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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P15202 | CATA_YEAST | MSKLGQEKNEVNYSDVREDRVVTNSTGNPINEPFVTQRIGEHGPLLLQDYNLIDSLAHFNRENIPQRNPHAHGSGAFGYFEVTDDITDICGSAMFSKIGKRTKCLTRFSTVGGDKGSADTVRDPRGFATKFYTEEGNLDWVYNNTPVFFIRDPSKFPHFIHTQKRNPQTNLRDADMFWDFLTTPENQVAIHQVMILFSDRGTPANYRSMHGYSGHTYKWSNKNGDWHYVQVHIKTDQGIKNLTIEEATKIAGSNPDYCQQDLFEAIQNGNYPSWTVYIQTMTERDAKKLPFSVFDLTKVWPQGQFPLRRVGKIVLNENPL... | 1.11.1.6 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000269|PubMed:9931255}; | hydrogen peroxide catabolic process [GO:0042744]; response to hydrogen peroxide [GO:0042542]; response to reactive oxygen species [GO:0000302] | cytoplasm [GO:0005737]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; peroxisomal matrix [GO:0005782]; peroxisome [GO:0005777] | 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 matrix {ECO:0000269|PubMed:1986244}. | 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: Catalyzes the degradation of hydrogen peroxide (H(2)O(2)) generated by peroxisomal oxidases to water and oxygen, thereby protecting cells from the toxic effects of hydrogen peroxide. {ECO:0000250|UniProtKB:P04040}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P15203 | TGFB3_PIG | MHLQRALVVLALLNFATVSLSMSTCTTLDFDHIKRKRVEAIRGQILSKLRLTSPPDPSMLANIPTQVLDLYNSTRELLEEVHGERGDDCTQENTESEYYAKEIYKFDMIQGLEEHNDLAVCPKGITSKIFRFNVSSVEKNETNLFRAEFRVLRMPNPSSKRSEQRIELFQILQPDEHIAKQRYIDGKNLPTRGAAEWLSFDVTDTVREWLLRRESNLGLEISIHCPCHTFQPNGDILENIQEVMEIKFKGVDSEDDPGRGDLGRLKKKKEHSPHLILMMIPPDRLDNPGLGAQRKKRALDTNYCFRNLEENCCVRPLYID... | null | null | cell-cell junction organization [GO:0045216]; detection of hypoxia [GO:0070483]; face morphogenesis [GO:0060325]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of macrophage cytokine production [GO:0010936]; positive regulation of cell division [GO:0051781]; positive regulation ... | extracellular matrix [GO:0031012]; extracellular space [GO:0005615] | cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; identical protein binding [GO:0042802]; transforming growth factor beta binding [GO:0050431]; type I transforming growth factor beta receptor binding [GO:0034713]; type II transforming growth factor beta receptor binding [GO:0005114]; type III transfo... | PF00019;PF00688; | 2.60.120.970;2.10.90.10; | TGF-beta family | PTM: Transforming growth factor beta-3 proprotein: The precursor proprotein is cleaved in the Golgi apparatus to form Transforming growth factor beta-3 (TGF-beta-3) and Latency-associated peptide (LAP) chains, which remain non-covalently linked, rendering TGF-beta-3 inactive. {ECO:0000250|UniProtKB:P01137}. | SUBCELLULAR LOCATION: [Latency-associated peptide]: Secreted, extracellular space, extracellular matrix {ECO:0000250|UniProtKB:P01137}.; SUBCELLULAR LOCATION: [Transforming growth factor beta-3]: Secreted {ECO:0000250|UniProtKB:P01137}. | null | null | null | null | null | FUNCTION: Transforming growth factor beta-3 proprotein: Precursor of the Latency-associated peptide (LAP) and Transforming growth factor beta-3 (TGF-beta-3) chains, which constitute the regulatory and active subunit of TGF-beta-3, respectively. {ECO:0000250|UniProtKB:P01137, ECO:0000250|UniProtKB:P04202}.; FUNCTION: [L... | Sus scrofa (Pig) |
P15204 | THAA_XENLA | MDQNLSGLDCLSEPDEKRWPDGKRKRKNSQCMGKSGMSGDSLVSLPSAGYIPSYLDKDEPCVVCSDKATGYHYRCITCEGCKGFFRRTIQKNLHPSYSCKYDGCCIIDKITRNQCQLCRFKKCIAVGMAMDLVLDDSKRVAKRKLIEENRQRRRKEEMIKTLQQRPEPSSEEWELIRIVTEAHRSTNAQGSHWKQRRKFLPEDIGQSPMASMPDGDKVDLEAFSEFTKIITPAITRVVDFAKKLPMFSELTCEDQIILLKGCCMEIMSLRAAVRYDPDSETLTLSGEMAVKREQLKNGGLGVVSDAIFDLGRSLAAFNLD... | 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]; nuclear thyroid hormone receptor binding [GO:0046966]; protein heterodimerization activity [GO:0046982]; protein homodimerization activity [GO:0042803]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:000... | 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:2587261}. | Xenopus laevis (African clawed frog) |
P15205 | MAP1B_RAT | MATVVVEATEPEPSGSIGNPAATTSPSLSHRFLDSKFYLLVVVGETVTEEHLRRAIGNIELGIRSWDTNLIECNLDQELKLFVSRHSARFSPEVPGQKILHHRSDVLETVVLINPSDEAVSTEVRLMITDAARHKLLVLTGQCFENTGELILQSGSFSFQNFIEIFTDQEIGELLSTTHPANKASLTLFCPEEGDWKNSNLDRHNLQDFINIKLNSASILPEMEGLSEFTEYLSESVEVPSPFDILEPPTSGGFLKLSKPCCYIFPGGRGDSALFAVNGFNMLINGGSERKSCFWKLIRHLDRVDSILLTHIGDDNLPGI... | null | null | axon extension [GO:0048675]; axonogenesis [GO:0007409]; cellular response to growth factor stimulus [GO:0071363]; cellular response to peptide hormone stimulus [GO:0071375]; dendrite development [GO:0016358]; developmental maturation [GO:0021700]; establishment of monopolar cell polarity [GO:0061162]; induction of syna... | apical dendrite [GO:0097440]; axon [GO:0030424]; basal dendrite [GO:0097441]; cytosol [GO:0005829]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; growth cone [GO:0030426]; hippocampal mossy fiber [GO:0097457]; microtubule [GO:0005874]; microtubule associated complex [GO:0005875]; neuronal cell body [GO:0043025];... | actin binding [GO:0003779]; microtubule binding [GO:0008017]; phospholipid binding [GO:0005543]; protein-containing complex binding [GO:0044877] | PF00414; | null | MAP1 family | PTM: LC1 is coexpressed with MAP1B. It is a polypeptide generated from MAP1B by proteolytic processing. It is free to associate with both MAP1A and MAP1B. It interacts with the N-terminal region of MAP1B (By similarity). {ECO:0000250}.; PTM: S-nitrosylation at Cys-2457 enhances interaction with microtubules, and may ac... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}. Cytoplasm {ECO:0000250}. Synapse {ECO:0000250}. Cell projection, dendritic spine {ECO:0000250}. Note=Colocalizes with DAPK1 in the microtubules and cortical actin fibers. {ECO:0000250}.; SUBCELLULAR LOCATION: [MAP1 light chain LC1]: Cytoplasm {ECO:0000250|Uni... | null | null | null | null | null | FUNCTION: Required for proper microtubule dynamics. Plays a role in the cytoskeletal changes that accompany neuronal differentiation and neurite extension (By similarity). Possibly MAP1B binds to at least two tubulin subunits in the polymer, and this bridging of subunits might be involved in nucleating microtubule poly... | Rattus norvegicus (Rat) |
P15207 | ANDR_RAT | MEVQLGLGRVYPRPPSKTYRGAFQNLFQSVREAIQNPGPRHPEAASIAPPGACLQQRQETSPRRRRRQQHPEDGSPQAHIRGTTGYLALEEEQQPSQQQSASEGHPESGCLPEPGAATAPGKGLPQQPPAPPDQDDSAAPSTLSLLGPTFPGLSSCSADIKDILSEAGTMQLLQQQQQQQQQQQQQQQQQQQQQQEVISEGSSSVRAREATGAPSSSKDSYLGGNSTISDSAKELCKAVSVSMGLGVEALEHLSPGEQLRGDCMYASLLGGPPAVRPTPCAPLAECKGLSLDEGPGKGTEETAEYSSFKGGYAKGLEGES... | null | null | activation of prostate induction by androgen receptor signaling pathway [GO:0060520]; androgen receptor signaling pathway [GO:0030521]; animal organ formation [GO:0048645]; cellular response to estrogen stimulus [GO:0071391]; cellular response to follicle-stimulating hormone stimulus [GO:0071372]; cellular response to ... | axon [GO:0030424]; chromatin [GO:0000785]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; nuclear speck [GO:0016607]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991] | androgen binding [GO:0005497]; ATPase binding [GO:0051117]; beta-catenin binding [GO:0008013]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; enzyme binding [GO:00198... | PF02166;PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family, NR3 subfamily | PTM: Phosphorylated in prostate cancer cells in response to several growth factors including EGF. Phosphorylation is induced by c-Src kinase (CSK). Tyr-517 is one of the major phosphorylation sites and an increase in phosphorylation and Src kinase activity is associated with prostate cancer progression (By similarity).... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:9725910}. Cytoplasm {ECO:0000250|UniProtKB:P10275}. Note=Detected at the promoter of target genes. Predominantly cytoplasmic in unligated form but translocates to the nucleus upon ligand-binding. Can also translocate to the nucleus in unligated form in the presence of R... | null | null | null | null | null | FUNCTION: Steroid hormone receptors are ligand-activated transcription factors that regulate eukaryotic gene expression and affect cellular proliferation and differentiation in target tissues. Transcription factor activity is modulated by bound coactivator and corepressor proteins like ZBTB7A that recruits NCOR1 and NC... | Rattus norvegicus (Rat) |
P15208 | INSR_MOUSE | MGFGRGCETTAVPLLVAVAALLVGTAGHLYPGEVCPGMDIRNNLTRLHELENCSVIEGHLQILLMFKTRPEDFRDLSFPKLIMITDYLLLFRVYGLESLKDLFPNLTVIRGSRLFFNYALVIFEMVHLKELGLYNLMNITRGSVRIEKNNELCYLATIDWSRILDSVEDNYIVLNKDDNEECGDVCPGTAKGKTNCPATVINGQFVERCWTHSHCQKVCPTICKSHGCTAEGLCCHKECLGNCSEPDDPTKCVACRNFYLDGQCVETCPPPYYHFQDWRCVNFSFCQDLHFKCRNSRKPGCHQYVIHNNKCIPECPSGYT... | 2.7.10.1 | null | adrenal gland development [GO:0030325]; amyloid-beta clearance [GO:0097242]; animal organ morphogenesis [GO:0009887]; cellular response to growth factor stimulus [GO:0071363]; dendritic spine maintenance [GO:0097062]; epidermis development [GO:0008544]; exocrine pancreas development [GO:0031017]; G protein-coupled rece... | axon [GO:0030424]; caveola [GO:0005901]; dendrite membrane [GO:0032590]; endosome [GO:0005768]; external side of plasma membrane [GO:0009897]; insulin receptor complex [GO:0005899]; late endosome [GO:0005770]; lysosome [GO:0005764]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; neuronal cell body membrane [GO... | 3-phosphoinositide-dependent protein kinase binding [GO:0043423]; amyloid-beta binding [GO:0001540]; ATP binding [GO:0005524]; cargo receptor activity [GO:0038024]; GTP binding [GO:0005525]; insulin binding [GO:0043559]; insulin receptor activity [GO:0005009]; insulin receptor substrate binding [GO:0043560]; insulin-li... | PF00041;PF00757;PF17870;PF07714;PF01030; | 2.60.40.10;3.80.20.20;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, Insulin receptor subfamily | PTM: After being transported from the endoplasmic reticulum to the Golgi apparatus, the single glycosylated precursor is further glycosylated and then cleaved, followed by its transport to the plasma membrane. {ECO:0000250|UniProtKB:P06213}.; PTM: Autophosphorylated on tyrosine residues in response to insulin (By simil... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27322061}; Single-pass type I membrane protein {ECO:0000305}. Recycling endosome membrane {ECO:0000269|PubMed:27322061}. Late endosome {ECO:0000269|PubMed:27322061}. Lysosome {ECO:0000305|PubMed:27322061}. Note=Binding of insulin to INSR induces internalization an... | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Receptor tyrosine kinase which mediates the pleiotropic actions of insulin. Binding of insulin leads to phosphorylation of several intracellular substrates, including, insulin receptor substrates (IRS1, 2, 3, 4), SHC, GAB1, CBL and other signaling intermediates. Each of these phosphorylated proteins serve as ... | Mus musculus (Mouse) |
P15209 | NTRK2_MOUSE | MSPWLKWHGPAMARLWGLCLLVLGFWRASLACPTSCKCSSARIWCTEPSPGIVAFPRLEPNSVDPENITEILIANQKRLEIINEDDVEAYVGLRNLTIVDSGLKFVAYKAFLKNSNLRHINFTRNKLTSLSRRHFRHLDLSDLILTGNPFTCSCDIMWLKTLQETKSSPDTQDLYCLNESSKNMPLANLQIPNCGLPSARLAAPNLTVEEGKSVTLSCSVGGDPLPTLYWDVGNLVSKHMNETSHTQGSLRITNISSDDSGKQISCVAENLVGEDQDSVNLTVHFAPTITFLESPTSDHHWCIPFTVRGNPKPALQWFYN... | 2.7.10.1 | null | brain-derived neurotrophic factor receptor signaling pathway [GO:0031547]; calcium-mediated signaling using intracellular calcium source [GO:0035584]; cellular response to amino acid stimulus [GO:0071230]; cellular response to brain-derived neurotrophic factor stimulus [GO:1990416]; central nervous system neuron develo... | axon [GO:0030424]; axon terminus [GO:0043679]; cell surface [GO:0009986]; cytosol [GO:0005829]; dendrite [GO:0030425]; dendritic spine [GO:0043197]; early endosome [GO:0005769]; early endosome membrane [GO:0031901]; endosome [GO:0005768]; excitatory synapse [GO:0060076]; glutamatergic synapse [GO:0098978]; growth cone ... | ATP binding [GO:0005524]; brain-derived neurotrophic factor binding [GO:0048403]; brain-derived neurotrophic factor receptor activity [GO:0060175]; neurotrophin binding [GO:0043121]; neurotrophin receptor activity [GO:0005030]; protease binding [GO:0002020]; protein homodimerization activity [GO:0042803]; receptor tyro... | PF07679;PF13855;PF16920;PF07714; | 2.60.40.10;3.80.10.10;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, Insulin receptor subfamily | PTM: Phosphorylated. Undergoes ligand-mediated autophosphorylation that is required for interaction with SHC1 and PLCG1 and other downstream effectors (PubMed:27457814). Some isoforms are not phosphorylated (By similarity). {ECO:0000250, ECO:0000269|PubMed:27457814}.; PTM: Ubiquitinated. Undergoes polyubiquitination up... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14581459}; Single-pass type I membrane protein {ECO:0000269|PubMed:14581459}. Endosome membrane {ECO:0000269|PubMed:14581459}; Single-pass type I membrane protein {ECO:0000269|PubMed:14581459}. Early endosome membrane {ECO:0000269|PubMed:21849472}. Cell projection... | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.1; Evidence={ECO:0000255|PROSITE-ProRule:PRU100... | null | null | null | null | FUNCTION: Receptor tyrosine kinase involved in the development and the maturation of the central and the peripheral nervous systems through regulation of neuron survival, proliferation, migration, differentiation, and synapse formation and plasticity. Receptor for BDNF/brain-derived neurotrophic factor and NTF4/neurotr... | Mus musculus (Mouse) |
P15215 | LAMC1_DROME | MKRSRWSHSGSSTARLLLIGVLFASCSTAILGAQRPPINSAGGHELRGTTFMPALECYDPYGRPQKCLPEFINAAYQLQIESTNTCGEQNDNHFCIQTMNQNHKNCEFCKYNDHNPSFLTDLHDPQSPTWWQSETMFEGIQHPNYVNLTLHLGKSYDITYVRILFRSPRPESFTIYKRTSESGPWIPYQFYSATCRDTYSLPDSRAIRKGEGEAHALCTSEYSDISPLRDGEIAFSTLEGRPSGINFERSGELQEWVTATDIRITLDRLNTFGDELFGDSQVLKSYFYAISDIAVGARCKCNGHASKCVPSTGMHGERTL... | null | null | animal organ morphogenesis [GO:0009887]; axon guidance [GO:0007411]; basement membrane assembly [GO:0070831]; basement membrane organization [GO:0071711]; cell adhesion mediated by integrin [GO:0033627]; endodermal digestive tract morphogenesis [GO:0061031]; extracellular matrix assembly [GO:0085029]; midgut developmen... | basement membrane [GO:0005604]; extracellular region [GO:0005576] | null | PF00052;PF00053;PF00055; | 2.60.120.260;2.10.25.10; | null | null | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix, basement membrane. Note=Major component. | null | null | null | null | null | FUNCTION: Binding to cells via a high affinity receptor, laminin is thought to mediate the attachment, migration and organization of cells into tissues during embryonic development by interacting with other extracellular matrix components. | Drosophila melanogaster (Fruit fly) |
P15226 | SCX1_TITSE | MKGMILFISCLLLIGIVVECKEGYLMDHEGCKLSCFIRPSGYCGRECGIKKGSSGYCAWPACYCYGLPNWVKVWDRATNKCGKK | null | null | defense response to fungus [GO:0050832]; killing of cells of another organism [GO:0031640] | extracellular region [GO:0005576] | sodium channel inhibitor activity [GO:0019871]; toxin activity [GO:0090729] | PF00537; | 3.30.30.10; | Long (4 C-C) scorpion toxin superfamily, Sodium channel inhibitor family | PTM: C-terminal amidation is important for high activity. {ECO:0000269|PubMed:24560880, ECO:0000269|PubMed:24989851}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1926167, ECO:0000269|PubMed:1993690, ECO:0000269|PubMed:25199494, ECO:0000269|PubMed:4052021, ECO:0000269|PubMed:6477555, ECO:0000269|Ref.7}. | null | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5-7.5. Is almost completely inactivated at pH 11.5. {ECO:0000269|PubMed:3651476}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 25-60 degrees Celsius. All temperatures tested are optimal. {ECO:0000269|PubMed:3651476}; | FUNCTION: Voltage-gated sodium channels (Nav) gating-modifier. Acts both as alpha- and beta-toxin, since it affects not only activation but also inactivation of Nav channels (Probable) (PubMed:25862296). Binds to Nav domain DII and impairs the four Nav channel voltage sensors movements (PubMed:17698594, PubMed:19005548... | Tityus serrulatus (Brazilian scorpion) |
P15244 | CEO2_LACLL | MKIGLVKANFPGERRVPLLPKDIKDFKNEILVEEGFGKFLDIDDQEYSDKGCHILSRAEVFAESEAIFSLKLIQPTDYYHLREGQMIIGWTHPFGSGQSFMKEQALPKKLIVVDLDSNSPCIYYENEIFESGIPKGLLYKNSFYAGYAGVLDALLQYGLIPTEETKIAILGSGNVAQGAFSSISKYSSNIRMYYRKTMSIFKENYTKYDIIINGIEIGKDDDPILSFSEQKSLKKGTLIIDVAADAGNTIEGSHFTSIDAPIYENAGKYYYVVPNTPSLIYRNVSQELSKILSENIFRKDCSRFIEKVKPLNK | 1.5.1.24 | null | alanine catabolic process [GO:0006524]; ornithine metabolic process [GO:0006591] | plasma membrane [GO:0005886] | alanine dehydrogenase activity [GO:0000286]; N5-(carboxyethyl)ornithine synthase activity [GO:0047126] | PF01262;PF05222; | 3.40.50.720; | AlaDH/PNT family, CEOS subfamily | null | null | CATALYTIC ACTIVITY: Reaction=H2O + N(5)-[1(S)-1-carboxyethyl]-L-ornithine + NADP(+) = H(+) + L-ornithine + NADPH + pyruvate; Xref=Rhea:RHEA:18661, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:46911, ChEBI:CHEBI:57783, ChEBI:CHEBI:57889, ChEBI:CHEBI:58349; EC=1.5.1.24; Evidence={ECO:0000269|PubMe... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.3 mM for L-ornithine {ECO:0000269|PubMed:2498334}; KM=18.2 mM for L-lysine {ECO:0000269|PubMed:2498334}; KM=150 uM for pyruvate {ECO:0000269|PubMed:2498334}; KM=6.6 uM for NADPH {ECO:0000269|PubMed:2498334}; Vmax=7.9 umol/min/mg enzyme with L-ornithine as substra... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.0. Active over a broad pH range of 6.5-9.0. {ECO:0000269|PubMed:2498334}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Stable to heating at 50 degrees Celsius for 10 minutes. Rapidly inactivated by heating at 60 degrees Celsius. {ECO:0000269|PubMed:2498334}; | FUNCTION: Catalyzes the NADPH-dependent reductive condensation between pyruvic acid and the side chain amino group of L-ornithine to form N(5)-(L-1-carboxyethyl)-L-ornithine. To a lesser extent, can also use L-lysine as substrate (yielding N(6)-(L-1-carboxyethyl)-L-lysine). NADH cannot replace NADPH in the condensation... | Lactococcus lactis subsp. lactis (Streptococcus lactis) |
P15245 | PHHY_CUTCT | MTKYSESYCDVLIVGAGPAGLMAARVLSEYVRQKPDLKVRIIDKRSTKVYNGQADGLQCRTLESLKNLGLADKILSEANDMSTIALYNPDENGHIRRTDRIPDTLPGISRYHQVVLHQGRIERHILDSIAEISDTRIKVERPLIPEKMEIDSSKAEDPEAYPVTMTLRYMSDHESTPLQFGHKTENSLFHSNLQTQEEEDANYRLPEGKEAGEIETVHCKYVIGCDGGHSWVRRTLGFEMIGEQTDYIWGVLDAVPASNFPDIRSPCAIHSAESGSIMIIPRENNLVRFYVQLQARAEKGGRVDRTKFTPEVVIANAKKI... | 1.14.13.7 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:12925790, ECO:0000269|PubMed:4146224, ECO:0000269|PubMed:9634698}; | phenol-containing compound catabolic process [GO:0019336] | null | FAD binding [GO:0071949]; phenol 2-monooxygenase activity [GO:0018662] | PF01494;PF07976; | 3.40.30.20;3.30.9.10;3.50.50.60; | PheA/TfdB FAD monooxygenase family | null | null | CATALYTIC ACTIVITY: Reaction=H(+) + NADPH + O2 + phenol = catechol + H2O + NADP(+); Xref=Rhea:RHEA:17061, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:15882, ChEBI:CHEBI:18135, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; EC=1.14.13.7; Evidence={ECO:0000269|PubMed:11591156, ECO:0000269|PubMed:1429434, ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=18 uM for phenol {ECO:0000269|PubMed:4146224}; KM=71 uM for NADPH {ECO:0000269|PubMed:4146224}; KM=53 uM for O(2) {ECO:0000269|PubMed:4146224}; | PATHWAY: Aromatic compound metabolism; phenol degradation. {ECO:0000269|PubMed:1429434}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.2-7.6. {ECO:0000269|PubMed:3203745, ECO:0000269|PubMed:4146224}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 30 degrees Celsius. {ECO:0000269|PubMed:3203745}; | FUNCTION: Hydroxylates phenol to catechol (PubMed:11591156, PubMed:1429434, PubMed:2022646, PubMed:3203745, PubMed:4146224, PubMed:7851397, PubMed:7858421). Phenol is the best substrate, but the enzyme also accepts isomeric diphenols, hydroxyl-, amino-, halogen- or methyl-substituted phenols and, to a lesser degree, cr... | Cutaneotrichosporon cutaneum (Yeast) (Trichosporon cutaneum) |
P15247 | IL9_MOUSE | MLVTYILASVLLFSSVLGQRCSTTWGIRDTNYLIENLKDDPPSKCSCSGNVTSCLCLSVPTDDCTTPCYREGLLQLTNATQKSRLLPVFHRVKRIVEVLKNITCPSFSCEKPCNQTMAGNTLSFLKSLLGTFQKTEMQRQKSRP | null | null | B cell differentiation [GO:0030183]; B cell proliferation [GO:0042100]; immunoglobulin mediated immune response [GO:0016064]; positive regulation of cell growth [GO:0030307]; positive regulation of interleukin-5 production [GO:0032754]; regulation of peptidyl-tyrosine phosphorylation [GO:0050730]; regulation of recepto... | extracellular space [GO:0005615] | cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; interleukin-9 receptor binding [GO:0005140] | null | null | IL-7/IL-9 family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Multifunctional cytokine secreted mainly by T-helper 2 lymphocytes and also mast cells or NKT cells that plays important roles in the immune response against parasites (PubMed:11070175, PubMed:19433802). Affects intestinal epithelial permeability and adaptive immunity (PubMed:12704113). In addition, induces t... | Mus musculus (Mouse) |
