | CCN family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Promotes cell proliferation, chemotaxis, angiogenesis and cell adhesion. Appears to play a role in wound healing by up-regulating, in skin fibroblasts, the expression of a number of genes involved in angiogenesis, inflammation and matrix remodeling including VEGA-A, VEGA-C, MMP1, MMP3, TIMP1, uPA, PAI-1 and i... | Mus musculus (Mouse) |
P18409 | MDM10_YEAST | MLPYMDQVLRAFYQSTHWSTQNSYEDITATSRTLLDFRIPSAIHLQISNKSTPNTFNSLDFSTRSRINGSLSYLYSDAQQLEKFMRNSTDIPLQDATETYRQLQPNLNFSVSSANTLSSDNTTVDNDKKLLHDSKFVKKSLYYGRMYYPSSDLEAMIIKRLSPQTQFMLKGVSSFKESLNVLTCYFQRDSHRNLQEWIFSTSDLLCGYRVLHNFLTTPSKFNTSLYNNSSLSLGAEFWLGLVSLSPGCSTTLRYYTHSTNTGRPLTLTLSWNPLFGHISSTYSAKTGTNSTFCAKYDFNLYSIESNLSFGCEFWQKKHHL... | null | null | establishment of mitochondrion localization [GO:0051654]; mitochondrial genome maintenance [GO:0000002]; mitochondrial outer membrane translocase complex assembly [GO:0070096]; mitochondrion organization [GO:0007005]; mitochondrion-endoplasmic reticulum membrane tethering [GO:1990456]; phospholipid homeostasis [GO:0055... | ERMES complex [GO:0032865]; mitochondrial outer membrane [GO:0005741]; outer mitochondrial membrane protein complex [GO:0098799]; SAM complex [GO:0001401] | null | PF12519; | null | MDM10 family | null | SUBCELLULAR LOCATION: Mitochondrion outer membrane {ECO:0000255|HAMAP-Rule:MF_03102, ECO:0000269|PubMed:13679517, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:16407407, ECO:0000269|PubMed:19556461, ECO:0000269|PubMed:8089171}; Multi-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03102, ECO:0000269|PubMed:13679517,... | null | null | null | null | null | FUNCTION: Component of the ERMES/MDM complex, which serves as a molecular tether to connect the endoplasmic reticulum and mitochondria. Components of this complex are involved in the control of mitochondrial shape and protein biogenesis and may function in phospholipid exchange. MDM10 is involved in the late assembly s... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P18410 | SPO7_YEAST | MEPESIGDVGNHAQDDSASIVSGPRRRSTSKTSSAKNIRNSSNISPASMIFRNLLILEDDLRRQAHEQKILKWQFTLFLASMAGVGAFTFYELYFTSDYVKGLHRVILQFTLSFISITVVLFHISGQYRRTIVIPRRFFTSTNKGIRQFNVKLVKVQSTWDEKYTDSVRFVSRTIAYCNIYCLKKFLWLKDDNAIVKFWKSVTIQSQPRIGAVDVKLVLNPRAFSAEIREGWEIYRDEFWAREGARRRKQAHELRPKSE | null | null | lipid metabolic process [GO:0006629]; negative regulation of phospholipid biosynthetic process [GO:0071072]; nuclear envelope organization [GO:0006998]; regulation of phospholipid biosynthetic process [GO:0071071]; reticulophagy [GO:0061709]; sporulation resulting in formation of a cellular spore [GO:0030435] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; Nem1-Spo7 phosphatase complex [GO:0071595]; nuclear membrane [GO:0031965] | phosphoprotein phosphatase activity [GO:0004721]; protein phosphatase regulator activity [GO:0019888] | PF03907; | null | null | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:9822591}; Multi-pass membrane protein {ECO:0000269|PubMed:9822591}. Nucleus membrane {ECO:0000269|PubMed:9822591}; Multi-pass membrane protein {ECO:0000269|PubMed:9822591}. | null | null | null | null | null | FUNCTION: Regulatory component of the NEM1-SPO7 complex which acts as a phosphatase and dephosphorylates the phosphatidic acid phosphohydrolase PAH1 (PubMed:15889145). Essential for the formation of a spherical nucleus and meiotic division (PubMed:9822591). The NEM1-SPOo7 protein phosphatase is required for efficient m... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P18412 | TEC1_YEAST | MSLKEDDFGKDNSRNIESYTGRIFDVYIQKDSYSQSALDDMFPEAVVSTAACVKNEAEDNINLIDTHPQFELVNTGLGAKSDDLKSPSAKATFTDKQRKNEVPNISVSNYFPGQSSETSSTTESWTIGCDKWSEKVEEAFLEALRLIMKNGTTKIKIRNANFGRNELISLYIKHKTNEFRTKKQISSHIQVWKKTIQNKIKDSLTLSSKEKELLHLIEHGAEQTTENSNLFYDIFEEIIDSLPSVSDSGSLTPKNLYVSNNSSGLSVHSKLLTPITASNEKKIENFIKTNAASQAKTPLIYAKHIYENIDGYKCVPSKRP... | null | null | hippo signaling [GO:0035329]; invasive growth in response to glucose limitation [GO:0001403]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of pseudohyphal growth [GO:2000222]; positive regulation of transcrip... | nucleus [GO:0005634]; Tec1p-Ste12p-Dig1p complex [GO:1990527]; transcription regulator complex [GO:0005667] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-... | PF01285; | 6.10.20.40; | TEC1 family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: TEC1 is involved in the activation of TY1 and TY1-mediated gene expression. It is not involved in mating or sporulation processes. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P18418 | CALR_RAT | MLLSVPLLLGLLGLAAADPAIYFKEQFLDGDAWTNRWVESKHKSDFGKFVLSSGKFYGDQEKDKGLQTSQDARFYALSARFEPFSNKGQTLVVQFTVKHEQNIDCGGGYVKLFPGGLDQKDMHGDSEYNIMFGPDICGPGTKKVHVIFNYKGKNVLINKDIRCKDDEFTHLYTLIVRPDNTYEVKIDNSQVESGSLEDDWDFLPPKKIKDPDAAKPEDWDERAKIDDPTDSKPEDWDKPEHIPDPDAKKPEDWDEEMDGEWEPPVIQNPEYKGEWKPRQIDNPDYKGTWIHPEIDNPEYSPDANIYAYDSFAVLGLDLWQ... | null | null | cardiac muscle cell differentiation [GO:0055007]; cellular response to electrical stimulus [GO:0071257]; cellular response to lithium ion [GO:0071285]; cellular response to organic substance [GO:0071310]; cellular response to virus [GO:0098586]; cellular senescence [GO:0090398]; cortical actin cytoskeleton organization... | acrosomal vesicle [GO:0001669]; cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; cortical granule [GO:0060473]; cytolytic granule [GO:0044194]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticul... | calcium ion binding [GO:0005509]; carbohydrate binding [GO:0030246]; complement component C1q complex binding [GO:0001849]; hormone binding [GO:0042562]; integrin binding [GO:0005178]; iron ion binding [GO:0005506]; molecular sequestering activity [GO:0140313]; mRNA binding [GO:0003729]; nuclear androgen receptor bindi... | PF00262; | 2.60.120.200;2.10.250.10; | Calreticulin family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:12782144}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:P27797}. Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P27797}. Cell surface {ECO:0000250|UniProtKB:P27797}. Sarcoplasmic reticulum lumen {ECO:0000250|UniProtKB:P28491}... | null | null | null | null | null | FUNCTION: Calcium-binding chaperone that promotes folding, oligomeric assembly and quality control in the endoplasmic reticulum (ER) via the calreticulin/calnexin cycle. This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts with the DNA-binding... | Rattus norvegicus (Rat) |
