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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O00488 | ZN593_HUMAN | MGRSRRTGAHRAHSLARQMKAKRRRPDLDEIHRELRPQGSARPQPDPNAEFDPDLPGGGLHRCLACARYFIDSTNLKTHFRSKDHKKRLKQLSVEPYSQEEAERAAGMGSYVPPRRLAVPTEVSTEVPEMDTST | null | null | negative regulation of RNA polymerase II regulatory region sequence-specific DNA binding [GO:1903026]; positive regulation of transcription by RNA polymerase II [GO:0045944]; ribosome biogenesis [GO:0042254] | cytoplasm [GO:0005737]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654] | DNA binding [GO:0003677]; preribosome binding [GO:1990275]; zinc ion binding [GO:0008270] | PF12171; | 3.30.160.60; | ZNF593/BUD20 C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849}. Cytoplasm {ECO:0000250|UniProtKB:Q08004}. Note=Shuttles between the nucleus and the cytoplasm. {ECO:0000250|UniProtKB:Q08004}. | null | null | null | null | null | FUNCTION: Involved in pre-60S ribosomal particles maturation by promoting the nuclear export of the 60S ribosome (PubMed:32669547). Negatively modulates the DNA binding activity of Oct-2 and therefore its transcriptional regulatory activity (PubMed:9115366). {ECO:0000269|PubMed:9115366, ECO:0000305|PubMed:32669547}. | Homo sapiens (Human) |
O00499 | BIN1_HUMAN | MAEMGSKGVTAGKIASNVQKKLTRAQEKVLQKLGKADETKDEQFEQCVQNFNKQLTEGTRLQKDLRTYLASVKAMHEASKKLNECLQEVYEPDWPGRDEANKIAENNDLLWMDYHQKLVDQALLTMDTYLGQFPDIKSRIAKRGRKLVDYDSARHHYESLQTAKKKDEAKIAKPVSLLEKAAPQWCQGKLQAHLVAQTNLLRNQAEEELIKAQKVFEEMNVDLQEELPSLWNSRVGFYVNTFQSIAGLEENFHKEMSKLNQNLNDVLVGLEKQHGSNTFTVKAQPSDNAPAKGNKSPSPPDGSPAATPEIRVNHEPEPAG... | null | null | cytoskeleton organization [GO:0007010]; endocytosis [GO:0006897]; endosome to lysosome transport [GO:0008333]; lipid tube assembly [GO:0060988]; negative regulation of amyloid-beta formation [GO:1902430]; negative regulation of aspartic-type endopeptidase activity involved in amyloid precursor protein catabolic process... | actin cytoskeleton [GO:0015629]; axon [GO:0030424]; axon initial segment [GO:0043194]; axon terminus [GO:0043679]; cerebellar mossy fiber [GO:0044300]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; dendrite [GO:0030425]; endosome [GO:0005768]; extrinsic component of synaptic vesicle membrane [GO:0098850]; glutamatergic... | actin filament binding [GO:0051015]; aspartic-type endopeptidase inhibitor activity [GO:0019828]; clathrin binding [GO:0030276]; GTPase binding [GO:0051020]; identical protein binding [GO:0042802]; phospholipid binding [GO:0005543]; protease binding [GO:0002020]; protein-folding chaperone binding [GO:0051087]; RNA poly... | PF03114;PF14604; | 1.20.1270.60;2.30.30.40; | null | PTM: Phosphorylated by protein kinase C. {ECO:0000250}. | SUBCELLULAR LOCATION: [Isoform BIN1]: Nucleus {ECO:0000269|PubMed:8782822}. Cytoplasm {ECO:0000269|PubMed:9182667}. Endosome {ECO:0000250|UniProtKB:O08539}. Cell membrane, sarcolemma, T-tubule {ECO:0000250|UniProtKB:O08839}.; SUBCELLULAR LOCATION: [Isoform IIA]: Cytoplasm {ECO:0000269|PubMed:9182667}. | null | null | null | null | null | FUNCTION: Is a key player in the control of plasma membrane curvature, membrane shaping and membrane remodeling. Required in muscle cells for the formation of T-tubules, tubular invaginations of the plasma membrane that function in depolarization-contraction coupling (PubMed:24755653). Is a negative regulator of endocy... | Homo sapiens (Human) |
O00501 | CLD5_HUMAN | MGSAALEILGLVLCLVGWGGLILACGLPMWQVTAFLDHNIVTAQTTWKGLWMSCVVQSTGHMQCKVYDSVLALSTEVQAARALTVSAVLLAFVALFVTLAGAQCTTCVAPGPAKARVALTGGVLYLFCGLLALVPLCWFANIVVREFYDPSVPVSQKYELGAALYIGWAATALLMVGGCLLCCGAWVCTGRPDLSFPVKYSAPRRPTATGDYDKKNYV | null | null | bicellular tight junction assembly [GO:0070830]; calcium-independent cell-cell adhesion via plasma membrane cell-adhesion molecules [GO:0016338]; cell adhesion [GO:0007155]; cell-cell junction assembly [GO:0007043]; establishment of blood-retinal barrier [GO:1990963]; face morphogenesis [GO:0060325]; learning [GO:00076... | apicolateral plasma membrane [GO:0016327]; bicellular tight junction [GO:0005923]; cell junction [GO:0030054]; cell-cell junction [GO:0005911]; lateral plasma membrane [GO:0016328]; membrane [GO:0016020]; paranode region of axon [GO:0033270]; plasma membrane [GO:0005886]; Schmidt-Lanterman incisure [GO:0043220]; tight ... | identical protein binding [GO:0042802]; structural molecule activity [GO:0005198] | PF00822; | 1.20.140.150; | Claudin family | null | SUBCELLULAR LOCATION: Cell junction, tight junction. Cell membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Plays a major role in tight junction-specific obliteration of the intercellular space. {ECO:0000250}. | Homo sapiens (Human) |
O00505 | IMA4_HUMAN | MAENPSLENHRIKSFKNKGRDVETMRRHRNEVTVELRKNKRDEHLLKKRNVPQEESLEDSDVDADFKAQNVTLEAILQNATSDNPVVQLSAVQAARKLLSSDRNPPIDDLIKSGILPILVKCLERDDNPSLQFEAAWALTNIASGTSAQTQAVVQSNAVPLFLRLLRSPHQNVCEQAVWALGNIIGDGPQCRDYVISLGVVKPLLSFISPSIPITFLRNVTWVIVNLCRNKDPPPPMETVQEILPALCVLIYHTDINILVDTVWALSYLTDGGNEQIQMVIDSGVVPFLVPLLSHQEVKVQTAALRAVGNIVTGTDEQTQ... | null | null | NLS-bearing protein import into nucleus [GO:0006607]; protein import into nucleus [GO:0006606]; protein-containing complex assembly [GO:0065003]; symbiont entry into host cell [GO:0046718]; viral penetration into host nucleus [GO:0075732] | cytosol [GO:0005829]; host cell [GO:0043657]; NLS-dependent protein nuclear import complex [GO:0042564]; nuclear pore [GO:0005643]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | nuclear import signal receptor activity [GO:0061608]; nuclear localization sequence binding [GO:0008139] | PF00514;PF16186;PF01749; | 1.20.5.690;1.25.10.10; | Importin alpha family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:34564892}. Nucleus {ECO:0000269|PubMed:34564892}. | null | null | null | null | null | FUNCTION: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin... | Homo sapiens (Human) |
O00506 | STK25_HUMAN | MAHLRGFANQHSRVDPEELFTKLDRIGKGSFGEVYKGIDNHTKEVVAIKIIDLEEAEDEIEDIQQEITVLSQCDSPYITRYFGSYLKSTKLWIIMEYLGGGSALDLLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKRNTFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDLHPMRVLFLIPKNSPPTLEGQHSKPFKEFVEACLNKDPRFRPTAKELLKHKFITRYTKKTSFLTELIDRYKRWKSEGHGEESSSEDSDIDGEAEDGEQGPIWT... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; | axonogenesis [GO:0007409]; cellular response to oxidative stress [GO:0034599]; establishment of Golgi localization [GO:0051683]; establishment or maintenance of cell polarity [GO:0007163]; Golgi localization [GO:0051645]; Golgi reassembly [GO:0090168]; intrinsic apoptotic signaling pathway in response to hydrogen perox... | cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; Golgi apparatus [GO:0005794] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF20929;PF00069; | 1.10.12.70;1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, STE20 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15037601}. Golgi apparatus {ECO:0000269|PubMed:15037601}. Note=Localizes to the Golgi apparatus. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Oxidant stress-activated serine/threonine kinase that may play a role in the response to environmental stress. Targets to the Golgi apparatus where it appears to regulate protein transport events, cell adhesion, and polarity complexes important for cell migration. Part of the striatin-interacting phosphatase ... | Homo sapiens (Human) |
O00507 | USP9Y_HUMAN | MTAITHGSPVGGNDSQGQVLDGQSQHLFQQNQTSSPDSSNENSVATPPPEEQGQGDAPPQHEDEEPAFPHTELANLDDMINRPRWVVPVLPKGELEVLLEAAIDLSVKGLDVKSEACQRFFRDGLTISFTKILMDEAVSGWKFEIHRCIINNTHRLVELCVAKLSQDWFPLLELLAMALNPHCKFHIYNGTRPCELISSNAQLPEDELFARSSDPRSPKGWLVDLINKFGTLNGFQILHDRFFNGSALNIQIIAALIKPFGQCYEFLSQHTLKKYFIPVIEIVPHLLENLTDEELKKEAKNEAKNDALSMIIKSLKNLAS... | 3.4.19.12 | null | BMP signaling pathway [GO:0030509]; cell migration [GO:0016477]; protein deubiquitination [GO:0016579]; proteolysis [GO:0006508]; spermatogenesis [GO:0007283]; transforming growth factor beta receptor signaling pathway [GO:0007179] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleus [GO:0005634] | co-SMAD binding [GO:0070410]; cysteine-type deubiquitinase activity [GO:0004843]; cysteine-type peptidase activity [GO:0008234] | PF12030;PF00443; | 3.90.70.10; | Peptidase C19 family | null | null | 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:12895410}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:12895410}. | null | null | FUNCTION: Deubiquitinase that mediates deubiquitination of target proteins (PubMed:12895410). May stabilize target proteins that are important for male germ cell development (PubMed:12895410). {ECO:0000269|PubMed:12895410}. | Homo sapiens (Human) |
O00512 | BCL9_HUMAN | MHSSNPKVRSSPSGNTQSSPKSKQEVMVRPPTVMSPSGNPQLDSKFSNQGKQGGSASQSQPSPCDSKSGGHTPKALPGPGGSMGLKNGAGNGAKGKGKRERSISADSFDQRDPGTPNDDSDIKECNSADHIKSQDSQHTPHSMTPSNATAPRSSTPSHGQTTATEPTPAQKTPAKVVYVFSTEMANKAAEAVLKGQVETIVSFHIQNISNNKTERSTAPLNTQISALRNDPKPLPQQPPAPANQDQNSSQNTRLQPTPPIPAPAPKPAAPPRPLDRESPGVENKLIPSVGSPASSTPLPPDGTGPNSTPNNRAVTPVSQG... | null | null | canonical Wnt signaling pathway [GO:0060070]; myoblast differentiation [GO:0045445]; myotube differentiation involved in skeletal muscle regeneration [GO:0014908]; positive regulation of transcription by RNA polymerase II [GO:0045944]; skeletal muscle cell differentiation [GO:0035914]; somatic stem cell population main... | beta-catenin-TCF complex [GO:1990907]; cis-Golgi network [GO:0005801]; nucleoplasm [GO:0005654]; sarcoplasm [GO:0016528] | beta-catenin binding [GO:0008013]; transcription coactivator activity [GO:0003713] | PF11502; | 3.30.40.10; | BCL9 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | null | null | null | null | null | FUNCTION: Involved in signal transduction through the Wnt pathway. Promotes beta-catenin's transcriptional activity (By similarity). {ECO:0000250, ECO:0000269|PubMed:11955446}. | Homo sapiens (Human) |
O00519 | FAAH1_HUMAN | MVQYELWAALPGASGVALACCFVAAAVALRWSGRRTARGAVVRARQRQRAGLENMDRAAQRFRLQNPDLDSEALLALPLPQLVQKLHSRELAPEAVLFTYVGKAWEVNKGTNCVTSYLADCETQLSQAPRQGLLYGVPVSLKECFTYKGQDSTLGLSLNEGVPAECDSVVVHVLKLQGAVPFVHTNVPQSMFSYDCSNPLFGQTVNPWKSSKSPGGSSGGEGALIGSGGSPLGLGTDIGGSIRFPSSFCGICGLKPTGNRLSKSGLKGCVYGQEAVRLSVGPMARDVESLALCLRALLCEDMFRLDPTVPPLPFREEVYT... | 3.1.1.-; 3.5.1.99 | null | arachidonic acid metabolic process [GO:0019369]; fatty acid catabolic process [GO:0009062]; monoacylglycerol catabolic process [GO:0052651]; positive regulation of vasoconstriction [GO:0045907] | cytoskeleton [GO:0005856]; endoplasmic reticulum membrane [GO:0005789]; organelle membrane [GO:0031090] | acylglycerol lipase activity [GO:0047372]; amidase activity [GO:0004040]; fatty acid amide hydrolase activity [GO:0017064]; identical protein binding [GO:0042802]; phospholipid binding [GO:0005543] | PF01425; | 3.90.1300.10; | Amidase family | null | SUBCELLULAR LOCATION: Endomembrane system {ECO:0000269|PubMed:17015445}; Single-pass membrane protein {ECO:0000269|PubMed:17015445}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17015445}. Note=Seems to be attached to intracellular membranes and a portion of the cytoskeletal network. | CATALYTIC ACTIVITY: Reaction=H2O + N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine = (5Z,8Z,11Z,14Z)-eicosatetraenoate + ethanolamine; Xref=Rhea:RHEA:26136, ChEBI:CHEBI:2700, ChEBI:CHEBI:15377, ChEBI:CHEBI:32395, ChEBI:CHEBI:57603; EC=3.5.1.99; Evidence={ECO:0000269|PubMed:17015445, ECO:0000269|PubMed:19926788, ECO:000... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: Vmax=9.7 nmol/min/mg enzyme for the hydrolysis of oleamide ((9Z)-octadecenamide) {ECO:0000269|PubMed:17015445}; Vmax=2.1 nmol/min/mg enzyme for the hydrolysis of N-palmitoyl ethanolamine (N-hexadecanoyl ethanolamine) {ECO:0000269|PubMed:17015445}; Vmax=5.6 nmol/min/mg... | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is around 9.0. {ECO:0000269|PubMed:17015445}; | null | FUNCTION: Catalyzes the hydrolysis of endogenous amidated lipids like the sleep-inducing lipid oleamide ((9Z)-octadecenamide), the endocannabinoid anandamide (N-(5Z,8Z,11Z,14Z-eicosatetraenoyl)-ethanolamine), as well as other fatty amides, to their corresponding fatty acids, thereby regulating the signaling functions o... | Homo sapiens (Human) |
O00522 | KRIT1_HUMAN | MGNPENIEDAYVAVIRPKNTASLNSREYRAKSYEILLHEVPIEGQKKKRKKVLLETKLQGNSEITQGILDYVVETTKPISPANQGIRGKRVVLMKKFPLDGEKMGREASLFIVPSVVKDNTKYTYTPGCPIFYCLQDIMRVCSESSTHFATLTARMLIALDKWLDERHAQSHFIPALFRPSPLERIKTNVINPAYATESGQTENSLHMGYSALEIKSKMLALEKADTCIYNPLFGSDLQYTNRVDKVVINPYFGLGAPDYSKIQIPKQEKWQRSMSSVTEDKERQWVDDFPLHRSACEGDSELLSRLLSERFSVNQLDSD... | null | null | angiogenesis [GO:0001525]; cell redox homeostasis [GO:0045454]; endothelium development [GO:0003158]; integrin activation [GO:0033622]; negative regulation of angiogenesis [GO:0016525]; negative regulation of endothelial cell apoptotic process [GO:2000352]; negative regulation of endothelial cell migration [GO:0010596]... | cell-cell junction [GO:0005911]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; extracellular space [GO:0005615]; plasma membrane [GO:0005886]; protein-containing complex [GO:0032991] | GTPase regulator activity [GO:0030695]; microtubule binding [GO:0008017]; phosphatidylinositol-4,5-bisphosphate binding [GO:0005546] | PF13857;PF00373;PF16705; | 1.20.80.10;1.25.40.20;3.30.70.2240;2.30.29.30; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell membrane; Peripheral membrane protein. Cell junction. Note=KRIT1 and CDH5 reciprocally regulate their localization to endothelial cell-cell junctions. Association with RAP1 relocalizes KRIT1 from microtubules to cell junction membranes. Translocates from the cytoplasm... | null | null | null | null | null | FUNCTION: Component of the CCM signaling pathway which is a crucial regulator of heart and vessel formation and integrity (By similarity). Negative regulator of angiogenesis. Inhibits endothelial proliferation, apoptosis, migration, lumen formation and sprouting angiogenesis in primary endothelial cells. Promotes AKT p... | Homo sapiens (Human) |
O00526 | UPK2_HUMAN | MAPLLPIRTLPLILILLALLSPGAADFNISSLSGLLSPALTESLLVALPPCHLTGGNATLMVRRANDSKVVTSSFVVPPCRGRRELVSVVDSGAGFTVTRLSAYQVTNLVPGTKFYISYLVKKGTATESSREIPMSTLPRRNMESIGLGMARTGGMVVITVLLSVAMFLLVLGFIIALALGSRK | null | null | epithelial cell differentiation [GO:0030855] | apical plasma membrane [GO:0016324]; extracellular exosome [GO:0070062]; plasma membrane [GO:0005886] | null | PF07353; | null | Uroplakin-2 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=Heterodimer formation with UPK1A is a prerequisite to exit out of the endoplasmic reticulum (ER). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Component of the asymmetric unit membrane (AUM); a highly specialized biomembrane elaborated by terminally differentiated urothelial cells. May play an important role in regulating the assembly of the AUM (By similarity). {ECO:0000250}. | Homo sapiens (Human) |
O00533 | NCHL1_HUMAN | MEPLLLGRGLIVYLMFLLLKFSKAIEIPSSVQQVPTIIKQSKVQVAFPFDEYFQIECEAKGNPEPTFSWTKDGNPFYFTDHRIIPSNNSGTFRIPNEGHISHFQGKYRCFASNKLGIAMSEEIEFIVPSVPKFPKEKIDPLEVEEGDPIVLPCNPPKGLPPLHIYWMNIELEHIEQDERVYMSQKGDLYFANVEEKDSRNDYCCFAAFPRLRTIVQKMPMKLTVNSSNSIKQRKPKLLLPPTESGSESSITILKGEILLLECFAEGLPTPQVDWNKIGGDLPKGRETKENYGKTLKIENVSYQDKGNYRCTASNFLGTAT... | null | null | adult locomotory behavior [GO:0008344]; axon guidance [GO:0007411]; brain development [GO:0007420]; cell adhesion [GO:0007155]; cognition [GO:0050890]; exploration behavior [GO:0035640]; negative regulation of neuron apoptotic process [GO:0043524]; neuron migration [GO:0001764]; signal transduction [GO:0007165] | apical part of cell [GO:0045177]; axon [GO:0030424]; dendrite [GO:0030425]; extracellular exosome [GO:0070062]; membrane [GO:0016020]; plasma membrane [GO:0005886] | cell-cell adhesion mediator activity [GO:0098632]; protease binding [GO:0002020] | PF13882;PF00041;PF07679;PF00047;PF13927; | 2.60.40.10; | Immunoglobulin superfamily, L1/neurofascin/NgCAM family | PTM: Cleavage by metalloprotease ADAM8 in the extracellular part generates 2 soluble forms (125 kDa and 165 kDa) in vitro and is inhibited by metalloprotease inhibitors (By similarity). Cleaved by BACE1 (By similarity). {ECO:0000250|UniProtKB:P70232}.; PTM: N-glycosylated. Contains N-linked oligosaccharides with a sulf... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Note=Soluble forms produced by cleavage/shedding also exist. {ECO:0000250}.; SUBCELLULAR LOCATION: [Processed neural cell adhesion molecule L1-like protein]: Secreted, extracellular space, extracellular matrix {ECO:000... | null | null | null | null | null | FUNCTION: Extracellular matrix and cell adhesion protein that plays a role in nervous system development and in synaptic plasticity. Both soluble and membranous forms promote neurite outgrowth of cerebellar and hippocampal neurons and suppress neuronal cell death. Plays a role in neuronal positioning of pyramidal neuro... | Homo sapiens (Human) |