P15248 | IL9_HUMAN | MLLAMVLTSALLLCSVAGQGCPTLAGILDINFLINKMQEDPASKCHCSANVTSCLCLGIPSDNCTRPCFSERLSQMTNTTMQTRYPLIFSRVKKSVEVLKNNKCPYFSCEQPCNQTTAGNALTFLKSLLEIFQKEKMRGMRGKI | null | null | B cell differentiation [GO:0030183]; B cell proliferation [GO:0042100]; immunoglobulin mediated immune response [GO:0016064]; inflammatory response [GO:0006954]; positive regulation of cell growth [GO:0030307]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of interleukin-5 produ... | extracellular region [GO:0005576]; extracellular space [GO:0005615] | cytokine activity [GO:0005125]; growth factor activity [GO:0008083]; interleukin-9 receptor binding [GO:0005140] | null | null | IL-7/IL-9 family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Multifunctional cytokine secreted mainly by T-helper 2 lymphocytes and also mast cells or NKT cells that plays important roles in the immune response against parasites (PubMed:29742432). Affects intestinal epithelial permeability and adaptive immunity (PubMed:29742432). In addition, induces the differentiatio... | Homo sapiens (Human) |
P15253 | CALR_RABIT | MLLPVPLLLGLLGLAAAEPVVYFKEQFLDGDGWTERWIESKHKSDFGKFVLSSGKFYGDQEKDKGLQTSQDARFYALSARFEPFSNKGQPLVVQFTVKHEQNIDCGGGYVKLFPAGLDQKDMHGDSEYNIMFGPDICGPGTKKVHVIFNYKGKNVLINKDIRCKDDEFTHLYTLIVRPDNTYEVKIDNSQVESGSLEDDWDFLPPKKIKDPDASKPEDWDERAKIDDPTDSKPEDWDKPEHIPDPDAKKPEDWDEEMDGEWEPPVIQNPEYKGEWKPRQIDNPDYKGTWIHPEIDNPEYSPDANIYAYDSFAVLGLDLWQ... | null | null | protein folding [GO:0006457]; protein stabilization [GO:0050821] | cell surface [GO:0009986]; cortical granule [GO:0060473]; cytolytic granule [GO:0044194]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; extracellular region [GO:0005576]; sarcoplasmic reticulum [GO:0016529]; sarcoplasmic reticulum lumen [GO:0033018] | calcium ion binding [GO:0005509]; carbohydrate binding [GO:0030246]; unfolded protein binding [GO:0051082] | PF00262; | 2.60.120.200;2.10.250.10; | Calreticulin family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:P27797}. 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 (PubMed:10581245). This lectin interacts transiently with almost all of the monoglucosylated glycoproteins that are synthesized in the ER. Interacts wi... | Oryctolagus cuniculus (Rabbit) |
P15254 | PUR4_ECOLI | MMEILRGSPALSAFRINKLLARFQAARLPVHNIYAEYVHFADLNAPLNDDEHAQLERLLKYGPALASHAPQGKLLLVTPRPGTISPWSSKATDIAHNCGLQQVNRLERGVAYYIEAGTLTNEQWQQVTAELHDRMMETVFFALDDAEQLFAHHQPTPVTSVDLLGQGRQALIDANLRLGLALAEDEIDYLQDAFTKLGRNPNDIELYMFAQANSEHCRHKIFNADWVIDGEQQPKSLFKMIKNTFETTPDHVLSAYKDNAAVMEGSEVGRYFADHETGRYDFHQEPAHILMKVETHNHPTAISPWPGAATGSGGEIRDEG... | 6.3.5.3 | null | 'de novo' IMP biosynthetic process [GO:0006189]; glutamine metabolic process [GO:0006541]; purine nucleotide biosynthetic process [GO:0006164] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; metal ion binding [GO:0046872]; phosphoribosylformylglycinamidine synthase activity [GO:0004642] | PF02769;PF18072;PF18076;PF13507; | 3.40.50.880;1.10.8.750;3.90.650.10;3.30.1330.10; | FGAMS family | PTM: Both N-terminus methionine truncation and retention have been observed for this protein. {ECO:0000269|PubMed:2659070}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00419, ECO:0000269|PubMed:2659070}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O + L-glutamine + N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + ADP + H(+) + L-glutamate + phosphate; Xref=Rhea:RHEA:17129, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:4... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=64 uM for glutamine (at pH 7.25 and 37 degrees Celsius) {ECO:0000269|PubMed:2659070}; KM=51 uM for ATP (at pH 7.25 and 37 degrees Celsius) {ECO:0000269|PubMed:2659070}; KM=30 uM for FGAR (formylglycinamide ribonucleotide at pH 7.25 and 37 degrees Celsius) {ECO:0000... | PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00419}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.2 with only 50% of this activity retains at pH 6.2 or 8.0. {ECO:0000269|PubMed:2659070}; | null | FUNCTION: Phosphoribosylformylglycinamidine synthase involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. {ECO:0000255|HAMAP-Rule:MF_00419, ECO:0000269|PubMed:265907... | Escherichia coli (strain K12) |
P15257 | HNF1A_RAT | MVSKLSQLQTELLAALLESGLSKEALIQALGEPGPYLMVGDGPLDKGESCGGTRGDLTELPNGLGETRGSEDDTDDDGEDFAPPILKELENLSPEEAAHQKAVVESLLQEDPWRVAKMVKSYLQQHNIPQREVVDTTGLNQSHLSQHLNKGTPMKTQKRAALYTWYVRKQREVAQQFTHAGQGGLIEEPTGDELPTKKGRRNRFKWGPASQQILFQAYERQKNPSKEERETLVEECNRAECIQRGVSPSQAQGLGSNLVTEVRVYNWFANRRKEEAFRHKLAMDTYNGPPPGPGPGPALPAHSSPGLPTTTLSPSKVHGV... | null | null | apoptotic nuclear changes [GO:0030262]; bile acid and bile salt transport [GO:0015721]; bile acid biosynthetic process [GO:0006699]; blastocyst development [GO:0001824]; bone resorption [GO:0045453]; cellular response to glucose stimulus [GO:0071333]; cellular response to leucine [GO:0071233]; cellular response to rapa... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; photoreceptor outer segment [GO:0001750]; pronucleus [GO:0045120]; protein-containing complex [GO:0032991]; transcription regulator complex [GO:0005667] | chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; double-stranded DNA binding [GO:000... | PF04814;PF04813;PF04812; | 1.10.10.60;1.10.260.40; | HNF1 homeobox family | PTM: Ubiquitinated in s SPOP-dependent manner; leading to prteasomal degradation. {ECO:0000250|UniProtKB:P20823}. | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Transcriptional activator that regulates the tissue specific expression of multiple genes, especially in pancreatic islet cells and in liver (By similarity). Binds to the inverted palindrome 5'-GTTAATNATTAAC-3' (By similarity). Activates the transcription of CYP1A2, CYP2E1 and CYP3A11 (By similarity). {ECO:00... | Rattus norvegicus (Rat) |
P15259 | PGAM2_HUMAN | MATHRLVMVRHGESTWNQENRFCGWFDAELSEKGTEEAKRGAKAIKDAKMEFDICYTSVLKRAIRTLWAILDGTDQMWLPVVRTWRLNERHYGGLTGLNKAETAAKHGEEQVKIWRRSFDIPPPPMDEKHPYYNSISKERRYAGLKPGELPTCESLKDTIARALPFWNEEIVPQIKAGKRVLIAAHGNSLRGIVKHLEGMSDQAIMELNLPTGIPIVYELNKELKPTKPMQFLGDEETVRKAMEAVAAQGKAK | 5.4.2.11; 5.4.2.4 | null | canonical glycolysis [GO:0061621]; gluconeogenesis [GO:0006094]; glycolytic process [GO:0006096]; Notch signaling pathway [GO:0007219]; response to mercury ion [GO:0046689]; spermatogenesis [GO:0007283]; striated muscle contraction [GO:0006941] | cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleus [GO:0005634] | 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity [GO:0046538]; bisphosphoglycerate mutase activity [GO:0004082]; hydrolase activity [GO:0016787]; identical protein binding [GO:0042802]; phosphoglycerate mutase activity [GO:0004619] | PF00300; | 3.40.50.1240; | Phosphoglycerate mutase family, BPG-dependent PGAM subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate; Xref=Rhea:RHEA:15901, ChEBI:CHEBI:58272, ChEBI:CHEBI:58289; EC=5.4.2.11; Evidence={ECO:0000250|UniProtKB:P18669}; CATALYTIC ACTIVITY: Reaction=(2R)-3-phospho-glyceroyl phosphate = (2R)-2,3-bisphosphoglycerate + H(+); Xref=Rhea:RHEA:17765, C... | null | null | null | null | FUNCTION: Interconversion of 3- and 2-phosphoglycerate with 2,3-bisphosphoglycerate as the primer of the reaction. Can also catalyze the reaction of EC 5.4.2.4 (synthase), but with a reduced activity. | Homo sapiens (Human) |
P15260 | INGR1_HUMAN | MALLFLLPLVMQGVSRAEMGTADLGPSSVPTPTNVTIESYNMNPIVYWEYQIMPQVPVFTVEVKNYGVKNSEWIDACINISHHYCNISDHVGDPSNSLWVRVKARVGQKESAYAKSEEFAVCRDGKIGPPKLDIRKEEKQIMIDIFHPSVFVNGDEQEVDYDPETTCYIRVYNVYVRMNGSEIQYKILTQKEDDCDEIQCQLAIPVSSLNSQYCVSAEGVLHVWGVTTEKSKEVCITIFNSSIKGSLWIPVVAALLLFLVLSLVFICFYIKKINPLKEKSIILPKSLISVVRSATLETKPESKYVSLITSYQPFSLEKEV... | null | null | astrocyte activation [GO:0048143]; cellular response to virus [GO:0098586]; cytokine-mediated signaling pathway [GO:0019221]; microglial cell activation [GO:0001774]; negative regulation of amyloid-beta clearance [GO:1900222]; positive regulation of amyloid-beta formation [GO:1902004]; positive regulation of gene expre... | membrane [GO:0016020]; plasma membrane [GO:0005886] | cytokine binding [GO:0019955]; cytokine receptor activity [GO:0004896]; type II interferon receptor activity [GO:0004906] | PF07140;PF20634;PF01108; | 2.60.40.10; | Type II cytokine receptor family | PTM: Phosphorylated at Ser/Thr residues. Phosphorylation of Tyr-457 is required for IFNG receptor signal transduction (PubMed:8156998). Influenza virus infection leads to phosphorylation in a CSNK1A1-dependent manner (PubMed:29343571). {ECO:0000269|PubMed:29343571, ECO:0000269|PubMed:7615558, ECO:0000269|PubMed:7673114... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10811850, ECO:0000269|PubMed:28883123}; Single-pass type I membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Receptor subunit for interferon gamma/INFG that plays crucial roles in antimicrobial, antiviral, and antitumor responses by activating effector immune cells and enhancing antigen presentation (PubMed:20015550). Associates with transmembrane accessory factor IFNGR2 to form a functional receptor (PubMed:1098646... | Homo sapiens (Human) |
P15261 | INGR1_MOUSE | MGPQAAAGRMILLVVLMLSAKVGSGALTSTEDPEPPSVPVPTNVLIKSYNLNPVVCWEYQNMSQTPIFTVQVKVYSGSWTDSCTNISDHCCNIYEQIMYPDVSAWARVKAKVGQKESDYARSKEFLMCLKGKVGPPGLEIRRKKEEQLSVLVFHPEVVVNGESQGTMFGDGSTCYTFDYTVYVEHNRSGEILHTKHTVEKEECNETLCELNISVSTLDSRYCISVDGISSFWQVRTEKSKDVCIPPFHDDRKDSIWILVVAPLTVFTVVILVFAYWYTKKNSFKRKSIMLPKSLLSVVKSATLETKPESKYSLVTPHQPA... | null | null | astrocyte activation [GO:0048143]; cytokine-mediated signaling pathway [GO:0019221]; defense response to virus [GO:0051607]; microglial cell activation [GO:0001774]; negative regulation of amyloid-beta clearance [GO:1900222]; positive regulation of amyloid-beta formation [GO:1902004]; positive regulation of gene expres... | dendrite [GO:0030425]; plasma membrane [GO:0005886]; vesicle [GO:0031982] | cytokine binding [GO:0019955]; cytokine receptor activity [GO:0004896] | PF07140;PF20634;PF01108; | 2.60.40.10; | Type II cytokine receptor family | PTM: Phosphorylated at Ser/Thr residues. Phosphorylation of Tyr-445 is required for IFNG receptor signal transduction. Influenza virus infection leads to phosphorylation in a CSNK1A1-dependent manner. {ECO:0000250|UniProtKB:P15260}.; PTM: Ubiquitinated after phosphorylation in a CSNK1A1-dependent manner, leading to the... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2137461, ECO:0000269|PubMed:2530216, ECO:0000269|PubMed:2530582, ECO:0000269|PubMed:2531896, ECO:0000269|PubMed:2532365}; Single-pass type I membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Receptor subunit for interferon gamma/INFG that plays crucial roles in antimicrobial, antiviral, and antitumor responses by activating effector immune cells and enhancing antigen presentation (, PubMed:20926559, PubMed:27286456). Associates with transmembrane accessory factor IFNGR2 to form a functional recep... | Mus musculus (Mouse) |
P15274 | AMPD_YEAST | MDNQATQRLNDLSLEPAPSHDEQDGSGLVIDIDQRKIGDEQAGVVVDDETPPLEQQDSHESLAADSRNANFSYHENQQLLENGTKQLALDEHDSHSAILEQPSHSTNCSSSNIAAMNKGHDSADHASQNSGGKPRTLSASAQHILPETLKSFAGAPVVNKQVRTSASYKMGMLADDASQQFLDDPSSELIDLYSKVAECRNLRAKYQTISVQNDDQNPKNKPGWVVYPPPPKPSYNSDTKTVVPVTNKPDAEVFDFTKCEIPGEDPDWEFTLNDDDSYVVHRSGKTDELIAQIPTLRDYYLDLEKMISISSDGPAKSFAY... | 3.5.4.6 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | AMP metabolic process [GO:0046033]; guanine salvage [GO:0006178]; IMP biosynthetic process [GO:0006188]; IMP salvage [GO:0032264]; purine nucleotide metabolic process [GO:0006163] | cytoplasm [GO:0005737]; cytosol [GO:0005829] | AMP deaminase activity [GO:0003876]; metal ion binding [GO:0046872] | PF19326; | 4.10.800.20;3.20.20.140; | Metallo-dependent hydrolases superfamily, Adenosine and AMP deaminases family | null | null | CATALYTIC ACTIVITY: Reaction=AMP + H(+) + H2O = IMP + NH4(+); Xref=Rhea:RHEA:14777, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, ChEBI:CHEBI:58053, ChEBI:CHEBI:456215; EC=3.5.4.6; Evidence={ECO:0000269|PubMed:2690949}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:14778; Evidence={ECO:0000269|PubMed:... | null | PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP from AMP: step 1/1. {ECO:0000305|PubMed:2690949}. | null | null | FUNCTION: AMP deaminase plays a critical role in energy metabolism. {ECO:0000305|PubMed:2690949}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P15278 | FAS3_DROME | MSRIVFICLAAILTDALTWAQVNVEPNTALLNEGDRTELLCRYGRSINYCRIEIPGEQKVLNLSPEWSKTPGFTYFGAGLTAGQCGVSIERVKASNNGQVKCSLGVEGEELSGTIDLVVALRPQQPIIELLSRPNREGYFNEGTEFRARCSVRDGRPPANISWYIDNMPANKRTTPLEVMSSTNDNVELSTSVQEIQWHLSPEDSNRKLVCRSHHQTDRESVPPQEAAYIINVRYAPVHQPDAAVYGLYLEHTAIVNITIRASPQPKIEWTIDGAIVGQGRTDGRYSAYEPQYLGNDEYNVTLAIAGLTLEDTTKIYNLR... | null | null | axon guidance [GO:0007411]; axonal fasciculation [GO:0007413]; heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules [GO:0007157]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; synaptic target recognition [GO:0008039] | adherens junction [GO:0005912]; neuromuscular junction [GO:0031594]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037]; smooth septate junction [GO:0005920] | null | PF08205; | 2.60.40.10; | null | null | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Mediates cell adhesion in a Ca(2+)-independent manner (PubMed:2509076). It plays a role in axon outgrowth, guidance and fasciculation of the developing nervous system (PubMed:2509076). Function in neurons is essential for adult survival, and is important for climbing behavior and activity (PubMed:37041188). {... | Drosophila melanogaster (Fruit fly) |
P15280 | GLGS2_ORYSJ | MAMAAAMGVASPYHAAHAAASTSCDSLRLLVAEGRPRRPRGVASSSSSSSSAGRRRRPLVFSPRAVSDSKSSQTCLDPDASTSVLGIILGGGAGTRLYPLTKKRAKPAVPLGANYRLIDIPVSNCLNSNISKIYVLTQFNSASLNRHLSRAYGNNIGGYKNEGFVEVLAAQQSPDNPNWFQGTADAVRQYLWLFEEHNVMEFLILAGDHLYRMDYEKFIQAHRETDSDITVAALPMDEKRATAFGLMKIDEEGRIVEFAEKPKGEQLKAMMVDTTILGLDDVRAKEMPYIASMGIYVISKNVMLQLLREQFPGANDFGSE... | 2.7.7.27 | null | glycogen biosynthetic process [GO:0005978]; starch biosynthetic process [GO:0019252]; starch metabolic process [GO:0005982] | amyloplast [GO:0009501]; chloroplast [GO:0009507]; cytosol [GO:0005829] | ATP binding [GO:0005524]; glucose-1-phosphate adenylyltransferase activity [GO:0008878] | PF00483; | 2.160.10.10; | Bacterial/plant glucose-1-phosphate adenylyltransferase family | null | SUBCELLULAR LOCATION: [Isoform 1]: Plastid, chloroplast {ECO:0000269|PubMed:17406793}. Plastid, amyloplast {ECO:0000305|PubMed:17406793}. Note=Found in the chloroplast in leaf. Found in the plastid in the developing endosperm. {ECO:0000305|PubMed:17406793}.; SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm, cytosol {ECO:00... | CATALYTIC ACTIVITY: Reaction=alpha-D-glucose 1-phosphate + ATP + H(+) = ADP-alpha-D-glucose + diphosphate; Xref=Rhea:RHEA:12120, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57498, ChEBI:CHEBI:58601; EC=2.7.7.27; Evidence={ECO:0000269|PubMed:24747952}; | null | PATHWAY: Glycan biosynthesis; starch biosynthesis. {ECO:0000305}. | null | null | FUNCTION: Involved in synthesis of starch. Catalyzes the synthesis of ADP-glucose, a molecule that serves as an activated glycosyl donor for alpha-1,4-glucan synthesis. The chloroplastic isoform 1 is essential for starch synthesis in leaf chloroplasts and the cytosolic isoform 2 for synthesis in seed endosperm. {ECO:00... | Oryza sativa subsp. japonica (Rice) |
P15288 | PEPD_ECOLI | MSELSQLSPQPLWDIFAKICSIPHPSYHEEQLAEYIVGWAKEKGFHVERDQVGNILIRKPATAGMENRKPVVLQAHLDMVPQKNNDTVHDFTKDPIQPYIDGEWVKARGTTLGADNGIGMASALAVLADENVVHGPLEVLLTMTEEAGMDGAFGLQGNWLQADILINTDSEEEGEIYMGCAGGIDFTSNLHLDREAVPAGFETFKLTLKGLKGGHSGGEIHVGLGNANKLLVRFLAGHAEELDLRLIDFNGGTLRNAIPREAFATIAVAADKVDVLKSLVNTYQEILKNELAEKEKNLALLLDSVANDKAALIAKSRDTF... | 3.4.13.18 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:7988883}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000269|PubMed:7988883}; Note=Binds 2 Zn(2+) ions per subunit. Can also use Co(2+). {ECO:0000269|PubMed:7988883}; | peptide catabolic process [GO:0043171]; proteolysis [GO:0006508] | cytosol [GO:0005829] | alanylglutamate dipeptidase activity [GO:0103046]; dipeptidase activity [GO:0016805]; metallodipeptidase activity [GO:0070573]; protein homodimerization activity [GO:0042803]; zinc ion binding [GO:0008270] | PF07687;PF01546; | 3.40.630.10; | Peptidase M20C family | null | null | CATALYTIC ACTIVITY: Reaction=Hydrolysis of dipeptides, preferentially hydrophobic dipeptides including prolyl amino acids.; EC=3.4.13.18; Evidence={ECO:0000269|PubMed:355237, ECO:0000269|PubMed:7988883}; | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 9. {ECO:0000269|PubMed:7988883}; | BIOPHYSICOCHEMICAL PROPERTIES: Temperature dependence: Optimum temperature is 37 degrees Celsius. {ECO:0000269|PubMed:7988883}; | FUNCTION: Dipeptidase with broad substrate specificity. Requires dipeptide substrates with an unblocked N-terminus and the amino group in the alpha or beta position. Non-protein amino acids and proline are not accepted in the C-terminal position, whereas some dipeptide amides and formyl amino acids are hydrolyzed. Also... | Escherichia coli (strain K12) |
P15289 | ARSA_HUMAN | MGAPRSLLLALAAGLAVARPPNIVLIFADDLGYGDLGCYGHPSSTTPNLDQLAAGGLRFTDFYVPVSLCTPSRAALLTGRLPVRMGMYPGVLVPSSRGGLPLEEVTVAEVLAARGYLTGMAGKWHLGVGPEGAFLPPHQGFHRFLGIPYSHDQGPCQNLTCFPPATPCDGGCDQGLVPIPLLANLSVEAQPPWLPGLEARYMAFAHDLMADAQRQDRPFFLYYASHHTHYPQFSGQSFAERSGRGPFGDSLMELDAAVGTLMTAIGDLGLLEETLVIFTADNGPETMRMSRGGCSGLLRCGKGTTYEGGVREPALAFWPG... | 3.1.6.8 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:12888274}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:12888274}; | lipid metabolic process [GO:0006629] | azurophil granule lumen [GO:0035578]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; lysosomal lumen [GO:0043202]; lysosome [GO:0005764] | arylsulfatase activity [GO:0004065]; calcium ion binding [GO:0005509]; cerebroside-sulfatase activity [GO:0004098]; sulfuric ester hydrolase activity [GO:0008484] | PF00884;PF14707; | 3.30.1120.10;3.40.720.10; | Sulfatase family | PTM: The conversion to 3-oxoalanine (also known as C-formylglycine, FGly), of a serine or cysteine residue in prokaryotes and of a cysteine residue in eukaryotes, is critical for catalytic activity. This post-translational modification is severely defective in multiple sulfatase deficiency (MSD). {ECO:0000269|PubMed:76... | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000269|PubMed:9342345}. Lysosome {ECO:0000305|PubMed:2562955}. | CATALYTIC ACTIVITY: Reaction=H2O + N-acyl-1-beta-D-(3-O-sulfo)-galactosyl-sphing-4-enine = a beta-D-galactosyl-(1<->1')-N-acylsphing-4-enine + H(+) + sulfate; Xref=Rhea:RHEA:21300, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16189, ChEBI:CHEBI:18390, ChEBI:CHEBI:75956; EC=3.1.6.8; Evidence={ECO:0000269|PubMed:107... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.099 mM for galactosyl-3-sulfate ceramide {ECO:0000269|PubMed:24294900}; Note=kcat is 0.087 sec(-1) with galactosyl-3-sulfate ceramide as substrate. {ECO:0000269|PubMed:24294900}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 4.5. {ECO:0000269|PubMed:24294900}; | null | FUNCTION: Hydrolyzes cerebroside sulfate. {ECO:0000269|PubMed:10751093, ECO:0000269|PubMed:24294900}. | Homo sapiens (Human) |
P15291 | B4GT1_HUMAN | MRLREPLLSGSAAMPGASLQRACRLLVAVCALHLGVTLVYYLAGRDLSRLPQLVGVSTPLQGGSNSAAAIGQSSGELRTGGARPPPPLGASSQPRPGGDSSPVVDSGPGPASNLTSVPVPHTTALSLPACPEESPLLVGPMLIEFNMPVDLELVAKQNPNVKMGGRYAPRDCVSPHKVAIIIPFRNRQEHLKYWLYYLHPVLQRQQLDYGIYVINQAGDTIFNRAKLLNVGFQEALKDYDYTCFVFSDVDLIPMNDHNAYRCFSQPRHISVAMDKFGFSLPYVQYFGGVSALSKQQFLTINGFPNNYWGWGGEDDDIFNR... | 2.4.1.-; 2.4.1.22; 2.4.1.275; 2.4.1.38; 2.4.1.90 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:16157350, ECO:0000269|PubMed:16497331, ECO:0000269|PubMed:19106107}; | acute inflammatory response [GO:0002526]; angiogenesis involved in wound healing [GO:0060055]; binding of sperm to zona pellucida [GO:0007339]; cell adhesion [GO:0007155]; development of secondary sexual characteristics [GO:0045136]; epithelial cell development [GO:0002064]; epithelial cell proliferation [GO:0050673]; ... | azurophil granule membrane [GO:0035577]; basolateral plasma membrane [GO:0016323]; brush border membrane [GO:0031526]; desmosome [GO:0030057]; external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; filopodium [GO:0030175]; Golgi apparatus [GO:0005794]; Golgi... | alpha-tubulin binding [GO:0043014]; beta-N-acetylglucosaminylglycopeptide beta-1,4-galactosyltransferase activity [GO:0003831]; beta-tubulin binding [GO:0048487]; cytoskeletal protein binding [GO:0008092]; galactosyltransferase activity [GO:0008378]; identical protein binding [GO:0042802]; lactose synthase activity [GO... | PF02709;PF13733; | null | Glycosyltransferase 7 family | PTM: The soluble form derives from the membrane forms by proteolytic processing. | SUBCELLULAR LOCATION: [Isoform Long]: Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:1714903, ECO:0000269|PubMed:20378551}; Single-pass type II membrane protein. Cell membrane {ECO:0000269|PubMed:1714903}; Single-pass type II membrane protein. Cell surface {ECO:0000269|PubMed:1714903}. Cell projection, filop... | CATALYTIC ACTIVITY: Reaction=D-glucose + UDP-alpha-D-galactose = H(+) + lactose + UDP; Xref=Rhea:RHEA:12404, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378, ChEBI:CHEBI:17716, ChEBI:CHEBI:58223, ChEBI:CHEBI:66914; EC=2.4.1.22; Evidence={ECO:0000269|PubMed:16157350}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:12405; Evid... | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000269|PubMed:16157350}. | null | null | FUNCTION: [Beta-1,4-galactosyltransferase 1]: The Golgi complex form catalyzes the production of lactose in the lactating mammary gland and could also be responsible for the synthesis of complex-type N-linked oligosaccharides in many glycoproteins as well as the carbohydrate moieties of glycolipids. {ECO:0000269|PubMed... | Homo sapiens (Human) |