P18420 | PSA1_RAT | MFRNQYDNDVTVWSPQGRIHQIEYAMEAVKQGSATVGLKSKTHAVLVALKRAQSELAAHQKKILHVDNHIGISIAGLTADARLLCNFMRQECLDSRFVFDRPLPVSRLVSLIGSKTQIPTQRYGRRPYGVGLLIAGYDDMGPHVFQTCPSANYFDCRAMSIGARSQSARTYLERHMSEFMQCNLDELVKHGLRALRETLPAEQDLTTKNVSIGIVGKDLEFTIYDDDDVSPFLDGLEERPQRKAQPSQAADEPAEKADEPMEH | null | null | immune system process [GO:0002376]; negative regulation of inflammatory response to antigenic stimulus [GO:0002862]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161] | centrosome [GO:0005813]; cytoplasm [GO:0005737]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; proteasome complex [GO:0000502]; proteasome core complex [GO:0005839]; proteasome core complex, alpha-subunit complex [GO:0019773] | lipopolysaccharide binding [GO:0001530] | PF00227;PF10584; | 3.60.20.10; | Peptidase T1A family | PTM: Proteolytically cleaved from a C-terminal extension in the course of the conversion of the proteasome from its latent form into its active form. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P25786}. Nucleus {ECO:0000250|UniProtKB:P25786}. Note=Translocated from the cytoplasm into the nucleus following interaction with AKIRIN2, which bridges the proteasome with the nuclear import receptor IPO9. {ECO:0000250|UniProtKB:P25786}. | null | null | null | null | null | FUNCTION: Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus p... | Rattus norvegicus (Rat) |
P18424 | LCAT_RAT | MGLPGSPWQWVLLLLGLLLPPATSFWLLNVLFPPHTTPKAELSNHTRPVILVPGCMGNRLEAKLDKPNVVNWLCYRKTEDFFTIWLDFNMFLPLGVDCWIDNTRVVYNRSSGHMSNAPGVQIRVPGFGKTYSVEYLDDNKLAGYLHTLVQNLVNNGYVRDETVRAAPYDWRLAPRQQDEYYQKLAGLVEEMYAAYGKPVFLIGHSLGCLHVLHFLLRQPQSWKDHFIDGFISLGAPWGGSIKPMRILASGDNQGIPIMSNIKLREEQRITTTSPWMFPAHHVWPEDHVFISTPNFNYTGQDFERFFADLHFEEGWHMFLQ... | 2.3.1.43; 3.1.1.47 | null | aflatoxin metabolic process [GO:0046222]; 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 meta... | 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:14636062, ECO:0000269|PubMed:8820107, ECO:0000269|PubMed:9219904}. 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:1463... | 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... | Rattus norvegicus (Rat) |
P18428 | LBP_HUMAN | MGALARALPSILLALLLTSTPEALGANPGLVARITDKGLQYAAQEGLLALQSELLRITLPDFTGDLRIPHVGRGRYEFHSLNIHSCELLHSALRPVPGQGLSLSISDSSIRVQGRWKVRKSFFKLQGSFDVSVKGISISVNLLLGSESSGRPTVTASSCSSDIADVEVDMSGDLGWLLNLFHNQIESKFQKVLESRICEMIQKSVSSDLQPYLQTLPVTTEIDSFADIDYSLVEAPRATAQMLEVMFKGEIFHRNHRSPVTLLAAVMSLPEEHNKMVYFAISDYVFNTASLVYHEEGYLNFSITDDMIPPDSNIRLTTKS... | null | null | acute-phase response [GO:0006953]; cell surface pattern recognition receptor signaling pathway [GO:0002752]; cellular defense response [GO:0006968]; cellular response to lipopolysaccharide [GO:0071222]; cellular response to lipoteichoic acid [GO:0071223]; defense response to Gram-negative bacterium [GO:0050829]; defens... | cell surface [GO:0009986]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane [GO:0016020] | coreceptor activity [GO:0015026]; lipopeptide binding [GO:0071723]; lipopolysaccharide binding [GO:0001530]; lipoteichoic acid binding [GO:0070891]; signaling receptor binding [GO:0005102] | PF01273;PF02886; | null | BPI/LBP/Plunc superfamily, BPI/LBP family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2402637, ECO:0000269|PubMed:24120359, ECO:0000269|PubMed:7517398}. Cytoplasmic granule membrane {ECO:0000250|UniProtKB:P17213}. Note=Membrane-associated in polymorphonuclear Leukocytes (PMN) granules. {ECO:0000250|UniProtKB:P17213}. | null | null | null | null | null | FUNCTION: Plays a role in the innate immune response. Binds to the lipid A moiety of bacterial lipopolysaccharides (LPS), a glycolipid present in the outer membrane of all Gram-negative bacteria (PubMed:24120359, PubMed:7517398). Acts as an affinity enhancer for CD14, facilitating its association with LPS. Promotes the... | Homo sapiens (Human) |