O00541 | PESC_HUMAN | MGGLEKKKYERGSATNYITRNKARKKLQLSLADFRRLCILKGIYPHEPKHKKKVNKGSTAARTFYLIKDIRFLLHEPIVNKFREYKVFVRKLRKAYGKSEWNTVERLKDNKPNYKLDHIIKERYPTFIDALRDLDDALSMCFLFSTFPRTGKCHVQTIQLCRRLTVEFMHYIIAARALRKVFLSIKGIYYQAEVLGQPIVWITPYAFSHDHPTDVDYRVMATFTEFYTTLLGFVNFRLYQLLNLHYPPKLEGQAQAEAKAGEGTYALDSESCMEKLAALSASLARVVVPATEEEAEVDEFPTDGEMSAQEEDRRKELEAQ... | null | null | cell population proliferation [GO:0008283]; maturation of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000466]; maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [GO:0000463]; regulation of cell cycle [GO:0051726]; ribosomal large subunit biogen... | chromosome [GO:0005694]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; PeBoW complex [GO:0070545]; preribosome, large subunit precursor [GO:0030687] | ribonucleoprotein complex binding [GO:0043021]; RNA binding [GO:0003723] | PF16589;PF06732; | 3.40.50.10190; | Pescadillo family | PTM: Sumoylated. | SUBCELLULAR LOCATION: Nucleus, nucleolus. Nucleus, nucleoplasm. Chromosome. Note=Appears to localize to the periphery of metaphase chromosomes during mitosis and to the prenucleolar bodies that form in mitotic cells prior to the actual nucleoli. {ECO:0000255|HAMAP-Rule:MF_03028}. | null | null | null | null | null | FUNCTION: Component of the PeBoW complex, which is required for maturation of 28S and 5.8S ribosomal RNAs and formation of the 60S ribosome. {ECO:0000255|HAMAP-Rule:MF_03028, ECO:0000269|PubMed:16738141, ECO:0000269|PubMed:17189298, ECO:0000269|PubMed:17353269}. | Homo sapiens (Human) |
O00548 | DLL1_HUMAN | MGSRCALALAVLSALLCQVWSSGVFELKLQEFVNKKGLLGNRNCCRGGAGPPPCACRTFFRVCLKHYQASVSPEPPCTYGSAVTPVLGVDSFSLPDGGGADSAFSNPIRFPFGFTWPGTFSLIIEALHTDSPDDLATENPERLISRLATQRHLTVGEEWSQDLHSSGRTDLKYSYRFVCDEHYYGEGCSVFCRPRDDAFGHFTCGERGEKVCNPGWKGPYCTEPICLPGCDEQHGFCDKPGECKCRVGWQGRYCDECIRYPGCLHGTCQQPWQCNCQEGWGGLFCNQDLNYCTHHKPCKNGATCTNTGQGSYTCSCRPGY... | null | null | astrocyte development [GO:0014002]; cell differentiation [GO:0030154]; cell fate determination [GO:0001709]; cerebellar molecular layer formation [GO:0021688]; cerebellar Purkinje cell layer structural organization [GO:0021693]; clathrin-dependent endocytosis [GO:0072583]; compartment pattern specification [GO:0007386]... | adherens junction [GO:0005912]; apical plasma membrane [GO:0016324]; cytoplasmic vesicle [GO:0031410]; extracellular region [GO:0005576]; membrane raft [GO:0045121]; plasma membrane [GO:0005886] | calcium ion binding [GO:0005509]; Notch binding [GO:0005112]; receptor ligand activity [GO:0048018]; scaffold protein binding [GO:0097110]; Tat protein binding [GO:0030957] | PF21700;PF01414;PF00008;PF07657; | 2.10.25.140;2.60.40.3510;2.10.25.10; | null | PTM: Ubiquitinated by MIB (MIB1 or MIB2), leading to its endocytosis and subsequent degradation (By similarity). Ubiquitinated; promotes recycling back to the plasma membrane and confers a strong affinity for NOTCH1. Multi-ubiquitination of Lys-613 by MIB1 promotes both cis and trans-interaction with NOTCH1, as well as... | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:Q61483}; Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q61483}. Cell junction, adherens junction {ECO:0000250|UniProtKB:Q61483}. Membrane raft {ECO:0000250|UniProtKB:Q61483}. Note=Distributed around adherens junction in the apical endfeet th... | null | null | null | null | null | FUNCTION: Transmembrane ligand protein of NOTCH1, NOTCH2 and NOTCH3 receptors that binds the extracellular domain (ECD) of Notch receptor in a cis and trans fashion manner (PubMed:11006133). Following transinteraction, ligand cells produce mechanical force that depends of a clathrin-mediated endocytosis, requiring liga... | Homo sapiens (Human) |
O00555 | CAC1A_HUMAN | MARFGDEMPARYGGGGSGAAAGVVVGSGGGRGAGGSRQGGQPGAQRMYKQSMAQRARTMALYNPIPVRQNCLTVNRSLFLFSEDNVVRKYAKKITEWPPFEYMILATIIANCIVLALEQHLPDDDKTPMSERLDDTEPYFIGIFCFEAGIKIIALGFAFHKGSYLRNGWNVMDFVVVLTGILATVGTEFDLRTLRAVRVLRPLKLVSGIPSLQVVLKSIMKAMIPLLQIGLLLFFAILIFAIIGLEFYMGKFHTTCFEEGTDDIQGESPAPCGTEEPARTCPNGTKCQPYWEGPNNGITQFDNILFAVLTVFQCITMEGW... | null | null | calcium ion import across plasma membrane [GO:0098703]; calcium ion transmembrane transport [GO:0070588]; cellular response to amyloid-beta [GO:1904646]; chemical synaptic transmission [GO:0007268]; modulation of chemical synaptic transmission [GO:0050804]; positive regulation of cytosolic calcium ion concentration [GO... | cell projection [GO:0042995]; cytoplasm [GO:0005737]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; synapse [GO:0045202]; voltage-gated calcium channel complex [GO:0005891] | amyloid-beta binding [GO:0001540]; high voltage-gated calcium channel activity [GO:0008331]; metal ion binding [GO:0046872]; syntaxin binding [GO:0019905]; voltage-gated calcium channel activity [GO:0005245] | PF08763;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, CACNA1A subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10049321, ECO:0000269|PubMed:26716990}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671, ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:10049321, ECO:0000269|PubMed:10753886, ECO:0000269|PubMed:11723274, ECO:0000269|PubMed:15293273, ECO:0000269|PubMed:19232643, ECO:0000269|PubMed:24836863, ECO:0000269|PubMed:26716990}; | null | null | null | null | FUNCTION: Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha... | Homo sapiens (Human) |
O00559 | RCAS1_HUMAN | MAITQFRLFKFCTCLATVFSFLKRLICRSGRGRKLSGDQITLPTTVDYSSVPKQTDVEEWTSWDEDAPTSVKIEGGNGNVATQQNSLEQLEPDYFKDMTPTIRKTQKIVIKKREPLNFGIPDGSTGFSSRLAATQDLPFIHQSSELGDLDTWQENTNAWEEEEDAAWQAEEVLRQQKLADREKRAAEQQRKKMEKEAQRLMKKEQNKIGVKLS | null | null | adaptive immune memory response involving T cells and B cells [GO:0090717]; regulation of cell growth [GO:0001558]; T cell mediated cytotoxicity [GO:0001913] | Golgi membrane [GO:0000139]; secretory granule [GO:0030141] | peptidase activator activity involved in apoptotic process [GO:0016505] | null | null | null | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000269|PubMed:12672804}; Single-pass type III membrane protein {ECO:0000269|PubMed:12672804}. Note=According to PubMed:10426319, it also exists as a soluble form which has the same biological activities. The existence of such soluble form is however uncertain. | null | null | null | null | null | FUNCTION: May participate in suppression of cell proliferation and induces apoptotic cell death through activation of interleukin-1-beta converting enzyme (ICE)-like proteases. {ECO:0000269|PubMed:12054692, ECO:0000269|PubMed:12138241, ECO:0000269|PubMed:12672804}. | Homo sapiens (Human) |
O00560 | SDCB1_HUMAN | MSLYPSLEDLKVDKVIQAQTAFSANPANPAILSEASAPIPHDGNLYPRLYPELSQYMGLSLNEEEIRANVAVVSGAPLQGQLVARPSSINYMVAPVTGNDVGIRRAEIKQGIREVILCKDQDGKIGLRLKSIDNGIFVQLVQANSPASLVGLRFGDQVLQINGENCAGWSSDKAHKVLKQAFGEKITMTIRDRPFERTITMHKDSTGHVGFIFKNGKITSIVKDSSAARNGLLTEHNICEINGQNVIGLKDSQIADILSTSGTVVTITIMPAFIFEHIIKRMAPSIMKSLMDHTIPEV | null | null | actin cytoskeleton organization [GO:0030036]; chemical synaptic transmission [GO:0007268]; intracellular signal transduction [GO:0035556]; negative regulation of receptor internalization [GO:0002091]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of cell growth [GO:0030307]... | adherens junction [GO:0005912]; azurophil granule lumen [GO:0035578]; blood microparticle [GO:0072562]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:000... | cell adhesion molecule binding [GO:0050839]; cytoskeletal anchor activity [GO:0008093]; ephrin receptor binding [GO:0046875]; frizzled binding [GO:0005109]; growth factor binding [GO:0019838]; identical protein binding [GO:0042802]; interleukin-5 receptor binding [GO:0005137]; ionotropic glutamate receptor binding [GO:... | PF00595; | 2.30.42.10; | null | PTM: Phosphorylated on tyrosine residues. | SUBCELLULAR LOCATION: Cell junction, focal adhesion {ECO:0000269|PubMed:11179419}. Cell junction, adherens junction {ECO:0000269|PubMed:11179419}. Cell membrane {ECO:0000269|PubMed:11179419, ECO:0000269|PubMed:25893292, ECO:0000269|PubMed:27386966}; Peripheral membrane protein {ECO:0000269|PubMed:11179419, ECO:0000269|... | null | null | null | null | null | FUNCTION: Multifunctional adapter protein involved in diverse array of functions including trafficking of transmembrane proteins, neuro and immunomodulation, exosome biogenesis, and tumorigenesis (PubMed:26291527). Positively regulates TGFB1-mediated SMAD2/3 activation and TGFB1-induced epithelial-to-mesenchymal transi... | Homo sapiens (Human) |
O00562 | PITM1_HUMAN | MLIKEYHILLPMSLDEYQVAQLYMIQKKSREESSGEGSGVEILANRPYTDGPGGSGQYTHKVYHVGSHIPGWFRALLPKAALQVEEESWNAYPYTRTRYTCPFVEKFSIEIETYYLPDGGQQPNVFNLSGAERRQRILDTIDIVRDAVAPGEYKAEEDPRLYHSVKTGRGPLSDDWARTAAQTGPLMCAYKLCKVEFRYWGMQAKIEQFIHDVGLRRVMLRAHRQAWCWQDEWTELSMADIRALEEETARMLAQRMAKCNTGSEGSEAQPPGKPSTEARSAASNTGTPDGPEAPPGPDASPDASFGKQWSSSSRSSYSSQ... | null | null | brain development [GO:0007420]; lipid metabolic process [GO:0006629]; phosphatidylinositol biosynthetic process [GO:0006661]; phospholipid transport [GO:0015914]; phototransduction [GO:0007602]; protein transport [GO:0015031] | cell body [GO:0044297]; cleavage furrow [GO:0032154]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; Golgi cisterna membrane [GO:0032580]; intracellular membrane-bounded organelle [GO:0043231]; lipid droplet [GO:0005811]; membrane [GO:0016020]; midbody [GO:0030496] | calcium ion binding [GO:0005509]; phosphatidic acid binding [GO:0070300]; phosphatidylcholine binding [GO:0031210]; phosphatidylcholine transporter activity [GO:0008525]; phosphatidylinositol binding [GO:0035091]; phosphatidylinositol transfer activity [GO:0008526]; receptor tyrosine kinase binding [GO:0030971] | PF02862;PF02121; | 3.30.530.20;3.40.50.1000; | PtdIns transfer protein family, PI transfer class IIA subfamily | PTM: Phosphorylated on multiple sites by CDK1 at the onset of mitosis. Phosphorylation facilitates dissociation from the Golgi complex and is required for interaction with PLK1.; PTM: Phosphorylated on threonine residues upon treatment with oleic acid.; PTM: Phosphorylated on tyrosine residues by PTK2B. | SUBCELLULAR LOCATION: Cytoplasm. Golgi apparatus, Golgi stack membrane {ECO:0000269|PubMed:12225667}; Peripheral membrane protein. Endoplasmic reticulum membrane {ECO:0000269|PubMed:12225667}; Peripheral membrane protein. Lipid droplet {ECO:0000269|PubMed:12225667}. Cleavage furrow {ECO:0000269|PubMed:15125835}. Midbod... | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(in) = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(out); Xref=Rhea:RHEA:38691, ChEBI:CHEBI:57880; Evidence={ECO:0000269|PubMed:10531358, ECO:0000269|PubMed:22822086}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:38692; Evide... | null | null | null | null | FUNCTION: Catalyzes the transfer of phosphatidylinositol (PI) between membranes (PubMed:10531358, PubMed:22822086). Binds PI, phosphatidylcholine (PC) and phosphatidic acid (PA) with the binding affinity order of PI > PA > PC (PubMed:22822086). Regulates RHOA activity, and plays a role in cytoskeleton remodeling (PubMe... | Homo sapiens (Human) |
O00566 | MPP10_HUMAN | MAPQVWRRRTLERCLTEVGKATGRPECFLTIQEGLASKFTSLTKVLYDFNKILENGRIHGSPLQKLVIENFDDEQIWQQLELQNEPILQYFQNAVSETINDEDISLLPESEEQEREEDGSEIEADDKEDLEDLEEEEVSDMGNDDPEMGERAENSSKSDLRKSPVFSDEDSDLDFDISKLEQQSKVQNKGQGKPREKSIVDDKFFKLSEMEAYLENIEKEEERKDDNDEEEEDIDFFEDIDSDEDEGGLFGSKKLKSGKSSRNLKYKDFFDPVESDEDITNVHDDELDSNKEDDEIAEEEAEELSISETDEDDDLQENED... | null | null | maturation of SSU-rRNA [GO:0030490]; ribosomal small subunit biogenesis [GO:0042274]; RNA processing [GO:0006396]; RNA splicing [GO:0008380]; RNA splicing, via transesterification reactions [GO:0000375] | chromosome [GO:0005694]; Mpp10 complex [GO:0034457]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; small-subunit processome [GO:0032040]; sno(s)RNA-containing ribonucleoprotein complex [GO:0005732] | RNA binding [GO:0003723] | PF04006; | null | MPP10 family | PTM: Phosphorylated in M (mitotic) phase. | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:12655004, ECO:0000269|PubMed:34516797, ECO:0000269|PubMed:9450966}. Chromosome {ECO:0000269|PubMed:9450966}. Note=Fibrillar region of the nucleolus (PubMed:9450966). After dissolution of the nucleolus in early M phase becomes asso... | null | null | null | null | null | FUNCTION: Component of the 60-80S U3 small nucleolar ribonucleoprotein (U3 snoRNP). Required for the early cleavages during pre-18S ribosomal RNA processing (PubMed:12655004). Part of the small subunit (SSU) processome, first precursor of the small eukaryotic ribosomal subunit. During the assembly of the SSU processome... | Homo sapiens (Human) |
O00567 | NOP56_HUMAN | MVLLHVLFEHAVGYALLALKEVEEISLLQPQVEESVLNLGKFHSIVRLVAFCPFASSQVALENANAVSEGVVHEDLRLLLETHLPSKKKKVLLGVGDPKIGAAIQEELGYNCQTGGVIAEILRGVRLHFHNLVKGLTDLSACKAQLGLGHSYSRAKVKFNVNRVDNMIIQSISLLDQLDKDINTFSMRVREWYGYHFPELVKIINDNATYCRLAQFIGNRRELNEDKLEKLEELTMDGAKAKAILDASRSSMGMDISAIDLINIESFSSRVVSLSEYRQSLHTYLRSKMSQVAPSLSALIGEAVGARLIAHAGSLTNLAK... | null | null | ribosomal small subunit biogenesis [GO:0042274]; rRNA processing [GO:0006364] | box C/D RNP complex [GO:0031428]; cytoplasm [GO:0005737]; fibrillar center [GO:0001650]; membrane [GO:0016020]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; pre-snoRNP complex [GO:0070761]; small-subunit processome [GO:0032040]; sno(s)RNA-containing ribonucleoprotein complex [GO:0005732] | cadherin binding [GO:0045296]; histone methyltransferase binding [GO:1990226]; RNA binding [GO:0003723]; snoRNA binding [GO:0030515] | PF01798;PF08156; | 1.10.287.4070;1.10.246.90; | NOP5/NOP56 family | null | SUBCELLULAR LOCATION: Nucleus, nucleolus {ECO:0000269|PubMed:12429849, ECO:0000269|PubMed:12777385, ECO:0000269|PubMed:34516797, ECO:0000269|PubMed:9372940}. Cytoplasm {ECO:0000250|UniProtKB:Q9D6Z1}. Nucleus, nucleoplasm {ECO:0000305|PubMed:15574333}. | null | null | null | null | null | FUNCTION: Involved in the early to middle stages of 60S ribosomal subunit biogenesis. Core component of box C/D small nucleolar ribonucleoprotein (snoRNP) particles. Required for the biogenesis of box C/D snoRNAs such U3, U8 and U14 snoRNAs (PubMed:12777385, PubMed:15574333). Part of the small subunit (SSU) processome,... | Homo sapiens (Human) |
O00571 | DDX3X_HUMAN | MSHVAVENALGLDQQFAGLDLNSSDNQSGGSTASKGRYIPPHLRNREATKGFYDKDSSGWSSSKDKDAYSSFGSRSDSRGKSSFFSDRGSGSRGRFDDRGRSDYDGIGSRGDRSGFGKFERGGNSRWCDKSDEDDWSKPLPPSERLEQELFSGGNTGINFEKYDDIPVEATGNNCPPHIESFSDVEMGEIIMGNIELTRYTRPTPVQKHAIPIIKEKRDLMACAQTGSGKTAAFLLPILSQIYSDGPGEALRAMKENGRYGRRKQYPISLVLAPTRELAVQIYEEARKFSYRSRVRPCVVYGGADIGQQIRDLERGCHLL... | 3.6.4.13 | null | cell differentiation [GO:0030154]; cellular response to arsenic-containing substance [GO:0071243]; cellular response to osmotic stress [GO:0071470]; cellular response to virus [GO:0098586]; chromosome segregation [GO:0007059]; cytosolic ribosome assembly [GO:0042256]; extrinsic apoptotic signaling pathway via death dom... | cell leading edge [GO:0031252]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; cytoplasmic stress granule [GO:0010494]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; ficolin-1-rich granule lumen [GO:1904813]; lamellipodium [GO:0030027]; NLRP3 inflammasome complex [GO:007... | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; cadherin binding [GO:0045296]; CTPase activity [GO:0043273]; DNA binding [GO:0003677]; DNA helicase activity [GO:0003678]; eukaryotic initiation factor 4E binding [GO:0008190]; gamma-tubulin binding [GO:0043015]; GTPase activity [GO:0003924]; mRNA 5'-UTR b... | PF00270;PF00271; | 3.40.50.300; | DEAD box helicase family, DDX3/DED1 subfamily | PTM: Phosphorylated by TBK1; the phosphorylation is required for the synergistic induction of IFNB mediated by TBK1 and DDX3X (PubMed:18583960). Phosphorylated by IKBKE at Ser-102 after ssRNA viral infection; enhances the induction of INFB promoter by IRF3 (PubMed:18583960, PubMed:23478265). The cytoplasmic form is hig... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23413191, ECO:0000269|PubMed:29899501}. Nucleus {ECO:0000269|PubMed:10329544, ECO:0000269|PubMed:15507209, ECO:0000269|PubMed:16818630, ECO:0000269|PubMed:18596238, ECO:0000269|PubMed:18636090, ECO:0000269|PubMed:22034099, ECO:0000269|PubMed:29899501, ECO:0000269|... | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.13; Evidence={ECO:0000269|PubMed:15507209, ECO:0000269|PubMed:17357160, ECO:0000269|PubMed:21589879, ECO:0000269|PubMed:31300642... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.04 mM for ATP (in the absence of nucleic acid) {ECO:0000269|PubMed:17357160}; KM=0.03 mM for ATP (in the presence of ssDNA oligonucleoside dA200) {ECO:0000269|PubMed:17357160}; KM=0.062 mM for ATP (in the absence of nucleic acid) {ECO:0000269|PubMed:21589879}; KM... | null | null | null | FUNCTION: Multifunctional ATP-dependent RNA helicase (PubMed:17357160, PubMed:21589879, PubMed:31575075). The ATPase activity can be stimulated by various ribo-and deoxynucleic acids indicative for a relaxed substrate specificity (PubMed:29222110). In vitro can unwind partially double-stranded DNA with a preference for... | Homo sapiens (Human) |