P15303 | SEC23_YEAST | MDFETNEDINGVRFTWNVFPSTRSDANSNVVPVGCLYTPLKEYDELNVAPYNPVVCSGPHCKSILNPYCVIDPRNSSWSCPICNSRNHLPPQYTNLSQENMPLELQSTTIEYITNKPVTVPPIFFFVVDLTSETENLDSLKESIITSLSLLPPNALIGLITYGNVVQLHDLSSETIDRCNVFRGDREYQLEALTEMLTGQKPTGPGGAASHLPNAMNKVTPFSLNRFFLPLEQVEFKLNQLLENLSPDQWSVPAGHRPLRATGSALNIASLLLQGCYKNIPARIILFASGPGTVAPGLIVNSELKDPLRSHHDIDSDHAQ... | null | null | COPII-coated vesicle cargo loading [GO:0090110]; intracellular protein transport [GO:0006886]; macroautophagy [GO:0016236]; positive regulation of ER to Golgi vesicle-mediated transport [GO:1902953]; positive regulation of protein exit from endoplasmic reticulum [GO:0070863]; regulation of COPII vesicle coating [GO:000... | COPII vesicle coat [GO:0030127]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum exit site [GO:0070971]; endoplasmic reticulum membrane [GO:0005789]; Golgi membrane [GO:0000139] | GTPase activator activity [GO:0005096]; zinc ion binding [GO:0008270] | PF00626;PF08033;PF04815;PF04811;PF04810; | 2.60.40.1670;1.20.120.730;3.40.20.10;3.40.50.410;2.30.30.380; | SEC23/SEC24 family, SEC23 subfamily | PTM: Ubiquitinated. Ubiquitination is required for the formation of the SEC23/24 complex. Deubiquitinated by the UBP3/BRE5 complex. {ECO:0000269|PubMed:12778054}. | SUBCELLULAR LOCATION: Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000269|PubMed:10720463, ECO:0000269|PubMed:11086000, ECO:0000269|PubMed:12235121, ECO:0000269|PubMed:8548805, ECO:0000269|PubMed:9568718}; Peripheral membrane protein {ECO:0000269|PubMed:11086000, ECO:0000269|PubMed:8548805}; Cytoplasmic sid... | null | null | null | null | null | FUNCTION: Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules. SEC23 interacts with BET3... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P15304 | LIPS_RAT | MKPRRPISFTREITAMEPSSTSVSRPEWRPEAQQTLTDYPGSRELQEFGIPQKQSLPNEATAQQGAEFQQEQGVQQSTLLQKLLTPLAFPVPQQSFPSHKVHSDQQEATSQNGPGAGKVHTTQKELEHRDEHVGTAESGPAEPPPATEVEATSIAQAVSGPDKKLPTQTDLVSQERAEQSDPTAQQTPLVQGVKSDQGSLIESGILARLQKLAIQQPSQEWKTFLDCVTESDMEKYLNSSSKSNPPEPSGGTVIPGTLPSKQKPDCGKMSGYGGKLPHGKKGILQKHKHYWDTASAFSHSMDLRTMTQSLVALAEDNMAF... | 3.1.1.23; 3.1.1.79 | null | cellular response to cold [GO:0070417]; cholesterol metabolic process [GO:0008203]; diacylglycerol catabolic process [GO:0046340]; ether lipid metabolic process [GO:0046485]; female pregnancy [GO:0007565]; lipid catabolic process [GO:0016042]; long-chain fatty acid catabolic process [GO:0042758]; response to xenobiotic... | caveola [GO:0005901]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular space [GO:0005615]; lipid droplet [GO:0005811]; membrane [GO:0016020]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | 1,2-diacylglycerol acylhydrolase activity [GO:0102259]; 1,3-diacylglycerol acylhydrolase activity [GO:0102258]; acylglycerol lipase activity [GO:0047372]; all-trans-retinyl-palmitate hydrolase, all-trans-retinol forming activity [GO:0047376]; hormone-sensitive lipase activity [GO:0033878]; hydrolase activity, acting on... | PF07859;PF06350; | 3.40.50.1820; | 'GDXG' lipolytic enzyme family | PTM: Phosphorylation by AMPK reduces its translocation towards the lipid droplets. {ECO:0000269|PubMed:15878856}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q05469}. Membrane, caveola {ECO:0000250|UniProtKB:Q05469}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q05469}. Lipid droplet {ECO:0000269|PubMed:15878856}. Note=Found in the high-density caveolae (By similarity). Translocates to the cytoplasm from the caveolae u... | CATALYTIC ACTIVITY: Reaction=a diacylglycerol + H2O = a fatty acid + a monoacylglycerol + H(+); Xref=Rhea:RHEA:32731, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17408, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.79; Evidence={ECO:0000269|PubMed:6643478}; CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = ... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=161 uM for retinyl palmitate {ECO:0000269|PubMed:9162045}; KM=33 uM for 1,2-dioleoylglycerol {ECO:0000269|PubMed:6643478}; KM=33 uM for 1,3-dioleoylglycerol {ECO:0000269|PubMed:6643478}; KM=2.2 uM for cholesteryl (9Z-octadecenoate) (dimeric form) {ECO:0000269|PubMe... | PATHWAY: Glycerolipid metabolism; triacylglycerol degradation. | null | null | FUNCTION: Lipase with broad substrate specificity, catalyzing the hydrolysis of triacylglycerols (TAGs), diacylglycerols (DAGs), monoacylglycerols (MAGs), cholesteryl esters and retinyl esters (PubMed:10694408, PubMed:6643478, PubMed:9162045). Shows a preferential hydrolysis of DAGs over TAGs and MAGs and preferentiall... | Rattus norvegicus (Rat) |
P15306 | TRBM_MOUSE | MLGIFFLGVLAPASLGLSALAKLQPTGSQCVEHECFALFQGPATFLDASQACQRLQGHLMTVRSSVAADVISLLLSQSSMDLGPWIGLQLPQGCDDPVHLGPLRGFQWVTGDNHTSYSRWARPNDQTAPLCGPLCVTVSTATEAAPGEPAWEEKPCETETQGFLCEFYFTASCRPLTVNTRDPEAAHISSTYNTPFGVSGADFQTLPVGSSAAVEPLGLELVCRAPPGTSEGHWAWEATGAWNCSVENGGCEYLCNRSTNEPRCLCPRDMDLQADGRSCARPVVQSCNELCEHFCVSNAEVPGSYSCMCETGYQLAADGH... | null | null | blood coagulation [GO:0007596]; female pregnancy [GO:0007565]; negative regulation of coagulation [GO:0050819]; response to cAMP [GO:0051591]; response to lipopolysaccharide [GO:0032496]; response to X-ray [GO:0010165] | apicolateral plasma membrane [GO:0016327]; external side of plasma membrane [GO:0009897]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; serine-type endopeptidase complex [GO:1905370]; vacuolar membrane [GO:0005774] | calcium ion binding [GO:0005509]; transmembrane signaling receptor activity [GO:0004888] | PF12662;PF07645;PF14670;PF00059;PF09064; | 2.10.25.10;3.10.100.10; | null | null | SUBCELLULAR LOCATION: Membrane; Single-pass type I membrane protein. | null | null | null | null | null | FUNCTION: Thrombomodulin is a specific endothelial cell receptor that forms a 1:1 stoichiometric complex with thrombin. This complex is responsible for the conversion of protein C to the activated protein C (protein Ca). Once evolved, protein Ca scissions the activated cofactors of the coagulation mechanism, factor Va ... | Mus musculus (Mouse) |
P15307 | REL_MOUSE | MASSGYNPYVEIIEQPRQRGMRFRYKCEGRSAGSIPGERSTDNNRTYPSVQIMNYYGKGKIRITLVTKNDPYKPHPHDLVGKDCRDGYYEAEFGPERRPLFFQNLGIRCVKKKEVKGAIILRISAGINPFNVGEQQLLDIEDCDLNVVRCVFMFFLPDEDGNFTTALPPIVSNPIYDNRAPNTAELRICRVNKNCGSVRGGDEIFLLCDKVQKDDIEVRFVLNDWEARGVFSQADVHRQVAIVFKTPPYCKAILEPVTVKMQLRRPSDQEVSESMDFRYLPDEKDAYGNKSKKQKTTLIFQKLLQDCGHFTEKPRTAPLG... | null | null | canonical NF-kappaB signal transduction [GO:0007249]; cellular response to stress [GO:0033554]; inflammatory response [GO:0006954]; innate immune response [GO:0045087]; non-canonical NF-kappaB signal transduction [GO:0038061]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of inter... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | 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-specific DNA binding [GO:0043565] | PF16179;PF00554; | 2.60.40.10;2.60.40.340; | null | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Proto-oncogene that may play a role in differentiation and lymphopoiesis. NF-kappa-B is a pleiotropic transcription factor which is present in almost all cell types and is involved in many biological processes such as inflammation, immunity, differentiation, cell growth, tumorigenesis and apoptosis. NF-kappa-... | Mus musculus (Mouse) |
P15309 | PPAP_HUMAN | MRAAPLLLARAASLSLGFLFLLFFWLDRSVLAKELKFVTLVFRHGDRSPIDTFPTDPIKESSWPQGFGQLTQLGMEQHYELGEYIRKRYRKFLNESYKHEQVYIRSTDVDRTLMSAMTNLAALFPPEGVSIWNPILLWQPIPVHTVPLSEDQLLYLPFRNCPRFQELESETLKSEEFQKRLHPYKDFIATLGKLSGLHGQDLFGIWSKVYDPLYCESVHNFTLPSWATEDTMTKLRELSELSLLSLYGIHKQKEKSRLQGGVLVNEILNHMKRATQIPSYKKLIMYSAHDTTVSGLQMALDVYNGLLPPYASCHLTELYF... | 3.1.3.2; 3.1.3.48; 3.1.3.5 | null | adenosine metabolic process [GO:0046085]; dephosphorylation [GO:0016311]; lipid metabolic process [GO:0006629]; lysosome organization [GO:0007040]; nucleotide metabolic process [GO:0009117]; positive regulation of adenosine receptor signaling pathway [GO:0060168]; purine nucleobase metabolic process [GO:0006144]; regul... | apical part of cell [GO:0045177]; azurophil granule membrane [GO:0035577]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; filopodium [GO:0030175]; Golgi cisterna [GO:0031985]; lysosomal membrane [GO:0005765]; lysosome [GO:0005764]; multivesicular body [GO:0005771]; nucleus [... | 5'-nucleotidase activity [GO:0008253]; acid phosphatase activity [GO:0003993]; choline binding [GO:0033265]; identical protein binding [GO:0042802]; lysophosphatidic acid phosphatase activity [GO:0052642]; molecular adaptor activity [GO:0060090]; phosphatase activity [GO:0016791]; protein homodimerization activity [GO:... | PF00328; | 3.40.50.1240; | Histidine acid phosphatase family | PTM: N-glycosylated. High mannose content, partially sialylated and fucosylated biantennary complex. Also fucosylated with partially sialylated triantennary complex oligosaccharides. {ECO:0000269|PubMed:10639192, ECO:0000269|PubMed:12525165}.; PTM: Proteolytically cleaved in seminal fluid to produce several peptides. P... | SUBCELLULAR LOCATION: [Isoform 1]: Secreted {ECO:0000305|PubMed:17638863}.; SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane {ECO:0000269|PubMed:17638863, ECO:0000269|PubMed:17897319, ECO:0000269|PubMed:20498373}; Single-pass type I membrane protein {ECO:0000255}. Lysosome membrane {ECO:0000269|PubMed:17638863, ECO:000... | CATALYTIC ACTIVITY: Reaction=a phosphate monoester + H2O = an alcohol + phosphate; Xref=Rhea:RHEA:15017, ChEBI:CHEBI:15377, ChEBI:CHEBI:30879, ChEBI:CHEBI:43474, ChEBI:CHEBI:67140; EC=3.1.3.2; Evidence={ECO:0000269|PubMed:10506173, ECO:0000269|PubMed:15280042, ECO:0000269|PubMed:9584846}; CATALYTIC ACTIVITY: Reaction=1... | null | null | null | null | FUNCTION: A non-specific tyrosine phosphatase that dephosphorylates a diverse number of substrates under acidic conditions (pH 4-6) including alkyl, aryl, and acyl orthophosphate monoesters and phosphorylated proteins (PubMed:10506173, PubMed:15280042, PubMed:20498373, PubMed:9584846). Has lipid phosphatase activity an... | Homo sapiens (Human) |
P15311 | EZRI_HUMAN | MPKPINVRVTTMDAELEFAIQPNTTGKQLFDQVVKTIGLREVWYFGLHYVDNKGFPTWLKLDKKVSAQEVRKENPLQFKFRAKFYPEDVAEELIQDITQKLFFLQVKEGILSDEIYCPPETAVLLGSYAVQAKFGDYNKEVHKSGYLSSERLIPQRVMDQHKLTRDQWEDRIQVWHAEHRGMLKDNAMLEYLKIAQDLEMYGINYFEIKNKKGTDLWLGVDALGLNIYEKDDKLTPKIGFPWSEIRNISFNDKKFVIKPIDKKAPDFVFYAPRLRINKRILQLCMGNHELYMRRRKPDTIEVQQMKAQAREEKHQKQLER... | null | null | actin cytoskeleton organization [GO:0030036]; actin filament bundle assembly [GO:0051017]; astral microtubule organization [GO:0030953]; cellular response to cAMP [GO:0071320]; cortical microtubule organization [GO:0043622]; establishment of centrosome localization [GO:0051660]; establishment of endothelial barrier [GO... | actin cytoskeleton [GO:0015629]; actin filament [GO:0005884]; adherens junction [GO:0005912]; apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; brush border [GO:0005903]; cell periphery [GO:0071944]; cell projection [GO:0042995]; ciliary basal body [GO:0036... | actin binding [GO:0003779]; actin filament binding [GO:0051015]; ATPase binding [GO:0051117]; cadherin binding [GO:0045296]; cell adhesion molecule binding [GO:0050839]; disordered domain specific binding [GO:0097718]; identical protein binding [GO:0042802]; microtubule binding [GO:0008017]; protein domain specific bin... | PF00769;PF20492;PF09380;PF00373;PF09379; | 1.20.5.450;1.20.80.10;6.10.360.10;2.30.29.30; | null | PTM: Phosphorylated by tyrosine-protein kinases. Phosphorylation by ROCK2 suppresses the head-to-tail association of the N-terminal and C-terminal halves resulting in an opened conformation which is capable of actin and membrane-binding (By similarity). {ECO:0000250}.; PTM: S-nitrosylation is induced by interferon-gamm... | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:18046454}; Peripheral membrane protein {ECO:0000269|PubMed:18046454}; Cytoplasmic side {ECO:0000269|PubMed:18046454}. Cell projection {ECO:0000269|PubMed:18046454}. Cell projection, microvillus membrane {ECO:0000269|PubMed:18046454}; Peripheral membrane pro... | null | null | null | null | null | FUNCTION: Probably involved in connections of major cytoskeletal structures to the plasma membrane. In epithelial cells, required for the formation of microvilli and membrane ruffles on the apical pole. Along with PLEKHG6, required for normal macropinocytosis. {ECO:0000269|PubMed:17881735, ECO:0000269|PubMed:18270268, ... | Homo sapiens (Human) |
P15313 | VATB1_HUMAN | MAMEIDSRPGGLPGSSCNLGAAREHMQAVTRNYITHPRVTYRTVCSVNGPLVVLDRVKFAQYAEIVHFTLPDGTQRSGQVLEVAGTKAIVQVFEGTSGIDARKTTCEFTGDILRTPVSEDMLGRVFNGSGKPIDKGPVVMAEDFLDINGQPINPHSRIYPEEMIQTGISPIDVMNSIARGQKIPIFSAAGLPHNEIAAQICRQAGLVKKSKAVLDYHDDNFAIVFAAMGVNMETARFFKSDFEQNGTMGNVCLFLNLANDPTIERIITPRLALTTAEFLAYQCEKHVLVILTDMSSYAEALREVSAAREEVPGRRGFPGY... | null | null | adult behavior [GO:0030534]; ATP metabolic process [GO:0046034]; calcium ion homeostasis [GO:0055074]; chloride ion homeostasis [GO:0055064]; inner ear morphogenesis [GO:0042472]; olfactory behavior [GO:0042048]; ossification [GO:0001503]; pH reduction [GO:0045851]; potassium ion homeostasis [GO:0055075]; prostaglandin... | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extrinsic component of synaptic vesicle membrane [GO:0098850]; lateral plasma membrane [GO:0016328]; microvillus [GO:0005902]; vacuolar proton-transporting V-t... | ATP binding [GO:0005524]; protein-containing complex binding [GO:0044877]; proton transmembrane transporter activity [GO:0015078]; proton-transporting ATPase activity, rotational mechanism [GO:0046961] | PF00006;PF02874; | 3.40.50.12240; | ATPase alpha/beta chains family | null | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:16769747, ECO:0000269|PubMed:29993276}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q91YH6}. | null | null | null | null | null | FUNCTION: Non-catalytic subunit of the V1 complex of vacuolar(H+)-ATPase (V-ATPase), a multisubunit enzyme composed of a peripheral complex (V1) that hydrolyzes ATP and a membrane integral complex (V0) that translocates protons (PubMed:16769747). V-ATPase is responsible for acidifying and maintaining the pH of intracel... | Homo sapiens (Human) |
P15314 | IRF1_MOUSE | MPITRMRMRPWLEMQINSNQIPGLIWINKEEMIFQIPWKHAAKHGWDINKDACLFRSWAIHTGRYKAGEKEPDPKTWKANFRCAMNSLPDIEEVKDQSRNKGSSAVRVYRMLPPLTRNQRKERKSKSSRDTKSKTKRKLCGDVSPDTFSDGLSSSTLPDDHSSYTTQGYLGQDLDMERDITPALSPCVVSSSLSEWHMQMDIIPDSTTDLYNLQVSPMPSTSEAATDEDEEGKIAEDLMKLFEQSEWQPTHIDGKGYLLNEPGTQLSSVYGDFSCKEEPEIDSPRGDIGIGIQHVFTEMKNMDSIMWMDSLLGNSVRLPP... | null | null | apoptotic process [GO:0006915]; canonical NF-kappaB signal transduction [GO:0007249]; CD8-positive, alpha-beta T cell differentiation [GO:0043374]; cellular response to interferon-beta [GO:0035458]; cellular response to interleukin-1 [GO:0071347]; cellular response to mechanical stimulus [GO:0071260]; cellular response... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; 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]; RNA polymerase II cis-regulatory region sequence-specific DNA bindi... | PF00605; | 1.10.10.10; | IRF family | PTM: Phosphorylated by CK2 and this positively regulates its activity. {ECO:0000250|UniProtKB:P10914}.; PTM: Ubiquitinated in a SPOP-depedent manner. Sumoylation represses the transcriptional activity and displays enhanced resistance to protein degradation (PubMed:12387893, PubMed:18955028). Sumolyated by UBE2I/UBC9 an... | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17018642, ECO:0000269|PubMed:30635240}. Cytoplasm {ECO:0000269|PubMed:17018642}. Note=MYD88-associated IRF1 migrates into the nucleus more efficiently than non-MYD88-associated IRF1. {ECO:0000269|PubMed:17018642}. | null | null | null | null | null | FUNCTION: Transcriptional regulator which displays a remarkable functional diversity in the regulation of cellular responses (PubMed:11244049, PubMed:11846971, PubMed:11846974, PubMed:16932750, PubMed:20049431, PubMed:25774715). Regulates transcription of IFN and IFN-inducible genes, host response to viral and bacteria... | Mus musculus (Mouse) |
P15315 | CUP2_YEAST | MVVINGVKYACETCIRGHRAAQCTHTDGPLQMIRRKGRPSTTCGHCKELRRTKNFNPSGGCMCASARRPAVGSKEDETRCRCDEGEPCKCHTKRKSSRKSKGGSCHRRANDEAAHVNGLGIADLDVLLGLNGRSSDVDMTTTLPSLKPPLQNGEIKADSIDNLDLASLDPLEQSPSISMEPVSINETGSAYTTTNTALNDIDIPFSINELNELYKQVSSHNSHSQ | null | null | intracellular copper ion homeostasis [GO:0006878]; intracellular iron ion homeostasis [GO:0006879]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006357]; response to copper ion [GO:0046688] | nucleus [GO:0005634] | copper ion binding [GO:0005507]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00649; | 3.90.430.10; | null | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Trans-acting regulatory protein that activates transcription of the CUP1 gene (metallothionein) in response to copper ions. Binds to the CUP1 UAS sequence 5'-GCTTCTTTTCCGCTGA-3'. Binds DNA only in presence of copper or silver. Copper seems to alter the conformation of the protein. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P15322 | ALL1_SINAL | PAGPFRIPKCRKEFQQAQHLRACQQWLHKQAMQSGSGPSWTLDDEFDFEDDMENPQGPQQRPPLLQQCCNELHQEEPLCVCPTLKGASKAVKQQVRQQLGQQGQQGPHLQHVISRIYQTATHLPKVCNIRQVSVCPFKKTMPGPS | null | null | null | null | nutrient reservoir activity [GO:0045735] | PF00234; | 1.10.110.10; | 2S seed storage albumins family | null | null | null | null | null | null | null | FUNCTION: This is a 2S seed storage protein. | Sinapis alba (White mustard) (Brassica hirta) |
P15327 | PMGE_MOUSE | MSKHKLIILRHGEGQWNKENRFCSWVDQKLNNDGLEEARNCGRQLKALNFEFDLVFTSILNRSIHTAWLILEELGQEWVPVESSWRLNERHYGALIGLNREKMALNHGEEQVRLWRRSYNVTPPPIEESHPYFHEIYSDRRYKVCDVPLDQLPRSESLKDVLERLLPYWKERIAPEILKGKSILISAHGNSSRALLKHLEGISDEDIINITLPTGVPILLELDENLRAVGPHQFLGNQEAIQAAIKKVDDQGKVKQGKQ | 5.4.2.11; 5.4.2.4 | null | defense response to protozoan [GO:0042832]; erythrocyte development [GO:0048821]; establishment of blood-brain barrier [GO:0060856]; glycolytic process [GO:0006096]; neuroinflammatory response [GO:0150076]; nucleoside phosphate metabolic process [GO:0006753]; oxygen transport [GO:0015671] | null | 2,3-bisphosphoglycerate-dependent phosphoglycerate mutase activity [GO:0046538]; bisphosphoglycerate mutase activity [GO:0004082]; hydrolase activity [GO:0016787] | PF00300; | 3.40.50.1240; | Phosphoglycerate mutase family, BPG-dependent PGAM subfamily | null | null | CATALYTIC ACTIVITY: Reaction=(2R)-3-phospho-glyceroyl phosphate = (2R)-2,3-bisphosphoglycerate + H(+); Xref=Rhea:RHEA:17765, ChEBI:CHEBI:15378, ChEBI:CHEBI:57604, ChEBI:CHEBI:58248; EC=5.4.2.4; Evidence={ECO:0000250|UniProtKB:P07738}; CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate; Xref=... | null | null | null | null | FUNCTION: Plays a major role in regulating hemoglobin oxygen affinity by controlling the levels of its allosteric effector 2,3-bisphosphoglycerate (2,3-BPG). Also exhibits mutase (EC 5.4.2.11) activity. {ECO:0000250|UniProtKB:P07738}. | Mus musculus (Mouse) |
P15328 | FOLR1_HUMAN | MAQRMTTQLLLLLVWVAVVGEAQTRIAWARTELLNVCMNAKHHKEKPGPEDKLHEQCRPWRKNACCSTNTSQEAHKDVSYLYRFNWNHCGEMAPACKRHFIQDTCLYECSPNLGPWIQQVDQSWRKERVLNVPLCKEDCEQWWEDCRTSYTCKSNWHKGWNWTSGFNKCAVGAACQPFHFYFPTPTVLCNEIWTHSYKVSNYSRGSGRCIQMWFDPAQGNPNEEVARFYAAAMSGAGPWAAWPFLLSLALMLLWLLS | null | null | anterior neural tube closure [GO:0061713]; axon regeneration [GO:0031103]; cardiac neural crest cell migration involved in outflow tract morphogenesis [GO:0003253]; cell adhesion [GO:0007155]; cellular response to folic acid [GO:0071231]; folic acid metabolic process [GO:0046655]; folic acid transport [GO:0015884]; fus... | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; brush border membrane [GO:0031526]; cell surface [GO:0009986]; clathrin-coated vesicle [GO:0030136]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; endosome [GO:000576... | folic acid binding [GO:0005542]; folic acid receptor activity [GO:0061714]; signaling receptor activity [GO:0038023] | PF03024; | null | Folate receptor family | PTM: The secreted form is derived from the membrane-bound form either by cleavage of the GPI anchor, or/and by proteolysis catalyzed by a metalloprotease. {ECO:0000305|PubMed:3476960}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:2527252, ECO:0000269|PubMed:8033114, ECO:0000269|PubMed:8567728}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:17566972, ECO:0000269|PubMed:7578066}. Apical cell membrane {ECO:0000269|PubMed:10787414}; Lipid-anchor, GPI-anchor {ECO:0000269|PubMed:17566972, ECO:000... | null | null | null | null | null | FUNCTION: Binds to folate and reduced folic acid derivatives and mediates delivery of 5-methyltetrahydrofolate and folate analogs into the interior of cells (PubMed:19074442, PubMed:23851396, PubMed:23934049, PubMed:2527252, PubMed:8033114, PubMed:8567728). Has high affinity for folate and folic acid analogs at neutral... | Homo sapiens (Human) |