P18431 | SGG_DROME | MSGRPRTSSFAEGNKQSPSLVLGGVKTCSRDGSKITTVVATPGQGTDRVQEVSYTDTKVIGNGSFGVVFQAKLCDTGELVAIKKVLQDRRFKNRELQIMRKLEHCNIVKLLYFFYSSGEKRDEVFLNLVLEYIPETVYKVARQYAKTKQTIPINFIRLYMYQLFRSLAYIHSLGICHRDIKPQNLLLDPETAVLKLCDFGSAKQLLHGEPNVSYICSRYYRAPELIFGAINYTTKIDVWSAGCVLAELLLGQPIFPGDSGVDQLVEVIKVLGTPTREQIREMNPNYTEFKFPQIKSHPWQKVFRIRTPTEAINLVSLLLE... | 2.7.11.1 | null | cell differentiation [GO:0030154]; chaeta development [GO:0022416]; chaeta morphogenesis [GO:0008407]; chitin-based larval cuticle pattern formation [GO:0035293]; circadian rhythm [GO:0007623]; entrainment of circadian clock [GO:0009649]; epithelial cell morphogenesis [GO:0003382]; establishment of epithelial cell plan... | axon [GO:0030424]; beta-catenin destruction complex [GO:0030877]; cell cortex [GO:0005938]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; female germline ring canal [GO:0035324]; fusome [GO:0045169]; mitotic spindle [GO:0072686]; neuromuscular junction [GO:0031594]; nucleoplasm [GO:0005654]; nu... | ATP binding [GO:0005524]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein serine/threonine/tyrosine kinase activity [GO:0004712] | PF00069; | 1.10.510.10; | Protein kinase superfamily, CMGC Ser/Thr protein kinase family, GSK-3 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cell cortex. Synapse. Cell projection, axon. Note=In syncytial embryos, detected at the centrosomes throughout the cell cycle, and in the mitotic spindle and pseudocleavage furrows invaginating from ... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Required for several developmental events such as syncytial blastoderm formation and embryonic segmentation. Is involved in transcriptional regulation. Required for arm phosphorylation. Wg signaling operates by inactivating the sgg repression of en autoactivation. Negatively controls the neuromuscular junctio... | Drosophila melanogaster (Fruit fly) |
P18432 | MLR_DROME | MADEKKKVKKKKTKEEGGTSETASEAASEAATPAPAATPAPAASATGSKRASGGSRGSRKSKRAGSSVFSVFSQKQIAEFKEAFQLMDADKDGIIGKNDLRAAFDSVGKIANDKELDAMLGEASGPINFTQLLTLFANRMATSGANDEDEVVIAAFKTFDNDGLIDGDKFREMLMNFGDKFTMKEVDDAYDQMVIDDKNQIDTAALIEMLTGKGEEEEEEAA | null | null | flight [GO:0060361]; locomotion [GO:0040011]; muscle system process [GO:0003012]; myofibril assembly [GO:0030239]; post-embryonic development [GO:0009791] | cytoplasm [GO:0005737]; myofibril [GO:0030016]; myosin II complex [GO:0016460] | calcium ion binding [GO:0005509]; myosin heavy chain binding [GO:0032036] | PF13405; | 1.10.238.10; | null | null | null | null | null | null | null | null | null | Drosophila melanogaster (Fruit fly) |
P18433 | PTPRA_HUMAN | MDSWFILVLLGSGLICVSANNATTVAPSVGITRLINSSTAEPVKEEAKTSNPTSSLTSLSVAPTFSPNITLGPTYLTTVNSSDSDNGTTRTASTNSIGITISPNGTWLPDNQFTDARTEPWEGNSSTAATTPETFPPSGNSDSKDRRDETPIIAVMVALSSLLVIVFIIIVLYMLRFKKYKQAGSHSNSFRLSNGRTEDVEPQSVPLLARSPSTNRKYPPLPVDKLEEEINRRMADDNKLFREEFNALPACPIQATCEAASKEENKEKNRYVNILPYDHSRVHLTPVEGVPDSDYINASFINGYQEKNKFIAAQGPKEET... | 3.1.3.48 | null | dephosphorylation [GO:0016311]; insulin receptor signaling pathway [GO:0008286]; integrin-mediated signaling pathway [GO:0007229]; modulation of chemical synaptic transmission [GO:0050804]; regulation of focal adhesion assembly [GO:0051893] | extracellular exosome [GO:0070062]; focal adhesion [GO:0005925]; membrane [GO:0016020]; plasma membrane [GO:0005886]; receptor complex [GO:0043235]; Schaffer