O00574 | CXCR6_HUMAN | MAEHDYHEDYGFSSFNDSSQEEHQDFLQFSKVFLPCMYLVVFVCGLVGNSLVLVISIFYHKLQSLTDVFLVNLPLADLVFVCTLPFWAYAGIHEWVFGQVMCKSLLGIYTINFYTSMLILTCITVDRFIVVVKATKAYNQQAKRMTWGKVTSLLIWVISLLVSLPQIIYGNVFNLDKLICGYHDEAISTVVLATQMTLGFFLPLLTMIVCYSVIIKTLLHAGGFQKHRSLKIIFLVMAVFLLTQMPFNLMKFIRSTHWEYYAMTSFHYTIMVTEAIAYLRACLNPVLYAFVSLKFRKNFWKLVKDIGCLPYLGVSHQWKS... | null | null | calcium-mediated signaling [GO:0019722]; cell chemotaxis [GO:0060326]; G protein-coupled receptor signaling pathway [GO:0007186]; immune response [GO:0006955]; inflammatory response [GO:0006954]; positive regulation of cytosolic calcium ion concentration [GO:0007204]; viral genome replication [GO:0019079] | external side of plasma membrane [GO:0009897]; plasma membrane [GO:0005886] | C-C chemokine binding [GO:0019957]; C-C chemokine receptor activity [GO:0016493]; C-X-C chemokine receptor activity [GO:0016494]; coreceptor activity [GO:0015026]; G protein-coupled receptor activity [GO:0004930] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Receptor for the C-X-C chemokine CXCL16. Used as a coreceptor by SIVs and by strains of HIV-2 and m-tropic HIV-1. | Homo sapiens (Human) |
O00584 | RNT2_HUMAN | MRPAALRGALLGCLCLALLCLGGADKRLRDNHEWKKLIMVQHWPETVCEKIQNDCRDPPDYWTIHGLWPDKSEGCNRSWPFNLEEIKDLLPEMRAYWPDVIHSFPNRSRFWKHEWEKHGTCAAQVDALNSQKKYFGRSLELYRELDLNSVLLKLGIKPSINYYQVADFKDALARVYGVIPKIQCLPPSQDEEVQTIGQIELCLTKQDQQLQNCTEPGEQPSPKQEVWLANGAAESRGLRVCEDGPVFYPPPKKTKH | 4.6.1.19 | null | innate immune response [GO:0045087]; RNA catabolic process [GO:0006401] | azurophil granule lumen [GO:0035578]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; lysosomal lumen [GO:0043202]; lysosome [GO:0005764]; mitochondrial intermembrane space [GO:0005758] | ribonuclease T2 activity [GO:0033897]; RNA binding [GO:0003723]; RNA endonuclease activity [GO:0004521]; RNA nuclease activity [GO:0004540] | PF00445; | 3.90.730.10; | RNase T2 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:15809705, ECO:0000269|PubMed:16620762}. Lysosome lumen {ECO:0000269|PubMed:16620762}. Endoplasmic reticulum lumen {ECO:0000269|PubMed:16620762}. Mitochondrion intermembrane space {ECO:0000269|PubMed:28730546, ECO:0000269|PubMed:30184494, ECO:0000269|PubMed:30385512}. N... | CATALYTIC ACTIVITY: Reaction=a ribonucleotidyl-ribonucleotide-RNA + H2O = a 3'-end 3'-phospho-ribonucleotide-RNA + a 5'-end dephospho-ribonucleoside-RNA + H(+); Xref=Rhea:RHEA:68052, Rhea:RHEA-COMP:10463, Rhea:RHEA-COMP:13936, Rhea:RHEA-COMP:17355, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:83062, ChEBI:CHEBI:13... | null | null | null | null | FUNCTION: Ribonuclease that plays an essential role in innate immune response by recognizing and degrading RNAs from microbial pathogens that are subsequently sensed by TLR8 (PubMed:31778653). Cleaves preferentially single-stranded RNA molecules between purine and uridine residues, which critically contributes to the s... | Homo sapiens (Human) |
O00585 | CCL21_HUMAN | MAQSLALSLLILVLAFGIPRTQGSDGGAQDCCLKYSQRKIPAKVVRSYRKQEPSLGCSIPAILFLPRKRSQAELCADPKELWVQQLMQHLDKTPSPQKPAQGCRKDRGASKTGKKGKGSKGCKRTERSQTPKGP | null | null | cell chemotaxis [GO:0060326]; cell maturation [GO:0048469]; cell-cell signaling [GO:0007267]; cellular response to chemokine [GO:1990869]; cellular response to interleukin-1 [GO:0071347]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to type II interferon [GO:0071346]; chemokine (C-C motif)... | extracellular region [GO:0005576]; extracellular space [GO:0005615] | CCR chemokine receptor binding [GO:0048020]; CCR7 chemokine receptor binding [GO:0031732]; chemokine activity [GO:0008009]; chemokine receptor binding [GO:0042379] | PF00048; | 2.40.50.40; | Intercrine beta (chemokine CC) family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Inhibits hemopoiesis and stimulates chemotaxis. Chemotactic in vitro for thymocytes and activated T-cells, but not for B-cells, macrophages, or neutrophils. Shows preferential activity towards naive T-cells. May play a role in mediating homing of lymphocytes to secondary lymphoid organs. Binds to atypical che... | Homo sapiens (Human) |
O00587 | MFNG_HUMAN | MQCRLPRGLAGALLTLLCMGLLCLRYHLNLSPQRVQGTPELSQPNPGPPKLQLHDVFIAVKTTRAFHRLRLELLLDTWVSRTREQTFVFTDSPDKGLQERLGSHLVVTNCSAEHSHPALSCKMAAEFDTFLASGLRWFCHVDDDNYVNPRALLQLLRAFPLARDVYVGRPSLNRPIHASEPQPHNRTRLVQFWFATGGAGFCINRKLALKMAPWASGSRFMDTSALIRLPDDCTMGYIIECKLGGRLQPSPLFHSHLETLQLLRTAQLPEQVTLSYGVFEGKLNVIKLQGPFSPEEDPSRFRSLHCLLYPDTPWCPQLGA... | 2.4.1.222 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:O09008}; Note=Has some activity with cobalt, magnesium and calcium, but not zinc. {ECO:0000250|UniProtKB:O09008}; | blastocyst formation [GO:0001825]; marginal zone B cell differentiation [GO:0002315]; pattern specification process [GO:0007389]; positive regulation of Notch signaling pathway [GO:0045747]; regulation of Notch signaling pathway [GO:0008593] | extracellular space [GO:0005615]; Golgi membrane [GO:0000139] | metal ion binding [GO:0046872]; O-fucosylpeptide 3-beta-N-acetylglucosaminyltransferase activity [GO:0033829] | PF02434; | 3.90.550.50; | Glycosyltransferase 31 family | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Single-pass type II membrane protein {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=3-O-(alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(N-acetyl-beta-D-glucosaminyl-(1->3)-alpha-L-fucosyl)-L-threonyl-[EGF-like domain protein] + H(+) + UDP; Xref=Rhea:RHEA:70531, Rhea:RHEA-COMP:17922, Rhea:RHEA-COMP:17923, ChEBI:CHEBI:15378, C... | null | null | null | null | FUNCTION: Glycosyltransferase that initiates the elongation of O-linked fucose residues attached to EGF-like repeats in the extracellular domain of Notch molecules (By similarity). Modulates NOTCH1 activity by modifying O-fucose residues at specific EGF-like domains resulting in inhibition of NOTCH1 activation by JAG1 ... | Homo sapiens (Human) |
O00590 | ACKR2_HUMAN | MAATASPQPLATEDADSENSSFYYYDYLDEVAFMLCRKDAVVSFGKVFLPVFYSLIFVLGLSGNLLLLMVLLRYVPRRRMVEIYLLNLAISNLLFLVTLPFWGISVAWHWVFGSFLCKMVSTLYTINFYSGIFFISCMSLDKYLEIVHAQPYHRLRTRAKSLLLATIVWAVSLAVSIPDMVFVQTHENPKGVWNCHADFGGHGTIWKLFLRFQQNLLGFLLPLLAMIFFYSRIGCVLVRLRPAGQGRALKIAAALVVAFFVLWFPYNLTLFLHTLLDLQVFGNCEVSQHLDYALQVTESIAFLHCCFSPILYAFSSHRFR... | null | null | calcium-mediated signaling [GO:0019722]; cell chemotaxis [GO:0060326]; immune response [GO:0006955]; inflammatory response [GO:0006954]; intracellular signal transduction [GO:0035556]; positive regulation of cytosolic calcium ion concentration [GO:0007204] | actin filament [GO:0005884]; cytosol [GO:0005829]; early endosome [GO:0005769]; external side of plasma membrane [GO:0009897]; intracellular membrane-bounded organelle [GO:0043231]; nuclear membrane [GO:0031965]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; recycling endosome [GO:0055037] | C-C chemokine binding [GO:0019957]; C-C chemokine receptor activity [GO:0016493]; chemokine receptor activity [GO:0004950]; scavenger receptor activity [GO:0005044] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family, Atypical chemokine receptor subfamily | PTM: Phosphorylated on serine residues in the C-terminal cytoplasmic tail. {ECO:0000269|PubMed:18201974}. | SUBCELLULAR LOCATION: Early endosome. Recycling endosome. Cell membrane; Multi-pass membrane protein. Note=Predominantly localizes to endocytic vesicles, and upon stimulation by the ligand is internalized via clathrin-coated pits. Once internalized, the ligand dissociates from the receptor, and is targeted to degradati... | null | null | null | null | null | FUNCTION: Atypical chemokine receptor that controls chemokine levels and localization via high-affinity chemokine binding that is uncoupled from classic ligand-driven signal transduction cascades, resulting instead in chemokine sequestration, degradation, or transcytosis. Also known as interceptor (internalizing recept... | Homo sapiens (Human) |
O00591 | GBRP_HUMAN | MNYSLHLAFVCLSLFTERMCIQGSQFNVEVGRSDKLSLPGFENLTAGYNKFLRPNFGGEPVQIALTLDIASISSISESNMDYTATIYLRQRWMDQRLVFEGNKSFTLDARLVEFLWVPDTYIVESKKSFLHEVTVGNRLIRLFSNGTVLYALRITTTVACNMDLSKYPMDTQTCKLQLESWGYDGNDVEFTWLRGNDSVRGLEHLRLAQYTIERYFTLVTRSQQETGNYTRLVLQFELRRNVLYFILETYVPSTFLVVLSWVSFWISLDSVPARTCIGVTTVLSMTTLMIGSRTSLPNTNCFIKAIDVYLGICFSFVFGA... | null | null | chemical synaptic transmission [GO:0007268]; chloride transmembrane transport [GO:1902476]; nervous system process [GO:0050877]; regulation of membrane potential [GO:0042391]; signal transduction [GO:0007165] | chloride channel complex [GO:0034707]; GABA-A receptor complex [GO:1902711]; neuron projection [GO:0043005]; plasma membrane [GO:0005886]; postsynaptic membrane [GO:0045211]; synapse [GO:0045202]; transmembrane transporter complex [GO:1902495] | chloride channel activity [GO:0005254]; extracellular ligand-gated monoatomic ion channel activity [GO:0005230]; GABA-A receptor activity [GO:0004890]; neurotransmitter receptor activity [GO:0030594] | 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, GABRP sub-subfamily | null | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein {ECO:0000255}. Apical cell membrane {ECO:0000250|UniProtKB:O09028}; Multi-pass membrane protein {ECO:0000255}. Note=Located on the apical plasma membrane of alveolar epithelial type II cells. {ECO:0000250|UniProtKB:O09028}. | CATALYTIC ACTIVITY: Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823, ChEBI:CHEBI:17996; Evidence={ECO:0000269|PubMed:10462548}; | null | null | null | null | FUNCTION: Pi subunit of the heteropentameric ligand-gated chloride channel gated by gamma-aminobutyric acid (GABA) (PubMed:10462548). GABA-gated chloride channels, also named GABA(A) receptors (GABAAR), consist of five subunits arranged around a central pore and contain GABA active binding site(s) located at the alpha ... | Homo sapiens (Human) |
O00592 | PODXL_HUMAN | MRCALALSALLLLLSTPPLLPSSPSPSPSPSQNATQTTTDSSNKTAPTPASSVTIMATDTAQQSTVPTSKANEILASVKATTLGVSSDSPGTTTLAQQVSGPVNTTVARGGGSGNPTTTIESPKSTKSADTTTVATSTATAKPNTTSSQNGAEDTTNSGGKSSHSVTTDLTSTKAEHLTTPHPTSPLSPRQPTSTHPVATPTSSGHDHLMKISSSSSTVAIPGYTFTSPGMTTTLLETVFHHVSQAGLELLTSGDLPTLASQSAGITASSVISQRTQQTSSQMPASSTAPSSQETVQPTSPATALRTPTLPETMSSSPTA... | null | null | cell adhesion [GO:0007155]; cell migration [GO:0016477]; epithelial tube formation [GO:0072175]; negative regulation of cell adhesion [GO:0007162]; negative regulation of cell-cell adhesion [GO:0022408]; podocyte development [GO:0072015]; positive regulation of cell migration [GO:0030335]; positive regulation of cell-c... | apical plasma membrane [GO:0016324]; centriolar satellite [GO:0034451]; cytoplasm [GO:0005737]; extracellular exosome [GO:0070062]; extracellular space [GO:0005615]; filopodium [GO:0030175]; intracellular membrane-bounded organelle [GO:0043231]; lamellipodium [GO:0030027]; membrane raft [GO:0045121]; microvillus membra... | null | PF06365; | null | Podocalyxin family | PTM: N- and O-linked glycosylated. Sialoglycoprotein (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Apical cell membrane. Cell projection, lamellipodium. Cell projection, filopodium. Cell projection, ruffle. Cell projection, microvillus {ECO:0000250}. Membrane raft {ECO:0000250}. Membrane {ECO:0000305}; Single-pass type I membrane protein {ECO:0000305}. Note=In single attached epithelial cells i... | null | null | null | null | null | FUNCTION: Involved in the regulation of both adhesion and cell morphology and cancer progression. Functions as an anti-adhesive molecule that maintains an open filtration pathway between neighboring foot processes in the podocyte by charge repulsion. Acts as a pro-adhesive molecule, enhancing the adherence of cells to ... | Homo sapiens (Human) |
O00602 | FCN1_HUMAN | MELSGATMARGLAVLLVLFLHIKNLPAQAADTCPEVKVVGLEGSDKLTILRGCPGLPGAPGPKGEAGVIGERGERGLPGAPGKAGPVGPKGDRGEKGMRGEKGDAGQSQSCATGPRNCKDLLDRGYFLSGWHTIYLPDCRPLTVLCDMDTDGGGWTVFQRRMDGSVDFYRDWAAYKQGFGSQLGEFWLGNDNIHALTAQGSSELRVDLVDFEGNHQFAKYKSFKVADEAEKYKLVLGAFVGGSAGNSLTGHNNNFFSTKDQDNDVSSSNCAEKFQGAWWYADCHASNLNGLYLMGPHESYANGINWSAAKGYKYSYKVSE... | null | null | cell surface pattern recognition receptor signaling pathway [GO:0002752]; complement activation, lectin pathway [GO:0001867]; G protein-coupled receptor signaling pathway [GO:0007186]; negative regulation of viral entry into host cell [GO:0046597]; positive regulation of interleukin-8 production [GO:0032757]; positive ... | collagen trimer [GO:0005581]; collagen-containing extracellular matrix [GO:0062023]; external side of plasma membrane [GO:0009897]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; ficolin-1-rich granule lumen [GO:1904813]; plasma membrane [GO:0005886]; secretory granule lumen [GO:0034774]; serine-t... | antigen binding [GO:0003823]; carbohydrate binding [GO:0030246]; carbohydrate derivative binding [GO:0097367]; G protein-coupled receptor binding [GO:0001664]; metal ion binding [GO:0046872]; pattern recognition receptor activity [GO:0038187]; sialic acid binding [GO:0033691]; signaling receptor binding [GO:0005102] | PF01391;PF00147; | 3.90.215.10; | Ficolin lectin family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:20400674, ECO:0000269|PubMed:21037097}. Cell membrane {ECO:0000269|PubMed:20400674, ECO:0000269|PubMed:21037097}; Peripheral membrane protein {ECO:0000269|PubMed:20400674, ECO:0000269|PubMed:21037097}; Extracellular side {ECO:0000269|PubMed:20400674, ECO:0000269|PubMed... | null | null | null | null | null | FUNCTION: Extracellular lectin functioning as a pattern-recognition receptor in innate immunity. Binds the sugar moieties of pathogen-associated molecular patterns (PAMPs) displayed on microbes and activates the lectin pathway of the complement system. May also activate monocytes through a G protein-coupled receptor, F... | Homo sapiens (Human) |
O00622 | CCN1_HUMAN | MSSRIARALALVVTLLHLTRLALSTCPAACHCPLEAPKCAPGVGLVRDGCGCCKVCAKQLNEDCSKTQPCDHTKGLECNFGASSTALKGICRAQSEGRPCEYNSRIYQNGESFQPNCKHQCTCIDGAVGCIPLCPQELSLPNLGCPNPRLVKVTGQCCEEWVCDEDSIKDPMEDQDGLLGKELGFDASEVELTRNNELIAVGKGSSLKRLPVFGMEPRILYNPLQGQKCIVQTTSWSQCSKTCGTGISTRVTNDNPECRLVKETRICEVRPCGQPVYSSLKKGKKCSKTKKSPEPVRFTYAGCLSVKKYRPKYCGSCVDG... | null | null | apoptotic process involved in heart morphogenesis [GO:0003278]; atrial septum morphogenesis [GO:0060413]; atrioventricular valve morphogenesis [GO:0003181]; cell adhesion [GO:0007155]; chemotaxis [GO:0006935]; chondroblast differentiation [GO:0060591]; chorio-allantoic fusion [GO:0060710]; extracellular matrix organiza... | collagen-containing extracellular matrix [GO:0062023]; endoplasmic reticulum lumen [GO:0005788]; extracellular space [GO:0005615] | extracellular matrix binding [GO:0050840]; growth factor binding [GO:0019838]; heparin binding [GO:0008201]; integrin binding [GO:0005178] | PF00007;PF00219;PF19035;PF00093; | 2.10.70.10;2.20.100.10; | CCN family | null | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: Promotes cell proliferation, chemotaxis, angiogenesis and cell adhesion. Appears to play a role in wound healing by up-regulating, in skin fibroblasts, the expression of a number of genes involved in angiogenesis, inflammation and matrix remodeling including VEGA-A, VEGA-C, MMP1, MMP3, TIMP1, uPA, PAI-1 and i... | Homo sapiens (Human) |