P15330 | DORS_DROME | MFPNQNNGAAPGQGPAVDGQQSLNYNGLPAQQQQQLAQSTKNVRKKPYVKITEQPAGKALRFRYECEGRSAGSIPGVNSTPENKTYPTIEIVGYKGRAVVVVSCVTKDTPYRPHPHNLVGKEGCKKGVCTLEINSETMRAVFSNLGIQCVKKKDIEAALKAREEIRVDPFKTGFSHRFQPSSIDLNSVRLCFQVFMESEQKGRFTSPLPPVVSEPIFDKKAMSDLVICRLCSCSATVFGNTQIILLCEKVAKEDISVRFFEEKNGQSVWEAFGDFQHTDVHKQTAITFKTPRYHTLDITEPAKVFIQLRRPSDGVTSEAL... | null | null | canonical NF-kappaB signal transduction [GO:0007249]; cellular response to stress [GO:0033554]; dorsal/ventral axis specification [GO:0009950]; dorsal/ventral pattern formation [GO:0009953]; immune response [GO:0006955]; innate immune response [GO:0045087]; melanization defense response [GO:0035006]; non-canonical NF-k... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; neuromuscular junction [GO:0031594]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; subsynaptic reticulum [GO:0071212] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; DNA-binding transcription factor binding [GO:0140297]; high mobility group box 1 binding [GO:0070379]; identical protein binding [GO:0042802]; RNA po... | PF16179;PF00554; | 2.60.40.10;2.60.40.340; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:14638854, ECO:0000269|PubMed:17032737, ECO:0000269|PubMed:2598266}. Nucleus {ECO:0000269|PubMed:14638854, ECO:0000269|PubMed:17032737, ECO:0000269|PubMed:2598266}. Note=In ventral regions it is first cytoplasmic, then the protein is relocalized in the nucleus (PubMed:... | null | null | null | null | null | FUNCTION: Embryonic developmental transcription factor (PubMed:10072776, PubMed:2598266, PubMed:30982648). The lateral or ventral identity of a cell depends upon the concentration of this protein in its nucleus during the blastoderm stage (PubMed:2598266). Acts as a morphogenetic transcription factor that specifically ... | Drosophila melanogaster (Fruit fly) |
P15331 | PERI_MOUSE | MPSSASMSHHHSSGLRSSISSTSYRRTFGPPPSLSPGAFSYSSSSRFSSSRLLGSGSPSSSARLGSFRAPRAGALRLPSERLDFSMAEALNQEFLATRSNEKQELQELNDRFANFIEKVRFLEQQNAALRGELSQARGQEPARADQLCQQELRELRRELELLGRERDRVQVERDGLAEDLAALKQRLEEETRKREDAEHNLVLFRKDVDDATLSRLELERKIESLMDEIEFLKKLHEEELRDLQVSVESQQVQQVEVEATVKPELTAALRDIRAQYENIAAKNLQEAEEWYKSKYADLSDAANRNHEALRQAKQEMNESR... | null | null | intermediate filament cytoskeleton organization [GO:0045104]; intermediate filament organization [GO:0045109] | axon [GO:0030424]; C-fiber [GO:0044299]; intermediate filament [GO:0005882]; neurofilament [GO:0005883]; neuronal cell body [GO:0043025]; perikaryon [GO:0043204]; photoreceptor outer segment [GO:0001750]; photoreceptor outer segment membrane [GO:0042622]; plasma membrane [GO:0005886]; terminal bouton [GO:0043195]; type... | protein-containing complex binding [GO:0044877]; structural constituent of cytoskeleton [GO:0005200] | PF00038;PF04732; | 1.20.5.170;1.20.5.500;1.20.5.1160; | Intermediate filament family | PTM: Phosphorylated; phosphorylation increases after nerve injury in regenerating neurons. {ECO:0000250|UniProtKB:P21807}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:10426285, ECO:0000269|PubMed:15322088, ECO:0000269|PubMed:18709437, ECO:0000269|PubMed:20132868, ECO:0000269|PubMed:22723690, ECO:0000269|PubMed:23179371, ECO:0000269|PubMed:9971739}. Cell projection, axon {ECO:0000269|PubMed:17899157, ECO:0000269|PubMed... | null | null | null | null | null | FUNCTION: Class-III neuronal intermediate filament protein (By similarity). May form an independent structural network without the involvement of other neurofilaments or may cooperate with the neuronal intermediate filament proteins NEFL, NEFH, NEFM and INA to form filamentous networks (PubMed:10426285, PubMed:15322088... | Mus musculus (Mouse) |
P15336 | ATF2_HUMAN | MKFKLHVNSARQYKDLWNMSDDKPFLCTAPGCGQRFTNEDHLAVHKHKHEMTLKFGPARNDSVIVADQTPTPTRFLKNCEEVGLFNELASPFENEFKKASEDDIKKMPLDLSPLATPIIRSKIEEPSVVETTHQDSPLPHPESTTSDEKEVPLAQTAQPTSAIVRPASLQVPNVLLTSSDSSVIIQQAVPSPTSSTVITQAPSSNRPIVPVPGPFPLLLHLPNGQTMPVAIPASITSSNVHVPAAVPLVRPVTMVPSVPGIPGPSSPQPVQSEAKMRLKAALTQQHPPVTNGDTVKGHGSGLVRTQSEESRPQSLQQPAT... | null | null | abducens nucleus development [GO:0021742]; adipose tissue development [GO:0060612]; apoptotic process involved in development [GO:1902742]; BMP signaling pathway [GO:0030509]; brainstem development [GO:0003360]; cellular lipid metabolic process [GO:0044255]; cellular response to anisomycin [GO:0072740]; cellular respon... | chromatin [GO:0000785]; cytoplasm [GO:0005737]; H4 histone acetyltransferase complex [GO:1902562]; mitochondrial outer membrane [GO:0005741]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]; site of double-strand break [GO:0035861] | cAMP response element binding [GO:0035497]; cAMP response element binding protein binding [GO:0008140]; cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-bin... | PF00170; | 1.20.5.170;3.30.160.60; | BZIP family, ATF subfamily | PTM: Phosphorylation of Thr-69 by MAPK14 and MAPK11, and at Thr-71 by MAPK1/ERK2, MAPK3/ERK1, MAPK11, MAPK12 and MAPK14 in response to external stimulus like insulin causes increased transcriptional activity (PubMed:12110590, PubMed:9430721). Phosphorylated by PLK3 following hyperosmotic stress (PubMed:21098032). Also ... | SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Mitochondrion outer membrane. Note=Shuttles between the cytoplasm and the nucleus and heterodimerization with JUN is essential for the nuclear localization. Localization to the cytoplasm is observed under conditions of cellular stress and in disease states. Localizes at the mit... | null | null | null | null | null | FUNCTION: Transcriptional activator which regulates the transcription of various genes, including those involved in anti-apoptosis, cell growth, and DNA damage response. Dependent on its binding partner, binds to CRE (cAMP response element) consensus sequences (5'-TGACGTCA-3') or to AP-1 (activator protein 1) consensus... | Homo sapiens (Human) |
P15337 | CREB1_RAT | MTMDSGADNQQSGDAAVTEAESQQMTVQAQPQIATLAQVSMPAAHATSSAPTVTLVQLPNGQTVQVHGVIQAAQPSVIQSPQVQTVQISTIAESEDSQESVDSVTDSQKRREILSRRPSYRKILNDLSSDAPGVPRIEEEKSEEETSAPAITTVTVPTPIYQTSSGQYIAITQGGAIQLANNGTDGVQGLQTLTMTNAAATQPGTTILQYAQTTDGQQILVPSNQVVVQAASGDVQTYQIRTAPTSTIAPGVVMASSPALPTQPAEEAARKREVRLMKNREAARECRRKKKEYVKCLENRVAVLENQNKTLIEELKALKD... | null | null | axonogenesis [GO:0007409]; cAMP-mediated signaling [GO:0019933]; cellular response to fatty acid [GO:0071398]; cellular response to forskolin [GO:1904322]; cellular response to growth factor stimulus [GO:0071363]; cellular response to hepatocyte growth factor stimulus [GO:0035729]; cellular response to insulin-like gro... | ATF4-CREB1 transcription factor complex [GO:1990589]; axon [GO:0030424]; chromatin [GO:0000785]; euchromatin [GO:0000791]; mitochondrial matrix [GO:0005759]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575]; transcription regulator complex [GO:0005667] | arrestin family protein binding [GO:1990763]; cAMP response element binding [GO:0035497]; DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polymerase II-... | PF00170;PF02173; | 1.20.5.170; | BZIP family | PTM: Phosphorylation of Ser-119 allows CREBBP binding. Stimulated by phosphorylation. Phosphorylation of both Ser-128 and Ser-119 in the SCN regulates the activity of CREB and participate in circadian rhythm generation (By similarity). Phosphorylated upon calcium influx by CaMK4 and CaMK2 on Ser-119. CaMK4 is much more... | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Phosphorylation-dependent transcription factor that stimulates transcription upon binding to the DNA cAMP response element (CRE), a sequence present in many viral and cellular promoters (By similarity). Transcription activation is enhanced by the TORC coactivators which act independently of Ser-119 phosphoryl... | Rattus norvegicus (Rat) |
P15348 | TOP2_DROME | MENGNKALSIEQMYQKKSQLEHILLRPDSYIGSVEFTKELMWVYDNSQNRMVQKEISFVPGLYKIFDEILVNAADNKQRDKSMNTIKIDIDPERNMVSVWNNGQGIPVTMHKEQKMYVPTMIFGHLLTSSNYNDDEKKVTGGRNGYGAKLCNIFSTSFTVETATREYKKSFKQTWGNNMGKASDVQIKDFNGTDYTRITFSPDLAKFKMDRLDEDIVALMSRRAYDVAASSKGVSVFLNGNKLGVRNFKDYIDLHIKNTDDDSGPPIKIVHEVANERWEVACCPSDRGFQQVSFVNSIATYKGGRHVDHVVDNLIKQLLE... | 5.6.2.2 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:1328202, ECO:0000269|PubMed:2547764, ECO:0000269|PubMed:6308011, ECO:0000269|PubMed:8383533}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00995}; Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMe... | chromosome condensation [GO:0030261]; DNA topological change [GO:0006265]; heterochromatin formation [GO:0031507]; male meiosis chromosome segregation [GO:0007060]; meiotic cell cycle [GO:0051321]; metaphase chromosome alignment [GO:0051310]; mitotic cell cycle [GO:0000278]; mitotic chromosome condensation [GO:0007076]... | chromosome [GO:0005694]; cytoplasm [GO:0005737]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity [GO:0003918]; four-way junction DNA binding [GO:0000400]; metal ion binding [GO:0046872]; mRNA binding [GO:0003729]; rDNA bind... | PF00204;PF00521;PF02518;PF01751;PF16898; | 3.30.1360.40;3.30.1490.30;3.30.230.10;3.40.50.670;3.30.565.10;3.90.199.10;1.10.268.10; | Type II topoisomerase family | PTM: Phosphorylated (PubMed:10751154, PubMed:1328202, PubMed:8383533). Phosphorylation by casein kinase II enhances ATPase activity (PubMed:1328202). {ECO:0000269|PubMed:10751154, ECO:0000269|PubMed:1328202, ECO:0000269|PubMed:8383533}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10751154, ECO:0000269|PubMed:10885744, ECO:0000269|PubMed:11172718, ECO:0000269|PubMed:14600258}. Chromosome {ECO:0000269|PubMed:14600258, ECO:0000269|PubMed:18752348, ECO:0000269|PubMed:21304601, ECO:0000269|PubMed:8978614}. Cytoplasm {ECO:0000269|PubMed:10885744}. Not... | CATALYTIC ACTIVITY: Reaction=ATP-dependent breakage, passage and rejoining of double-stranded DNA.; EC=5.6.2.2; Evidence={ECO:0000269|PubMed:10751154, ECO:0000269|PubMed:10786800, ECO:0000269|PubMed:1328202, ECO:0000269|PubMed:2547764, ECO:0000269|PubMed:6308011, ECO:0000269|PubMed:8978614, ECO:0000269|PubMed:9545289}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=200 uM for negatively supercoiled double-stranded plasmid DNA (at 30 degrees Celsius) {ECO:0000269|PubMed:6308011}; KM=140 uM for negatively supercoiled double-stranded viral DNA (at 30 degrees Celsius) {ECO:0000269|PubMed:6308011}; KM=270 uM for positively superco... | null | null | null | FUNCTION: Control of topological states of DNA by transient breakage and subsequent rejoining of DNA strands (PubMed:10786800, PubMed:1328202, PubMed:2547764, PubMed:6308011, PubMed:8383533, PubMed:8978614). Topoisomerase II makes double-strand breaks (PubMed:10786800, PubMed:1328202, PubMed:2547764, PubMed:6308011, Pu... | Drosophila melanogaster (Fruit fly) |
P15357 | RS27A_DROME | MQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGAKKRKKKNYSTPKKIKHKRKKVKLAVLKYYKVDENGKIHRLRRECPGENCGAGVFMAAHEDRHYCGKCNLTFVFSKPEEK | null | null | cytoplasmic translation [GO:0002181]; modification-dependent protein catabolic process [GO:0019941]; protein ubiquitination [GO:0016567]; ribosomal small subunit biogenesis [GO:0042274] | cytosol [GO:0005829]; cytosolic ribosome [GO:0022626]; cytosolic small ribosomal subunit [GO:0022627]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; small-subunit processome [GO:0032040] | metal ion binding [GO:0046872]; protein tag activity [GO:0031386]; RNA binding [GO:0003723]; structural constituent of ribosome [GO:0003735]; ubiquitin protein ligase binding [GO:0031625] | PF01599;PF00240; | 6.20.50.150; | Ubiquitin family; Eukaryotic ribosomal protein eS31 family | null | SUBCELLULAR LOCATION: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.; SUBCELLULAR LOCATION: [Small ribosomal subunit protein eS31]: Nucleus, nucleolus {ECO:0000250|UniProtKB:P62979}. | null | null | null | null | null | FUNCTION: [Ubiquitin]: 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 lin... | Drosophila melanogaster (Fruit fly) |
P15358 | ANTA_HAEOF | MIKLAILLLFTVAIVRCQGPFGPGCEEAGCPEGSACNIITDRCTCSGVRCRMHCPHGFQRSRYGCEFCKCRLEPMKATCDISECPEGMMCSRLTNKCDCKIDINCRKTCPNGLKRDKLGCEYCECRPKRKLIPRLS | null | null | negative regulation of coagulation [GO:0050819] | extracellular region [GO:0005576] | heparin binding [GO:0008201]; serine-type endopeptidase inhibitor activity [GO:0004867] | PF02822; | null | Protease inhibitor I15 (antistasin) family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: This highly disulfide-bonded protein is a potent inhibitor of factor Xa. May have therapeutic utility as an anticoagulant. Also exhibits a strong metastatic activity. | Haementeria officinalis (Mexican leech) |
P15367 | SEC11_YEAST | MNLRFELQKLLNVCFLFASAYMFWQGLAIATNSASPIVVVLSGSMEPAFQRGDILFLWNRNTFNQVGDVVVYEVEGKQIPIVHRVLRQHNNHADKQFLLTKGDNNAGNDISLYANKKIYLNKSKEIVGTVKGYFPQLGYITIWISENKYAKFALLGMLGLSALLGGE | 3.4.21.89 | null | protein targeting to ER [GO:0045047]; signal peptide processing [GO:0006465] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; signal peptidase complex [GO:0005787] | peptidase activity [GO:0008233]; serine-type endopeptidase activity [GO:0004252] | PF00717; | null | Peptidase S26B family | PTM: N-glycosylated. {ECO:0000269|PubMed:10206957}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:10206957, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:2644273}; Single-pass type II membrane protein {ECO:0000269|PubMed:10206957, ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:2644273}. | CATALYTIC ACTIVITY: Reaction=Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.; EC=3.4.21.89; Evidence={ECO:0000269|PubMed:10206957}; | null | null | null | null | FUNCTION: Catalytic component of the signal peptidase complex (SPC) which catalyzes the cleavage of N-terminal signal sequences from nascent proteins as they are translocated into the lumen of the endoplasmic reticulum (PubMed:10206957, PubMed:11058593, PubMed:2644273, PubMed:7615509). Specifically cleaves N-terminal s... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P15368 | FAS2_PENPA | MRPEVEQELAHTLLVELLAYQFASPVRWIETQDVILAEQRTERIVEIGPADTLGGMARRTLASKYEAYDAATSVQRQILCYNKDAKEIYYDVDPVEEEPEATEPAPSATPAAPAAAPAAGAPPPPPSAGPAASVEDIPVTAVDILRTLVAQKLKKSLADVPLSKAIKDLVGGKSTLQNEILGDLGKEFGSTPEKPEDVPLDELGASMQATFNGQLGKQSSSLIARMVSSKMPGGFNITSVRKYLETRWGLGSGRQDGVLLLALTMEPAARLGSEVDAKAYLDDVTNKYAASAGVNLSAPVAGGDSGGAGGGMVMDPAAID... | 1.1.1.100; 2.3.1.41; 2.3.1.86 | null | heterocycle biosynthetic process [GO:0018130]; long-chain fatty acid biosynthetic process [GO:0042759]; organic cyclic compound biosynthetic process [GO:1901362]; secondary metabolite biosynthetic process [GO:0044550] | fatty acid synthase complex [GO:0005835] | 3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity [GO:0004316]; 3-oxoacyl-[acyl-carrier-protein] synthase activity [GO:0004315]; fatty acid synthase activity [GO:0004312]; fatty-acyl-CoA synthase activity [GO:0004321]; holo-[acyl-carrier-protein] synthase activity [GO:0008897]; magnesium ion binding [GO:00002... | PF01648;PF18325;PF18314;PF00109;PF02801; | 3.30.70.2490;3.40.47.10;3.90.25.70;6.10.140.1390;6.10.140.1410;6.10.250.1930;6.10.250.1940;3.90.470.20;3.40.50.720; | Thiolase-like superfamily, Fungal fatty acid synthetase subunit alpha family | null | null | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + 2n H(+) + n malonyl-CoA + 2n NADPH = a long-chain fatty acyl-CoA + n CO2 + n CoA + H2O + 2n NADP(+); Xref=Rhea:RHEA:22896, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349, ChE... | null | null | null | null | FUNCTION: Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The alpha subunit contains domains for: acyl carrier protein, 3-oxoacyl-[acyl-carrier-protein] reductase, and 3-oxoacyl-[acyl-carrier-protein] synthase. | Penicillium patulum (Penicillium griseofulvum) |
P15370 | EGON_DROME | MNQLCKVCGEPAAGFHFGAFTCEGCKSFFGRTYNNIAAIAGCKHNGDCVINKKNRTACKACRLRKCLLVGMSKSGSRYGRRSNWFKIHCLLQEQQTTSGLGGGSSVGSGSGGGVSSASLEQLARLQQASNQARQTYQDKTNPCIKSATATTSPRIEGAAVGTGIGGGASPSFLQAAKLHHQRQLKLDSRLSNTPSDSGASSAGDPNEDGVTSVLGGQIATPSSTNATSLPKLDLRHPNFPATSEPDADMQRQRHQELLEIFRSHSEPLYSSFAPFSHLPPVLLAAGVPQLPIFKDQFKAELLFPTTSSPELEEPIDLSFR... | null | null | cell differentiation [GO:0030154]; central nervous system development [GO:0007417]; intracellular steroid hormone receptor signaling pathway [GO:0030518]; regulation of DNA-templated transcription [GO:0006355]; regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634] | estrogen response element binding [GO:0034056]; nuclear receptor activity [GO:0004879]; zinc ion binding [GO:0008270] | PF00105; | 3.30.50.10; | Nuclear hormone receptor family, NR0 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}. | null | null | null | null | null | FUNCTION: May play a critical role in development of the progeny of eagle-positive neuroblasts. {ECO:0000269|PubMed:8625804}. | Drosophila melanogaster (Fruit fly) |
P15372 | ARRA_DROME | MVVNFKVFKKCSPNNMITLYMNRRDFVDSVTQVEPIDGIIVLDDEYVRQNRKIFVQLVCNFRYGREDDEMIGLRFQKELTLVSQQVCPPQKQDIQLTKMQERLLKKLGSNAYPFVMQMPPSSPASVVLQQKASDESQPCGVQYFVKIFTGDSDCDRSHRRSTINLGIRKVQYAPTKQGIQPCTVVRKDFLLSPGELELEVTLDKQLYHHGEKISVNICVRNNSNKVVKKIKAMVQQGVDVVLFQNGQFRNTIAFMETSEGCPLNPGSSLQKVMYLVPTLVANCDRAGIAVEGDIKRKDTALASTTLIASQDARDAFGIIV... | null | null | deactivation of rhodopsin mediated signaling [GO:0016059]; desensitization of G protein-coupled receptor signaling pathway [GO:0002029]; endocytosis [GO:0006897]; G protein-coupled receptor internalization [GO:0002031]; metarhodopsin inactivation [GO:0016060]; photoreceptor cell maintenance [GO:0045494]; sensory percep... | cytoplasm [GO:0005737]; rhabdomere [GO:0016028] | G protein-coupled receptor binding [GO:0001664]; opsin binding [GO:0002046] | PF02752;PF00339; | 2.60.40.640;2.60.40.840; | Arrestin family | PTM: Phosphorylated, but does not undergo light-induced phosphorylation. {ECO:0000269|PubMed:1905538}. | SUBCELLULAR LOCATION: Cell projection, rhabdomere {ECO:0000269|PubMed:8316831}. | null | null | null | null | null | FUNCTION: Regulates photoreceptor cell deactivation (PubMed:8316831). Arr1 and Arr2 proteins are mediators of rhodopsin inactivation and are essential for the termination of the phototransduction cascade (PubMed:8316831). Involved in regulating normal cycles of per nuclear accumulation in brain circadian neurons and th... | Drosophila melanogaster (Fruit fly) |
P15373 | PRLF_ECOLI | MPANARSHAVLTTESKVTIRGQTTIPAPVREALKLKPGQDSIHYEILPGGQVFMCRLGDEQEDHTMNAFLRFLDADIQNNPQKTRPFNIQQGKKLVAGMDVNIDDEIGDDE | null | null | negative regulation of DNA-templated transcription [GO:0045892]; regulation of cell growth [GO:0001558]; regulation of DNA-templated transcription [GO:0006355]; regulation of growth [GO:0040008]; single-species biofilm formation [GO:0044010] | cytoplasm [GO:0005737]; toxin-antitoxin complex [GO:0110001] | DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; enzyme binding [GO:0019899]; identical protein binding [GO:0042802]; toxin sequestering activity [GO:0097351] | PF15937; | 2.10.260.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | null | null | null | null | null | FUNCTION: Antitoxin component of a type II toxin-antitoxin (TA) system. Labile antitoxin that binds to the YhaV toxin and neutralizes its ribonuclease activity. Also acts as a transcription factor. The YhaV/PrlF complex binds the prlF-yhaV operon, probably negatively regulating its expression. {ECO:0000269|PubMed:17706... | Escherichia coli (strain K12) |
P15374 | UCHL3_HUMAN | MEGQRWLPLEANPEVTNQFLKQLGLHPNWQFVDVYGMDPELLSMVPRPVCAVLLLFPITEKYEVFRTEEEEKIKSQGQDVTSSVYFMKQTISNACGTIGLIHAIANNKDKMHFESGSTLKKFLEESVSMSPEERARYLENYDAIRVTHETSAHEGQTEAPSIDEKVDLHFIALVHVDGHLYELDGRKPFPINHGETSDETLLEDAIEVCKKFMERDPDELRFNAIALSAA | 3.4.19.12 | null | post-translational protein modification [GO:0043687]; protein catabolic process [GO:0030163]; protein deubiquitination [GO:0016579]; protein ubiquitination [GO:0016567]; ubiquitin-dependent protein catabolic process [GO:0006511] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654] | cysteine-type deubiquitinase activity [GO:0004843]; deNEDDylase activity [GO:0019784]; peptidase activity [GO:0008233]; ubiquitin binding [GO:0043130] | PF01088; | 3.40.532.10; | Peptidase C12 family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=Thiol-dependent hydrolysis of ester, thioester, amide, peptide and isopeptide bonds formed by the C-terminal Gly of ubiquitin (a 76-residue protein attached to proteins as an intracellular targeting signal).; EC=3.4.19.12; Evidence={ECO:0000269|PubMed:15157086, ECO:0000269|PubMed:15531586, ... | null | null | null | null | FUNCTION: Deubiquitinating enzyme (DUB) that controls levels of cellular ubiquitin through processing of ubiquitin precursors and ubiquitinated proteins. Thiol protease that recognizes and hydrolyzes a peptide bond at the C-terminal glycine of either ubiquitin or NEDD8. Has a 10-fold preference for Arg and Lys at posit... | Homo sapiens (Human) |
P15375 | MYF6_MOUSE | MMMDLFETGSYFFYLDGENVTLQPLEVAEGSPLYPGSDGTLSPCQDQMPQEAGSDSSGEEHVLAPPGLQPPHCPGQCLIWACKTCKRKSAPTDRRKAATLRERRRLKKINEAFEALKRRTVANPNQRLPKVEILRSAISYIERLQDLLHRLDQQEKMQELGVDPYSYKPKQEILEGADFLRTCSPQWPSVSDHSRGLVITAKEGGANVDASASSSLQRLSSIVDSISSEERKLPSVEEVVEK | null | null | muscle tissue morphogenesis [GO:0060415]; negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of myoblast differentiation [GO:0045663]; positive regulation of skeletal muscle fiber development [GO:0048743]; regulation of t... | cytosol [GO:0005829]; mitotic spindle [GO:0072686]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; protein dimerization activity [GO:0046983]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF01586;PF00010; | 4.10.280.10; | null | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Involved in muscle differentiation (myogenic factor). Induces fibroblasts to differentiate into myoblasts. Probable sequence specific DNA-binding protein. | Mus musculus (Mouse) |