collateral - CA1 synapse [GO:0098685]; synaptic membrane [GO:0097060] | protein tyrosine phosphatase activity [GO:0004725]; transmembrane receptor protein tyrosine phosphatase activity [GO:0005001] | PF00102; | 3.90.190.10; | Protein-tyrosine phosphatase family, Receptor class 4 subfamily | PTM: Integrin binding to extracellular matrix induces phosphorylation at Tyr-798 which induces PTPRA localization and recruitment of BCAR3, BCAR1 and CRK to focal adhesions. {ECO:0000269|PubMed:22801373}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255}; Single-pass type I membrane protein {ECO:0000255}. Cell junction, focal adhesion {ECO:0000250|UniProtKB:P18052}. Note=Localizes to focal adhesion sites following integrin engagement. {ECO:0000250|UniProtKB:P18052}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044}; | null | null | null | null | FUNCTION: Tyrosine protein phosphatase which is involved in integrin-mediated focal adhesion formation (By similarity). Following integrin engagement, specifically recruits BCAR3, BCAR1 and CRK to focal adhesions thereby promoting SRC-mediated phosphorylation of BRAC1 and the subsequent activation of PAK and small GTPa... | Homo sapiens (Human) |
P18434 | ATP4B_PIG | MAALQEKKSCSQRMEEFQRYCWNPDTGQMLGRTLSRWVWISLYYVAFYVVMSGIFALCIYVLMRTIDPYTPDYQDQLKSPGVTLRPDVYGEKGLDISYNVSDSTTWAGLAHTLHRFLAGYSPAAQEGSINCTSEKYFFQESFLAPNHTKFSCKFTADMLQNCSGRPDPTFGFAEGKPCFIIKMNRIVKFLPGNSTAPRVDCAFLDQPRDGPPLQVEYFPANGTYSLHYFPYYGKKAQPHYSNPLVAAKLLNVPRNRDVVIVCKILAEHVSFDNPHDPYEGKVEFKLKIQK | null | null | cell adhesion [GO:0007155]; intracellular potassium ion homeostasis [GO:0030007]; intracellular sodium ion homeostasis [GO:0006883]; potassium ion import across plasma membrane [GO:1990573]; potassium ion transmembrane transport [GO:0071805]; proton transmembrane transport [GO:1902600]; sodium ion export across plasma ... | apical plasma membrane [GO:0016324]; potassium:proton exchanging ATPase complex [GO:0005889]; sodium:potassium-exchanging ATPase complex [GO:0005890] | ATPase activator activity [GO:0001671] | PF00287; | 1.20.5.170;2.60.40.1660; | X(+)/potassium ATPases subunit beta family | PTM: N-glycosylation is necessary for assembly and functional expression of the pump at the plasma membrane. {ECO:0000250|UniProtKB:P18597}. | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:P20648}; Single-pass type II membrane protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:21224846}; Single-pass type II membrane protein {ECO:0000255}. Note=Localized in the apical canalicular membrane of parietal cells. {ECO:0000250|UniProtKB:P206... | null | null | null | null | null | FUNCTION: The beta subunit of the gastric H(+)/K(+) ATPase pump which transports H(+) ions in exchange for K(+) ions across the apical membrane of parietal cells. Plays a structural and regulatory role in the assembly and membrane targeting of a functionally active pump (By similarity). Within a transport cycle, the tr... | Sus scrofa (Pig) |