O00623 | PEX12_HUMAN | MAEHGAHFTAASVADDQPSIFEVVAQDSLMTAVRPALQHVVKVLAESNPTHYGFLWRWFDEIFTLLDLLLQQHYLSRTSASFSENFYGLKRIVMGDTHKSQRLASAGLPKQQLWKSIMFLVLLPYLKVKLEKLVSSLREEDEYSIHPPSSRWKRFYRAFLAAYPFVNMAWEGWFLVQQLRYILGKAQHHSPLLRLAGVQLGRLTVQDIQALEHKPAKASMMQQPARSVSEKINSALKKAVGGVALSLSTGLSVGVFFLQFLDWWYSSENQETIKSLTALPTPPPPVHLDYNSDSPLLPKMKTVCPLCRKTRVNDTVLATS... | null | null | cellular response to reactive oxygen species [GO:0034614]; peroxisome organization [GO:0007031]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein import into peroxisome matrix [GO:0016558]; protein import into peroxisome matrix, receptor recycling [GO:0016562]; protein import into... | cytosol [GO:0005829]; peroxisomal importomer complex [GO:1990429]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777] | protein transmembrane transporter activity [GO:0008320]; ubiquitin ligase activator activity [GO:1990757]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270] | PF04757; | 3.30.40.10; | Pex2/pex10/pex12 family | null | SUBCELLULAR LOCATION: Peroxisome membrane {ECO:0000269|PubMed:9922452}; Multi-pass membrane protein {ECO:0000255}. | null | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:24662292}. | null | null | FUNCTION: Component of a retrotranslocation channel required for peroxisome organization by mediating export of the PEX5 receptor from peroxisomes to the cytosol, thereby promoting PEX5 recycling (PubMed:24662292, PubMed:9354782, PubMed:9632816). The retrotranslocation channel is composed of PEX2, PEX10 and PEX12; each... | Homo sapiens (Human) |
O00624 | NPT3_HUMAN | MDGKPATRKGPDFCSLRYGLALIMHFSNFTMITQRVSLSIAIIAMVNTTQQQGLSNASTEGPVADAFNNSSISIKEFDTKASVYQWSPETQGIIFSSINYGIILTLIPSGYLAGIFGAKKMLGAGLLISSLLTLFTPLAADFGVILVIMVRTVQGMAQGMAWTGQFTIWAKWAPPLERSKLTTIAGSGSAFGSFIILCVGGLISQALSWPFIFYIFGSTGCVCCLLWFTVIYDDPMHHPCISVREKEHILSSLAQQPSSPGRAVPIKAMVTCLPLWAIFLGFFSHFWLCTIILTYLPTYISTLLHVNIRDSGVLSSLPFI... | null | null | monoatomic anion transport [GO:0006820]; phosphate-containing compound metabolic process [GO:0006796]; sodium ion transport [GO:0006814] | apical plasma membrane [GO:0016324]; membrane [GO:0016020]; plasma membrane [GO:0005886] | sodium:phosphate symporter activity [GO:0005436]; transmembrane transporter activity [GO:0022857]; urate transmembrane transporter activity [GO:0015143] | PF07690; | 1.20.1250.20; | Major facilitator superfamily, Sodium/anion cotransporter family | null | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000250|UniProtKB:Q5SZA1}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=3 Na(+)(out) + phosphate(out) = 3 Na(+)(in) + phosphate(in); Xref=Rhea:RHEA:71255, ChEBI:CHEBI:29101, ChEBI:CHEBI:43474; Evidence={ECO:0000250|UniProtKB:Q5SZA1}; CATALYTIC ACTIVITY: Reaction=n chloride(in) + urate(out) = n chloride(out) + urate(in); Xref=Rhea:RHEA:72319, ChEBI:CHEBI:17775, ... | null | null | null | null | FUNCTION: Acts as a membrane potential-dependent organic anion transporter, the transport requires a low concentration of chloride ions (By similarity). Mediates chloride-dependent transport of urate (By similarity). Can actively transport inorganic phosphate into cells via Na(+) cotransport (By similarity). {ECO:00002... | Homo sapiens (Human) |
O00625 | PIR_HUMAN | MGSSKKVTLSVLSREQSEGVGARVRRSIGRPELKNLDPFLLFDEFKGGRPGGFPDHPHRGFETVSYLLEGGSMAHEDFCGHTGKMNPGDLQWMTAGRGILHAEMPCSEEPAHGLQLWVNLRSSEKMVEPQYQELKSEEIPKPSKDGVTVAVISGEALGIKSKVYTRTPTLYLDFKLDPGAKHSQPIPKGWTSFIYTISGDVYIGPDDAQQKIEPHHTAVLGEGDSVQVENKDPKRSHFVLIAGEPLREPVIQHGPFVMNTNEEISQAILDFRNAKNGFERAKTWKSKIGN | 1.13.11.24 | COFACTOR: Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000269|PubMed:14573596, ECO:0000269|PubMed:20711196}; Note=Binds 1 Fe cation per subunit. {ECO:0000269|PubMed:14573596, ECO:0000269|PubMed:20711196}; | digestion [GO:0007586]; monocyte differentiation [GO:0030224]; transcription by RNA polymerase II [GO:0006366] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear body [GO:0016604]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | metal ion binding [GO:0046872]; quercetin 2,3-dioxygenase activity [GO:0008127]; transcription coregulator activity [GO:0003712] | PF02678;PF05726; | 2.60.120.10; | Pirin family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20089166, ECO:0000269|PubMed:9079676}. Cytoplasm {ECO:0000269|PubMed:20089166}. Note=Predominantly localized in dot-like subnuclear structures. Cytoplasmic localization of PIR seems to positively correlate with melanoma progression. {ECO:0000269|PubMed:20089166, ECO:000... | CATALYTIC ACTIVITY: Reaction=O2 + quercetin = 2-(3,4-dihydroxybenzoyloxy)-4,6-dihydroxybenzoate + CO; Xref=Rhea:RHEA:15381, ChEBI:CHEBI:15379, ChEBI:CHEBI:17245, ChEBI:CHEBI:57628, ChEBI:CHEBI:57694; EC=1.13.11.24; Evidence={ECO:0000269|PubMed:15951572}; | null | PATHWAY: Flavonoid metabolism; quercetin degradation. {ECO:0000305|PubMed:15951572}. | null | null | FUNCTION: Transcriptional coregulator of NF-kappa-B which facilitates binding of NF-kappa-B proteins to target kappa-B genes in a redox-state-dependent manner. May be required for efficient terminal myeloid maturation of hematopoietic cells. Has quercetin 2,3-dioxygenase activity (in vitro). {ECO:0000269|PubMed:1595157... | Homo sapiens (Human) |
O00626 | CCL22_HUMAN | MDRLQTALLVVLVLLAVALQATEAGPYGANMEDSVCCRDYVRYRLPLRVVKHFYWTSDSCPRPGVVLLTFRDKEICADPRVPWVKMILNKLSQ | null | null | cell-cell signaling [GO:0007267]; cellular response to interleukin-1 [GO:0071347]; cellular response to tumor necrosis factor [GO:0071356]; cellular response to type II interferon [GO:0071346]; chemokine-mediated signaling pathway [GO:0070098]; chemotaxis [GO:0006935]; eosinophil chemotaxis [GO:0048245]; G protein-coup... | extracellular region [GO:0005576]; extracellular space [GO:0005615] | CCR chemokine receptor binding [GO:0048020]; chemokine activity [GO:0008009] | PF00048; | 2.40.50.40; | Intercrine beta (chemokine CC) family | PTM: The N-terminal processed forms MDC(3-69), MDC(5-69) and MDC(7-69) are produced by proteolytic cleavage after secretion from monocyte derived dendrocytes. {ECO:0000269|PubMed:11241286}. | SUBCELLULAR LOCATION: Secreted. | null | null | null | null | null | FUNCTION: May play a role in the trafficking of activated/effector T-lymphocytes to inflammatory sites and other aspects of activated T-lymphocyte physiology. Chemotactic for monocytes, dendritic cells and natural killer cells. Mild chemoattractant for primary activated T-lymphocytes and a potent chemoattractant for ch... | Homo sapiens (Human) |
O00628 | PEX7_HUMAN | MSAVCGGAARMLRTPGRHGYAAEFSPYLPGRLACATAQHYGIAGCGTLLILDPDEAGLRLFRSFDWNDGLFDVTWSENNEHVLITCSGDGSLQLWDTAKAAGPLQVYKEHAQEVYSVDWSQTRGEQLVVSGSWDQTVKLWDPTVGKSLCTFRGHESIIYSTIWSPHIPGCFASASGDQTLRIWDVKAAGVRIVIPAHQAEILSCDWCKYNENLLVTGAVDCSLRGWDLRNVRQPVFELLGHTYAIRRVKFSPFHASVLASCSYDFTVRFWNFSKPDSLLETVEHHTEFTCGLDFSLQSPTQVADCSWDETIKIYDPACLT... | null | null | endochondral ossification [GO:0001958]; ether lipid biosynthetic process [GO:0008611]; fatty acid beta-oxidation [GO:0006635]; neuron migration [GO:0001764]; peroxisome organization [GO:0007031]; protein import into peroxisome matrix [GO:0016558]; protein targeting to peroxisome [GO:0006625] | cytosol [GO:0005829]; peroxisomal matrix [GO:0005782]; peroxisomal membrane [GO:0005778]; peroxisome [GO:0005777] | enzyme binding [GO:0019899]; peroxisome matrix targeting signal-2 binding [GO:0005053]; protein homodimerization activity [GO:0042803] | PF00400; | 2.130.10.10; | WD repeat peroxin-7 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:11931631, ECO:0000269|PubMed:25538232}. Peroxisome matrix {ECO:0000269|PubMed:11546814, ECO:0000269|PubMed:11931631, ECO:0000269|PubMed:25538232}. Note=Translocated into the peroxisome matrix together with PTS2-containing cargo proteins and PEX5. {ECO:0000269... | null | null | null | null | null | FUNCTION: Receptor required for the peroxisomal import of proteins containing a C-terminal PTS2-type peroxisomal targeting signal (PubMed:11931631, PubMed:22057399, PubMed:25538232, PubMed:9090381). Specifically binds to cargo proteins containing a PTS2 peroxisomal targeting signal in the cytosol (PubMed:11931631, PubM... | Homo sapiens (Human) |
O00629 | IMA3_HUMAN | MADNEKLDNQRLKNFKNKGRDLETMRRQRNEVVVELRKNKRDEHLLKRRNVPHEDICEDSDIDGDYRVQNTSLEAIVQNASSDNQGIQLSAVQAARKLLSSDRNPPIDDLIKSGILPILVHCLERDDNPSLQFEAAWALTNIASGTSEQTQAVVQSNAVPLFLRLLHSPHQNVCEQAVWALGNIIGDGPQCRDYVISLGVVKPLLSFISPSIPITFLRNVTWVMVNLCRHKDPPPPMETIQEILPALCVLIHHTDVNILVDTVWALSYLTDAGNEQIQMVIDSGIVPHLVPLLSHQEVKVQTAALRAVGNIVTGTDEQTQ... | null | null | dopamine secretion [GO:0014046]; gene expression [GO:0010467]; NLS-bearing protein import into nucleus [GO:0006607]; protein import into nucleus [GO:0006606] | cytosol [GO:0005829]; NLS-dependent protein nuclear import complex [GO:0042564]; nuclear membrane [GO:0031965]; nuclear pore [GO:0005643]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | nuclear import signal receptor activity [GO:0061608]; nuclear localization sequence binding [GO:0008139] | PF00514;PF16186;PF01749; | 1.20.5.690;1.25.10.10; | Importin alpha family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}. | null | null | null | null | null | FUNCTION: Functions in nuclear protein import as an adapter protein for nuclear receptor KPNB1. Binds specifically and directly to substrates containing either a simple or bipartite NLS motif. Docking of the importin/substrate complex to the nuclear pore complex (NPC) is mediated by KPNB1 through binding to nucleoporin... | Homo sapiens (Human) |
O00631 | SARCO_HUMAN | MGINTRELFLNFTIVLITVILMWLLVRSYQY | null | null | calcium ion transport [GO:0006816]; negative regulation of ATPase-coupled calcium transmembrane transporter activity [GO:1901895]; negative regulation of calcium ion binding [GO:1901877]; negative regulation of calcium ion import [GO:0090281]; negative regulation of calcium ion transmembrane transporter activity [GO:19... | membrane [GO:0016020]; sarcoplasmic reticulum [GO:0016529]; sarcoplasmic reticulum membrane [GO:0033017] | ATPase binding [GO:0051117]; enzyme inhibitor activity [GO:0004857] | PF05366; | null | Sarcolipin family | null | SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:11781085, ECO:0000269|PubMed:9575189}; Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:P42532}; Single-pass membrane protein {ECO:0000250}. | null | null | null | null | null | FUNCTION: Reversibly inhibits the activity of ATP2A1 and ATP2A2 in sarcoplasmic reticulum by decreasing the apparent affinity of the ATPase for Ca(2+). Modulates calcium re-uptake during muscle relaxation and plays an important role in calcium homeostasis in muscle. Required for muscle-based, non-shivering thermogenesi... | Homo sapiens (Human) |
O00635 | TRI38_HUMAN | MASTTSTKKMMEEATCSICLSLMTNPVSINCGHSYCHLCITDFFKNPSQKQLRQETFCCPQCRAPFHMDSLRPNKQLGSLIEALKETDQEMSCEEHGEQFHLFCEDEGQLICWRCERAPQHKGHTTALVEDVCQGYKEKLQKAVTKLKQLEDRCTEQKLSTAMRITKWKEKVQIQRQKIRSDFKNLQCFLHEEEKSYLWRLEKEEQQTLSRLRDYEAGLGLKSNELKSHILELEEKCQGSAQKLLQNVNDTLSRSWAVKLETSEAVSLELHTMCNVSKLYFDVKKMLRSHQVSVTLDPDTAHHELILSEDRRQVTRGYTQ... | 2.3.2.27 | null | innate immune response [GO:0045087]; negative regulation of defense response to virus [GO:0050687]; positive regulation of autophagy [GO:0010508]; positive regulation of canonical NF-kappaB signal transduction [GO:0043123]; positive regulation of DNA-binding transcription factor activity [GO:0051091]; positive regulati... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; nucleoplasm [GO:0005654] | protein homodimerization activity [GO:0042803]; protein kinase binding [GO:0019901]; transcription coactivator activity [GO:0003713]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270] | PF13765;PF00622;PF00643;PF15227; | 2.60.120.920;3.30.160.60;3.30.40.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q5SZ99}. | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; EC=2.3.2.27; Evidence={ECO:0000305|PubMed:23056470}; | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:23056470}.; PATHWAY: Protein modification; protein sumoylation. {ECO:0000250|UniProtKB:Q5SZ99}. | null | null | FUNCTION: E3 ubiquitin-protein and E3 SUMO-protein ligase that acts as a regulator of innate immunity (PubMed:23056470). Acts as a negative regulator of type I interferon IFN-beta production by catalyzing 'Lys-48'-linked polyubiquitination of AZI2/NAP1, leading to its degradation (By similarity). Mediates 'Lys-48'-link... | Homo sapiens (Human) |
O00712 | NFIB_HUMAN | MMYSPICLTQDEFHPFIEALLPHVRAIAYTWFNLQARKRKYFKKHEKRMSKDEERAVKDELLSEKPEIKQKWASRLLAKLRKDIRQEYREDFVLTVTGKKHPCCVLSNPDQKGKIRRIDCLRQADKVWRLDLVMVILFKGIPLESTDGERLMKSPHCTNPALCVQPHHITVSVKELDLFLAYYVQEQDSGQSGSPSHNDPAKNPPGYLEDSFVKSGVFNVSELVRVSRTPITQGTGVNFPIGEIPSQPYYHDMNSGVNLQRSLSSPPSSKRPKTISIDENMEPSPTGDFYPSPSSPAAGSRTWHERDQDMSSPTTMKKPE... | null | null | anterior commissure morphogenesis [GO:0021960]; brain development [GO:0007420]; cell differentiation involved in salivary gland development [GO:0060689]; cell proliferation in forebrain [GO:0021846]; chondrocyte differentiation [GO:0002062]; club cell differentiation [GO:0060486]; commissural neuron axon guidance [GO:0... | cerebellar mossy fiber [GO:0044300]; chromatin [GO:0000785]; fibrillar center [GO:0001650]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific double-stranded DNA b... | PF00859;PF03165;PF10524; | null | CTF/NF-I family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Transcriptional activator of GFAP, essential for proper brain development (PubMed:30388402). Recognizes and binds the palindromic sequence 5'-TTGGCNNNNNGCCAA-3' present in viral and cellular promoters and in the origin of replication of adenovirus type 2. These proteins are individually capable of activating ... | Homo sapiens (Human) |
O00716 | E2F3_HUMAN | MRKGIQPALEQYLVTAGGGEGAAVVAAAAAASMDKRALLASPGFAAAAAAAAAPGAYIQILTTNTSTTSCSSSLQSGAVAAGPLLPSAPGAEQTAGSLLYTTPHGPSSRAGLLQQPPALGRGGSGGGGGPPAKRRLELGESGHQYLSDGLKTPKGKGRAALRSPDSPKTPKSPSEKTRYDTSLGLLTKKFIQLLSQSPDGVLDLNKAAEVLKVQKRRIYDITNVLEGIHLIKKKSKNNVQWMGCSLSEDGGMLAQCQGLSKEVTELSQEEKKLDELIQSCTLDLKLLTEDSENQRLAYVTYQDIRKISGLKDQTVIVVKA... | null | null | G1/S transition of mitotic cell cycle [GO:0000082]; negative regulation of fat cell proliferation [GO:0070345]; positive regulation of cell population proliferation [GO:0008284]; positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of vascular associated smooth muscle cell apoptot... | chromatin [GO:0000785]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA polymerase II transcription regulator complex [GO:0090575] | cis-regulatory region sequence-specific DNA binding [GO:0000987]; DNA-binding transcription activator activity [GO:0001216]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription factor activity [GO:0003700]; DNA-binding transcription factor activity, RNA polym... | PF16421;PF02319; | 6.10.250.540;1.10.10.10; | E2F/DP family | null | SUBCELLULAR LOCATION: Nucleus. | null | null | null | null | null | FUNCTION: Transcription activator that binds DNA cooperatively with DP proteins through the E2 recognition site, 5'-TTTC[CG]CGC-3' found in the promoter region of a number of genes whose products are involved in cell cycle regulation or in DNA replication. The DRTF1/E2F complex functions in the control of cell-cycle pr... | Homo sapiens (Human) |
O00743 | PPP6_HUMAN | MAPLDLDKYVEIARLCKYLPENDLKRLCDYVCDLLLEESNVQPVSTPVTVCGDIHGQFYDLCELFRTGGQVPDTNYIFMGDFVDRGYYSLETFTYLLALKAKWPDRITLLRGNHESRQITQVYGFYDECQTKYGNANAWRYCTKVFDMLTVAALIDEQILCVHGGLSPDIKTLDQIRTIERNQEIPHKGAFCDLVWSDPEDVDTWAISPRGAGWLFGAKVTNEFVHINNLKLICRAHQLVHEGYKFMFDEKLVTVWSAPNYCYRCGNIASIMVFKDVNTREPKLFRAVPDSERVIPPRTTTPYFL | 3.1.3.16 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:P36873}; Note=Binds 2 manganese ions per subunit. {ECO:0000250|UniProtKB:P36873}; | COPII vesicle coating [GO:0048208]; G1/S transition of mitotic cell cycle [GO:0000082]; innate immune response [GO:0045087]; negative regulation of cGAS/STING signaling pathway [GO:0160049]; protein dephosphorylation [GO:0006470] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; nucleoplasm [GO:0005654] | metal ion binding [GO:0046872]; myosin phosphatase activity [GO:0017018]; protein serine/threonine phosphatase activity [GO:0004722] | PF00149; | 3.60.21.10; | PPP phosphatase family, PP-6 (PP-V) subfamily | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:29053956}. Cytoplasm {ECO:0000269|PubMed:16769727, ECO:0000269|PubMed:17568194}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-seryl-[protein] = L-seryl-[protein] + phosphate; Xref=Rhea:RHEA:20629, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15377, ChEBI:CHEBI:29999, ChEBI:CHEBI:43474, ChEBI:CHEBI:83421; EC=3.1.3.16; Evidence={ECO:0000269|PubMed:29053956, ECO:0000269|PubMed:32474700}; C... | null | null | null | null | FUNCTION: Catalytic subunit of protein phosphatase 6 (PP6) (PubMed:17079228, PubMed:29053956, PubMed:32474700). PP6 is a component of a signaling pathway regulating cell cycle progression in response to IL2 receptor stimulation (PubMed:10227379). N-terminal domain restricts G1 to S phase progression in cancer cells, in... | Homo sapiens (Human) |