P15379 | CD44_MOUSE | MDKFWWHTAWGLCLLQLSLAHQQIDLNVTCRYAGVFHVEKNGRYSISRTEAADLCQAFNSTLPTMDQMKLALSKGFETCRYGFIEGNVVIPRIHPNAICAANHTGVYILVTSNTSHYDTYCFNASAPPEEDCTSVTDLPNSFDGPVTITIVNRDGTRYSKKGEYRTHQEDIDASNIIDDDVSSGSTIEKSTPEGYILHTYLPTEQPTGDQDDSFFIRSTLATIASTVHSKSHAAAQKQNNWIWSWFGNSQSTTQTQEPTTSATTALMTTPETPPKRQEAQNWFSWLFQPSESKSHLHTTTKMPGTESNTNPTGWEPNEEN... | null | null | branching involved in prostate gland morphogenesis [GO:0060442]; branching involved in ureteric bud morphogenesis [GO:0001658]; cell adhesion [GO:0007155]; cell migration [GO:0016477]; hyaluronan catabolic process [GO:0030214]; inflammatory response [GO:0006954]; macrophage fusion [GO:0034238]; negative regulation of C... | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; cell projection [GO:0042995]; cell surface [GO:0009986]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; lamellipodium membrane [GO:0031258]; macrophage migration inhibitory factor receptor complex [GO:00356... | cargo receptor activity [GO:0038024]; channel regulator activity [GO:0016247]; cytokine receptor activity [GO:0004896]; epidermal growth factor receptor binding [GO:0005154]; hyaluronic acid binding [GO:0005540]; phosphoprotein binding [GO:0051219]; protein kinase binding [GO:0019901]; transmembrane signaling receptor ... | PF00193; | 3.10.100.10; | null | PTM: N-glycosylated. {ECO:0000250|UniProtKB:P16070}.; PTM: O-glycosylated; contains chondroitin sulfate glycans which can be more or less sulfated. {ECO:0000250|UniProtKB:P16070}.; PTM: Phosphorylated; activation of PKC results in the dephosphorylation of Ser-742 (constitutive phosphorylation site), and the phosphoryla... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17403031, ECO:0000269|PubMed:25065622}; Single-pass type I membrane protein {ECO:0000269|PubMed:17403031}. Cell projection, microvillus {ECO:0000269|PubMed:9472040}. Secreted {ECO:0000250|UniProtKB:P16070}. Note=Colocalizes with actin in membrane protrusionFs at w... | null | null | null | null | null | FUNCTION: Cell-surface receptor that plays a role in cell-cell interactions, cell adhesion and migration, helping them to sense and respond to changes in the tissue microenvironment. Participates thereby in a wide variety of cellular functions including the activation, recirculation and homing of T-lymphocytes, hematop... | Mus musculus (Mouse) |
P15381 | CAC1C_RABIT | MLRALVQPATPAYQPLPSHLSAETESTCKGTVVHEAQLNHFYISPGGSNYGSPRPAHANMNANAAAGLAPEHIPTPGAALSWQAAIDAARQAKLMGSAGNATISTVSSTQRKRQQYGKPKKQGSTTATRPPRALLCLTLKNPIRRACISIVEWKPFEIIILLTIFANCVALAIYIPFPEDDSNATNSNLERVEYLFLIIFTVEAFLKVIAYGLLFHPNAYLRNGWNLLDFIIVVVGLFSAILEQATKADGANALGGKGAGFDVKALRAFRVLRPLRLVSGVPSLQVVLNSIIKAMVPLLHIALLVLFVIIIYAIIGLELF... | null | null | calcium ion import across plasma membrane [GO:0098703]; calcium ion transmembrane transport [GO:0070588]; calcium ion transmembrane transport via high voltage-gated calcium channel [GO:0061577]; calcium ion transport into cytosol [GO:0060402]; cardiac conduction [GO:0061337]; positive regulation of adenylate cyclase ac... | dendrite [GO:0030425]; L-type voltage-gated calcium channel complex [GO:1990454]; membrane [GO:0016020]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; postsynaptic density membrane [GO:0098839]; sarcolemma [GO:0042383]; T-tubule [GO:0030315]; voltage-gated calcium channel com... | calmodulin binding [GO:0005516]; high voltage-gated calcium channel activity [GO:0008331]; metal ion binding [GO:0046872]; voltage-gated calcium channel activity [GO:0005245] | PF08763;PF16885;PF16905;PF00520; | 1.10.287.70;6.10.250.2180;6.10.250.2500;1.20.120.350; | Calcium channel alpha-1 subunit (TC 1.A.1.11) family, CACNA1C subfamily | PTM: Phosphorylation by PKA at Ser-1928 activates the channel (PubMed:1325377). Elevated levels of blood glucose lead to increased phosphorylation by PKA (By similarity). {ECO:0000250|UniProtKB:Q01815, ECO:0000269|PubMed:1325377}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:15615847, ECO:0000269|PubMed:17525370, ECO:0000269|PubMed:21127204, ECO:0000269|PubMed:2169433, ECO:0000269|PubMed:22649239, ECO:0000269|PubMed:2474130, ECO:0000269|PubMed:25548159, ECO:0000269|PubMed:8232554, ECO:0000269|PubMed:9278523, ECO:0000269|PubMed:9502794... | null | null | null | null | null | FUNCTION: Pore-forming, alpha-1C subunit of the voltage-gated calcium channel that gives rise to L-type calcium currents (PubMed:15615847, PubMed:17525370, PubMed:21127204, PubMed:2169433, PubMed:22649239, PubMed:22928916, PubMed:23145875, PubMed:2474130, PubMed:29363593, PubMed:8232554, PubMed:9278523, PubMed:9502794)... | Oryctolagus cuniculus (Rabbit) |
P15382 | KCNE1_HUMAN | MILSNTTAVTPFLTKLWQETVQQGGNMSGLARRSPRSSDGKLEALYVLMVLGFFGFFTLGIMLSYIRSKKLEHSNDPFNVYIESDAWQEKDKAYVQARVLESYRSCYVVENHLAIEQPNTHLPETKPSP | null | null | cardiac muscle cell action potential involved in contraction [GO:0086002]; cellular response to acidic pH [GO:0071468]; cellular response to cAMP [GO:0071320]; cellular response to light stimulus [GO:0071482]; epithelial cell maturation [GO:0002070]; male gonad development [GO:0008584]; membrane repolarization [GO:0086... | apical plasma membrane [GO:0016324]; cell surface [GO:0009986]; lysosome [GO:0005764]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]; voltage-gated potassium channel complex [GO:0008076]; Z disc [GO:0030018] | delayed rectifier potassium channel activity [GO:0005251]; potassium channel regulator activity [GO:0015459]; protein-containing complex binding [GO:0044877]; telethonin binding [GO:0031433]; transmembrane transporter binding [GO:0044325]; voltage-gated potassium channel activity involved in ventricular cardiac muscle ... | PF02060; | null | Potassium channel KCNE family | PTM: Phosphorylation inhibits the potassium current. {ECO:0000250}.; PTM: N-glycosylation at Asn-26 occurs post-translationally, and requires prior cotranslational glycosylation at Asn-5. {ECO:0000269|PubMed:21669976, ECO:0000269|PubMed:21676880}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19219384}; Single-pass type I membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000250|UniProtKB:P15383}. Membrane raft {ECO:0000269|PubMed:20533308}. Note=Colocalizes with KCNB1 at the plasma membrane (By similarity). Targets to the membrane raft when as... | null | null | null | null | null | FUNCTION: Ancillary protein that assembles as a beta subunit with a voltage-gated potassium channel complex of pore-forming alpha subunits. Modulates the gating kinetics and enhances stability of the channel complex. Assembled with KCNB1 modulates the gating characteristics of the delayed rectifier voltage-dependent po... | Homo sapiens (Human) |
P15383 | KCNE1_RAT | MALSNSTTVLPFLASLWQETDEPGGNMSADLARRSQLRDDSKLEALYILMVLGFFGFFTLGIMLSYIRSKKLEHSHDPFNVYIESDAWQEKGKALFQARVLESFRACYVIENQAAVEQPATHLPELKPLS | null | null | cardiac muscle cell action potential involved in contraction [GO:0086002]; cellular response to acidic pH [GO:0071468]; cellular response to cAMP [GO:0071320]; cellular response to light stimulus [GO:0071482]; epithelial cell maturation [GO:0002070]; heart contraction [GO:0060047]; male gonad development [GO:0008584]; ... | apical plasma membrane [GO:0016324]; cell surface [GO:0009986]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]; voltage-gated potassium channel complex [GO:0008076]; Z disc [GO:0030018] | delayed rectifier potassium channel activity [GO:0005251]; potassium channel regulator activity [GO:0015459]; protein-containing complex binding [GO:0044877]; telethonin binding [GO:0031433]; transmembrane transporter binding [GO:0044325]; voltage-gated potassium channel activity [GO:0005249] | PF02060; | null | Potassium channel KCNE family | PTM: Phosphorylation inhibits the potassium current.; PTM: N-glycosylation at Asn-26 occurs post-translationally, and requires prior cotranslational glycosylation at Asn-5. {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14679187, ECO:0000269|PubMed:19219384}; Single-pass type I membrane protein {ECO:0000305}. Apical cell membrane {ECO:0000269|PubMed:19219384}. Membrane raft {ECO:0000250|UniProtKB:P15382}. Note=Colocalizes with KCNB1 at the plasma membrane. Restrictively localized... | null | null | null | null | null | FUNCTION: Ancillary protein that assembles as a beta subunit with a voltage-gated potassium channel complex of pore-forming alpha subunits. Modulates the gating kinetics and enhances stability of the channel complex. Assembled with KCNB1 modulates the gating characteristics of the delayed rectifier voltage-dependent po... | Rattus norvegicus (Rat) |
P15384 | KCNA3_RAT | MTVVPGDHLLEPEAAGGGGGDPPQGGCVSGGGCDRYEPLPPALPAAGEQDCCGERVVINISGLRFETQLKTLCQFPETLLGDPKRRMRYFDPLRNEYFFDRNRPSFDAILYYYQSGGRIRRPVNVPIDIFSEEIRFYQLGEEAMEKFREDEGFLREEERPLPRRDFQRQVWLLFEYPESSGPARGIAIVSVLVILISIVIFCLETLPEFRDEKDYPASPSQDVFEAANNSTSGASSGASSFSDPFFVVETLCIIWFSFELLVRFFACPSKATFSRNIMNLIDIVAIIPYFITLGTELAERQGNGQQAMSLAILRVIRLVR... | null | null | corpus callosum development [GO:0022038]; optic nerve development [GO:0021554]; potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813]; protein homooligomerization [GO:0051260] | axon [GO:0030424]; calyx of Held [GO:0044305]; glutamatergic synapse [GO:0098978]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; presynaptic membrane [GO:0042734]; voltage-gated potassium channel complex [GO:0008076] | delayed rectifier potassium channel activity [GO:0005251]; outward rectifier potassium channel activity [GO:0015271]; voltage-gated potassium channel activity [GO:0005249] | PF02214;PF00520; | 1.10.287.70;1.20.120.350; | Potassium channel family, A (Shaker) (TC 1.A.1.2) subfamily, Kv1.3/KCNA3 sub-subfamily | PTM: N-glycosylation promotes the cell surface expression. {ECO:0000269|PubMed:22613618}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22613618}; Multi-pass membrane protein {ECO:0000269|PubMed:22613618}. | null | null | null | null | null | FUNCTION: Mediates the voltage-dependent potassium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a potassium-selective channel through which potassium ions may pass in accordance with their electrochemical gr... | Rattus norvegicus (Rat) |
P15385 | KCNA4_RAT | MEVAMVSAESSGCNSHMPYGYAAQARARERERLAHSRAAAAAAVAAATAAVEGTGGSGGGPHHHHQTRGAYSSHDPQGSRGSREEEATRTEKKKKLHHRQSSFPHCSDLMPSGSEEKILRELSEEEEDEEEEEEEEEEGRFYYSEEDHGDGCSYTDLLPQDDGGGGGYSSVRYSDCCERVVINVSGLRFETQMKTLAQFPETLLGDPEKRTQYFDPLRNEYFFDRNRPSFDAILYYYQSGGRLKRPVNVPFDIFTEEVKFYQLGEEALLKFREDEGFVREEEDRALPENEFKKQIWLLFEYPESSSPARGIAIVSVLVIL... | null | null | monoatomic ion transmembrane transport [GO:0034220]; potassium ion transmembrane transport [GO:0071805]; potassium ion transport [GO:0006813]; protein homooligomerization [GO:0051260]; regulation of presynaptic membrane potential [GO:0099505] | asymmetric synapse [GO:0032279]; axon [GO:0030424]; axon initial segment [GO:0043194]; cell surface [GO:0009986]; dendritic shaft [GO:0043198]; dendritic spine [GO:0043197]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; presynaptic membrane ... | delayed rectifier potassium channel activity [GO:0005251]; monoatomic ion channel activity [GO:0005216]; potassium channel activity [GO:0005267]; potassium ion binding [GO:0030955]; voltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential [GO:0099508]; voltage-gated potassi... | PF02214;PF00520;PF07941; | 1.10.287.70;1.20.5.600;1.20.120.350; | Potassium channel family, A (Shaker) (TC 1.A.1.2) subfamily, Kv1.4/KCNA4 sub-subfamily | PTM: N-glycosylated. {ECO:0000269|PubMed:10896669}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10896669, ECO:0000269|PubMed:2348860, ECO:0000269|PubMed:2384173}; Multi-pass membrane protein {ECO:0000255}. Cell projection, axon {ECO:0000269|PubMed:10896669, ECO:0000269|PubMed:1497894, ECO:0000305|PubMed:8361540}. | null | null | null | null | null | FUNCTION: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes. Forms tetrameric potassium-selective channels through which potassium ions pass in accordance with their electrochemical gradient. The channel alternates between opened and closed conformations in response ... | Rattus norvegicus (Rat) |
P15387 | KCNB1_RAT | MPAGMTKHGSRSTSSLPPEPMEIVRSKACSRRVRLNVGGLAHEVLWRTLDRLPRTRLGKLRDCNTHDSLLQVCDDYSLEDNEYFFDRHPGAFTSILNFYRTGRLHMMEEMCALSFSQELDYWGIDEIYLESCCQARYHQKKEQMNEELKREAETLREREGEEFDNTCCAEKRKKLWDLLEKPNSSVAAKILAIISIMFIVLSTIALSLNTLPELQSLDEFGQSTDNPQLAHVEAVCIAWFTMEYLLRFLSSPKKWKFFKGPLNAIDLLAILPYYVTIFLTESNKSVLQFQNVRRVVQIFRIMRILRILKLARHSTGLQSL... | null | null | action potential [GO:0001508]; cellular response to calcium ion [GO:0071277]; cellular response to glucose stimulus [GO:0071333]; cellular response to nutrient levels [GO:0031669]; clustering of voltage-gated potassium channels [GO:0045163]; glucose homeostasis [GO:0042593]; glutamate receptor signaling pathway [GO:000... | apical plasma membrane [GO:0016324]; axon [GO:0030424]; cell surface [GO:0009986]; cholinergic synapse [GO:0098981]; dendrite [GO:0030425]; dendrite membrane [GO:0032590]; lateral plasma membrane [GO:0016328]; neuronal cell body [GO:0043025]; neuronal cell body membrane [GO:0032809]; perikaryon [GO:0043204]; perinuclea... | delayed rectifier potassium channel activity [GO:0005251]; outward rectifier potassium channel activity [GO:0015271]; protein heterodimerization activity [GO:0046982]; SNARE binding [GO:0000149]; transmembrane transporter binding [GO:0044325]; voltage-gated potassium channel activity [GO:0005249] | PF02214;PF00520;PF03521; | 1.10.287.70;1.20.120.350; | Potassium channel family, B (Shab) (TC 1.A.1.2) subfamily, Kv2.1/KCNB1 sub-subfamily | PTM: Phosphorylated (PubMed:15195093, PubMed:16319318, PubMed:16407566, PubMed:18463252, PubMed:8083226). Differential C-terminal phosphorylation on a subset of serines allows graded activity-dependent regulation of channel gating in hippocampal neurons (PubMed:16917065, PubMed:17192433, PubMed:9351973). Ser-607 and Ty... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10024359, ECO:0000269|PubMed:10414968, ECO:0000269|PubMed:10618149, ECO:0000269|PubMed:10719893, ECO:0000269|PubMed:12127166, ECO:0000269|PubMed:12403834, ECO:0000269|PubMed:12451110, ECO:0000269|PubMed:12560340, ECO:0000269|PubMed:12615930, ECO:0000269|PubMed:126... | null | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Note=Homotetrameric channels expressed in xenopus oocytes or in mammalian non-neuronal cells display delayed-rectifier voltage-dependent potassium currents which are activated during membrane depolarization, i.e within a risetime of about 20 msec (PubMed:2770868). Aft... | null | null | null | FUNCTION: Voltage-gated potassium channel that mediates transmembrane potassium transport in excitable membranes, primarily in the brain, but also in the pancreas and cardiovascular system. Contributes to the regulation of the action potential (AP) repolarization, duration and frequency of repetitive AP firing in neuro... | Rattus norvegicus (Rat) |
P15388 | KCNC1_MOUSE | MGQGDESERIVINVGGTRHQTYRSTLRTLPGTRLAWLAEPDAHSHFDYDPRADEFFFDRHPGVFAHILNYYRTGKLHCPADVCGPLYEEELAFWGIDETDVEPCCWMTYRQHRDAEEALDSFGGAPLDNSADDADADGPGDSGDGEDELEMTKRLALSDSPDGRPGGFWRRWQPRIWALFEDPYSSRYARYVAFASLFFILVSITTFCLETHERFNPIVNKTEIENVRNGTQVRYYREAETEAFLTYIEGVCVVWFTFEFLMRVVFCPNKVEFIKNSLNIIDFVAILPFYLEVGLSGLSSKAAKDVLGFLRVVRFVRILR... | null | null | cellular response to xenobiotic stimulus [GO:0071466]; cerebellum development [GO:0021549]; corpus callosum development [GO:0022038]; globus pallidus development [GO:0021759]; optic nerve development [GO:0021554]; positive regulation of monoatomic ion transmembrane transport [GO:0034767]; positive regulation of potassi... | axolemma [GO:0030673]; axon terminus [GO:0043679]; calyx of Held [GO:0044305]; cell surface [GO:0009986]; dendrite [GO:0030425]; dendrite membrane [GO:0032590]; neuron projection membrane [GO:0032589]; neuronal cell body [GO:0043025]; neuronal cell body membrane [GO:0032809]; postsynaptic membrane [GO:0045211]; presyna... | delayed rectifier potassium channel activity [GO:0005251]; kinesin binding [GO:0019894]; transmembrane transporter binding [GO:0044325]; voltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential [GO:0099508] | PF02214;PF00520; | 1.10.287.70;1.20.120.350; | Potassium channel family, C (Shaw) (TC 1.A.1.2) subfamily, Kv3.1/KCNC1 sub-subfamily | PTM: N-glycosylated; contains sialylated glycans. {ECO:0000250|UniProtKB:P25122}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1400413, ECO:0000269|PubMed:2599109}; Multi-pass membrane protein {ECO:0000255}. Cell projection, axon {ECO:0000250|UniProtKB:P25122}. Presynaptic cell membrane {ECO:0000250|UniProtKB:P25122}. Note=Localizes in parallel fiber membranes, distributed on the perisyna... | null | null | null | null | null | FUNCTION: Voltage-gated potassium channel that plays an important role in the rapid repolarization of fast-firing brain neurons. The channel opens in response to the voltage difference across the membrane, forming a potassium-selective channel through which potassium ions pass in accordance with their electrochemical g... | Mus musculus (Mouse) |
P15389 | SCN5A_RAT | MANLLLPRGTSSFRRFTRESLAAIEKRMAEKQARGGSATSQESREGLQEEEAPRPQLDLQASKKLPDLYGNPPRELIGEPLEDLDPFYSTQKTFIVLNKGKTIFRFSATNALYVLSPFHPVRRAAVKILVHSLFSMLIMCTILTNCVFMAQHDPPPWTKYVEYTFTAIYTFESLVKILARGFCLHAFTFLRDPWNWLDFSVIVMAYTTEFVDLGNVSALRTFRVLRALKTISVISGLKTIVGALIQSVKKLADVMVLTVFCLSVFALIGLQLFMGNLRHKCVRNFTELNGTNGSVEADGLVWNSLDVYLNDPANYLLKNG... | null | null | atrial cardiac muscle cell action potential [GO:0086014]; AV node cell action potential [GO:0086016]; AV node cell to bundle of His cell communication [GO:0086067]; brainstem development [GO:0003360]; bundle of His cell action potential [GO:0086043]; cardiac muscle cell action potential involved in contraction [GO:0086... | axon [GO:0030424]; caveola [GO:0005901]; cell surface [GO:0009986]; endoplasmic reticulum [GO:0005783]; intercalated disc [GO:0014704]; lateral plasma membrane [GO:0016328]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]; plasma membrane [GO:0005886]; sarcolemma [GO:0042383]; sodium channel complex... | ankyrin binding [GO:0030506]; calmodulin binding [GO:0005516]; enzyme binding [GO:0019899]; fibroblast growth factor binding [GO:0017134]; nitric-oxide synthase binding [GO:0050998]; protein domain specific binding [GO:0019904]; protein kinase binding [GO:0019901]; scaffold protein binding [GO:0097110]; transmembrane t... | PF00520;PF06512;PF11933; | 1.10.287.70;1.10.238.10;1.20.5.1190;1.20.120.350; | Sodium channel (TC 1.A.1.10) family, Nav1.5/SCN5A subfamily | PTM: Phosphorylation at Ser-1505 by PKC in a highly conserved cytoplasmic loop slows inactivation of the sodium channel and reduces peak sodium currents. Regulated through phosphorylation by CaMK2D. {ECO:0000250|UniProtKB:Q14524, ECO:0000250|UniProtKB:Q9JJV9}.; PTM: Ubiquitinated by NEDD4L; which promotes its endocytos... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21617128}; Multi-pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}. Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q14524}. Cell membrane, sarcolemma, T-tubule {ECO:0000269|PubMed:15579534}. Cell junction {ECO:0000269|PubMed:19661460}. Note=RANGRF promote... | null | null | null | null | null | FUNCTION: This protein mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical... | Rattus norvegicus (Rat) |
P15390 | SCN4A_RAT | MASSSLPNLVPPGPHCLRPFTPESLAAIEQRAVEEEARLQRNKQMEIEEPERKPRSDLEAGKNLPLIYGDPPPEVIGIPLEDLDPYYSDKKTFIVLNKGKAIFRFSATPALYLLSPFSIVRRVAIKVLIHALFSMFIMITILTNCVFMTMSNPPSWSKHVEYTFTGIYTFESLIKMLARGFCIDDFTFLRDPWNWLDFSVITMAYVTEFVDLGNISALRTFRVLRALKTITVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALVGLQLFMGNLRQKCVRWPPPMNDTNTTWYGNDTWYSNDTWYGNDTWYINDTWNS... | null | null | choline transport [GO:0015871]; membrane depolarization during action potential [GO:0086010]; monoatomic cation transport [GO:0006812]; neuronal action potential [GO:0019228]; potassium ion transport [GO:0006813]; regulation of skeletal muscle contraction by action potential [GO:0100001]; sodium ion transmembrane trans... | axon [GO:0030424]; plasma membrane [GO:0005886]; voltage-gated sodium channel complex [GO:0001518] | voltage-gated sodium channel activity [GO:0005248] | PF00520;PF06512; | 1.10.287.70;1.10.238.10;1.20.5.1190;1.20.120.350; | Sodium channel (TC 1.A.1.10) family, Nav1.4/SCN4A subfamily | PTM: Phosphorylation at Ser-1321 by PKC in a highly conserved cytoplasmic loop slows inactivation of the sodium channel and reduces peak sodium currents. {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16303569, ECO:0000269|PubMed:2559760, ECO:0000269|PubMed:28012039}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P35499}. | null | null | null | null | null | FUNCTION: Pore-forming subunit of a voltage-gated sodium channel complex through which Na(+) ions pass in accordance with their electrochemical gradient (PubMed:16303569, PubMed:2559760, PubMed:28012039). Alternates between resting, activated and inactivated states (PubMed:28012039). Required for normal muscle fiber ex... | Rattus norvegicus (Rat) |