P18440 | ARY1_HUMAN | MDIEAYLERIGYKKSRNKLDLETLTDILQHQIRAVPFENLNIHCGDAMDLGLEAIFDQVVRRNRGGWCLQVNHLLYWALTTIGFETTMLGGYVYSTPAKKYSTGMIHLLLQVTIDGRNYIVDAGFGRSYQMWQPLELISGKDQPQVPCVFRLTEENGFWYLDQIRREQYIPNEEFLHSDLLEDSKYRKIYSFTLKPRTIEDFESMNTYLQTSPSSVFTSKSFCSLQTPDGVHCLVGFTLTHRRFNYKDNTDLIEFKTLSEEEIEKVLKNIFNISLQRKLVPKHGDRFFTI | 2.3.1.5 | null | xenobiotic metabolic process [GO:0006805] | cytosol [GO:0005829] | arylamine N-acetyltransferase activity [GO:0004060] | PF00797; | 3.30.2140.20; | Arylamine N-acetyltransferase family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + an arylamine = an N-acetylarylamine + CoA; Xref=Rhea:RHEA:16613, ChEBI:CHEBI:13790, ChEBI:CHEBI:50471, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288; EC=2.3.1.5; | null | null | null | null | FUNCTION: Participates in the detoxification of a plethora of hydrazine and arylamine drugs. Catalyzes the N- or O-acetylation of various arylamine and heterocyclic amine substrates and is able to bioactivate several known carcinogens. | Homo sapiens (Human) |
P18459 | TY3H_DROME | MMAVAAAQKNREMFAIKKSYSIENGYPSRRRSLVDDARFETLVVKQTKQTVLEEARSKANDDSLEDCIVQAQEHIPSEQDVELQDEHANLENLPLEEYVPVEEDVEFESVEQEQSESQSQEPEGNQQPTKNDYGLTEDEILLANAASESSDAEAAMQSAALVVRLKEGISSLGRILKAIETFHGTVQHVESRQSRVEGVDHDVLIKLDMTRGNLLQLIRSLRQSGSFSSMNLMADNNLNVKAPWFPKHASELDNCNHLMTKYEPDLDMNHPGFADKVYRQRRKEIAEIAFAYKYGDPIPFIDYSDVEVKTWRSVFKTVQD... | 1.14.16.2 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; | adult chitin-containing cuticle pigmentation [GO:0048085]; adult locomotory behavior [GO:0008344]; catecholamine metabolic process [GO:0006584]; courtship behavior [GO:0007619]; cuticle pigmentation [GO:0048067]; developmental pigmentation [GO:0048066]; dopamine biosynthetic process [GO:0042416]; dopamine biosynthetic ... | axon [GO:0030424]; cytoplasm [GO:0005737]; perikaryon [GO:0043204]; perinuclear region of cytoplasm [GO:0048471] | iron ion binding [GO:0005506]; tyrosine 3-monooxygenase activity [GO:0004511] | PF00351; | 1.10.800.10; | Biopterin-dependent aromatic amino acid hydroxylase family | null | SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:P24529}. Cell projection, axon {ECO:0000250|UniProtKB:P24529}. Note=Expressed in dopaminergic axons and axon terminals. {ECO:0000250|UniProtKB:P24529}. | CATALYTIC ACTIVITY: Reaction=(6R)-L-erythro-5,6,7,8-tetrahydrobiopterin + L-tyrosine + O2 = (4aS,6R)-4a-hydroxy-L-erythro-5,6,7,8-tetrahydrobiopterin + L-dopa; Xref=Rhea:RHEA:18201, ChEBI:CHEBI:15379, ChEBI:CHEBI:15642, ChEBI:CHEBI:57504, ChEBI:CHEBI:58315, ChEBI:CHEBI:59560; EC=1.14.16.2; | null | PATHWAY: Catecholamine biosynthesis; dopamine biosynthesis; dopamine from L-tyrosine: step 1/2. | null | null | FUNCTION: Plays an important role in the physiology of adrenergic neurons. | Drosophila melanogaster (Fruit fly) |
P18460 | FGFR3_CHICK | MRAAWGSVWCLCLAAAVGALPAARRRGAERSGGQAAEYLRSETAFLEELVFGSGDTIELSCNTQSSSVSVFWFKDGIGIAPSNRTHIGQKLLKIINVSYDDSGLYSCKPRHSNEVLGNFTVRVTDSPSSGDDEDDDDESEDTGVPFWTRPDKMEKKLLAVPAANTVRFRCPAGGNPTPTIYWLKNGKEFKGEHRIGGIKLRHQQWSLVMESVVPSDRGNYTCVVENKYGNIRHTYQLDVLERSPHRPILQAGLPANQTVVVGSNVEFHCKVYSDAQPHIQWLKHVEVNGSKYGPDGTPYVTVLKTAGVNTTDKELEILYL... | 2.7.10.1 | null | apoptotic process [GO:0006915]; cell differentiation [GO:0030154]; phosphorylation [GO:0016310]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of MAPK cascade [GO:0043410]; regulation of macromolecule metabolic process [GO:0060255] | plasma membrane [GO:0005886]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; fibroblast growth factor binding [GO:0017134]; fibroblast growth factor receptor activity [GO:0005007] | PF21165;PF07679;PF00047;PF13927;PF07714; | 6.10.250.1740;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 (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. | 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 cell proliferation, differentiation and apoptosis. Plays an essential role in the regulation of chondrocyte differentiation, proliferation and apoptosis, and is required ... | Gallus gallus (Chicken) |