O00744 | WN10B_HUMAN | MLEEPRPRPPPSGLAGLLFLALCSRALSNEILGLKLPGEPPLTANTVCLTLSGLSKRQLGLCLRNPDVTASALQGLHIAVHECQHQLRDQRWNCSALEGGGRLPHHSAILKRGFRESAFSFSMLAAGVMHAVATACSLGKLVSCGCGWKGSGEQDRLRAKLLQLQALSRGKSFPHSLPSPGPGSSPSPGPQDTWEWGGCNHDMDFGEKFSRDFLDSREAPRDIQARMRIHNNRVGRQVVTENLKRKCKCHGTSGSCQFKTCWRAAPEFRAVGAALRERLGRAIFIDTHNRNSGAFQPRLRPRRLSGELVYFEKSPDFCER... | null | null | bone trabecula formation [GO:0060346]; canonical Wnt signaling pathway [GO:0060070]; cell fate commitment [GO:0045165]; cellular response to cAMP [GO:0071320]; cellular response to parathyroid hormone stimulus [GO:0071374]; cellular response to retinoic acid [GO:0071300]; chondrocyte differentiation [GO:0002062]; epith... | extracellular region [GO:0005576]; extracellular space [GO:0005615] | cytokine activity [GO:0005125]; frizzled binding [GO:0005109]; receptor ligand activity [GO:0048018] | PF00110; | 3.30.2460.20; | Wnt family | PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition. {ECO:0000250|UniProtKB:P27467, ECO:0000250|UniProtKB:P56704}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305}. Secreted {ECO:0000269|PubMed:26902720}. | null | null | null | null | null | FUNCTION: Member of the Wnt ligand gene family that encodes for secreted proteins, which activate the Wnt signaling cascade. Specifically activates canonical Wnt/beta-catenin signaling and thus triggers beta-catenin/LEF/TCF-mediated transcriptional programs. Involved in signaling networks controlling stemness, pluripot... | Homo sapiens (Human) |
O00746 | NDKM_HUMAN | MGGLFWRSALRGLRCGPRAPGPSLLVRHGSGGPSWTRERTLVAVKPDGVQRRLVGDVIQRFERRGFTLVGMKMLQAPESVLAEHYQDLRRKPFYPALIRYMSSGPVVAMVWEGYNVVRASRAMIGHTDSAEAAPGTIRGDFSVHISRNVIHASDSVEGAQREIQLWFQSSELVSWADGGQHSSIHPA | 2.7.4.6 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; | CTP biosynthetic process [GO:0006241]; GTP biosynthetic process [GO:0006183]; lipid transport [GO:0006869]; nucleoside metabolic process [GO:0009116]; phosphorylation [GO:0016310]; UTP biosynthetic process [GO:0006228] | mitochondrial inner membrane [GO:0005743]; mitochondrial intermembrane space [GO:0005758]; mitochondrial matrix [GO:0005759]; mitochondrion [GO:0005739] | ATP binding [GO:0005524]; cardiolipin binding [GO:1901612]; metal ion binding [GO:0046872]; nucleoside diphosphate kinase activity [GO:0004550] | PF00334; | 3.30.70.141; | NDK family | null | SUBCELLULAR LOCATION: Mitochondrion intermembrane space {ECO:0000269|PubMed:18635542}; Peripheral membrane protein. Mitochondrion matrix {ECO:0000305|PubMed:18635542}. Note=Predominantly localized in the mitochondrion intermembrane space (PubMed:18635542). Colocalizes with OPA1 in mitochondria (PubMed:24970086). {ECO:0... | 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; Evidence={ECO:0000269|PubMed:10799505}; CATALYTIC ACTIVITY: Reaction=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. Through the catalyzed exchange of gamma-phosphate between di- and triphosphonucleosides participa... | Homo sapiens (Human) |
O00748 | EST2_HUMAN | MRLHRLRARLSAVACGLLLLLVRGQGQDSASPIRTTHTGQVLGSLVHVKGANAGVQTFLGIPFAKPPLGPLRFAPPEPPESWSGVRDGTTHPAMCLQDLTAVESEFLSQFNMTFPSDSMSEDCLYLSIYTPAHSHEGSNLPVMVWIHGGALVFGMASLYDGSMLAALENVVVVIIQYRLGVLGFFSTGDKHATGNWGYLDQVAALRWVQQNIAHFGGNPDRVTIFGESAGGTSVSSLVVSPISQGLFHGAIMESGVALLPGLIASSADVISTVVANLSACDQVDSEALVGCLRGKSKEEILAINKPFKMIPGVVDGVFLP... | 3.1.1.1; 3.1.1.56; 3.1.1.84 | null | catabolic process [GO:0009056]; prostaglandin metabolic process [GO:0006693]; xenobiotic metabolic process [GO:0006805] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum lumen [GO:0005788]; intracellular membrane-bounded organelle [GO:0043231] | carboxylesterase activity [GO:0106435]; carboxylic ester hydrolase activity [GO:0052689]; methylumbelliferyl-acetate deacetylase activity [GO:0047374] | PF00135; | 3.40.50.1820; | Type-B carboxylesterase/lipase family | PTM: Glycosylated. {ECO:0000269|PubMed:19159218, ECO:0000269|PubMed:9169443}. | SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000269|PubMed:22446793}. | CATALYTIC ACTIVITY: Reaction=cocaine + H2O = benzoate + ecgonine methyl ester + H(+); Xref=Rhea:RHEA:27506, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16150, ChEBI:CHEBI:59908, ChEBI:CHEBI:60056; EC=3.1.1.84; Evidence={ECO:0000269|PubMed:9169443}; CATALYTIC ACTIVITY: Reaction=a carboxylic ester + H2O = a carboxy... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=0.39 mM for cocaine {ECO:0000269|PubMed:9169443}; KM=0.15 mM for 4-methylumbelliferyl acetate {ECO:0000269|PubMed:9169443}; KM=6.8 mM for heroin {ECO:0000269|PubMed:9169443}; KM=46 uM for 2-arachidonoylglycerol {ECO:0000269|PubMed:21049984}; KM=750 uM for prostagla... | null | null | null | FUNCTION: Involved in the detoxification of xenobiotics and in the activation of ester and amide prodrugs (PubMed:9169443). Shows high catalytic efficiency for hydrolysis of cocaine, 4-methylumbelliferyl acetate, heroin and 6-monoacetylmorphine (PubMed:9169443). Hydrolyzes aspirin, substrates with large alcohol group a... | Homo sapiens (Human) |
O00750 | P3C2B_HUMAN | MSSTQGNGEHWKSLESVGISRKELAMAEALQMEYDALSRLRHDKEENRAKQNADPSLISWDEPGVDFYSKPAGRRTDLKLLRGLSGSDPTLNYNSLSPQEGPPNHSTSQGPQPGSDPWPKGSLSGDYLYIFDGSDGGVSSSPGPGDIEGSCKKLSPPPLPPRASIWDTPPLPPRKGSPSSSKISQPSDINTFSLVEQLPGKLLEHRILEEEEVLGGGGQGRLLGSVDYDGINDAITRLNLKSTYDAEMLRDATRGWKEGRGPLDFSKDTSGKPVARSKTMPPQVPPRTYASRYGNRKNATPGKNRRISAAPVGSRPHTVA... | 2.7.1.137; 2.7.1.154 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:9830063}; Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:9830063}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:10805725}; | autophagosome organization [GO:1905037]; cell migration [GO:0016477]; cellular response to starvation [GO:0009267]; phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0043491]; phosphatidylinositol-3-phosphate biosynthetic process [GO:0036092]; phosphatidylinositol-mediated signaling [GO:0048015]; p... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; endocytic vesicle [GO:0030139]; endoplasmic reticulum [GO:0005783]; intracellular membrane-bounded organelle [GO:0043231]; nucleoplasm [GO:0005654]; phosphatidylinositol 3-kinase complex [GO:0005942]; plasma membrane [GO:0005886] | 1-phosphatidylinositol-3-kinase activity [GO:0016303]; 1-phosphatidylinositol-4-phosphate 3-kinase activity [GO:0035005]; ATP binding [GO:0005524]; phosphatidylinositol binding [GO:0035091] | PF00168;PF00454;PF00792;PF00794;PF00613;PF00787; | 2.60.40.150;1.10.1070.11;1.25.40.70;3.30.1520.10; | PI3/PI4-kinase family | null | SUBCELLULAR LOCATION: Microsome {ECO:0000269|PubMed:14563213, ECO:0000269|PubMed:9830063}. Cell membrane {ECO:0000269|PubMed:14563213, ECO:0000269|PubMed:9830063}. Cytoplasm, cytosol {ECO:0000269|PubMed:14563213, ECO:0000269|PubMed:9830063}. Nucleus {ECO:0000269|PubMed:14563213}. Endoplasmic reticulum {ECO:0000269|PubM... | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol 4-phosphate) + ATP = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3,4-bisphosphate) + ADP + H(+); Xref=Rhea:RHEA:18373, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57658, ChEBI:CHEBI:58178, ChEBI:CHEBI:456216; EC=2.7.1.154; Evid... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=120 uM for ATP-Mg(2+) {ECO:0000269|PubMed:9830063}; KM=120 uM for ATP-Ca(2+) {ECO:0000269|PubMed:9830063}; Vmax=737 nmol/min/mg enzyme for ATP-Mg(2+) {ECO:0000269|PubMed:9830063}; Vmax=737 nmol/min/mg enzyme for ATP-Ca(2+) {ECO:0000269|PubMed:9830063}; | null | null | null | FUNCTION: Phosphorylates PtdIns and PtdIns4P with a preference for PtdIns (PubMed:10805725, PubMed:11533253, PubMed:9830063). Does not phosphorylate PtdIns(4,5)P2 (PubMed:9830063). May be involved in EGF and PDGF signaling cascades (PubMed:10805725). {ECO:0000269|PubMed:10805725, ECO:0000269|PubMed:11533253, ECO:000026... | Homo sapiens (Human) |
O00754 | MA2B1_HUMAN | MGAYARASGVCARGCLDSAGPWTMSRALRPPLPPLCFFLLLLAAAGARAGGYETCPTVQPNMLNVHLLPHTHDDVGWLKTVDQYFYGIKNDIQHAGVQYILDSVISALLADPTRRFIYVEIAFFSRWWHQQTNATQEVVRDLVRQGRLEFANGGWVMNDEAATHYGAIVDQMTLGLRFLEDTFGNDGRPRVAWHIDPFGHSREQASLFAQMGFDGFFFGRLDYQDKWVRMQKLEMEQVWRASTSLKPPTADLFTGVLPNGYNPPRNLCWDVLCVDQPLVEDPRSPEYNAKELVDYFLNVATAQGRYYRTNHTVMTMGSDF... | 3.2.1.24 | COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250}; | learning or memory [GO:0007611]; mannose metabolic process [GO:0006013]; N-glycan processing [GO:0006491]; oligosaccharide catabolic process [GO:0009313]; protein deglycosylation [GO:0006517]; protein modification process [GO:0036211] | azurophil granule lumen [GO:0035578]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; Golgi membrane [GO:0000139]; intracellular membrane-bounded organelle [GO:0043231]; lysosomal lumen [GO:0043202]; lysosome [GO:0005764]; nucleoplasm [GO:0005654] | alpha-mannosidase activity [GO:0004559]; carbohydrate binding [GO:0030246]; metal ion binding [GO:0046872] | PF09261;PF07748;PF01074;PF21260; | 2.60.40.1360;3.20.110.10;1.20.1270.50;2.60.40.1180; | Glycosyl hydrolase 38 family | PTM: First processed into 3 peptides of 70 kDa, 42 kDa (D) and 13/15 kDa (E). The 70 kDa peptide is further processed into three peptides (A, B and C). The A, B and C peptides are disulfide-linked.; PTM: Heavily glycosylated. {ECO:0000269|PubMed:12754519, ECO:0000269|PubMed:19159218}. | SUBCELLULAR LOCATION: Lysosome. | CATALYTIC ACTIVITY: Reaction=Hydrolysis of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides.; EC=3.2.1.24; | null | null | null | null | FUNCTION: Necessary for the catabolism of N-linked carbohydrates released during glycoprotein turnover. Cleaves all known types of alpha-mannosidic linkages. | Homo sapiens (Human) |
O00755 | WNT7A_HUMAN | MNRKARRCLGHLFLSLGMVYLRIGGFSSVVALGASIICNKIPGLAPRQRAICQSRPDAIIVIGEGSQMGLDECQFQFRNGRWNCSALGERTVFGKELKVGSREAAFTYAIIAAGVAHAITAACTQGNLSDCGCDKEKQGQYHRDEGWKWGGCSADIRYGIGFAKVFVDAREIKQNARTLMNLHNNEAGRKILEENMKLECKCHGVSGSCTTKTCWTTLPQFRELGYVLKDKYNEAVHVEPVRASRNKRPTFLKIKKPLSYRKPMDTDLVYIEKSPNYCEEDPVTGSVGTQGRACNKTAPQASGCDLMCCGRGYNTHQYAR... | null | null | angiogenesis [GO:0001525]; apoptotic process [GO:0006915]; asymmetric protein localization involved in cell fate determination [GO:0045167]; axonogenesis [GO:0007409]; canonical Wnt signaling pathway [GO:0060070]; cartilage condensation [GO:0001502]; cell fate commitment [GO:0045165]; cell proliferation in forebrain [G... | cell surface [GO:0009986]; endocytic vesicle membrane [GO:0030666]; endoplasmic reticulum lumen [GO:0005788]; extracellular exosome [GO:0070062]; extracellular matrix [GO:0031012]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; glutamatergic synapse [GO:0098978]; Golgi lumen [GO:0005796]; plasma m... | cytokine activity [GO:0005125]; frizzled binding [GO:0005109]; receptor ligand activity [GO:0048018]; signaling receptor binding [GO:0005102] | PF00110; | 3.30.2460.20; | Wnt family | PTM: Palmitoleoylation is required for efficient binding to frizzled receptors. Depalmitoleoylation leads to Wnt signaling pathway inhibition. {ECO:0000250|UniProtKB:P27467, ECO:0000250|UniProtKB:P56704}. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000305}. Secreted {ECO:0000269|PubMed:26902720}. | null | null | null | null | null | FUNCTION: Ligand for members of the frizzled family of seven transmembrane receptors that functions in the canonical Wnt/beta-catenin signaling pathway (By similarity). Plays an important role in embryonic development, including dorsal versus ventral patterning during limb development, skeleton development and urogenit... | Homo sapiens (Human) |
O00757 | F16P2_HUMAN | MTDRSPFETDMLTLTRYVMEKGRQAKGTGELTQLLNSMLTAIKAISSAVRKAGLAHLYGIAGSVNVTGDEVKKLDVLSNSLVINMVQSSYSTCVLVSEENKDAIITAKEKRGKYVVCFDPLDGSSNIDCLASIGTIFAIYRKTSEDEPSEKDALQCGRNIVAAGYALYGSATLVALSTGQGVDLFMLDPALGEFVLVEKDVKIKKKGKIYSLNEGYAKYFDAATTEYVQKKKFPEDGSAPYGARYVGSMVADVHRTLVYGGIFLYPANQKSPKGKLRLLYECNPVAYIIEQAGGLATTGTQPVLDVKPEAIHQRVPLILG... | 3.1.3.11 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:16213487, ECO:0000269|PubMed:24086250}; Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000269|PubMed:16213487, ECO:0000269|PubMed:24086250}; | fructose 1,6-bisphosphate metabolic process [GO:0030388]; fructose 6-phosphate metabolic process [GO:0006002]; fructose metabolic process [GO:0006000]; gluconeogenesis [GO:0006094]; sucrose biosynthetic process [GO:0005986] | anchoring junction [GO:0070161]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; extracellular exosome [GO:0070062]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; Z disc [GO:0030018] | fructose 1,6-bisphosphate 1-phosphatase activity [GO:0042132]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872] | PF00316;PF18913; | 3.40.190.80;3.30.540.10; | FBPase class 1 family | null | SUBCELLULAR LOCATION: Cell junction {ECO:0000250}. Cytoplasm. Nucleus. Cytoplasm, myofibril, sarcomere, Z line. Note=In neonatal cardiomyocytes, distributed throughout the cytosol, accumulating in the intercalated disks which occur at the Z line of cardiomyocytes and connect adjacent cells, and also located in the nucl... | CATALYTIC ACTIVITY: Reaction=beta-D-fructose 1,6-bisphosphate + H2O = beta-D-fructose 6-phosphate + phosphate; Xref=Rhea:RHEA:11064, ChEBI:CHEBI:15377, ChEBI:CHEBI:32966, ChEBI:CHEBI:43474, ChEBI:CHEBI:57634; EC=3.1.3.11; Evidence={ECO:0000269|PubMed:17350621, ECO:0000269|PubMed:18214967}; | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=1.3 uM for fructose 1,6-bisphosphate {ECO:0000269|PubMed:16213487, ECO:0000269|PubMed:17350621}; KM=2.6 uM for fructose 1,6-bisphosphate {ECO:0000269|PubMed:16213487, ECO:0000269|PubMed:17350621}; Note=The kinetic constants are determined for the recombinant enzyme... | PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. | null | null | FUNCTION: Catalyzes the hydrolysis of fructose 1,6-bisphosphate to fructose 6-phosphate in the presence of divalent cations and probably participates in glycogen synthesis from carbohydrate precursors, such as lactate. {ECO:0000269|PubMed:17350621, ECO:0000269|PubMed:18214967, ECO:0000269|PubMed:33977262}. | Homo sapiens (Human) |
O00762 | UBE2C_HUMAN | MASQNRDPAATSVAAARKGAEPSGGAARGPVGKRLQQELMTLMMSGDKGISAFPESDNLFKWVGTIHGAAGTVYEDLRYKLSLEFPSGYPYNAPTVKFLTPCYHPNVDTQGNICLDILKEKWSALYDVRTILLSIQSLLGEPNIDSPLNTHAAELWKNPTAFKKYLQETYSKQVTSQEP | 2.3.2.23; 2.3.2.24 | null | anaphase-promoting complex-dependent catabolic process [GO:0031145]; cell division [GO:0051301]; exit from mitosis [GO:0010458]; free ubiquitin chain polymerization [GO:0010994]; positive regulation of exit from mitosis [GO:0031536]; positive regulation of mitotic metaphase/anaphase transition [GO:0045842]; positive re... | anaphase-promoting complex [GO:0005680]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; ubiquitin ligase complex [GO:0000151] | ATP binding [GO:0005524]; ubiquitin conjugating enzyme activity [GO:0061631]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-like protein ligase binding [GO:0044389]; ubiquitin-protein transferase activity [GO:0004842] | PF00179; | 3.10.110.10; | Ubiquitin-conjugating enzyme family | PTM: Autoubiquitinated by the APC/C complex, leading to its degradation by the proteasome. Its degradation plays a central role in APC/C regulation, allowing cyclin-A accumulation before S phase entry. APC/C substrates inhibit the autoubiquitination of UBE2C/UBCH10 but not its E2 function, hence APC/C remaining active ... | null | CATALYTIC ACTIVITY: Reaction=S-ubiquitinyl-[E1 ubiquitin-activating enzyme]-L-cysteine + [E2 ubiquitin-conjugating enzyme]-L-cysteine = [E1 ubiquitin-activating enzyme]-L-cysteine + S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine.; EC=2.3.2.23; Evidence={ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000255|PROS... | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000255|PROSITE-ProRule:PRU00388, ECO:0000269|PubMed:18485873}. | null | null | FUNCTION: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-11'- and 'Lys-48'-linked polyubiquitination. Acts as an essential factor of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated ubiquitin ligase that controls progression... | Homo sapiens (Human) |