P15391 | CD19_HUMAN | MPPPRLLFFLLFLTPMEVRPEEPLVVKVEEGDNAVLQCLKGTSDGPTQQLTWSRESPLKPFLKLSLGLPGLGIHMRPLAIWLFIFNVSQQMGGFYLCQPGPPSEKAWQPGWTVNVEGSGELFRWNVSDLGGLGCGLKNRSSEGPSSPSGKLMSPKLYVWAKDRPEIWEGEPPCLPPRDSLNQSLSQDLTMAPGSTLWLSCGVPPDSVSRGPLSWTHVHPKGPKSLLSLELKDDRPARDMWVMETGLLLPRATAQDAGKYYCHRGNLTMSFHLEITARPVLWHWLLRTGGWKVSAVTLAYLIFCLCSLVGILHLQRALVLR... | null | null | antigen receptor-mediated signaling pathway [GO:0050851]; B cell proliferation involved in immune response [GO:0002322]; B cell receptor signaling pathway [GO:0050853]; B-1 B cell differentiation [GO:0001923]; immunoglobulin mediated immune response [GO:0016064]; positive regulation of phosphatidylinositol 3-kinase/pro... | external side of plasma membrane [GO:0009897]; extracellular exosome [GO:0070062]; membrane raft [GO:0045121]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991] | null | null | 2.60.40.10; | null | PTM: Phosphorylated on tyrosine following B-cell activation (PubMed:10706702, PubMed:12387743, PubMed:7684160, PubMed:7687539). Phosphorylated on tyrosine residues by LYN (PubMed:7687428). Tyrosine residues are phosphorylated sequentially after activation of the B cell receptor. Phosphorylation of Tyr-531 is extremely ... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:1373518, ECO:0000269|PubMed:1383329, ECO:0000269|PubMed:16672701, ECO:0000269|PubMed:1702139, ECO:0000269|PubMed:2463100, ECO:0000269|PubMed:9317126, ECO:0000269|PubMed:9382888}; Single-pass type I membrane protein {ECO:0000305}. Membrane raft {ECO:0000250|UniProt... | null | null | null | null | null | FUNCTION: Functions as a coreceptor for the B-cell antigen receptor complex (BCR) on B-lymphocytes. Decreases the threshold for activation of downstream signaling pathways and for triggering B-cell responses to antigens (PubMed:1373518, PubMed:16672701, PubMed:2463100). Activates signaling pathways that lead to the act... | Homo sapiens (Human) |
P15392 | CP2A4_MOUSE | MLTSGLLLVAAVAFLSVLVLMSVWKQRKLSGKLPPGPTPLPFVGNFLQLNTEQMYNSLMKISQRYGPVFTIYLGSRRIVVLCGQETVKEALVDQAEEFSGRGEQATFDWLFKGYGIAFSSGERAKQLRRFSITTLRDFGVGKRGIEERIQEEAGFLIDSFRKTNGAFIDPTFYLSRTVSNVISSIVFGDRFDYEDKEFLSLLRMMLGSLQFTATSMGQVYEMFSSVMKHLPGPQQQAFKELQGLEDFITKKVEHNQRTLDPNSPRDFIDSFLIRMLEEKKNPNTEFYMKNLVLTTLNLFFAGTETVSTTLRYGFLLLMKY... | 1.14.14.1 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250}; | coumarin metabolic process [GO:0009804]; epoxygenase P450 pathway [GO:0019373]; response to stilbenoid [GO:0035634]; xenobiotic metabolic process [GO:0006805] | cytoplasm [GO:0005737]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231] | arachidonic acid epoxygenase activity [GO:0008392]; aromatase activity [GO:0070330]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen, reduced flavin or flavoprotein as one donor, and incorporation of one atom... | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Peripheral membrane protein. Microsome membrane; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57... | null | null | null | null | FUNCTION: Highly active in the 15-alpha-hydroxylation of testosterone. Also active in the 15-alpha-hydroxylation of progesterone and androstenedione. Little or no activity on corticosterone, pregnenolone, dehydroepiandrosterone, estradiol or estriol. | Mus musculus (Mouse) |
P15393 | C11B1_RAT | MALRVTADVWLARPWQCLHRTRALGTTAKVAPKTLKPFEAIPQYSRNKWLKMIQILREQGQENLHLEMHQAFQELGPIFRHSAGGAQIVSVMLPEDAEKLHQVESILPHRMPLEPWVAHRELRGLRRGVFLLNGADWRFNRLQLNPNMLSPKAIQSFVPFVDVVARDFVENLKKRMLENVHGSMSINIQSNMFNYTMEASHFVISGERLGLTGHDLKPESVTFTHALHSMFKSTTQLMFLPKSLTRWTSTRVWKEHFDSWDIISEYVTKCIKNVYRELAEGRQQSWSVISEMVAQSTLSMDAIHANSMELIAGSVDTTAI... | 1.14.15.4 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P19099}; | adenosine metabolic process [GO:0046085]; aldosterone biosynthetic process [GO:0032342]; cellular response to peptide hormone stimulus [GO:0071375]; cellular response to type II interferon [GO:0071346]; cholesterol metabolic process [GO:0008203]; cortisol biosynthetic process [GO:0034651]; cortisol metabolic process [G... | mitochondrial inner membrane [GO:0005743] | corticosterone 18-monooxygenase activity [GO:0047783]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; steroid 11-beta-monooxygenase activity [GO:0004507]; steroid binding [GO:0005496] | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:P14137}; Peripheral membrane protein {ECO:0000250|UniProtKB:P14137}. | CATALYTIC ACTIVITY: Reaction=a steroid + 2 H(+) + O2 + 2 reduced [adrenodoxin] = an 11beta-hydroxysteroid + H2O + 2 oxidized [adrenodoxin]; Xref=Rhea:RHEA:15629, Rhea:RHEA-COMP:9998, Rhea:RHEA-COMP:9999, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:35341, Ch... | null | PATHWAY: Steroid biosynthesis; glucocorticoid biosynthesis. {ECO:0000250|UniProtKB:P15538}.; PATHWAY: Steroid hormone biosynthesis. {ECO:0000250|UniProtKB:P15538}. | null | null | FUNCTION: A cytochrome P450 monooxygenase involved in the biosynthesis of adrenal corticoids (PubMed:1562515, PubMed:1765101, PubMed:2738055). Catalyzes a variety of reactions that are essential for many species, including detoxification, defense, and the formation of endogenous chemicals like steroid hormones (By simi... | Rattus norvegicus (Rat) |
P15396 | ENPP3_BOVIN | MQSTLNLSTEEPVKRNTVKKYKIICIVLLILLVAVSLALGLVAGLRQQEEQGSCRKKCFDASHRGLEGCRCDVGCKGRGDCCWDFEDTCVQSTQIWTCNKFRCGETRLESSLCSCSDDCLQRKDCCADYKSVCQGETSWVDEDCSTAQQPQCPEGFDLPPVILFSMDGFRAEYLQTWSTLVPNINKLKTCGVHSQYLRPAYPTKTFPNHYTIVTGLYPESHGIIDNNMYDINLNKNFSLSSKEKDNPAWWQGQPIWLTAMYQGLKVGTYFWPGSDVAINGTFPSIYKIYNRSVTYEERIFTLLKWLDLPKAERPDFYTIY... | 3.1.4.1; 3.6.1.9 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250|UniProtKB:O14638}; Note=Binds 2 zinc ions per subunit. {ECO:0000250|UniProtKB:O14638}; | ATP metabolic process [GO:0046034]; basophil activation involved in immune response [GO:0002276]; negative regulation of inflammatory response [GO:0050728]; negative regulation of mast cell activation involved in immune response [GO:0033007]; negative regulation of mast cell proliferation [GO:0070667]; nucleoside triph... | apical plasma membrane [GO:0016324]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; nucleic acid binding [GO:0003676]; nucleoside triphosphate diphosphatase activity [GO:0047429]; phosphodiesterase I activity [GO:0004528]; zinc ion binding [GO:0008270] | PF01663;PF01033; | 4.10.410.20;3.40.720.10;3.40.570.10; | Nucleotide pyrophosphatase/phosphodiesterase family | PTM: N-glycosylated. N-glycosylation is necessary for normal transport to the cell membrane, but is not the apical targeting signal. {ECO:0000250|UniProtKB:P97675}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:O14638}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O14638}. Apical cell membrane {ECO:0000250|UniProtKB:O14638}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:O14638}. Secreted {ECO:0000250|UniProtKB:O14638}. Note=Detected at the... | CATALYTIC ACTIVITY: Reaction=Hydrolytically removes 5'-nucleotides successively from the 3'-hydroxy termini of 3'-hydroxy-terminated oligonucleotides.; EC=3.1.4.1; Evidence={ECO:0000250|UniProtKB:O14638}; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-phosphate + diphosphate +... | null | null | null | null | FUNCTION: Hydrolase that metabolizes extracellular nucleotides, including ATP, GTP, UTP and CTP (By similarity). Limits mast cell and basophil responses during inflammation and during the chronic phases of allergic responses by eliminating the extracellular ATP that functions as signaling molecule and activates basophi... | Bos taurus (Bovine) |
P15407 | FOSL1_HUMAN | MFRDFGEPGPSSGNGGGYGGPAQPPAAAQAAQQKFHLVPSINTMSGSQELQWMVQPHFLGPSSYPRPLTYPQYSPPQPRPGVIRALGPPPGVRRRPCEQISPEEEERRRVRRERNKLAAAKCRNRRKELTDFLQAETDKLEDEKSGLQREIEELQKQKERLELVLEAHRPICKIPEGAKEGDTGSTSGTSSPPAPCRPVPCISLSPGPVLEPEALHTPTLMTTPSLTPFTPSLVFTYPSTPEPCASAHRKSSSSSGDPSSDPLGSPTLLAL | null | null | cellular defense response [GO:0006968]; cellular response to extracellular stimulus [GO:0031668]; chemotaxis [GO:0006935]; cytokine-mediated signaling pathway [GO:0019221]; female pregnancy [GO:0007565]; gene expression [GO:0010467]; in utero embryonic development [GO:0001701]; inflammatory response [GO:0006954]; integ... | chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; presynaptic membrane [GO:0042734]; RNA polymerase II transcription regulator complex [GO:0090575] | 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]; promoter-specific chromatin binding [GO:1990841]; RNA polymerase II cis-regulatory region seq... | PF00170; | 1.20.5.170; | BZIP family, Fos subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P51145}. | null | null | null | null | null | null | Homo sapiens (Human) |
P15408 | FOSL2_HUMAN | MYQDYPGNFDTSSRGSSGSPAHAESYSSGGGGQQKFRVDMPGSGSAFIPTINAITTSQDLQWMVQPTVITSMSNPYPRSHPYSPLPGLASVPGHMALPRPGVIKTIGTTVGRRRRDEQLSPEEEEKRRIRRERNKLAAAKCRNRRRELTEKLQAETEELEEEKSGLQKEIAELQKEKEKLEFMLVAHGPVCKISPEERRSPPAPGLQPMRSGGGSVGAVVVKQEPLEEDSPSSSSAGLDKAQRSVIKPISIAGGFYGEEPLHTPIVVTSTPAVTPGTSNLVFTYPSVLEQESPASPSESCSKAHRRSSSSGDQSSDSLNS... | null | null | alveolar secondary septum development [GO:0061144]; B cell differentiation [GO:0030183]; B cell proliferation [GO:0042100]; bone mineralization [GO:0030282]; cell death [GO:0008219]; cell morphogenesis [GO:0000902]; chondrocyte differentiation [GO:0002062]; chondrocyte proliferation [GO:0035988]; collagen biosynthetic ... | chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575] | chromatin binding [GO:0003682]; 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... | PF00170; | 1.20.5.170; | BZIP family, Fos subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P51145}. | null | null | null | null | null | FUNCTION: Controls osteoclast survival and size (By similarity). As a dimer with JUN, activates LIF transcription (By similarity). Activates CEBPB transcription in PGE2-activated osteoblasts (By similarity). {ECO:0000250|UniProtKB:P47930, ECO:0000250|UniProtKB:P51145}. | Homo sapiens (Human) |
P15409 | OPSD_MOUSE | MNGTEGPNFYVPFSNVTGVVRSPFEQPQYYLAEPWQFSMLAAYMFLLIVLGFPINFLTLYVTVQHKKLRTPLNYILLNLAVADLFMVFGGFTTTLYTSLHGYFVFGPTGCNLEGFFATLGGEIALWSLVVLAIERYVVVCKPMSNFRFGENHAIMGVVFTWIMALACAAPPLVGWSRYIPEGMQCSCGIDYYTLKPEVNNESFVIYMFVVHFTIPMIVIFFCYGQLVFTVKEAAAQQQESATTQKAEKEVTRMVIIMVIFFLICWLPYASVAFYIFTHQGSNFGPIFMTLPAFFAKSSSIYNPVIYIMLNKQFRNCMLTT... | null | null | absorption of visible light [GO:0016038]; adaptation of rhodopsin mediated signaling [GO:0016062]; cellular response to light stimulus [GO:0071482]; detection of light stimulus [GO:0009583]; detection of temperature stimulus involved in thermoception [GO:0050960]; G protein-coupled receptor signaling pathway [GO:000718... | cell-cell junction [GO:0005911]; Golgi apparatus [GO:0005794]; membrane [GO:0016020]; photoreceptor disc membrane [GO:0097381]; photoreceptor inner segment [GO:0001917]; photoreceptor inner segment membrane [GO:0060342]; photoreceptor outer segment [GO:0001750]; photoreceptor outer segment membrane [GO:0042622]; plasma... | 11-cis retinal binding [GO:0005502]; G protein-coupled photoreceptor activity [GO:0008020]; metal ion binding [GO:0046872]; retinal binding [GO:0016918]; spectrin binding [GO:0030507] | PF00001;PF10413; | 1.20.1070.10; | G-protein coupled receptor 1 family, Opsin subfamily | PTM: Phosphorylated on some or all of the serine and threonine residues present in the C-terminal region. {ECO:0000269|PubMed:11910029}.; PTM: Contains one covalently linked retinal chromophore. Upon light absorption, the covalently bound 11-cis-retinal is converted to all-trans-retinal. After hydrolysis of the Schiff ... | SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P02699}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P02699}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:15961391, ECO:0000269|PubMed:27353443, ECO:0000269|PubMed:28151698}. Note=Synthesized in the inner segment (IS) of rod photo... | null | null | null | null | null | FUNCTION: Photoreceptor required for image-forming vision at low light intensity. Required for photoreceptor cell viability after birth (PubMed:9020854). Light-induced isomerization of 11-cis to all-trans retinal triggers a conformational change that activates signaling via G-proteins. Subsequent receptor phosphorylati... | Mus musculus (Mouse) |
P15423 | SPIKE_CVH22 | MFVLLVAYALLHIAGCQTTNGLNTSYSVCNGCVGYSENVFAVESGGYIPSDFAFNNWFLLTNTSSVVDGVVRSFQPLLLNCLWSVSGLRFTTGFVYFNGTGRGDCKGFSSDVLSDVIRYNLNFEENLRRGTILFKTSYGVVVFYCTNNTLVSGDAHIPFGTVLGNFYCFVNTTIGNETTSAFVGALPKTVREFVISRTGHFYINGYRYFTLGNVEAVNFNVTTAETTDFCTVALASYADVLVNVSQTSIANIIYCNSVINRLRCDQLSFDVPDGFYSTSPIQSVELPVSIVSLPVYHKHTFIVLYVDFKPQSGGGKCFNC... | null | null | endocytosis involved in viral entry into host cell [GO:0075509]; fusion of virus membrane with host endosome membrane [GO:0039654]; fusion of virus membrane with host plasma membrane [GO:0019064]; receptor-mediated virion attachment to host cell [GO:0046813] | host cell endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0044173]; membrane [GO:0016020]; viral envelope [GO:0019031]; virion membrane [GO:0055036] | null | PF01600;PF19209;PF01601;PF19214; | 1.20.5.300;2.60.40.3130; | Alphacoronaviruses spike protein family | null | SUBCELLULAR LOCATION: Virion membrane {ECO:0000255|HAMAP-Rule:MF_04200}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04200}. Host endoplasmic reticulum-Golgi intermediate compartment membrane {ECO:0000255|HAMAP-Rule:MF_04200}; Single-pass type I membrane protein {ECO:0000255|HAMAP-Rule:MF_04200}. Not... | null | null | null | null | null | FUNCTION: S1 region attaches the virion to the cell membrane by interacting with host ANPEP/aminopeptidase N, initiating the infection. Binding to the receptor probably induces conformational changes in the S glycoprotein unmasking the fusion peptide of S2 region and activating membranes fusion. S2 region belongs to th... | Human coronavirus 229E (HCoV-229E) |
P15424 | MS116_YEAST | MLTSILIKGRTPVLASRNLLAALSNCNHITWAVSRRLYNDGNRDQRNFGRNQRNNNSNRYRNSRFNSRPRTRSREDDDEVHFDKTTFSKLIHVPKEDNSKEVTLDSLLEEGVLDKEIHKAITRMEFPGLTPVQQKTIKPILSSEDHDVIARAKTGTGKTFAFLIPIFQHLINTKFDSQYMVKAVIVAPTRDLALQIEAEVKKIHDMNYGLKKYACVSLVGGTDFRAAMNKMNKLRPNIVIATPGRLIDVLEKYSNKFFRFVDYKVLDEADRLLEIGFRDDLETISGILNEKNSKSADNIKTLLFSATLDDKVQKLANNIM... | 3.6.4.13 | null | Group I intron splicing [GO:0000372]; Group II intron splicing [GO:0000373]; maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000463]; mitochondrial RNA processing [GO:0000963]; mRNA processing [GO:0006397]; regulation of translation [GO:0006417]; RNA folding [GO:0034337]; t... | mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739]; nucleolus [GO:0005730] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; mRNA binding [GO:0003729]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724]; RNA strand annealing activity [GO:0033592] | PF00270;PF00271; | 3.40.50.300; | DEAD box helicase family, DDX18/HAS1 subfamily | null | SUBCELLULAR LOCATION: Mitochondrion matrix {ECO:0000269|PubMed:14562095, ECO:0000269|PubMed:14576278}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; | null | null | null | null | FUNCTION: ATP-dependent RNA helicase required for mitochondrial splicing of group I and II introns. Specifically involved in the ATP-dependent splicing of the bl1 intron of COB. Also required for efficient mitochondrial translation. {ECO:0000269|PubMed:12402239, ECO:0000269|PubMed:15618406, ECO:0000269|PubMed:2535893, ... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P15425 | CYPR_DROME | MKSLLNRIILCSAFLAVASGLSFTVTSRIYMDVKHNKKPVGRITFGLFGKLAPKTVANFRHICLRGINGTSYVGSRFHRVVDRFLVQGGDIVNGDGTGSISIYGDYFPDEDKALAVEHNRPGYLGMANRGPDTNGCQFYVTTVGAKWLDGKHTVFGKVLEGMDTIYAIEDVKTDTDDFPVEPVVISNCGEIPTEQFEFYPDDFNILGWIKAAGLPVTSSFCVLLIFHYFFRQLNMYC | 5.2.1.8 | null | 'de novo' protein folding [GO:0006458]; intrinsic apoptotic signaling pathway in response to endoplasmic reticulum stress [GO:0070059]; N-glycan processing [GO:0006491]; protein deglycosylation [GO:0006517]; protein folding [GO:0006457]; rhodopsin biosynthetic process [GO:0016063]; visual perception [GO:0007601] | cytoplasm [GO:0005737]; cytoplasmic vesicle [GO:0031410]; endoplasmic reticulum lumen [GO:0005788]; endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231]; membrane [GO:0016020] | cyclosporin A binding [GO:0016018]; peptidyl-prolyl cis-trans isomerase activity [GO:0003755] | PF00160; | 2.40.100.10; | Cyclophilin-type PPIase family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:1707759}; Single-pass membrane protein {ECO:0000269|PubMed:1707759}. | 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; | null | null | null | null | FUNCTION: PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. Acts on the folding of rhodopsin RH1 and RH2 (but not RH3) and is required for visual transduction. {ECO:0000269|PubMed:1707759}. | Drosophila melanogaster (Fruit fly) |
P15428 | PGDH_HUMAN | MHVNGKVALVTGAAQGIGRAFAEALLLKGAKVALVDWNLEAGVQCKAALDEQFEPQKTLFIQCDVADQQQLRDTFRKVVDHFGRLDILVNNAGVNNEKNWEKTLQINLVSVISGTYLGLDYMSKQNGGEGGIIINMSSLAGLMPVAQQPVYCASKHGIVGFTRSAALAANLMNSGVRLNAICPGFVNTAILESIEKEENMGQYIEYKDHIKDMIKYYGILDPPLIANGLITLIEDDALNGAIMKITTSKGIHFQDYDTTPFQAKTQ | 1.1.1.-; 1.1.1.141; 1.1.1.232 | null | ductus arteriosus closure [GO:0097070]; female pregnancy [GO:0007565]; kidney development [GO:0001822]; lipoxygenase pathway [GO:0019372]; negative regulation of cell cycle [GO:0045786]; ovulation [GO:0030728]; parturition [GO:0007567]; positive regulation of apoptotic process [GO:0043065]; positive regulation of vascu... | basolateral plasma membrane [GO:0016323]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleoplasm [GO:0005654] | 15-hydroxyprostaglandin dehydrogenase (NAD+) activity [GO:0016404]; identical protein binding [GO:0042802]; NAD binding [GO:0051287]; NAD+ binding [GO:0070403]; oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor [GO:0016616]; prostaglandin E receptor activity [GO:0004957] | PF00106; | 3.40.50.720; | Short-chain dehydrogenases/reductases (SDR) family | null | SUBCELLULAR LOCATION: Cytoplasm. | CATALYTIC ACTIVITY: Reaction=NAD(+) + prostaglandin E2 = 15-oxoprostaglandin E2 + H(+) + NADH; Xref=Rhea:RHEA:11876, ChEBI:CHEBI:15378, ChEBI:CHEBI:57400, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945, ChEBI:CHEBI:606564; EC=1.1.1.141; Evidence={ECO:0000269|PubMed:15044627, ECO:0000269|PubMed:15574495, ECO:0000269|PubMed:167574... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.4 uM for prostaglandin E2 {ECO:0000269|PubMed:16828555, ECO:0000269|PubMed:8086429}; KM=5.5 uM for prostaglandin E1 {ECO:0000269|PubMed:8086429}; KM=4.5 uM for prostaglandin A1 {ECO:0000269|PubMed:8086429}; KM=22 uM for prostaglandin A2 {ECO:0000269|PubMed:808642... | null | null | null | FUNCTION: Catalyzes the NAD-dependent dehydrogenation (oxidation) of a broad array of hydroxylated polyunsaturated fatty acids (mainly eicosanoids and docosanoids, including prostaglandins, lipoxins and resolvins), yielding their corresponding keto (oxo) metabolites (PubMed:10837478, PubMed:16757471, PubMed:16828555, P... | Homo sapiens (Human) |
P15429 | ENOB_RAT | MAMQKIFAREILDSRGNPTVEVDLHTAKGRFRAAVPSGASTGIYEALELRDGDKSRYLGKGVLKAVEHINKTLGPALLEKKLSVVDQEKVDKFMIELDGTENKSKFGANAILGVSLAVCKAGAAEKGVPLYRHIADLAGNPDLVLPVPAFNVINGGSHAGNKLAMQEFMILPVGASSFKEAMRIGAEVYHHLKGVIKAKYGKDATNVGDEGGFAPNILENNEALELLKTAIQAAGYPDKVVIGMDVAASEFYRNGKYDLDFKSPDDPARHISGEKLGELYKSFIKNYPVVSIEDPFDQDDWATWTSFLSGVDIQIVGDDL... | 4.2.1.11 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Mg(2+) is required for catalysis and for stabilizing the dimer.; | canonical glycolysis [GO:0061621]; glycolytic process [GO:0006096]; response to xenobiotic stimulus [GO:0009410]; skeletal muscle tissue regeneration [GO:0043403] | cytosol [GO:0005829]; membrane [GO:0016020]; phosphopyruvate hydratase complex [GO:0000015] | identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; phosphopyruvate hydratase activity [GO:0004634]; protein-containing complex binding [GO:0044877] | PF00113;PF03952; | 3.20.20.120;3.30.390.10; | Enolase family | null | SUBCELLULAR LOCATION: Cytoplasm. Note=Localized to the Z line. Some colocalization with CKM at M-band (By similarity). {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate; Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289, ChEBI:CHEBI:58702; EC=4.2.1.11; Evidence={ECO:0000269|PubMed:8594891}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:10165; Evidence={ECO:0000305|PubMed:8594891}; | null | PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5. {ECO:0000305|PubMed:8594891}. | null | null | FUNCTION: Glycolytic enzyme that catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate. Appears to have a function in striated muscle development and regeneration. {ECO:0000269|PubMed:8594891}. | Rattus norvegicus (Rat) |