P18461 | FGFR2_CHICK | MVSWDSGCLICLVVVTMAGLSLARPSFNLVVEDATLEPEEPPTKYQISQPDVHSALPGEPLELRCQLKDAVMISWTKDGVPLGPDNRTVIIGEYLQIKDASPRDSGLYACTAIRTLDSDTLYFIVNVTDALSSGDDEDDNDGSEDFVNDSNQMRAPYWTHTDKMEKRLHAVPAANTVKFRCPAMGNPTPTMRWLKNGKEFKQEHRIGGYKVRNQHWSLIMESVVPSDKGNYTCIVENQYGSINHTYHLDVVERSPHRPILQAGLPANASAVVGGDVEFVCKVYSDAQPHIQWIKHVERNGSKYGPDGLPYLQVLKAAGVN... | 2.7.10.1 | null | apoptotic process [GO:0006915]; phosphorylation [GO:0016310]; positive regulation of cell population proliferation [GO:0008284] | cytoplasmic vesicle [GO:0031410]; Golgi apparatus [GO:0005794]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; fibroblast growth factor binding [GO:0017134]; fibroblast growth factor receptor activity [GO:0005007] | PF07679;PF13927;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 (By similarity). {ECO:0000250}.; PTM: N-glycos... | SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein. Golgi apparatus {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Note=Detected on osteoblast plasma membrane lipid rafts. After ligand binding, the activated receptor is rapidly internalized and degraded (By similarity). {ECO:0000250}. | 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 cell proliferation, differentiation, migration and apoptosis, and in the regulation of embryonic development. Required for normal embryonic patterning, limb bud developme... | Gallus gallus (Chicken) |
P18467 | DOB_PANTR | MGSGWVPWVVALLVNLTRLDSSMTQGTDSPEDFVIQAKADCYFTNGTEKVQFVVRFIFNLEEYVRFDSDVGMFVALTKLGQPDAEQWNSRLDLLERSRQAVDGVCRHNYRLGAPFTVGRKVQPEVTVYPERTPLLHQHNLLHCSVTGFYPGDIKIRWFLNGQEERARVMSTGPIRNGDWTFQTVVMLEMTPELGHVYTCLVDHSSLLSPVSVEWRAQSEYSWKKMLSGIAAFLLGLIFLLVGIVIQLRAQKGYVRTQMSGNEVSRAVLLPQSC | null | null | adaptive immune response [GO:0002250]; antigen processing and presentation of exogenous peptide antigen via MHC class II [GO:0019886]; peptide antigen assembly with MHC class II protein complex [GO:0002503]; positive regulation of immune response [GO:0050778]; positive regulation of T cell activation [GO:0050870] | late endosome membrane [GO:0031902]; lysosomal membrane [GO:0005765]; MHC class II protein complex [GO:0042613] | MHC class II protein complex binding [GO:0023026]; peptide antigen binding [GO:0042605] | PF07654;PF00969; | 2.60.40.10; | MHC class II family | null | SUBCELLULAR LOCATION: Endosome membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Lysosome membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Complexes with HLA-DM molecule during intracellular transport and in endosomal/lysosomal compartments. Heterotetramerization ... | null | null | null | null | null | FUNCTION: Important modulator in the HLA class II restricted antigen presentation pathway by interaction with the HLA-DM molecule in B-cells. Modifies peptide exchange activity of HLA-DM. | Pan troglodytes (Chimpanzee) |