O00763 | ACACB_HUMAN | MVLLLCLSCLIFSCLTFSWLKIWGKMTDSKPITKSKSEANLIPSQEPFPASDNSGETPQRNGEGHTLPKTPSQAEPASHKGPKDAGRRRNSLPPSHQKPPRNPLSSSDAAPSPELQANGTGTQGLEATDTNGLSSSARPQGQQAGSPSKEDKKQANIKRQLMTNFILGSFDDYSSDEDSVAGSSRESTRKGSRASLGALSLEAYLTTGEAETRVPTMRPSMSGLHLVKRGREHKKLDLHRDFTVASPAEFVTRFGGDRVIEKVLIANNGIAAVKCMRSIRRWAYEMFRNERAIRFVVMVTPEDLKANAEYIKMADHYVPV... | 6.4.1.2 | COFACTOR: Name=biotin; Xref=ChEBI:CHEBI:57586; Evidence={ECO:0000269|PubMed:16854592, ECO:0000269|PubMed:18247344}; COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE-ProRule:PRU00409, ECO:0000255|PROSITE-ProRule:PRU00969}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-Pro... | acetyl-CoA metabolic process [GO:0006084]; energy homeostasis [GO:0097009]; fatty acid biosynthetic process [GO:0006633]; fatty acid oxidation [GO:0019395]; glucose import [GO:0046323]; intracellular aspartate homeostasis [GO:0090459]; intracellular glutamate homeostasis [GO:0090461]; lactic acid secretion [GO:0046722]... | cytosol [GO:0005829]; mitochondrial fatty acid beta-oxidation multienzyme complex [GO:0016507]; mitochondrial outer membrane [GO:0005741]; mitochondrion [GO:0005739]; nucleus [GO:0005634] | acetyl-CoA carboxylase activity [GO:0003989]; ATP binding [GO:0005524]; biotin binding [GO:0009374]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872] | PF08326;PF21385;PF02785;PF00289;PF00364;PF01039;PF02786; | 2.40.50.100;3.40.50.20;3.30.1490.20;3.30.470.20;2.40.460.10;3.90.1770.10; | null | PTM: The biotin cofactor is covalently attached to the central biotinyl-binding domain and is required for the catalytic activity. {ECO:0000305|PubMed:18247344}.; PTM: Phosphorylation at Ser-222 by AMPK inactivates the enzyme (PubMed:12488245). Required for the maintenance of skeletal muscle lipid and glucose homeostas... | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000269|PubMed:10677481}. | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + ATP + hydrogencarbonate = ADP + H(+) + malonyl-CoA + phosphate; Xref=Rhea:RHEA:11308, ChEBI:CHEBI:15378, ChEBI:CHEBI:17544, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:57288, ChEBI:CHEBI:57384, ChEBI:CHEBI:456216; EC=6.4.1.2; Evidence={ECO:0000269|PubMed:16854592, ECO:000... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=120 uM for ATP {ECO:0000269|PubMed:16854592}; KM=110 uM for ATP (isoform 2) {ECO:0000269|PubMed:19190759}; KM=58 uM for acetyl-CoA {ECO:0000269|PubMed:16854592}; KM=94 uM for acetyl-CoA (isoform 3) {ECO:0000269|PubMed:19190759}; KM=6.5 mM for NaHCO3 (isoform 3) {EC... | PATHWAY: Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1. {ECO:0000269|PubMed:19900410, ECO:0000269|PubMed:26976583}. | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 7.5. {ECO:0000305|PubMed:19236960}; | null | FUNCTION: Mitochondrial enzyme that catalyzes the carboxylation of acetyl-CoA to malonyl-CoA and plays a central role in fatty acid metabolism (PubMed:16854592, PubMed:19236960, PubMed:19900410, PubMed:20457939, PubMed:20952656, PubMed:26976583). Catalyzes a 2 steps reaction starting with the ATP-dependent carboxylatio... | Homo sapiens (Human) |
O00764 | PDXK_HUMAN | MEEECRVLSIQSHVIRGYVGNRAATFPLQVLGFEIDAVNSVQFSNHTGYAHWKGQVLNSDELQELYEGLRLNNMNKYDYVLTGYTRDKSFLAMVVDIVQELKQQNPRLVYVCDPVLGDKWDGEGSMYVPEDLLPVYKEKVVPLADIITPNQFEAELLSGRKIHSQEEALRVMDMLHSMGPDTVVITSSDLPSPQGSNYLIVLGSQRRRNPAGSVVMERIRMDIRKVDAVFVGTGDLFAAMLLAWTHKHPNNLKVACEKTVSTLHHVLQRTIQCAKAQAGEGVRPSPMQLELRMVQSKRDIEDPEIVVQATVL | 2.7.1.35 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:10987144, ECO:0000269|PubMed:17766369, ECO:0000269|PubMed:19351586, ECO:0000269|PubMed:22879864, ECO:0000269|Ref.16}; Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000269|PubMed:10987144}; Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={EC... | phosphorylation [GO:0016310]; pyridoxal 5'-phosphate salvage [GO:0009443]; pyridoxal metabolic process [GO:0042817]; pyridoxamine metabolic process [GO:0042818] | cytosol [GO:0005829]; extracellular exosome [GO:0070062]; extracellular region [GO:0005576]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; secretory granule lumen [GO:0034774]; specific granule lumen [GO:0035580] | ATP binding [GO:0005524]; lithium ion binding [GO:0031403]; magnesium ion binding [GO:0000287]; potassium ion binding [GO:0030955]; protein homodimerization activity [GO:0042803]; pyridoxal kinase activity [GO:0008478]; pyridoxal phosphate binding [GO:0030170]; sodium ion binding [GO:0031402]; zinc ion binding [GO:0008... | PF08543; | 3.40.1190.20; | Pyridoxine kinase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:9099727}. | CATALYTIC ACTIVITY: Reaction=ATP + pyridoxal = ADP + H(+) + pyridoxal 5'-phosphate; Xref=Rhea:RHEA:10224, ChEBI:CHEBI:15378, ChEBI:CHEBI:17310, ChEBI:CHEBI:30616, ChEBI:CHEBI:456216, ChEBI:CHEBI:597326; EC=2.7.1.35; Evidence={ECO:0000269|PubMed:10987144, ECO:0000269|PubMed:17766369, ECO:0000269|PubMed:19351586, ECO:000... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.3 uM for pyridoxal (in the presence of K(+)) {ECO:0000269|PubMed:9099727}; KM=14.5 uM for pyridoxal (in the presence of K(+)) {ECO:0000269|PubMed:31187503}; KM=97 uM for pyridoxal (in the presence of K(+)) {ECO:0000269|PubMed:10987144}; KM=75 uM for pyridoxal (in... | PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxal 5'-phosphate from pyridoxal: step 1/1. {ECO:0000269|PubMed:31187503, ECO:0000305|PubMed:17766369}.; PATHWAY: Cofactor metabolism; pyridoxal 5'-phosphate salvage; pyridoxine 5'-phosphate from pyridoxine: step 1/1. {ECO:0000305|PubMed:17766369}.; PAT... | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.5-6.0. {ECO:0000269|PubMed:10987144}; | null | FUNCTION: Catalyzes the phosphorylation of the dietary vitamin B6 vitamers pyridoxal (PL), pyridoxine (PN) and pyridoxamine (PM) to form pyridoxal 5'-phosphate (PLP), pyridoxine 5'-phosphate (PNP) and pyridoxamine 5'-phosphate (PMP), respectively (Probable) (PubMed:10987144, PubMed:17766369, PubMed:19351586, PubMed:311... | Homo sapiens (Human) |
O00767 | SCD_HUMAN | MPAHLLQDDISSSYTTTTTITAPPSRVLQNGGDKLETMPLYLEDDIRPDIKDDIYDPTYKDKEGPSPKVEYVWRNIILMSLLHLGALYGITLIPTCKFYTWLWGVFYYFVSALGITAGAHRLWSHRSYKARLPLRLFLIIANTMAFQNDVYEWARDHRAHHKFSETHADPHNSRRGFFFSHVGWLLVRKHPAVKEKGSTLDLSDLEAEKLVMFQRRYYKPGLLMMCFILPTLVPWYFWGETFQNSVFVATFLRYAVVLNATWLVNSAAHLFGYRPYDKNISPRENILVSLGAVGEGFHNYHHSFPYDYSASEYRWHINFT... | 1.14.19.1 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000269|PubMed:18765284, ECO:0000305|PubMed:26098317}; Note=Expected to bind 2 Fe(2+) ions per subunit, instead of the Zn(2+) ions seen in the 3D-structure. {ECO:0000305|PubMed:26098317}; | monounsaturated fatty acid biosynthetic process [GO:1903966]; positive regulation of cold-induced thermogenesis [GO:0120162]; response to fatty acid [GO:0070542]; unsaturated fatty acid biosynthetic process [GO:0006636] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; nucleolus [GO:0005730] | iron ion binding [GO:0005506]; oxidoreductase activity [GO:0016491]; palmitoyl-CoA 9-desaturase activity [GO:0032896]; stearoyl-CoA 9-desaturase activity [GO:0004768] | null | null | Fatty acid desaturase type 1 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:15907797}; Multi-pass membrane protein {ECO:0000269|PubMed:18765284, ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=2 Fe(II)-[cytochrome b5] + 2 H(+) + O2 + octadecanoyl-CoA = (9Z)-octadecenoyl-CoA + 2 Fe(III)-[cytochrome b5] + 2 H2O; Xref=Rhea:RHEA:19721, Rhea:RHEA-COMP:10438, Rhea:RHEA-COMP:10439, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034, ChEBI:CHEBI... | null | null | null | null | FUNCTION: Stearoyl-CoA desaturase that utilizes O(2) and electrons from reduced cytochrome b5 to introduce the first double bond into saturated fatty acyl-CoA substrates (PubMed:15907797, PubMed:18765284). Catalyzes the insertion of a cis double bond at the delta-9 position into fatty acyl-CoA substrates including palm... | Homo sapiens (Human) |
O00835 | ERCC3_DICDI | MSSGDSNLKRRRGGNTGQSSKSYNTWTDYEEDLEESGEFNQSIKKTTNTSSATLTSSEEKGSLLDYSKRCILKQDNKSRPIWVCPDGHIFLETFSAIYKQASDFLVAIAEPVCRPQNIHEYQLTPYSLYAAVSVGLETNDIITVLGRLSKLALPKEVEQFVRQCTQSYGKVKLVLQKNKYFVESAYPEVLEFLLKDSSIATARIKPTLEESVVDPKTGFIINKEVVTGAQISGGLQANQSLDPVLKNDALSNLLEEEEEDTVNNSDQHFHSFEIDPQQVEEVKKRCIQLDYPVLEEYDFRNDTVNPNLNIDLKPTTMIRP... | 5.6.2.4 | null | DNA damage response [GO:0006974]; embryonic organ development [GO:0048568]; hair cell differentiation [GO:0035315]; nucleotide-excision repair [GO:0006289]; transcription by RNA polymerase II [GO:0006366]; transcription initiation at RNA polymerase II promoter [GO:0006367]; UV protection [GO:0009650] | nucleotide-excision repair factor 3 complex [GO:0000112]; transcription factor TFIIH holo complex [GO:0005675]; transcription preinitiation complex [GO:0097550] | 3'-5' DNA helicase activity [GO:0043138]; ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677] | PF16203;PF13625;PF04851; | 3.40.50.300; | Helicase family, RAD25/XPB subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.; EC=5.6.2.4; Evidence={ECO:0000250|UniProtKB:P19447}; CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:306... | null | null | null | null | FUNCTION: ATP-dependent 3'-5' DNA helicase/translocase; binds dsDNA rather than ssDNA, unzipping it in a translocase rather than classical helicase activity (By similarity). Component of the general transcription and DNA repair factor IIH (TFIIH) core complex. When complexed to CDK-activating kinase (CAK), involved in ... | Dictyostelium discoideum (Social amoeba) |
O00841 | CUDA_DICDI | MNQSQNFHNIDLGHYGAQGSNQSFNNNNNGNNGMMMNQQQMQQHVVPHLHHLQQQQQQPQQQQLRNVPDYSNSPNGTTNGSTMSPNCINTNNNNNNNNNNNNNSNNNNNNNNNASNNLTSNKSSSTNTPQIGQLQASPANLTNSPSAISSPITISNNSSLNSPSTTSSPNLLLNGTSNKRIMISQQTCLVEEKFSKNGVQKNVHVVVKNNPFLLTLSLLDSSLNFHQLTPEVQLVYDSESLKEVDSATVKPLEYKTRANEEGDQLTIELRIKVLSSQLEDMLFRAKVKIVDPRTRKETHGLSVITHPIRVVSKPDQVKKK... | null | null | cell differentiation [GO:0030154]; culmination involved in sorocarp development [GO:0031154]; positive regulation of gene expression [GO:0010628]; receptor signaling pathway via STAT [GO:0097696]; sporulation resulting in formation of a cellular spore [GO:0030435] | nucleoplasm [GO:0005654]; nucleus [GO:0005634] | sequence-specific DNA binding [GO:0043565] | null | null | null | null | SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:9226443}. | null | null | null | null | null | FUNCTION: Essential for normal culmination. May function as a transcriptional regulator. {ECO:0000269|PubMed:9226443}. | Dictyostelium discoideum (Social amoeba) |
O00899 | GAPA_DICDI | MEGLEIEDEDVILLDEDDDSSSSSTVNNSSSNIKNNGNTNNNIGNDDSNKVTLMTSLREKGWGSGMLVDKEKNQYGTIKSYKDDKSSPWFEERQVIATLYKARVLLHEMIYTKMNQERLLSGNLCVGEIQSLLNTQKEDVETDWIAEIQELKRNMVAEIRRNHLLERDVNKLDKRIALLIKHRSNIKDLLLEQNKGKKDKKKKGDDKAEYITLDQKQLESYQNLFYLLQTEPHYLAKLVTLIQADQMEDFLDTVFLTLFGDDFSPREEFLILSLFRLAIGQEMSRIKSAGDLLAVESVVPKMIITYTRRKQGHEFLKQII... | null | null | chemotaxis to cAMP [GO:0043327]; detection of mechanical stimulus [GO:0050982]; hyperosmotic response [GO:0006972]; mitotic actomyosin contractile ring assembly actin filament organization [GO:1903479]; mitotic cytokinesis [GO:0000281]; negative regulation of actin filament polymerization [GO:0030837]; protein localiza... | cell cortex [GO:0005938]; cell trailing edge [GO:0031254]; cleavage furrow [GO:0032154]; cytosol [GO:0005829]; filopodium [GO:0030175]; lamellipodium [GO:0030027] | actin filament binding [GO:0051015]; calmodulin binding [GO:0005516]; GTPase activator activity [GO:0005096]; identical protein binding [GO:0042802]; small GTPase binding [GO:0031267] | PF00616;PF03836; | null | null | null | null | null | null | null | null | null | FUNCTION: Part of signaling pathway that is required for completion of cytokinesis. gapA and rgaA control cortexillin localization to the cleavage furrow and hence may be involved in cleavage of the midbody in the final stage of cytokinesis by regulating the actin cytoskeleton. Forms a complex by linking activated rac1... | Dictyostelium discoideum (Social amoeba) |
O00909 | ARF1_DICDI | MGLAFGKLFSRFFGKKDMRILMVGLDAAGKTTILYKLKLGEIVTTIPTIGFNVETVEFKNINFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDSNDRERIQEACDELTKMLNEDELRDAVLLVFCNKQDLPNAMSVAEVTDKLNLHSLRSRKWYIQSTCATSGDGLYEGLDWLSNTLTSSSK | 3.6.5.2 | null | intracellular protein transport [GO:0006886]; mitotic cytokinesis [GO:0000281]; regulation of filopodium assembly [GO:0051489]; vesicle-mediated transport [GO:0016192] | cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; pathogen-containing vacuole [GO:0140220]; perinuclear region of cytoplasm [GO:0048471]; phagocytic vesicle [GO:0045335]; plasma membrane [GO:0005886] | GTP binding [GO:0005525]; GTPase activity [GO:0003924] | PF00025; | 3.40.50.300; | Small GTPase superfamily, Arf family | null | SUBCELLULAR LOCATION: Golgi apparatus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565, ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.2; Evidence={ECO:0000250|UniProtKB:P84077}; | null | null | null | null | FUNCTION: GTP-binding protein involved in protein trafficking; may modulate vesicle budding and uncoating within the Golgi apparatus. {ECO:0000250}. | Dictyostelium discoideum (Social amoeba) |
O00910 | STATA_DICDI | MSSAEFSMDDFEDTFDSNATISTKDLFEGSDRLPLNQSINTTIQNLYLPNGGFAIGDQSQQQYYQAMPPLNQSDQFNLGRSNNLTPRTNQLQQLQQQQQQQQQPQQQQQQQTYGTQSPIHMSQTPSSPLSSPLPSPTPFSRQQSYNNNNSNNTSSSQNYNNNNININNNNNNNNTNNNNNNNNGNNSNGNNGNNNNNNNNNNNNNTNNNNNNNQQQQQQQQQQQQQQQQQQQQQQQGNPNLSSPQPILDTIYKLLSEQEQTLVQMIHEQSLLLNRLPPTLDENSLAPLKSLSQKQITLSGQMNTEMSALDATKKGMILEP... | null | null | culmination involved in sorocarp development [GO:0031154]; defense response [GO:0006952]; negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of gene expression [GO:0010628]; receptor signaling pathway via JAK-STAT [GO:0007259]; receptor signaling pathway via STAT [GO:0097696]; regulati... | cytosol [GO:0005829]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; identical protein binding [GO:0042802]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF09267;PF17901;PF00017;PF18214; | 1.10.238.10;2.60.40.340;3.30.505.10; | Transcription factor STAT family | PTM: Tyrosine phosphorylated in response to cAMP. Not tyrosine phosphorylated in growing cells. Tyrosine phosphorylation is first detected at the tight mound stage, continues throughout the slug stage and early culmination, and starts to decrease at mid-culmination. Barely detectable in fruiting bodies. {ECO:0000269|Pu... | SUBCELLULAR LOCATION: Cytoplasm. Nucleus. Note=Cytoplasmic in growing cells. Translocated into the nucleus in response to cAMP-induced tyrosine phosphorylation. Nuclear at the tight mound stage and in the upper, prestalk region of tipped aggregates and in cells at the tip of the slug. Subject to crm1-dependent nuclear ... | null | null | null | null | null | FUNCTION: Transcription factor that binds to 5'-TTGAATTGA-3' elements in the promoter region of target genes. Functions as a repressor of the ecmB gene. Regulates the differentiation of prestalk cells during development. {ECO:0000269|PubMed:10393118, ECO:0000269|PubMed:11254360, ECO:0000269|PubMed:15053873, ECO:0000269... | Dictyostelium discoideum (Social amoeba) |
O01326 | RNC_CAEEL | MSDEKISMTLNFPKHKRARRKKYQKEYQERHKEEMMQQLGRRFQNQPSTSSAPPDTVEKIPLPTESTSALPFGDSPRLTEKDYETNYMIDPPVVSTHSAELIKSNRVVIKAEEAEKYMMIKAKSTTSKILQDFQTKILETVKTKRRLQADVPYIIHPCHSMKGRKTPKQKGGDESFTASDVSDDSNDSQDEASTSEPTNRQAPEADKTGEVKDEKQTCNRRNQQRKAKRLRNFEEKERQITLLKKGIDRKKTHPNGIHPDISFNEKGLGNEGPECRCPEPIKTCGLKHGYYAGEDKAIDCKKSNGENLHYYTLRVTPLPS... | 3.1.26.3 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9NRR4}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9NRR4}; Note=Each RNase III domain binds at least one Mg(2+) or Mn(2+) ion. {ECO:0000250|UniProtKB:Q9NRR4}; | cell differentiation [GO:0030154]; gonadal mesoderm development [GO:0007506]; pre-miRNA processing [GO:0031054]; primary miRNA processing [GO:0031053]; rRNA processing [GO:0006364]; sexual reproduction [GO:0019953]; termination of RNA polymerase II transcription [GO:0006369]; U4 snRNA 3'-end processing [GO:0034475] | microprocessor complex [GO:0070877]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | double-stranded RNA binding [GO:0003725]; metal ion binding [GO:0046872]; ribonuclease III activity [GO:0004525] | PF00035;PF14622;PF00636; | 3.30.160.20;1.10.1520.10; | Ribonuclease III family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.3; | null | null | null | null | FUNCTION: Executes the initial step of microRNA (miRNA) processing in the nucleus, that is the cleavage of pri-miRNA to release pre-miRNA. Involved in pre-rRNA processing. Cleaves double-strand RNA and does not cleave single-strand RNA. Involved in fertility. Required for the function or synthesis of the let-7 miRNA. {... | Caenorhabditis elegans |