P15431 | GBRB1_RAT | MWTVQNRESLGLLSFPVMVAMVCCAHSSNEPSNMSYVKETVDRLLKGYDIRLRPDFGGPPVDVGMRIDVASIDMVSEVNMDYTLTMYFQQSWKDKRLSYSGIPLNLTLDNRVADQLWVPDTYFLNDKKSFVHGVTVKNRMIRLHPDGTVLYGLRITTTAACMMDLRRYPLDEQNCTLEIESYGYTTDDIEFYWNGGEGAVTGVNKIELPQFSIVDYKMVSKKVEFTTGAYPRLSLSFRLKRNIGYFILQTYMPSTLITILSWVSFWINYDASAARVALGITTVLTMTTISTHLRETLPKIPYVKAIDIYLMGCFVFVFLA... | null | null | cellular response to histamine [GO:0071420]; central nervous system neuron development [GO:0021954]; chloride transmembrane transport [GO:1902476]; chloride transport [GO:0006821]; G protein-coupled receptor signaling pathway [GO:0007186]; gamma-aminobutyric acid signaling pathway [GO:0007214]; monoatomic ion transport... | chloride channel complex [GO:0034707]; dendrite [GO:0030425]; GABA-A receptor complex [GO:1902711]; GABA-ergic synapse [GO:0098982]; neuron projection [GO:0043005]; nuclear envelope [GO:0005635]; plasma membrane [GO:0005886]; postsynaptic specialization membrane [GO:0099634]; presynaptic active zone membrane [GO:004878... | G protein-coupled neurotransmitter receptor activity involved in regulation of presynaptic membrane potential [GO:0150047]; GABA receptor binding [GO:0050811]; GABA-A receptor activity [GO:0004890]; GABA-gated chloride ion channel activity [GO:0022851]; ligand-gated monoatomic ion channel activity [GO:0015276]; ligand-... | PF02931;PF02932; | 2.70.170.10;1.20.58.390; | Ligand-gated ion channel (TC 1.A.9) family, Gamma-aminobutyric acid receptor (TC 1.A.9.5) subfamily, GABRB1 sub-subfamily | null | SUBCELLULAR LOCATION: Postsynaptic cell membrane {ECO:0000250|UniProtKB:P08220}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P08220}. Cell membrane {ECO:0000250|UniProtKB:P08220}; Multi-pass membrane protein {ECO:0000250|UniProtKB:P08220}. | CATALYTIC ACTIVITY: Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:1977069}; | null | null | null | null | FUNCTION: Beta subunit of the heteropentameric ligand-gated chloride channel gated by gamma-aminobutyric acid (GABA), a major inhibitory neurotransmitter in the brain (PubMed:1977069). GABA-gated chloride channels, also named GABA(A) receptors (GABAAR), consist of five subunits arranged around a central pore and contai... | Rattus norvegicus (Rat) |
P15436 | DPOD_YEAST | MSEKRSLPMVDVKIDDEDTPQLEKKIKRQSIDHGVGSEPVSTIEIIPSDSFRKYNSQGFKAKDTDLMGTQLESTFEQELSQMEHDMADQEEHDLSSFERKKLPTDFDPSLYDISFQQIDAEQSVLNGIKDENTSTVVRFFGVTSEGHSVLCNVTGFKNYLYVPAPNSSDANDQEQINKFVHYLNETFDHAIDSIEVVSKQSIWGYSGDTKLPFWKIYVTYPHMVNKLRTAFERGHLSFNSWFSNGTTTYDNIAYTLRLMVDCGIVGMSWITLPKGKYSMIEPNNRVSSCQLEVSINYRNLIAHPAEGDWSHTAPLRIMSF... | 2.7.7.7; 3.1.11.- | COFACTOR: Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000269|PubMed:22119860}; Note=Binds 1 [4Fe-4S] cluster. {ECO:0000269|PubMed:22119860}; | base-excision repair, gap-filling [GO:0006287]; DNA metabolic process [GO:0006259]; DNA replication [GO:0006260]; DNA replication proofreading [GO:0045004]; DNA replication, removal of RNA primer [GO:0043137]; DNA-templated DNA replication [GO:0006261]; DNA-templated DNA replication maintenance of fidelity [GO:0045005]... | cytosol [GO:0005829]; delta DNA polymerase complex [GO:0043625]; replication fork [GO:0005657] | 3'-5'-DNA exonuclease activity [GO:0008296]; 4 iron, 4 sulfur cluster binding [GO:0051539]; DNA binding [GO:0003677]; DNA-directed DNA polymerase activity [GO:0003887]; metal ion binding [GO:0046872]; molecular adaptor activity [GO:0060090]; nucleotide binding [GO:0000166] | PF00136;PF03104;PF14260; | 2.40.50.730;1.10.132.60;1.10.287.690;3.90.1600.10;3.30.420.10; | DNA polymerase type-B family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:14562095}. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339, Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560, ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000269|PubMed:22119860}; | null | null | null | null | FUNCTION: Catalytic component of DNA polymerase delta (DNA polymerase III) which participates in chromosomal DNA replication (PubMed:22119860, PubMed:2670563, PubMed:31488849). Required during synthesis of the lagging DNA strands at the replication fork, binds at/or near replication origins and moves along DNA with the... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P15437 | AL1A1_HORSE | MSSSGTPDLPVLLTDLKFQYTKIFINNEWHDSVSGKKFPVFNPATEEKLCEVEEGDKEDVNKAVAAARQAFQIGSPWRTMDASERGRLLYKLADLVERDRLILATMESMNGGKLFSNAYLMDLGGCLKTLRYCAGWADKIQGRTIPSDGNFFTYTRHEPVGVCGQILPWNFPLLMFLWKIAPALSCGNTVVVKPAEQTPLSALHVATLIKEAGFPPGVVNIVPGYGPTAGAAISSHMDIDKVAFTGSTEVGKLIKEAAGKSNLKRVTLELGGKSPFIVFADADLETALEVTHQALFYHQGQCCVAASRLFVEESIYDEFV... | 1.2.1.19; 1.2.1.28; 1.2.1.3; 1.2.1.36 | null | cellular detoxification of aldehyde [GO:0110095]; fructosamine catabolic process [GO:0030392]; gamma-aminobutyric acid biosynthetic process [GO:0009449]; maintenance of lens transparency [GO:0036438]; retinoid metabolic process [GO:0001523]; retinol metabolic process [GO:0042572] | axon [GO:0030424]; cytosol [GO:0005829]; synapse [GO:0045202] | 3-deoxyglucosone dehydrogenase activity [GO:0106373]; aldehyde dehydrogenase (NAD+) activity [GO:0004029]; aminobutyraldehyde dehydrogenase activity [GO:0019145]; benzaldehyde dehydrogenase (NAD+) activity [GO:0018479]; glyceraldehyde-3-phosphate dehydrogenase (NAD+) (non-phosphorylating) activity [GO:0043878]; NAD bin... | PF00171; | null | Aldehyde dehydrogenase family | PTM: The N-terminus is blocked most probably by acetylation. {ECO:0000269|PubMed:6723662}. | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:P00352}. Cell projection, axon {ECO:0000250|UniProtKB:P24549}. | CATALYTIC ACTIVITY: Reaction=an aldehyde + H2O + NAD(+) = a carboxylate + 2 H(+) + NADH; Xref=Rhea:RHEA:16185, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17478, ChEBI:CHEBI:29067, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.2.1.3; Evidence={ECO:0000250|UniProtKB:P00352}; PhysiologicalDirection=left-to-right; Xref... | null | PATHWAY: Cofactor metabolism; retinol metabolism. {ECO:0000250|UniProtKB:P51647}. | null | null | FUNCTION: Cytosolic dehydrogenase that catalyzes the irreversible oxidation of a wide range of aldehydes to their corresponding carboxylic acid (By similarity). Functions downstream of retinol dehydrogenases and catalyzes the oxidation of retinaldehyde into retinoic acid, the second step in the oxidation of retinol/vit... | Equus caballus (Horse) |
P15442 | GCN2_YEAST | MSLSHLTLDQYYEIQCNELEAIRSIYMDDFTDLTKRKSSWDKQPQIIFEITLRSVDKEPVESSITLHFAMTPMYPYTAPEIEFKNVQNVMDSQLQMLKSEFKKIHNTSRGQEIIFEITSFTQEKLDEFQNVVNTQSLEDDRLQRIKETKEQLEKEEREKQQETIKKRSDEQRRIDEIVQRELEKRQDDDDDLLFNRTTQLDLQPPSEWVASGEAIVFSKTIKAKLPNNSMFKFKAVVNPKPIKLTSDIFSFSKQFLVKPYIPPESPLADFLMSSEMMENFYYLLSEIELDNSYFNTSNGKKEIANLEKELETVLKAKHDN... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:17202131}; | cellular response to amino acid starvation [GO:0034198]; cellular response to histidine [GO:0071232]; DNA damage checkpoint signaling [GO:0000077]; GCN2-mediated signaling [GO:0140469]; intracellular signal transduction [GO:0035556]; negative regulation of cytoplasmic translational initiation in response to stress [GO:... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; cytosolic ribosome [GO:0022626]; large ribosomal subunit [GO:0015934]; nucleus [GO:0005634]; small ribosomal subunit [GO:0015935] | ATP binding [GO:0005524]; double-stranded RNA binding [GO:0003725]; eukaryotic translation initiation factor 2alpha kinase activity [GO:0004694]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; protein kinase inhibitor activity [GO:0004860]; protein self-association [GO:0043621]; p... | PF12745;PF00069;PF05773;PF13393; | 3.40.50.800;1.10.510.10;3.10.110.10; | Protein kinase superfamily, Ser/Thr protein kinase family, GCN2 subfamily | PTM: Autophosphorylated, autophosphorylation on Thr-882 and Thr-887 increases kinase activity. {ECO:0000269|PubMed:10983975, ECO:0000269|PubMed:17202131, ECO:0000269|PubMed:2038314, ECO:0000269|PubMed:2188100, ECO:0000269|PubMed:8798780, ECO:0000269|PubMed:9528799}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:2038314}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:10983975, ECO:000026... | null | null | null | null | FUNCTION: Metabolic-stress sensing protein kinase that phosphorylates the alpha subunit of eukaryotic translation initiation factor 2 (eIF-2-alpha/SUI2) on 'Ser-52' in response to low amino acid, carbon, or purine availability (PubMed:10733573, PubMed:10983975, PubMed:17202131, PubMed:1739968, PubMed:33338396, PubMed:7... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P15445 | PA2A2_NAJNA | NLYQFKNMIKCTVPSRSWWDFADYGCYCGRGGSGTPVDDLDRCCQVHDNCYNEAEKISGCWPYFKTYSYECSQGTLTCKGDNNACAASVCDCDRLAAICFAGAPYNDNNYNIDLKARCQ | 3.1.1.4 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000305|PubMed:8419939}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000305|PubMed:8419939}; | arachidonic acid secretion [GO:0050482]; fatty acid biosynthetic process [GO:0006633]; lipid catabolic process [GO:0016042]; phospholipid metabolic process [GO:0006644]; positive regulation of fibroblast proliferation [GO:0048146] | extracellular region [GO:0005576] | calcium ion binding [GO:0005509]; calcium-dependent phospholipase A2 activity [GO:0047498]; phospholipid binding [GO:0005543]; signaling receptor binding [GO:0005102] | PF00068; | 1.20.90.10; | Phospholipase A2 family, Group I subfamily, D49 sub-subfamily | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20203422}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+); Xref=Rhea:RHEA:15801, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28868, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168; EC=3.1.1.4; Evidence={ECO:0000255|PROSITE-ProRule:PRU10035, ECO:0... | null | null | null | null | FUNCTION: PLA2 catalyzes the calcium-dependent hydrolysis of the 2-acyl groups in 3-sn-phosphoglycerides. | Naja naja (Indian cobra) |
P15454 | KGUA_YEAST | MSRPIVISGPSGTGKSTLLKKLFAEYPDSFGFSVSSTTRTPRAGEVNGKDYNFVSVDEFKSMIKNNEFIEWAQFSGNYYGSTVASVKQVSKSGKTCILDIDMQGVKSVKAIPELNARFLFIAPPSVEDLKKRLEGRGTETEESINKRLSAAQAELAYAETGAHDKVIVNDDLDKAYKELKDFIFAEK | 2.7.4.8 | null | GDP biosynthetic process [GO:0046711]; phosphorylation [GO:0016310]; purine nucleotide metabolic process [GO:0006163] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | ATP binding [GO:0005524]; guanylate kinase activity [GO:0004385] | PF00625; | 3.30.63.10;3.40.50.300; | Guanylate kinase family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + GMP = ADP + GDP; Xref=Rhea:RHEA:20780, ChEBI:CHEBI:30616, ChEBI:CHEBI:58115, ChEBI:CHEBI:58189, ChEBI:CHEBI:456216; EC=2.7.4.8; Evidence={ECO:0000269|PubMed:1334480}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20781; Evidence={ECO:0000305|PubMed:1334480}; | null | null | null | null | FUNCTION: Catalyzes the reversible transfer of the terminal phosphoryl group of ATP to the acceptor molecule GMP. Essential for recycling GMP and indirectly, cGMP. {ECO:0000305|PubMed:1334480}. | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P15455 | CRU1_ARATH | MARVSSLLSFCLTLLILFHGYAAQQGQQGQQFPNECQLDQLNALEPSHVLKSEAGRIEVWDHHAPQLRCSGVSFARYIIESKGLYLPSFFNTAKLSFVAKGRGLMGKVIPGCAETFQDSSEFQPRFEGQGQSQRFRDMHQKVEHIRSGDTIATTPGVAQWFYNDGQEPLVIVSVFDLASHQNQLDRNPRPFYLAGNNPQGQVWLQGREQQPQKNIFNGFGPEVIAQALKIDLQTAQQLQNQDDNRGNIVRVQGPFGVIRPPLRGQRPQEEEEEEGRHGRHGNGLEETICSARCTDNLDDPSRADVYKPQLGYISTLNSYD... | null | null | cellular response to abscisic acid stimulus [GO:0071215]; response to abscisic acid [GO:0009737]; seed maturation [GO:0010431] | protein storage vacuole [GO:0000326] | nutrient reservoir activity [GO:0045735] | PF00190; | 2.60.120.10; | 11S seed storage protein (globulins) family | PTM: Phosphorylated in seeds on some Tyr residues in response to abscisic acid (ABA). {ECO:0000269|PubMed:17313365, ECO:0000269|PubMed:18768909}.; PTM: Proteolytically processed during seed maturation at a conserved Asn-Gly peptide bond by an asparaginyl endopeptidase to produce two mature polypeptides referred to as a... | SUBCELLULAR LOCATION: Protein storage vacuole {ECO:0000305}. | null | null | null | null | null | FUNCTION: Seed storage protein. | Arabidopsis thaliana (Mouse-ear cress) |
P15456 | CRU2_ARATH | MGRVSSIISFSLTLLILFNGYTAQQWPNECQLDQLNALEPSQIIKSEGGRIEVWDHHAPQLRCSGFAFERFVIEPQGLFLPTFLNAGKLTFVVHGRGLMGRVIPGCAETFMESPVFGEGQGQGQSQGFRDMHQKVEHLRCGDTIATPSGVAQWFYNNGNEPLILVAAADLASNQNQLDRNLRPFLIAGNNPQGQEWLQGRKQQKQNNIFNGFAPEILAQAFKINVETAQQLQNQQDNRGNIVKVNGPFGVIRPPLRRGEGGQQPHEIANGLEETLCTMRCTENLDDPSDADVYKPSLGYISTLNSYNLPILRLLRLSALR... | null | null | cellular response to abscisic acid stimulus [GO:0071215]; response to abscisic acid [GO:0009737]; seed maturation [GO:0010431] | protein storage vacuole [GO:0000326] | nutrient reservoir activity [GO:0045735] | PF00190; | 2.60.120.10; | 11S seed storage protein (globulins) family | PTM: Ubiquitinated. {ECO:0000250}.; PTM: Proteolytically processed during seed maturation at a conserved Asn-Gly peptide bond by an asparaginyl endopeptidase to produce two mature polypeptides referred to as alpha and beta subunits that are joined together by a disulfide bond.; PTM: Phosphorylated in seeds on some Tyr ... | SUBCELLULAR LOCATION: Protein storage vacuole {ECO:0000305}. | null | null | null | null | null | FUNCTION: Seed storage protein. | Arabidopsis thaliana (Mouse-ear cress) |
P15473 | IBP3_RAT | MHPARPALWAAALTALTLLRGPPVARAGAGAVGAGPVVRCEPCDARALAQCAPPPTAPACTELVREPGCGCCLTCALREGDACGVYTERCGTGLRCQPRPAEQYPLKALLNGRGFCANASAASNLSAYLPSQPSPGNTTESEEDHNAGSVESQVVPSTHRVTDSKFHPLHSKMEVIIKGQARDSQRYKVDYESQSTDTQNFSSESKRETEYGPCRREMEDTLNHLKFLNVLSPRGVHIPNCDKKGFYKKKQCRPSKGRKRGFCWCVDKYGQPLPGYDTKGKDDVHCLSVQSQ | null | null | apoptotic process [GO:0006915]; cellular response to estradiol stimulus [GO:0071392]; cellular response to Thyroglobulin triiodothyronine [GO:1904017]; female pregnancy [GO:0007565]; MAPK cascade [GO:0000165]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of protein phosphorylat... | extracellular space [GO:0005615]; heterochromatin [GO:0000792]; insulin-like growth factor binary complex [GO:0042568]; insulin-like growth factor ternary complex [GO:0042567]; nucleus [GO:0005634]; platelet alpha granule [GO:0031091] | fibronectin binding [GO:0001968]; insulin-like growth factor binding [GO:0005520]; insulin-like growth factor I binding [GO:0031994]; insulin-like growth factor II binding [GO:0031995]; protein tyrosine phosphatase activator activity [GO:0008160] | PF00219;PF00086; | 4.10.40.20;4.10.800.10; | null | PTM: Phosphorylated by FAM20C in the extracellular medium. {ECO:0000250|UniProtKB:P17936}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: IGF-binding proteins prolong the half-life of the IGFs and have been shown to either inhibit or stimulate the growth promoting effects of the IGFs on cell culture. They alter the interaction of IGFs with their cell surface receptors. Also exhibits IGF-independent antiproliferative and apoptotic effects mediat... | Rattus norvegicus (Rat) |
P15474 | AROQ_STRCO | MPRSLANAPIMILNGPNLNLLGQRQPEIYGSDTLADVEALCVKAAAAHGGTVDFRQSNHEGELVDWIHEARLNHCGIVINPAAYSHTSVAILDALNTCDGLPVVEVHISNIHQREPFRHHSYVSQRADGVVAGCGVQGYVFGVERIAALAGAGSARA | 4.2.1.10 | null | amino acid biosynthetic process [GO:0008652]; aromatic amino acid family biosynthetic process [GO:0009073]; chorismate biosynthetic process [GO:0009423]; quinate catabolic process [GO:0019631] | null | 3-dehydroquinate dehydratase activity [GO:0003855] | PF01220; | 3.40.50.9100; | Type-II 3-dehydroquinase family | null | null | CATALYTIC ACTIVITY: Reaction=3-dehydroquinate = 3-dehydroshikimate + H2O; Xref=Rhea:RHEA:21096, ChEBI:CHEBI:15377, ChEBI:CHEBI:16630, ChEBI:CHEBI:32364; EC=4.2.1.10; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1100 uM for 3-dehydroquinate (at pH 8 and 25 degrees Celsius); | PATHWAY: Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7. | null | null | FUNCTION: Catalyzes a trans-dehydration via an enolate intermediate. {ECO:0000250}. | Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) |
P15480 | POLS_IBDVC | MTNLQDQTQQIVPFIRSLLMPTTGPASIPDDTLEKHTLRSETSTYNLTVGDTGSGLIVFFPGFPGSIVGAHYTLQSNGNYKFDQMLLTAQNLPASYNYCRLVSRSLTVRSSTLPGGVYALNGTINAVTFQGSLSELTDVSYNGLMSATANINDKIGNVLVGEGVTVLSLPTSYDLGYVRLGDPIPAIGLDPKMVATCDSSDRPRVYTITAADDYQFSSQYQPGGVTITLFSANIDAITSLSVGGELVFQTSVHGLVLGATIYLIGFDGTTVITRAVAANNGLTTGTDNLMPFNLVISTNEITQPITSIKLEIVTSKSGGQ... | 3.4.21.- | null | proteolysis [GO:0006508] | host cell cytoplasm [GO:0030430]; T=13 icosahedral viral capsid [GO:0039621] | metal ion binding [GO:0046872]; serine-type peptidase activity [GO:0008236]; structural molecule activity [GO:0005198] | PF01766;PF01767;PF01768; | 2.60.120.20;6.10.250.1030;1.10.8.880;1.10.150.620;2.60.120.660; | null | PTM: Specific enzymatic cleavages yield mature proteins. The capsid assembly seems to be regulated by polyprotein processing. The protease VP4 cleaves itself off the polyprotein, thus releasing pre-VP2 and VP3 within the infected cell. During capsid assembly, the C-terminus of pre-VP2 is further processed by VP4, givin... | SUBCELLULAR LOCATION: [Capsid protein VP2]: Virion {ECO:0000305}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Capsid protein VP3]: Virion {ECO:0000305}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Structural peptide 1]: Virion {ECO:0000305}. Host cytoplasm {ECO:0000305}.; SUBCELLULAR LOCATION: [Stru... | null | null | null | null | null | FUNCTION: Capsid protein VP2 self assembles to form an icosahedral capsid with a T=13 symmetry, about 70 nm in diameter, and consisting of 260 VP2 trimers. The capsid encapsulates the genomic dsRNA. VP2 is also involved in attachment and entry into the host cell by interacting with host ITGA4/ITGB1 (By similarity). {EC... | Avian infectious bursal disease virus (strain Cu-1) (IBDV) (Gumboro disease virus) |
P15493 | LIP_VIBCH | MNKIIILIALSLFSSSIWAGTSAHALSQQGYTQTRYPIVLVHGLFGFDTLAGMDYFHGIPQSLTRDGAQVYVAQVSATNSSERRGEQLLAQVESLLAVTGAKKVNLIGHSHGGPTIRYVASVRPDLVASVTSIGGVHKGSAVADLVRGVIPSGSVSEQVAVGLTQGLVALIDLLSGGKAHPQDPLASLAALTTEGSLKFNQYYPEGVPTSACGEGAYQVNGVRYYSWSGAATVTNILDPSDVAMGLIGLVFNEPNDGLVATCSTHLGKVIRDDYRMNHLDEINGLLGIHSLFETDPVTLYRQHANRLKQAGL | 3.1.1.3 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P26876}; Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P26876}; | lipid catabolic process [GO:0016042] | extracellular region [GO:0005576] | metal ion binding [GO:0046872]; triglyceride lipase activity [GO:0004806] | PF00561; | 3.40.50.1820; | AB hydrolase superfamily, Pseudomonas lipase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P26876}. | CATALYTIC ACTIVITY: Reaction=a triacylglycerol + H2O = a diacylglycerol + a fatty acid + H(+); Xref=Rhea:RHEA:12044, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17855, ChEBI:CHEBI:18035, ChEBI:CHEBI:28868; EC=3.1.1.3; Evidence={ECO:0000250|UniProtKB:P26876}; | null | null | null | null | FUNCTION: Catalyzes the hydrolysis of triacylglycerol. {ECO:0000269|PubMed:9371455, ECO:0000305|PubMed:8817490}. | Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) |
P15496 | IDI1_YEAST | MTADNNSMPHGAVSSYAKLVQNQTPEDILEEFPEIIPLQQRPNTRSSETSNDESGETCFSGHDEEQIKLMNENCIVLDWDDNAIGAGTKKVCHLMENIEKGLLHRAFSVFIFNEQGELLLQQRATEKITFPDLWTNTCCSHPLCIDDELGLKGKLDDKIKGAITAAVRKLDHELGIPEDETKTRGKFHFLNRIHYMAPSNEPWGEHEIDYILFYKINAKENLTVNPNVNEVRDFKWVSPNDLKTMFADPSYKFTPWFKIICENYLFNWWEQLDDLSEVENDRQIHRML | 5.3.3.2 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q46822}; Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q46822}; | dimethylallyl diphosphate biosynthetic process [GO:0050992]; ergosterol biosynthetic process [GO:0006696]; farnesyl diphosphate biosynthetic process [GO:0045337]; isopentenyl diphosphate biosynthetic process [GO:0009240] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634]; vacuole [GO:0005773] | isopentenyl-diphosphate delta-isomerase activity [GO:0004452]; metal ion binding [GO:0046872] | PF00293; | 3.90.79.10; | IPP isomerase type 1 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=isopentenyl diphosphate = dimethylallyl diphosphate; Xref=Rhea:RHEA:23284, ChEBI:CHEBI:57623, ChEBI:CHEBI:128769; EC=5.3.3.2; Evidence={ECO:0000269|PubMed:2223785, ECO:0000269|PubMed:2681212, ECO:0000269|PubMed:7908830}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23285; Evidence={... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=43 uM for isopentenyl-diphosphate {ECO:0000269|PubMed:7908830}; Vmax=20 umol/min/mg enzyme {ECO:0000269|PubMed:7908830}; | PATHWAY: Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from isopentenyl diphosphate: step 1/1. {ECO:0000269|PubMed:2223785, ECO:0000269|PubMed:2681212, ECO:0000269|PubMed:7908830}. | null | null | FUNCTION: Isopentenyl-diphosphate delta-isomerase; part of the second module of ergosterol biosynthesis pathway that includes the middle steps of the pathway (PubMed:2223785, PubMed:2681212, PubMed:7908830). IDI1 catalyzes the 1,3-allylic rearrangement of isopentenyl (IPP) to its highly electrophilic allylic isomer, di... | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
P15497 | APOA1_BOVIN | MKAVVLTLAVLFLTGSQARHFWQQDDPQSSWDRVKDFATVYVEAIKDSGRDYVAQFEASALGKQLNLKLLDNWDTLASTLSKVREQLGPVTQEFWDNLEKETASLRQEMHKDLEEVKQKVQPYLDEFQKKWHEEVEIYRQKVAPLGEEFREGARQKVQELQDKLSPLAQELRDRARAHVETLRQQLAPYSDDLRQRLTARLEALKEGGGSLAEYHAKASEQLKALGEKAKPVLEDLRQGLLPVLESLKVSILAAIDEASKKLNAQ | null | null | acylglycerol homeostasis [GO:0055090]; cholesterol efflux [GO:0033344]; cholesterol metabolic process [GO:0008203]; lipoprotein metabolic process [GO:0042157]; peptidyl-methionine modification [GO:0018206]; phosphatidylcholine metabolic process [GO:0046470]; phospholipid efflux [GO:0033700]; positive regulation of chol... | chylomicron [GO:0042627]; extracellular vesicle [GO:1903561]; high-density lipoprotein particle [GO:0034364]; low-density lipoprotein particle [GO:0034362]; very-low-density lipoprotein particle [GO:0034361] | cholesterol transfer activity [GO:0120020]; high-density lipoprotein particle receptor binding [GO:0070653]; phosphatidylcholine-sterol O-acyltransferase activator activity [GO:0060228]; phospholipid binding [GO:0005543]; protein homodimerization activity [GO:0042803] | PF01442; | 1.20.5.20;6.10.140.380;1.20.120.20; | Apolipoprotein A1/A4/E family | PTM: Glycosylated. {ECO:0000250}.; PTM: Palmitoylated. {ECO:0000250}.; PTM: Phosphorylation sites are present in the extracellular medium. {ECO:0000250}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility. | Bos taurus (Bovine) |