P18475 | TORSO_DROME | MLIFYAKYAFIFWFFVGSNQGEMLLMDKISHDKTLLNVTACTQNCLEKGQMDFRSCLKDCRINGTFPGALRKVQENYQMNMICRTESEIVFQIDWVQHSRGTEPAPNATYIIRVDAVKDDNKETALYLSDDNFLILPGLESNSTHNITALAMHGDGSYSLIAKDQTFATLIRGYQPSKMGAVNLLRFVPQPDDLHHIAAEIEWKPSAESNCYFDMVSYSTNSVNMDEPLEVQFRDRKKLYRHTVDNLEFDKQYHVGVRTVNIMNRLESDLQWLPIAVPSCLDWYPYNYTLCPPHKPENLTVTQKQYLPNILALNITWARP... | 2.7.10.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305}; | chorion-containing eggshell pattern formation [GO:0030381]; gastrulation [GO:0007369]; metamorphosis [GO:0007552]; negative phototaxis [GO:0046957]; negative regulation of hippo signaling [GO:0035331]; negative regulation of multicellular organism growth [GO:0040015]; peptidyl-tyrosine autophosphorylation [GO:0038083];... | plasma membrane [GO:0005886]; receptor complex [GO:0043235] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; transmembrane receptor protein tyrosine kinase activity [GO:0004714] | PF07714; | 1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family | PTM: May be auto-phosphorylated on tyrosine residues. {ECO:0000250|UniProtKB:D2IYS2}. | 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: Probable receptor tyrosine kinase which is required for determination of anterior and posterior terminal structures in the embryo (PubMed:2927509, PubMed:8423783). During postembryonic development, involved in the initiation of metamorphosis probably by inducing the production of ecdysone in response to proth... | Drosophila melanogaster (Fruit fly) |
P18479 | POLG_ZYMVC | MASIMIGSISVPIAKTEQCANTQVSNRANIVAPGHMATCPLPLKTHMYYRHESKKLMQSNKSIDILNNFFSTDEMKFRLTRNEMSKLKKGPSGRIVLRKPSKQRVFARIEQDEAARKEEAVFLEGNYDDSITNLARVLPPAVTHNVDVSLRSPFYKRTYKKERKKVAQKQIVQAPLNSLCTRVLKIARNKNIPVEMIGNKKTRHTLTFKRFRGCFVGKVSVAHEEGRMRHTEMSYEQFKWLLKAICQVTHTERIREEDIKPGCSGWVLGTNHTLTKRYSRLPHLVIRGRDDDGIVNALEQVLFYSEVDHSSSQPEVQFFQ... | 2.7.7.48; 3.4.-.-; 3.4.22.44; 3.4.22.45; 3.6.4.- | null | DNA-templated transcription [GO:0006351]; proteolysis [GO:0006508]; viral RNA genome replication [GO:0039694]; virus-mediated perturbation of host defense response [GO:0019049] | helical viral capsid [GO:0019029]; host cell cytoplasmic vesicle [GO:0044161]; host cell nucleus [GO:0042025] | ATP binding [GO:0005524]; cysteine-type endopeptidase activity [GO:0004197]; helicase activity [GO:0004386]; hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides [GO:0016818]; RNA binding [GO:0003723]; RNA-dependent RNA polymerase activity [GO:0003968]; serine-type peptidase activity [GO:0... | PF00270;PF00271;PF00863;PF00851;PF01577;PF00767;PF08440;PF13608;PF00680; | 3.30.70.270;3.90.70.150;3.40.50.300;2.40.10.10; | Potyviridae genome polyprotein family | PTM: [Viral genome-linked protein]: VPg is uridylylated by the polymerase and is covalently attached to the 5'-end of the genomic RNA. This uridylylated form acts as a nucleotide-peptide primer for the polymerase (By similarity). {ECO:0000250|UniProtKB:P09814}.; PTM: [Genome polyprotein]: Potyviral RNA is expressed as ... | SUBCELLULAR LOCATION: [6 kDa protein 1]: Host cytoplasmic vesicle. Note=Probably colocalizes with 6K2-induced vesicles associated with host chloroplasts. {ECO:0000250|UniProtKB:P13529}.; SUBCELLULAR LOCATION: [6 kDa protein 2]: Host cytoplasmic vesicle {ECO:0000250|UniProtKB:P09814}. Note=6K-induced vesicles associate ... | 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=Hydrolyz... | null | null | null | null | FUNCTION: [Helper component proteinase]: Required for aphid transmission and also has proteolytic activity. Only cleaves a Gly-Gly dipeptide at its own C-terminus. Interacts with virions and aphid stylets. Acts as a suppressor of RNA-mediated gene silencing, also known as post-transcriptional gene silencing (PTGS), a m... | Zucchini yellow mosaic virus (strain California) (ZYMV) |
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