O01346 | EGH_DROME | MNSTTKHLLHCTLLITVIVTFEVFSGGIKIDENSFTLVDPWTEYGQLATVLLYLLRFLTLLTLPQVLFNFCGLVFYNAFPEKVVLKGSPLLAPFICIRVVTRGDFPDLVKTNVLRNMNTCLDTGLENFLIEVVTDKAVNLSQHRRIREIVVPKEYKTRTGALFKSRALQYCLEDNVNVLNDSDWIVHLDEETLLTENSVRGIINFVLDGKHPFGQGLITYANENVVNWLTTLADSFRVSDDMGKLRLQFKLFHKPLFSWKGSYVVTQVSAERSVSFDNGIDGSVAEDCFFAMRAFSQGYTFNFIEGEMYEKSPFTLLDFL... | 2.4.1.- | null | axon guidance [GO:0007411]; border follicle cell migration [GO:0007298]; cell fate commitment [GO:0045165]; dsRNA transport [GO:0033227]; follicle cell of egg chamber development [GO:0030707]; follicle cell of egg chamber-cell adhesion [GO:0007299]; germ cell development [GO:0007281]; germarium-derived egg chamber form... | cytoplasm [GO:0005737]; membrane [GO:0016020] | beta-1,4-mannosyltransferase activity [GO:0019187] | PF13632; | null | Glycosyltransferase 2 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Glycosyltransferase with a proposed role in glycosphingolipid biosynthesis. Neurogenic protein implicated in epithelial development. Critical component of a differential oocyte-follicle cell adhesive system. {ECO:0000269|PubMed:12454022}. | Drosophila melanogaster (Fruit fly) |
O01367 | HOW_DROME | MSVCESKAVVQQQLQQHLQQQAAAAVVAVAQQQQAQAQAQAQAQAQQQQQAPQVVVPMTPQHLTPQQQQQSTQSIADYLAQLLKDRKQLAAFPNVFTHVERLLDEEIARVRASLFQINGVKKEPLTLPEPEGSVVTMNEKVYVPVREHPDFNFVGRILGPRGMTAKQLEQETGCKIMVRGKGSMRDKKKEDANRGKPNWEHLSDDLHVLITVEDTENRATVKLAQAVAEVQKLLVPQAEGEDELKKRQLMELAIINGTYRDTTAKSVAVCDEEWRRLVAASDSRLLTSTGLPGLAAQIRAPAAAPLGAPLILNPRMTVPT... | null | null | apposition of dorsal and ventral imaginal disc-derived wing surfaces [GO:0007475]; axon ensheathment [GO:0008366]; cell adhesion [GO:0007155]; cell differentiation [GO:0030154]; cell migration [GO:0016477]; germ-line stem cell population maintenance [GO:0030718]; glial cell migration [GO:0008347]; mesoderm development ... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | mRNA 3'-UTR binding [GO:0003730]; mRNA 5'-UTR binding [GO:0048027]; mRNA binding [GO:0003729] | PF00013;PF16544; | 1.20.5.4010;3.30.1370.10; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23788626, ECO:0000269|PubMed:9169854}. | null | null | null | null | null | FUNCTION: RNA-binding protein involved in muscle development and dosage compensation (PubMed:23788626, PubMed:9118803, PubMed:9169854, PubMed:9344542). Vital role in steroid regulation of muscle development and to control heart rate (PubMed:9169854). Required during embryogenesis, in late stages of somatic muscle devel... | Drosophila melanogaster (Fruit fly) |
O01382 | DRICE_DROME | MDATNNGESADQVGIRVGNPEQPNDHTDALGSVGSGGAGSSGLVAGSSHPYGSGAIGQLANGYSSPSSSYRKNVAKMVTDRHAAEYNMRHKNRGMALIFNHEHFEVPTLKSRAGTNVDCENLTRVLKQLDFEVTVYKDCRYKDILRTIEYAASQNHSDSDCILVAILSHGEMGYIYAKDTQYKLDNIWSFFTANHCPSLAGKPKLFFIQACQGDRLDGGVTMQRSQTETDGDSSMSYKIPVHADFLIAYSTVPGFYSWRNTTRGSWFMQSLCAELAANGKRLDILTLLTFVCQRVAVDFESCTPDTPEMHQQKQIPCITT... | 3.4.22.- | null | apoptotic process [GO:0006915]; negative regulation of peptidoglycan recognition protein signaling pathway [GO:0061060]; negative regulation of Toll signaling pathway [GO:0045751]; neuron remodeling [GO:0016322]; nurse cell apoptotic process [GO:0045476]; positive regulation of compound eye retinal cell programmed cell... | cytoplasm [GO:0005737]; nucleus [GO:0005634]; plasma membrane [GO:0005886] | BIR domain binding [GO:1990525]; cysteine-type endopeptidase activity [GO:0004197]; cysteine-type endopeptidase activity involved in apoptotic process [GO:0097153]; cysteine-type endopeptidase activity involved in apoptotic signaling pathway [GO:0097199]; cysteine-type endopeptidase activity involved in execution phase... | PF00656; | 3.40.50.1460; | Peptidase C14A family | null | null | null | null | null | null | null | FUNCTION: Involved in the activation cascade of caspases responsible for apoptosis execution. Acts downstream of rpr. Cleaves baculovirus p35 and lamin DmO in vitro. | Drosophila melanogaster (Fruit fly) |
O01404 | PHM_DROME | MPRISEIAASVGLLLLIGVISVDGLVKEGDYQNSLYQQNLESNSATGATASFPFLMPNVSPQTPDLYLCTPIKVDPTTTYYIVGFNPNATMNTAHHMLLYGCGEPGTSKTTWNCGEMNRASQEESASPCGPHSNSQIVYAWARDAQKLNLPEGVGFKVGKNSPIKYLVLQVHYAHIDKFKDGSTDDSGVFLDYTEEPRKKLAGTLLLGTDGQIPAMKTEHLETACEVNEQKVLHPFAYRVHTHGLGKVVSGYRVRTNSDGEQEWLQLGKRDPLTPQMFYNTSNTDPIIEGDKIAVRCTMQSTRHRTTKIGPTNEDEMCNF... | 1.14.17.3 | COFACTOR: Name=Cu(2+); Xref=ChEBI:CHEBI:29036; Evidence={ECO:0000305|PubMed:9006979}; Note=Binds 2 copper ions per subunit. {ECO:0000305|PubMed:9006979}; | memory [GO:0007613]; peptide metabolic process [GO:0006518]; regulation of imaginal disc-derived wing size [GO:0044719]; response to fungus [GO:0009620]; sexual reproduction [GO:0019953] | extracellular region [GO:0005576]; extracellular space [GO:0005615]; membrane [GO:0016020] | copper ion binding [GO:0005507]; peptidylglycine monooxygenase activity [GO:0004504] | PF03712;PF01082; | 2.60.120.230;2.60.120.310; | Copper type II ascorbate-dependent monooxygenase family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a [peptide]-C-terminal glycine + 2 L-ascorbate + O2 = a [peptide]-C-terminal (2S)-2-hydroxyglycine + H2O + 2 monodehydro-L-ascorbate radical; Xref=Rhea:RHEA:21452, Rhea:RHEA-COMP:13486, Rhea:RHEA-COMP:15321, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:38290, ChEBI:CHEBI:59513, ChEBI:C... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2.2 uM for alpha-N-acetyl-Tyr-Val-Gly {ECO:0000269|PubMed:9006979}; | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 5.0. {ECO:0000269|PubMed:9006979}; | null | FUNCTION: Monooxygenase that catalyzes an essential reaction in C-terminal alpha-amidation of peptides. Produces an unstable peptidyl(2-hydroxyglycine) intermediate. C-terminal amidation of peptides is required for normal developmental transitions and for biosynthesis of secretory peptides throughout the life. {ECO:000... | Drosophila melanogaster (Fruit fly) |
O01427 | AIR2_CAEEL | MENKPPVINLPEKETVNTPQKGGKFTINDFEIGRPLGKGKFGSVYLARTKTGHFHVAIKVLFKSQLISGGVEHQLEREIEIQSHLNHPNIIKLYTYFWDAKKIYLVLEYAPGGEMYKQLTVSKRFSEPTAAKYMYEIADALSYCHRKNVIHRDIKPENLLIGSQGELKIGDFGWSVHAPSNKRQTMCGTMDYLPPEMVNGADHSDAVDLWAIGVLCYEFLVGKPPFEHEDQSKTYAAIKAARFTYPDSVKKGARDLIGRLLVVDPKARCTLEQVKEHYWIQGMMEAKIRAEKQQKIEKEASLRNH | 2.7.11.1 | null | chromosome condensation [GO:0030261]; chromosome segregation [GO:0007059]; establishment of protein localization [GO:0045184]; meiotic spindle midzone assembly [GO:0051257]; mitotic cell cycle [GO:0000278]; mitotic cytokinesis [GO:0000281]; mitotic spindle midzone assembly [GO:0051256]; mitotic spindle organization [GO... | chromosome passenger complex [GO:0032133]; condensed chromosome [GO:0000793]; condensed nuclear chromosome [GO:0000794]; cytoplasm [GO:0005737]; kinetochore [GO:0000776]; microtubule cytoskeleton [GO:0015630]; midbody [GO:0030496]; spindle [GO:0005819]; spindle microtubule [GO:0005876]; spindle midzone [GO:0051233]; sp... | ATP binding [GO:0005524]; ATPase binding [GO:0051117]; histone H3 kinase activity [GO:0140996]; kinesin binding [GO:0019894]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, Ser/Thr protein kinase family, Aurora subfamily | PTM: Phosphorylated. Increased phosphorylation upon chromatin obstructions at anaphase. {ECO:0000269|PubMed:23684975}. | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:9852156}. Chromosome {ECO:0000269|PubMed:18923084, ECO:0000269|PubMed:23684975, ECO:0000269|PubMed:25475837, ECO:0000269|PubMed:9852156}. Midbody {ECO:0000269|PubMed:23684975, ECO:0000269|PubMed:9852156}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|Pub... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Serine/threonine-protein kinase component of the chromosomal passenger complex (CPC), a complex that acts as a key regulator of chromosome segregation and cytokinesis (PubMed:10354474, PubMed:10975519, PubMed:10983970, PubMed:11050384, PubMed:11050385, PubMed:12707312, PubMed:9852156). The CPC complex has ess... | Caenorhabditis elegans |
O01479 | TMOD_CAEEL | MSQAKTDYYSEEKTFSAPSANSQQGTQLPSKVYNKGLKDLEDNDIEGLLSSLSIDELEDLNNDFDPDNSMLPPSQRCRDQTDKEPTGPYKRDNLLKFLEDKAKTEKDWEDVCPYTPGQKRGKVYDSDSGRNSEEPENGKMEMPIEIDLDDDEEELECALVTAPEKDLVDLAGILGMHNVLNQPQYYNALKGKTQDESTGTTFNGIMQSYVPRIVPDEPDNDTDVESCINRLREDDTDLKEVNINNMKRVSKERIRSLIEAACNSKHIEKFSLANTAISDSEARGLIELIETSPSLRVLNVESNFLTPELLARLLRSTLVT... | null | null | actin filament organization [GO:0007015]; embryo development ending in birth or egg hatching [GO:0009792]; locomotion [GO:0040011]; muscle contraction [GO:0006936]; muscle thin filament assembly [GO:0071689]; myofibril assembly [GO:0030239]; negative regulation of actin filament depolymerization [GO:0030835]; nematode ... | cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; myofibril [GO:0030016]; striated muscle thin filament [GO:0005865]; terminal web [GO:1990357] | actin filament binding [GO:0051015]; tropomyosin binding [GO:0005523] | PF03250; | 3.80.10.10; | Tropomodulin family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. | null | null | null | null | null | FUNCTION: Acts as the pointed end capping protein which maintains the length and dynamics of the actin filament. Blocks the elongation and depolymerization of the actin filaments at the pointed end (By similarity). {ECO:0000250}. | Caenorhabditis elegans |
O01498 | STAM1_CAEEL | MKKQKSFPMSAYEDLLGKITAPTITVENWEGILAFCDMINNDFEGSKTGIKSLRKRLNNRDPHVVLLAISVLDSCWANCEERFRKEVSSAQFINELKALCTSSQRQVAEKMRLTVQKWVDTECKTEQSLSLIVTLHKNLVADGYSFVVDDPKSKTKAIDAKFANDPNYVGSAQEEEAIAKAIAASLADAEKQEKAKKSTSTMYPSAKASSPAVQTNSNIPEKNVRALYDFEAAESNELSFVAGDIITITDESNPHWWTGRIGTQQGLFPSSFVTNQLDDLKSKETDSSQKAPEVVASINEAILVRCLQVLHECDPTGERQ... | null | null | endosome to lysosome transport [GO:0008333]; ephrin receptor signaling pathway [GO:0048013]; negative regulation of MAPK cascade [GO:0043409]; protein localization to non-motile cilium [GO:0097499]; protein transport to vacuole involved in ubiquitin-dependent protein catabolic process via the multivesicular body sortin... | cilium [GO:0005929]; early endosome [GO:0005769]; endosome [GO:0005768]; ESCRT-0 complex [GO:0033565] | phosphatidylinositol binding [GO:0035091]; ubiquitin binding [GO:0043130] | PF00018;PF00790; | 1.20.5.1940;1.25.40.90;2.30.30.40; | STAM family | null | SUBCELLULAR LOCATION: Cell projection, cilium {ECO:0000269|PubMed:17581863}. Endosome {ECO:0000269|PubMed:17581863}. Note=Located to early endosomes at the ciliary base but not cilium proper of male-specific sensory neurons. {ECO:0000269|PubMed:17581863}. | null | null | null | null | null | FUNCTION: Binds, sorts and targets the polycystin complex (lov-1 and pkd-2) for lysosomal degradation, acting on early endosomes located at the ciliary base. Functions in the germline together with the ephrin receptor (vab-1) signaling pathway to negatively regulate MAPK activation. May have a role as a positive regula... | Caenorhabditis elegans |
O01501 | CCNE_CAEEL | MAGRKSSRTAERVPTTQKPERKSAILSPHDELRERLLETAIDMKENIPQRNTRNSSVGSQKSDCSETRKRRSTKEGPAAKRHSGEKHRNGSREDSLEYISEYSDDREVGSSSSQSSRTRGQPLPAMPEEEEVFDKSSSSDNLAESEESHEMVRLEERQDIEEEIEDDFDDEEEDVVNDKEEYEEIESEDEDDYPVQNEGFAVTKRLMNDEHMVTAPTFLSTAKCDGIGSPTKVWSLMVKRDEIPRATRFLLGNHPDMDDEKRRILIDWMMEVCESEKLHRETFHLAVDYVDRYLESSNVECSTDNFQLVGTAALFIAAKY... | null | null | cell division [GO:0051301]; DNA endoreduplication [GO:0042023]; embryo development ending in birth or egg hatching [GO:0009792]; G1/S transition of mitotic cell cycle [GO:0000082]; germ cell development [GO:0007281]; germline cell cycle switching, mitotic to meiotic cell cycle [GO:0051729]; gonad development [GO:000840... | centriole [GO:0005814]; centrosome [GO:0005813]; chromatin [GO:0000785]; cyclin E1-CDK2 complex [GO:0097134]; cyclin-dependent protein kinase holoenzyme complex [GO:0000307]; cytoplasm [GO:0005737]; nucleus [GO:0005634] | cyclin-dependent protein serine/threonine kinase regulator activity [GO:0016538] | PF00134; | 1.10.472.10; | Cyclin family, Cyclin E subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12606285}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole {ECO:0000269|PubMed:17115027}. Note=Co-localizes with cdk-2 in the sperm centrioles before the first embryonic mitosis and then to the male and female nuclei upon entry into mitosis... | null | null | null | null | null | FUNCTION: Essential for the control of the cell cycle at the G1/S (start) transition (PubMed:12606285). In association with cdk-2, regulates proliferation, quiescent state and cell fate during the development of several cell lineages (PubMed:10952902, PubMed:17476329, PubMed:21455289, PubMed:21558371). In the embryo, i... | Caenorhabditis elegans |
O01510 | SMG1_CAEEL | MITSRNNDIGNLIEQFRQRDTPQKERKAILARIEEILQTTKNVESLCVKWTYLLDNLCWPSLTKHDRNDMKTLAGKVIRLVGVLLFDTESYPEFLIYLGTLYQSVTKKSEETRADIVFSVYFIVGVISQKTENRLIATDTENVEKSLDWIIKVLPNSSISVYNHCLKGFVLVANTFPNVYAAMFESTLRAILTNLPDFNSHEKNFELLIDTVMRFSDQLNEKPHLAEEMVRIIRPDIKKNGLGNMRELKKRMKLTMALVKMAKSQKMLEETNQMISEMSIELEENGGKWSSASLITIVCDVFNELLILGKDDVKLQKGVE... | 2.7.11.1 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; | male genitalia development [GO:0030539]; negative regulation of macroautophagy [GO:0016242]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; phosphorylation [GO:0016310]; TOR signaling [GO:0031929] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; TORC1 complex [GO:0031931]; TORC2 complex [GO:0031932] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF02260;PF00454;PF15785; | 1.10.1070.11; | PI3/PI4-kinase family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15314158}. | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; CATALYTIC ACTIVITY: Reaction=ATP + L-threonyl-[pr... | null | null | null | null | FUNCTION: Serine/threonine protein kinase involved in mRNA surveillance. Recognizes the substrate consensus sequence [ST]-Q. Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons by phosphorylating smg-2. {ECO:0000269|PubMed:15314158, ECO:0000269|PubMed:2583479}. | Caenorhabditis elegans |
O01583 | MRCK_CAEEL | MAEPPPDDSAPVRLKTLENIYMDGPSKKPEALSFETLIDSLICLYDECCNSTLRKEKCIAEFVESVKTVISKAKKLRLSRDDFEVLKVIGKGAFGEVAVVRMRGVGEIYAMKILNKWEMVKRAETACFREERDVLVYGDRRWITNLHYAFQDEKNLYFVMDYYIGGDMLTLLSKFVDHIPESMAKFYIAEMVLAIDSLHRLGYVHRDVKPDNVLLDMQGHIRLADFGSCLRILADGSVASNVAVGTPDYISPEILRAMEDGRGRYGKECDWWSLGICMYEMLYGTTPFYSERLVDTYGKIMSHQDMLDFPDDEIDWVVSE... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q5VT25}; | actomyosin structure organization [GO:0031032]; embryo development ending in birth or egg hatching [GO:0009792]; embryonic body morphogenesis [GO:0010172]; embryonic morphogenesis [GO:0048598]; epithelial tube morphogenesis [GO:0060562]; nematode larval development [GO:0002119]; phosphorylation [GO:0016310]; positive r... | cytoplasm [GO:0005737]; cytoskeleton [GO:0005856] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00130;PF00780;PF00069;PF00433; | 3.30.60.20;2.30.29.30;1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, DMPK subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19675126}. Note=Forms parallel punctate bundles in dorsal and ventral epidermal cells. {ECO:0000269|PubMed:19675126}. | 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:0000250|UniProtKB:Q5VT25}; CATALYTI... | null | null | null | null | FUNCTION: Serine/threonine-protein kinase that may phosphorylate and inactivate the phosphatase mel-11, and thereby contribute to the regulation of myosin II contractility during embryonic elongation (PubMed:19675126). Involved in controlling canal length and Golgi/ER integrity during excretory canal elongation (PubMed... | Caenorhabditis elegans |