P15498 | VAV_HUMAN | MELWRQCTHWLIQCRVLPPSHRVTWDGAQVCELAQALRDGVLLCQLLNNLLPHAINLREVNLRPQMSQFLCLKNIRTFLSTCCEKFGLKRSELFEAFDLFDVQDFGKVIYTLSALSWTPIAQNRGIMPFPTEEESVGDEDIYSGLSDQIDDTVEEDEDLYDCVENEEAEGDEIYEDLMRSEPVSMPPKMTEYDKRCCCLREIQQTEEKYTDTLGSIQQHFLKPLQRFLKPQDIEIIFINIEDLLRVHTHFLKEMKEALGTPGAANLYQVFIKYKERFLVYGRYCSQVESASKHLDRVAAAREDVQMKLEECSQRANNGRF... | null | null | cell migration [GO:0016477]; cellular response to xenobiotic stimulus [GO:0071466]; Fc-epsilon receptor signaling pathway [GO:0038095]; Fc-gamma receptor signaling pathway involved in phagocytosis [GO:0038096]; G protein-coupled receptor signaling pathway [GO:0007186]; immune response [GO:0006955]; integrin-mediated si... | cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; plasma membrane [GO:0005886] | guanyl-nucleotide exchange factor activity [GO:0005085]; metal ion binding [GO:0046872]; phosphorylation-dependent protein binding [GO:0140031]; phosphotyrosine residue binding [GO:0001784] | PF00130;PF11971;PF00169;PF00621;PF00017;PF00018; | 3.30.60.20;1.10.418.10;1.20.900.10;2.30.29.30;3.30.505.10;2.30.30.40; | null | PTM: Phosphorylated on tyrosine residues by HCK in response to IFNG and bacterial lipopolysaccharide (LPS) (By similarity). Phosphorylated by FYN. {ECO:0000250, ECO:0000269|PubMed:11005864}. | null | null | null | null | null | null | FUNCTION: Couples tyrosine kinase signals with the activation of the Rho/Rac GTPases, thus leading to cell differentiation and/or proliferation. | Homo sapiens (Human) |
P15499 | PRPH2_MOUSE | MALLKVKFDQKKRVKLAQGLWLMNWLSVLAGIVLFSLGLFLKIELRKRSEVMNNSESHFVPNSLIGVGVLSCVFNSLAGKICYDALDPAKYAKWKPWLKPYLAVCIFFNVILFLVALCCFLLRGSLESTLAYGLKNGMKYYRDTDTPGRCFMKKTIDMLQIEFKCCGNNGFRDWFEIQWISNRYLDFSSKEVKDRIKSNVDGRYLVDGVPFSCCNPSSPRPCIQYQLTNNSAHYSYDHQTEELNLWLRGCRAALLNYYSSLMNSMGVVTLLVWLFEVSITAGLRYLHTALESVSNPEDPECESEGWLLEKSVPETWKAFL... | null | null | cell adhesion [GO:0007155]; detection of light stimulus involved in visual perception [GO:0050908]; photoreceptor cell outer segment organization [GO:0035845]; protein heterooligomerization [GO:0051291]; protein homooligomerization [GO:0051260]; protein localization to plasma membrane [GO:0072659]; protein maturation [... | membrane [GO:0016020]; photoreceptor inner segment [GO:0001917]; photoreceptor outer segment [GO:0001750] | protein homodimerization activity [GO:0042803] | PF00335; | 1.10.1450.10; | PRPH2/ROM1 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000250|UniProtKB:P17810}; Multi-pass membrane protein {ECO:0000255}. Cell projection, cilium, photoreceptor outer segment {ECO:0000269|PubMed:10802659, ECO:0000269|PubMed:17260955, ECO:0000269|PubMed:26406599, ECO:0000269|PubMed:29961824}. Photoreceptor inner segment {ECO:0000269|Pu... | null | null | null | null | null | FUNCTION: Essential for retina photoreceptor outer segment disk morphogenesis, may also play a role with ROM1 in the maintenance of outer segment disk structure (PubMed:6715580). Required for the maintenance of retinal outer nuclear layer thickness (PubMed:29961824, PubMed:6715580). Required for the correct development... | Mus musculus (Mouse) |
P15502 | ELN_HUMAN | MAGLTAAAPRPGVLLLLLSILHPSRPGGVPGAIPGGVPGGVFYPGAGLGALGGGALGPGGKPLKPVPGGLAGAGLGAGLGAFPAVTFPGALVPGGVADAAAAYKAAKAGAGLGGVPGVGGLGVSAGAVVPQPGAGVKPGKVPGVGLPGVYPGGVLPGARFPGVGVLPGVPTGAGVKPKAPGVGGAFAGIPGVGPFGGPQPGVPLGYPIKAPKLPGGYGLPYTTGKLPYGYGPGGVAGAAGKAGYPTGTGVGPQAAAAAAAKAAAKFGAGAAGVLPGVGGAGVPGVPGAIPGIGGIAGVGTPAAAAAAAAAAKAAKYGAAA... | null | null | animal organ morphogenesis [GO:0009887]; aortic valve morphogenesis [GO:0003180]; blood circulation [GO:0008015]; extracellular matrix assembly [GO:0085029]; outflow tract morphogenesis [GO:0003151]; regulation of actin filament polymerization [GO:0030833]; regulation of smooth muscle cell proliferation [GO:0048660]; r... | collagen-containing extracellular matrix [GO:0062023]; elastic fiber [GO:0071953]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576] | extracellular matrix binding [GO:0050840]; extracellular matrix constituent conferring elasticity [GO:0030023]; extracellular matrix structural constituent [GO:0005201] | null | null | Elastin family | PTM: Elastin is formed through the cross-linking of its soluble precursor tropoelastin. Cross-linking is initiated through the action of lysyl oxidase on exposed lysines to form allysine. Subsequent spontaneous condensation reactions with other allysine or unmodified lysine residues result in various bi-, tri-, and tet... | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:17035250}. Note=Extracellular matrix of elastic fibers. {ECO:0000269|PubMed:17035250}. | null | null | null | null | null | FUNCTION: Major structural protein of tissues such as aorta and nuchal ligament, which must expand rapidly and recover completely. Molecular determinant of the late arterial morphogenesis, stabilizing arterial structure by regulating proliferation and organization of vascular smooth muscle (By similarity). {ECO:0000250... | Homo sapiens (Human) |
P15505 | GCSP_CHICK | MQSCGRWWGRLAARGAPRHLRPAAGGPRRQQQRWGGGEAARCIEQLLPRHDDFCRRHIGPREREKREMLSAVGVQSVEELMDKTIPASIRLRRPLRMDDHVVENEILETLYNIASKNKIWRSYIGMGYYNCSVPQPIARNLLENAGWVTQYTPYQPEVSQGRLESLLNYQTMVCDITGMDVANASLLDEGTAAAEAMQLCHRQNKRRKFYIDARCHPQTIANYTGVITELKLPHEMDFSGKDVSGVLFQYPDTEGKVEDFSELIERAHQNGTLACCATDLLALCILKPPGEFGVDVVLGSSQRFGVPLCYGGPHAAFFAV... | 1.4.4.2 | COFACTOR: Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; Evidence={ECO:0000269|PubMed:7440562}; | glycine catabolic process [GO:0006546]; glycine decarboxylation via glycine cleavage system [GO:0019464]; response to lipoic acid [GO:1903442]; response to methylamine [GO:0036255] | cytosol [GO:0005829]; glycine cleavage complex [GO:0005960]; mitochondrion [GO:0005739] | glycine binding [GO:0016594]; glycine dehydrogenase (decarboxylating) activity [GO:0004375]; glycine dehydrogenase activity [GO:0047960]; lyase activity [GO:0016829]; protein homodimerization activity [GO:0042803]; pyridoxal binding [GO:0070280]; pyridoxal phosphate binding [GO:0030170] | PF01212;PF21478;PF02347; | 3.90.1150.10;3.40.640.10; | GcvP family | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:7440562}. | CATALYTIC ACTIVITY: Reaction=glycine + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage complex H protein] = CO2 + N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-L-lysyl-[glycine-cleavage complex H protein]; Xref=Rhea:RHEA:24304, Rhea:RHEA-COMP:10494, Rhea:RHEA-COMP:10495, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=20 mM for glycine in presence of GCSH {ECO:0000269|PubMed:7440563}; KM=27 mM for methylamine in presence of GCSH {ECO:0000269|PubMed:7440563}; KM=40 mM for glycine {ECO:0000269|PubMed:7440562}; KM=3.5 mM for lipoic acid {ECO:0000269|PubMed:7440562}; KM=63 mM for me... | null | null | null | FUNCTION: The glycine cleavage system catalyzes the degradation of glycine. The P protein (GLDC) binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein (GCSH). {ECO:0000269|Pub... | Gallus gallus (Chicken) |
P15508 | SPTB1_MOUSE | MTSATEFENVGNQPPFSRINARWDAPDDELDNDNSSARLFERSRIKALADEREVVQKKTFTKWVNSHLARVSCRISDLYKDLRDGRMLIKLLEVLSGEMLPRPTKGKMRIHCLENVDKALQFLKEQRVHLENMGSHDIVDGNHRLVLGLIWTIILRFQIQDIVVQTQEGREQRSAKDALLLWCQMKTAGYPHVNVTNFTSSWKDGLAFNALIHKHRPDLIDFDKLKDSNARHNLEHAFDVAERQLGIIPLLDPEDVFTENPDEKSIITYVVAFYHYFSKMKVLAVEGKRVGKVIDHAIETEKMIEKYSGLASDLLTWIEQ... | null | null | actin cytoskeleton organization [GO:0030036]; actin filament capping [GO:0051693]; hemopoiesis [GO:0030097]; plasma membrane organization [GO:0007009]; porphyrin-containing compound biosynthetic process [GO:0006779] | cell junction [GO:0030054]; cell projection [GO:0042995]; cortical actin cytoskeleton [GO:0030864]; cortical cytoskeleton [GO:0030863]; glutamatergic synapse [GO:0098978]; membrane [GO:0016020]; plasma membrane [GO:0005886]; postsynapse [GO:0098794]; spectrin [GO:0008091]; spectrin-associated cytoskeleton [GO:0014731] | actin binding [GO:0003779]; actin filament binding [GO:0051015]; structural constituent of cytoskeleton [GO:0005200] | PF00307;PF00435; | 1.20.58.60;1.10.418.10; | Spectrin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cytoplasm, cell cortex. | null | null | null | null | null | FUNCTION: Spectrin is the major constituent of the cytoskeletal network underlying the erythrocyte plasma membrane. It associates with band 4.1 and actin to form the cytoskeletal superstructure of the erythrocyte plasma membrane. | Mus musculus (Mouse) |
P15509 | CSF2R_HUMAN | MLLLVTSLLLCELPHPAFLLIPEKSDLRTVAPASSLNVRFDSRTMNLSWDCQENTTFSKCFLTDKKNRVVEPRLSNNECSCTFREICLHEGVTFEVHVNTSQRGFQQKLLYPNSGREGTAAQNFSCFIYNADLMNCTWARGPTAPRDVQYFLYIRNSKRRREIRCPYYIQDSGTHVGCHLDNLSGLTSRNYFLVNGTSREIGIQFFDSLLDTKKIERFNPPSNVTVRCNTTHCLVRWKQPRTYQKLSYLDFQYQLDVHRKNTQPGTENLLINVSGDLENRYNFPSSEPRAKHSVKIRAADVRILNWSSWSEAIEFGSDDG... | null | null | cytokine-mediated signaling pathway [GO:0019221]; granulocyte-macrophage colony-stimulating factor signaling pathway [GO:0038157]; positive regulation of leukocyte proliferation [GO:0070665]; receptor signaling pathway via JAK-STAT [GO:0007259] | external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; granulocyte macrophage colony-stimulating factor receptor complex [GO:0030526]; plasma membrane [GO:0005886]; receptor complex [GO:0043235] | cytokine binding [GO:0019955]; cytokine receptor activity [GO:0004896]; signaling receptor activity [GO:0038023] | PF18611;PF09240; | 2.60.40.10; | Type I cytokine receptor family, Type 5 subfamily | null | SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane protein.; SUBCELLULAR LOCATION: [Isoform 3]: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 4]: Secreted {ECO:0000305}.; SUBCELLULAR LOCATION: [Isoform 6]: Secreted {ECO:0000305}. | null | null | null | null | null | FUNCTION: Low affinity receptor for granulocyte-macrophage colony-stimulating factor. Transduces a signal that results in the proliferation, differentiation, and functional activation of hematopoietic cells. | Homo sapiens (Human) |
P15513 | MYOM1_APLCA | MQVYMLLPLAVFASLTYQGACEETAAAQTSSDASTSSASSEHAENELSRAKRGSYRMMRLGRGLHMLRLGKRGGPVEPESEENLETLLNLLQGYYSDVPEYPSEFDDTDLAYPYEEYDAPAHPRYRRSTPPTDGVVAPDVLQKGSSEFEDFGDSQLDESDEGYYGYDPENYLYGDFEDYLEPEEGGLGEEKRSLSMLRLGKRGLSMLRLGKREGEEGDEMDKKQDESLNDDFENDDIKRTLSMLRLGKRPMSMLRLGKRPMSMLRLGKRPMSMLRLGKRPMSMLRLGKRPMSMLRLGKRPMSMLRLGKRPMSMLRLGKRP... | null | null | neuropeptide signaling pathway [GO:0007218] | extracellular region [GO:0005576] | null | null | null | null | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Exogenous application of myomodulins potentiates ARC muscle contraction. {ECO:0000269|PubMed:1788132, ECO:0000269|PubMed:3474664, ECO:0000269|PubMed:7472354}. | Aplysia californica (California sea hare) |
P15514 | AREG_HUMAN | MRAPLLPPAPVVLSLLILGSGHYAAGLDLNDTYSGKREPFSGDHSADGFEVTSRSEMSSGSEISPVSEMPSSSEPSSGADYDYSEEYDNEPQIPGYIVDDSVRVEQVVKPPQNKTESENTSDKPKRKKKGGKNGKNRRNRKKKNPCNAEFQNFCIHGECKYIEHLEAVTCKCQQEYFGERCGEKSMKTHSMIDSSLSKIALAAIAAFMSAVILTAVAVITVQLRRQYVRKYEGEAEERKKLRQENGNVHAIA | null | null | cell-cell signaling [GO:0007267]; dichotomous subdivision of terminal units involved in mammary gland duct morphogenesis [GO:0060598]; epidermal growth factor receptor signaling pathway [GO:0007173]; epithelial cell proliferation involved in mammary gland duct elongation [GO:0060750]; ERBB2-EGFR signaling pathway [GO:0... | cell surface [GO:0009986]; clathrin-coated endocytic vesicle membrane [GO:0030669]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-Golgi intermediate compartment membrane [GO:0033116]; ER to Golgi transport vesicle membrane [GO:0012507]; extracellular region [GO:0005576]; extracellular space [GO:000... | cytokine activity [GO:0005125]; epidermal growth factor receptor binding [GO:0005154]; growth factor activity [GO:0008083]; receptor ligand activity [GO:0048018]; transmembrane receptor protein tyrosine kinase activator activity [GO:0030297] | null | 2.10.25.10; | Amphiregulin family | null | SUBCELLULAR LOCATION: Membrane; Single-pass membrane protein. | null | null | null | null | null | FUNCTION: Ligand of the EGF receptor/EGFR. Autocrine growth factor as well as a mitogen for a broad range of target cells including astrocytes, Schwann cells and fibroblasts. | Homo sapiens (Human) |
P15515 | HIS1_HUMAN | MKFFVFALVLALMISMISADSHEKRHHGYRRKFHEKHHSHREFPFYGDYGSNYLYDN | null | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Name=Cu(2+); Xref=ChEBI:CHEBI:29036; | biomineral tissue development [GO:0031214]; defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; killing of cells of another organism [GO:0031640]; positive regulation of cell-cell adhesion [GO:0022409]; positive regulation of metabolic process [GO:0009893]; positive regulation of substr... | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; extracellular region [GO:0005576]; mitochondrion [GO:0005739] | null | null | null | Histatin/statherin family | PTM: [Histatin-1]: Phosphorylated. {ECO:0000269|PubMed:17503797, ECO:0000269|PubMed:25903106, ECO:0000269|PubMed:3286634}. | SUBCELLULAR LOCATION: [Histatin-1]: Secreted. Mitochondrion {ECO:0000269|PubMed:32225006, ECO:0000269|PubMed:35970844}. Endoplasmic reticulum membrane {ECO:0000269|PubMed:32225006, ECO:0000269|PubMed:34233061, ECO:0000269|PubMed:35970844}. Note=Hst 1 co-localized with mitochondria as well as the endoplasmic reticulum (... | null | null | null | null | null | FUNCTION: Histatins (Hsts) are cationic and histidine-rich secreted peptides mainly synthesized by saliva glands of humans and higher primates (PubMed:3286634, PubMed:3944083). Hsts are considered to be major precursors of the protective proteinaceous structure on tooth surfaces (enamel pellicle). Hsts can be divided i... | Homo sapiens (Human) |
P15516 | HIS3_HUMAN | MKFFVFALILALMLSMTGADSHAKRHHGYKRKFHEKHHSHRGYRSNYLYDN | null | null | biomineral tissue development [GO:0031214]; defense response to bacterium [GO:0042742]; defense response to fungus [GO:0050832]; innate immune response [GO:0045087]; killing of cells of another organism [GO:0031640]; positive regulation of fibroblast proliferation [GO:0048146]; positive regulation of wound healing [GO:... | extracellular region [GO:0005576]; mitochondrion [GO:0005739] | metal ion binding [GO:0046872]; molecular adaptor activity [GO:0060090] | null | null | Histatin/statherin family | PTM: 24 proteolytic products are found in saliva. {ECO:0000269|PubMed:15272024}. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14966203}. Note=Secreted by serous acinar and demilune cells. {ECO:0000269|PubMed:14966203}.; SUBCELLULAR LOCATION: [His3-(20-43)-peptide]: Secreted {ECO:0000269|PubMed:14966203}. Mitochondrion {ECO:0000269|PubMed:32225006}. Note=Targeted to mitochondria in pathogen ce... | null | null | null | null | null | FUNCTION: Histatins are cationic and histidine-rich peptides mainly found in the saliva of higher primates (PubMed:3286634). They are considered to be major precursors of the protective proteinaceous structure on tooth surfaces (enamel pellicle). Hsts can be divided into two major groups according to their biological f... | Homo sapiens (Human) |
P15529 | MCP_HUMAN | MEPPGRRECPFPSWRFPGLLLAAMVLLLYSFSDACEEPPTFEAMELIGKPKPYYEIGERVDYKCKKGYFYIPPLATHTICDRNHTWLPVSDDACYRETCPYIRDPLNGQAVPANGTYEFGYQMHFICNEGYYLIGEEILYCELKGSVAIWSGKPPICEKVLCTPPPKIKNGKHTFSEVEVFEYLDAVTYSCDPAPGPDPFSLIGESTIYCGDNSVWSRAAPECKVVKCRFPVVENGKQISGFGKKFYYKATVMFECDKGFYLDGSDTIVCDSNSTWDPPVPKCLKVLPPSSTKPPALSHSVSTSSTTKSPASSASGPRPT... | null | null | adaptive immune response [GO:0002250]; complement activation, classical pathway [GO:0006958]; innate immune response [GO:0045087]; negative regulation of complement activation, classical pathway [GO:0045959]; negative regulation of gene expression [GO:0010629]; positive regulation of gene expression [GO:0010628]; posit... | cell surface [GO:0009986]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; focal adhesion [GO:0005925]; inner acrosomal membrane [GO:0002079]; plasma membrane [GO:0005886] | cadherin binding [GO:0045296]; signaling receptor activity [GO:0038023]; virus receptor activity [GO:0001618] | PF00084; | 2.10.70.10; | null | PTM: N-glycosylated on Asn-83; Asn-114 and Asn-273 in most tissues, but probably less N-glycosylated in testis. N-glycosylation on Asn-114 and Asn-273 is required for cytoprotective function. N-glycosylation on Asn-114 is required for Measles virus binding. N-glycosylation on Asn-273 is required for Neisseria binding. ... | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, acrosome inner membrane {ECO:0000269|PubMed:12112588, ECO:0000269|PubMed:14597734, ECO:0000269|PubMed:15307194}; Single-pass type I membrane protein {ECO:0000269|PubMed:12112588, ECO:0000269|PubMed:14597734, ECO:0000269|PubMed:15307194}. Note=Inner acrosomal... | null | null | null | null | null | FUNCTION: Acts as a cofactor for complement factor I, a serine protease which protects autologous cells against complement-mediated injury by cleaving C3b and C4b deposited on host tissue. May be involved in the fusion of the spermatozoa with the oocyte during fertilization. Also acts as a costimulatory factor for T-ce... | Homo sapiens (Human) |
P15530 | CD79B_MOUSE | MATLVLSSMPCHWLLFLLLLFSGEPVPAMTSSDLPLNFQGSPCSQIWQHPRFAAKKRSSMVKFHCYTNHSGALTWFRKRGSQQPQELVSEEGRIVQTQNGSVYTLTIQNIQYEDNGIYFCKQKCDSANHNVTDSCGTELLVLGFSTLDQLKRRNTLKDGIILIQTLLIILFIIVPIFLLLDKDDGKAGMEEDHTYEGLNIDQTATYEDIVTLRTGEVKWSVGEHPGQE | null | null | adaptive immune response [GO:0002250]; B cell differentiation [GO:0030183]; B cell receptor signaling pathway [GO:0050853]; response to bacterium [GO:0009617] | B cell receptor complex [GO:0019815]; external side of plasma membrane [GO:0009897]; IgM B cell receptor complex [GO:0071755]; plasma membrane [GO:0005886] | identical protein binding [GO:0042802]; transmembrane signaling receptor activity [GO:0004888] | PF02189;PF07686; | 2.60.40.10; | null | PTM: Phosphorylated on tyrosine upon B-cell activation by SRC-type Tyr-kinases such as BLK, LYN and SYK. {ECO:0000269|PubMed:15335855, ECO:0000269|PubMed:7592958}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10587346, ECO:0000269|PubMed:11238609, ECO:0000269|PubMed:15661879}; Single-pass type I membrane protein {ECO:0000269|PubMed:10587346, ECO:0000269|PubMed:11238609, ECO:0000269|PubMed:15661879}. Note=Following antigen binding, the BCR has been shown to translocate ... | null | null | null | null | null | FUNCTION: Required in cooperation with CD79A for initiation of the signal transduction cascade activated by the B-cell antigen receptor complex (BCR) which leads to internalization of the complex, trafficking to late endosomes and antigen presentation. Enhances phosphorylation of CD79A, possibly by recruiting kinases w... | Mus musculus (Mouse) |
P15531 | NDKA_HUMAN | MANCERTFIAIKPDGVQRGLVGEIIKRFEQKGFRLVGLKFMQASEDLLKEHYVDLKDRPFFAGLVKYMHSGPVVAMVWEGLNVVKTGRVMLGETNPADSKPGTIRGDFCIQVGRNIIHGSDSVESAEKEIGLWFHPEELVDYTSCAQNWIYE | 2.7.4.6 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; | cell differentiation [GO:0030154]; CTP biosynthetic process [GO:0006241]; endocytosis [GO:0006897]; GTP biosynthetic process [GO:0006183]; lactation [GO:0007595]; negative regulation of cell population proliferation [GO:0008285]; nervous system development [GO:0007399]; phosphorylation [GO:0016310]; positive regulation... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; early endosome [GO:0005769]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; nucleus [GO:0005634]; ruffle membrane [GO:0032587] | 3'-5' exonuclease activity [GO:0008408]; ATP binding [GO:0005524]; DNA nuclease activity [GO:0004536]; GTP binding [GO:0005525]; identical protein binding [GO:0042802]; magnesium ion binding [GO:0000287]; nucleoside diphosphate kinase activity [GO:0004550]; ribosomal small subunit binding [GO:0043024]; RNA binding [GO:... | PF00334; | 3.30.70.141; | NDK family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16442775}. Nucleus {ECO:0000269|PubMed:16442775}. Note=Cell-cycle dependent nuclear localization which can be induced by interaction with Epstein-barr viral proteins or by degradation of the SET complex by GzmA. | CATALYTIC ACTIVITY: Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640, ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316, ChEBI:CHEBI:456216; EC=2.7.4.6; CATALYTIC ACTIVITY: Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleosid... | null | null | null | null | FUNCTION: Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate. Possesses nucleoside-diphosphate kinase, serine/threonine-specific protein kinase, geranyl and fa... | Homo sapiens (Human) |
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