O01658 | NO66_CAEEL | MGKKKNSNKSAAAAPAVKHNDRWSSIELGEAKSAAVSHYKEPSKEPKFVHPAKLEKVKRIHDGLNIDRVLSHGPVPKQNGGTKRKHVEVTTQKLENKKPKVEVKKEDEKSKNKKMKNQNKHTALVQNETSTRSTYFVEEPDNENKVTLISNGREIAFKKTEVVESDDEQMIGLDSDEELEDEDETDIDEDEMMIDPKDIERYINFESVEDEEDMEDEEIEDEEFEDEEFEDEEEEADEQEEEEEDVSDEESVVSEMDADSDDEGFIAGKDREAHVISKDKFTRNAPAVDFDKFPFTDEDSVVTSSRAFGFMISPCDVQTF... | 1.14.11.-; 1.14.11.27 | COFACTOR: Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250}; Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000250}; | negative regulation of DNA-templated transcription [GO:0045892]; response to ethanol [GO:0045471]; response to heat [GO:0009408]; response to osmotic stress [GO:0006970]; response to oxidative stress [GO:0006979] | nucleolus [GO:0005730]; nucleus [GO:0005634] | 2-oxoglutarate-dependent dioxygenase activity [GO:0016706]; histone H3K36 demethylase activity [GO:0051864]; histone H3K36me/H3K36me2 demethylase activity [GO:0140680]; histone H3K4 demethylase activity [GO:0032453]; histone H3K4me/H3K4me2/H3K4me3 demethylase activity [GO:0034647]; iron ion binding [GO:0005506] | PF08007;PF21233; | 3.90.930.40;2.60.120.650;1.10.10.1500; | ROX family, NO66 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=2 2-oxoglutarate + N(6),N(6)-dimethyl-L-lysyl(36)-[histone H3] + 2 O2 = 2 CO2 + 2 formaldehyde + L-lysyl(36)-[histone H3] + 2 succinate; Xref=Rhea:RHEA:42032, Rhea:RHEA-COMP:9785, Rhea:RHEA-COMP:9787, ChEBI:CHEBI:15379, ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:16842, ChEBI:CHEBI:29... | null | null | null | null | FUNCTION: Oxygenase that can act as both a histone lysine demethylase and a ribosomal histidine hydroxylase. Specifically demethylates 'Lys-4' (H3K4me) and 'Lys-36' (H3K36me) of histone H3, thereby playing a central role in histone code (By similarity). Mediates response to multiple stress stimuli, including heat shock... | Caenorhabditis elegans |
O01668 | OPS6_DROME | MASLHPPSFAYMRDGRNLSLAESVPAEIMHMVDPYWYQWPPLEPMWFGIIGFVIAILGTMSLAGNFIVMYIFTSSKGLRTPSNMFVVNLAFSDFMMMFTMFPPVVLNGFYGTWIMGPFLCELYGMFGSLFGCVSIWSMTLIAYDRYCVIVKGMARKPLTATAAVLRLMVVWTICGAWALMPLFGWNRYVPEGNMTACGTDYFAKDWWNRSYIIVYSLWVYLTPLLTIIFSYWHIMKAVAAHEKAMREQAKKMNVASLRNSEADKSKAIEIKLAKVALTTISLWFFAWTPYTIINYAGIFESMHLSPLSTICGSVFAKANA... | null | null | cellular response to light stimulus [GO:0071482]; entrainment of circadian clock by photoperiod [GO:0043153]; G protein-coupled receptor signaling pathway [GO:0007186]; negative regulation of transcription by RNA polymerase II [GO:0000122]; phototransduction [GO:0007602]; sensory perception of sound [GO:0007605]; therm... | membrane [GO:0016020]; rhabdomere [GO:0016028] | G protein-coupled photoreceptor activity [GO:0008020] | PF00001; | 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:0000250}. | SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: Visual pigments are the light-absorbing molecules that mediate vision. They consist of an apoprotein, opsin, covalently linked to cis-retinal. | Drosophila melanogaster (Fruit fly) |
O01683 | SSP1B_CAEEL | MTELKFKGVYVEDIGHLTCGTLTLTENSINFIGDKGGKSVYITGTDVDKLKWQKLGNKPGLRVGLSDGGAHRFGGFLDDDLQKIQSFTSSNWSKSINQSNLFINGWNYGQADVKGKNIEFSWENEPIFEIPCTNVSNVIANKNEAILEFHQNEQSKVQLMEMRFHMPVDLENEEDTDKVEEFKKAVLAYAGLEAETEQPICLLTDILCTTPRGRYDIKVYPTSIALHGKTYDYKIPVKTINRLFLVPHKDGRQVYFVLSLNPPIRQGQTHYSYLIFEFGKDEEEDLELSLTDEQLDYFNGNLQREMTGPIYETISILFKS... | null | null | DNA repair [GO:0006281]; DNA replication [GO:0006260]; nematode pharynx development [GO:0160094]; nucleosome assembly [GO:0006334]; nucleosome disassembly [GO:0006337]; pharynx development [GO:0060465]; positive regulation of cell cycle [GO:0045787]; regulation of chromatin organization [GO:1902275]; regulation of embr... | FACT complex [GO:0035101]; nucleus [GO:0005634] | DNA binding [GO:0003677]; histone binding [GO:0042393]; nucleosome binding [GO:0031491] | PF00505;PF21103;PF17292;PF08512;PF03531; | 2.30.29.150;1.10.30.10;2.30.29.30;2.30.29.220; | SSRP1 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267, ECO:0000269|PubMed:30336114}. Chromosome {ECO:0000250|UniProtKB:Q08945}. | null | null | null | null | null | FUNCTION: Component of the FACT complex, a general chromatin factor that acts to reorganize nucleosomes. The FACT complex is involved in multiple processes that require DNA as a template such as mRNA elongation, DNA replication and DNA repair. During transcription elongation the FACT complex acts as a histone chaperone... | Caenorhabditis elegans |
O01700 | DLK1_CAEEL | MTSTTMVTTLDLVTPTSEEQPGPAPESSDFSTVVLSPDGSELVTQSAPNTPIQHREQANAEFGQKEGSPDPKNMVAATGNASKPSLNSFYADGLGQLRNGLFSCFQPVFGYFGTKTTVEIEKSEDELWEIPFDAISELEWLGSGSQGAVFRGQLENRTVAVKKVNQLKETEIKHLRHLRHQNIIEFLGVCSKSPCYCIVMEYCSKGQLCTVLKSRNTITRELFAQWVKEIADGMHYLHQNKVIHRDLKSPNILISAEDSIKICDFGTSHMQKKMDSTMMSFCGTVSWMAPEMIKKQPCNEKVDVYSFGVVLWEMLTRETP... | 2.7.11.25 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:O43283}; | axon extension involved in regeneration [GO:0048677]; axon regeneration [GO:0031103]; formation of growth cone in injured axon [GO:0048689]; MAPK cascade [GO:0000165]; microtubule polymerization [GO:0046785]; p38MAPK cascade [GO:0038066]; phosphorylation [GO:0016310]; positive regulation of axon extension [GO:0045773];... | axon [GO:0030424]; cilium [GO:0005929]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; neuronal cell body [GO:0043025]; synapse [GO:0045202] | ATP binding [GO:0005524]; MAP kinase kinase kinase activity [GO:0004709]; metal ion binding [GO:0046872]; protein kinase activity [GO:0004672]; protein serine kinase activity [GO:0106310]; ubiquitin protein ligase binding [GO:0031625] | PF00069; | 1.10.510.10; | Protein kinase superfamily, STE Ser/Thr protein kinase family, MAP kinase kinase kinase subfamily | PTM: Ubiquitinated by rpm-1. Negatively regulated by ubiquitination by fsn-1 bound rpm-1, followed by degradation. {ECO:0000269|PubMed:15707898}.; PTM: [Isoform a]: Phosphorylation at Ser-874 and/or at Ser-878 abolishes interaction with isoform c and promotes binding to isoform a kinase domain (likely in trans) resulti... | SUBCELLULAR LOCATION: Synapse {ECO:0000269|PubMed:15707898, ECO:0000269|PubMed:18224716, ECO:0000269|PubMed:23000142}. Cytoplasm {ECO:0000269|PubMed:26657059}. Cell projection, axon {ECO:0000269|PubMed:26657059}. Cell projection, dendrite {ECO:0000269|PubMed:26657059}. Cell projection, cilium {ECO:0000269|PubMed:266570... | 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=2.7.11.25; Evidence={ECO:0000250|UniProtKB:O43283}; CATALYT... | null | null | null | null | FUNCTION: Component of a MAP kinase pathway that functions presynaptically to regulate synaptic architecture and presynaptic differentiation (PubMed:15707898). Phosphorylates and activates mkk-4 (PubMed:15707898). Has a role in axonal regrowth following injury and synaptogenesis (PubMed:19164707, PubMed:19737525). Play... | Caenorhabditis elegans |
O01704 | EXT1_CAEEL | MQNVMKFHLVIFMLFGSVRLQNPTIERKQCTMSNCFDFSKCSTSKKVYIHPMEKRFEESPQSVIYSKILKHFLESNHYTNDPNEACIFLLGIDTTDRDVRSQNYVKNVNDYIESLDPSVWNNGRNHLIFNFYHGTFPDYDDHNLNFDTGEAMIARASSSENNFIKVFDVSLPLFHENHPYEIKESKSERNDDRIENQRKYLVSFKGKRYVYGIGSGTRNLVHHLHNGDDIVMVTTCKHNNDWQVYQDDRCQRDNDEYDRWEYDELLANSTFCLVPRGRRLGSFRFLETLRSGCVPVVISDSWILPFSETIDWNSAAIVVA... | null | null | heparan sulfate proteoglycan biosynthetic process [GO:0015012]; pharynx development [GO:0060465]; protein glycosylation [GO:0006486] | endoplasmic reticulum [GO:0005783]; Golgi apparatus [GO:0005794]; protein-containing complex [GO:0032991] | acetylglucosaminyltransferase activity [GO:0008375]; enzyme binding [GO:0019899]; glucuronosyltransferase activity [GO:0015020]; glycosyltransferase activity [GO:0016757] | PF03016; | null | Glycosyltransferase 47 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000305}. Golgi apparatus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Required for the biosynthesis of heparan sulfate by positively regulating N-acetylglucosamine transferase II (GlcNAcT-II) and glucuronyl transferase II (GlcAT-II) activities of glycosyltransferase rib-2 (PubMed:17237233). Probably not directly involved in chondroitin sulfate biosynthesis but negatively regula... | Caenorhabditis elegans |
O01705 | EXT2_CAEEL | MAIKLNGSSRSFVPSLRVSAFLIFIFFVITYIIIYNVSFSEPSWITQDALKQNIENLDDYDASCSGYSIGRILREQKRILASVRLELTESQVKIEEIRTVQEELQRLIPQKQLELSALEGEIEAAQRQLEELRETQNVKVFLPFSPLQIPRELEQPSQISPNQLDDIIDYSRCSISSFMPVYVDIITSGQSEKEWLNVFQEVIPNLVETPDKACIKIHISNGIASPNTTFNSILFNVGSPIINFQSKSIHVQASKIRSFDFPVDVNHIAVEKVDLTPLLPFQRENLISLIVDNTELNFSAFSSLSAEPSRRPIVIVKCSQ... | 2.4.1.223; 2.4.1.224; 2.4.1.225 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250|UniProtKB:Q9ES89}; | embryonic morphogenesis [GO:0048598]; heparan sulfate proteoglycan biosynthetic process [GO:0015012]; pharynx development [GO:0060465]; protein glycosylation [GO:0006486] | endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; protein-containing complex [GO:0032991] | acetylglucosaminyltransferase activity [GO:0008375]; enzyme binding [GO:0019899]; glucuronosyl-N-acetylglucosaminyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity [GO:0050508]; glucuronyl-galactosyl-proteoglycan 4-alpha-N-acetylglucosaminyltransferase activity [GO:0001888]; glycosyltransferase activity [... | PF03016;PF09258; | null | Glycosyltransferase 47 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q16394}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q16394}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q16394}; Single-pass type II membrane protein {ECO:0000250|UniProtKB:Q16394}. | CATALYTIC ACTIVITY: Reaction=3-O-(beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = 3-O-(alpha-D-GlcNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-Gal-(1->3)-beta-D-Gal-(1->4)-beta-D-Xyl)-L-seryl-[protein] + H(+) + UDP; Xref=Rhea:RHEA:16221, Rhea:RHEA-COMP:1... | null | PATHWAY: Glycan metabolism; heparan sulfate biosynthesis. {ECO:0000269|PubMed:11121397, ECO:0000269|PubMed:17237233}. | null | null | FUNCTION: Glycosyltransferase required for the biosynthesis of heparan sulfate (PubMed:11121397, PubMed:16828468, PubMed:17237233). Initiates heparan sulfate synthesis by transferring GlcNAc to the (GlcA-Gal-Gal-Xyl-)Ser core linker (GlcNAcT-I activity) (PubMed:11121397). In association with rib-1, is also responsible ... | Caenorhabditis elegans |
O01737 | SBNO_CAEEL | MDDILSAALAESGLDFLCQQSSPTPSTSGSIHDDAGQSFSNNTHTPSVSQFFDETSNDSHSSSAYYTPMATPFVSTEDGGVPTSFFGMDEEDGGCTIMTTAGTSGSNNIDGIEDAGGGMYYPHVKVIPRKHTAPTVNQSEPSTPTVTIVPKKEDPLFETNTADSPTPSGDTSTTASYEGNDGLEDQETTSDRQNPMFVQTARSTDGRLDTPSTSATVSPHITSSLTQRSHTSSPASSASEGTVVPPRKKGLPITTGSIVKRTVQTKDGLQTQYLKAFVNENGEKIYKLLSPVAASAVARGTLPPGMGRGGSTIGRGGTMV... | null | null | nematode male tail tip morphogenesis [GO:0045138]; positive regulation of cell fate specification [GO:0042660]; positive regulation of Ras protein signal transduction [GO:0046579]; regulation of DNA-templated transcription [GO:0006355]; vulval cell fate specification [GO:0072327] | nucleus [GO:0005634] | chromatin DNA binding [GO:0031490]; histone binding [GO:0042393] | PF13872;PF13871; | 3.40.50.300; | SBNO family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20230814}. | null | null | null | null | null | FUNCTION: Transcriptional activator that functions upstream of the let-60/Ras and let-23/EGFR signaling pathways to positively regulate lin-3 expression and thereby promote vulval induction (PubMed:20230814). Plays a role in excretory duct development (PubMed:20230814). Plays a role in male tail development (PubMed:202... | Caenorhabditis elegans |
O01739 | OXDD3_CAEEL | MLYALLLLFGGVSTVSSLRVAVVGEGVIGLSTATAILDLAEKRNIPAPEIHIFHHKPFEKILSRHIAGLFRIDSGSEIDRKYGYDTFEKLATLWREYGGLSGVQLVSGHILSDSKTKLDSQRESYGSLVYNYRDLAEPELFGPTSLFDLPRNTTTRGIHYTAYTSEGLRFCPFLKKELMTKGVRFTQRRIGNLEELGAEFDVVVNSAGLLGGVLAGDDAGNMKPIRGVLIRVDAPWQKHFLYRDFSTITIPVIDHVYMGTVKQEGAFGPNNVTSADIQDITSRYVALQPSFKRVHMLSSFVGYRPGRKQVRVEKQIRETN... | 1.4.3.1 | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000269|PubMed:20564561}; | D-amino acid catabolic process [GO:0019478] | cytoplasm [GO:0005737]; extracellular region [GO:0005576] | D-amino-acid oxidase activity [GO:0003884]; D-aspartate oxidase activity [GO:0008445]; D-glutamate oxidase activity [GO:0047821]; FAD binding [GO:0071949] | PF01266; | 3.30.9.10;3.40.50.720; | DAMOX/DASOX family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:30387556}. Note=In hermaphrodites, protein secreted from proximal gonadal sheath cells may be transferred to the oocyte surface (PubMed:30387556). In males, protein secreted from the seminal vesicle into the seminal fluid is transferred to the hermaphrodite uterus duri... | CATALYTIC ACTIVITY: Reaction=D-aspartate + H2O + O2 = H2O2 + NH4(+) + oxaloacetate; Xref=Rhea:RHEA:12512, ChEBI:CHEBI:15377, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240, ChEBI:CHEBI:16452, ChEBI:CHEBI:28938, ChEBI:CHEBI:29990; EC=1.4.3.1; Evidence={ECO:0000269|PubMed:20564561}; PhysiologicalDirection=left-to-right; Xref=Rhea:... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=3.81 mM for D-aspartate {ECO:0000269|PubMed:20564561}; KM=0.68 mM for D-glutamate {ECO:0000269|PubMed:20564561}; KM=8.87 mM for N-methyl D-aspartate {ECO:0000269|PubMed:20564561}; Note=The values given are for the recombinant protein. {ECO:0000269|PubMed:20564561}; | null | null | null | FUNCTION: Selectively catalyzes the oxidative deamination of acidic amino acids (PubMed:20564561). Plays a role in the egg-laying events and maturation processes of the reproductive organs (PubMed:22393259, PubMed:30387556). {ECO:0000269|PubMed:20564561, ECO:0000269|PubMed:22393259, ECO:0000269|PubMed:30387556}. | Caenorhabditis elegans |
O01761 | UNC89_CAEEL | MASRRQKQFDRKYSSYRKFTATEDVNYSTHSSRSSYRSESLTSRTDGRGRSTSSEIIAGSESRSYPVYIAIQDYTPDKEDVEAIPLEQGQIVEVLDKKNSVRWLVRTKARPPRSGWVPGSYFETPTEFYKQRRRTREIENVSLSDEQAALVKRDQVYHELLRSEEEFVSSLRTCVDDYIKVLDDPEVPEAVKKNREELTLNIPELYNFHANVMLKGLNYYSDDPGKVGQTFVRLEKDFESHVEFYKQYADTLKLLEEPEIKRFFEGLSAKNDAGASSFVDHVKEIADRMVQYQNYFKEFVKYSARAHGSSKSIQKALELV... | null | null | myosin filament assembly [GO:0031034]; nematode pharyngeal gland morphogenesis [GO:1905905]; positive regulation of gene expression [GO:0010628]; positive regulation of locomotion [GO:0040017]; positive regulation of protein localization to endoplasmic reticulum [GO:1905552]; positive regulation of sarcomere organizati... | A band [GO:0031672]; M band [GO:0031430] | ATP binding [GO:0005524]; guanyl-nucleotide exchange factor activity [GO:0005085]; MATH domain binding [GO:0090736]; phosphatase binding [GO:0019902]; protein kinase activity [GO:0004672]; small GTPase binding [GO:0031267] | PF00041;PF07679;PF00069;PF05177;PF00621; | 1.20.900.10;2.60.40.10;2.30.29.30;2.30.30.40;1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family | null | SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, M line {ECO:0000269|PubMed:15313609, ECO:0000269|PubMed:18337465, ECO:0000269|PubMed:19244614, ECO:0000269|PubMed:22621901, ECO:0000269|PubMed:22768340, ECO:0000269|PubMed:23283987, ECO:0000269|PubMed:27009202, ECO:0000269|PubMed:8603916}. Note=Colocalizes with scp... | null | null | null | null | null | FUNCTION: Structural component of the muscle M line which is involved in assembly and organization of sarcomere myofilaments (PubMed:15313609, PubMed:16453163, PubMed:18801371, PubMed:22621901, PubMed:23283987, PubMed:27009202). The large isoform a, isoform b, isoform d and isoform f play an essential role in maintaini... | Caenorhabditis elegans |
O01767 | EGG4_CAEEL | MALNSEVMFREQINAMRSQAGRKRATSLQSFCSGNTDDSSADSTDNMDMMVDYPQQKGVSCMRARFNSESTLSKSFRKKVKKLAQKDRRSKERLNGNSEEDAIEVPRGAPSTYAAPSKLRKSKALDCLVSEKPKDEGRREDSGHGADIEMAKGHFNNVRMKVFAARTAMQVEPALVMKTRKALEMKNAVLENHQSPGAFSLHAAYKIAASAESRVGSITPCNKKVTKEAMANLIRSSYDDTEITQELLFSSKFDTKWKGRYTDIYMRRDENGKKPKRPVNGQGWVMPLKSICEKFGINSTFFTNHRIDLKSARDQVLLMR... | null | null | cortical actin cytoskeleton organization [GO:0030866]; dephosphorylation [GO:0016311]; eggshell formation [GO:0030703]; motor neuron axon guidance [GO:0008045]; oocyte maturation [GO:0001556]; polar body extrusion after meiotic divisions [GO:0040038]; positive regulation of protein localization to cell cortex [GO:19047... | cell cortex [GO:0005938]; nucleus [GO:0005634] | protein kinase binding [GO:0019901]; protein kinase inhibitor activity [GO:0004860]; protein tyrosine phosphatase activity [GO:0004725] | PF00102; | 3.90.190.10; | Protein-tyrosine phosphatase family | null | SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000269|PubMed:19879147}. Note=Co-localizes with egg-3 to the cell cortex in developing oocytes and in newly fertilized embryos; cortical localization requires egg-3 and chitin synthase chs-1. At the beginning of meiosis anaphase I, egg-4 moves away from the cell cortex... | null | null | null | null | null | FUNCTION: Inactive phosphatase which acts redundantly with egg-5 in the oocyte-to-zygote transition (PubMed:19879147, PubMed:19879842). Required for the polarization of cortical actin cytoskeleton rearrangement in the oocyte before and after fertilization (PubMed:19879147). Together with egg-5, required for the cortica... | Caenorhabditis elegans |
O01775 | NEKL2_CAEEL | MDNYEKVRVVGRGAFGVCWLCRGKNDASHQKVIIKLINTHGMTEKEENSIQSEVNLLKKVQHPLIIGYIDSFIMDNQLGIVMQYAEGGTLERLINDQRAIKDSNMREYFPEKTVLDYFTQILIALNHMHQKNIVHRDLKPQNILMNRRKTVLKLSDFGISKELGTKSAASTVIGTPNYLSPEICESRPYNQKSDMWSLGCVLYELLQLERAFDGENLPAIVMKITRSKQNPLGDHVSNDVKMLVENLLKTHTDKRPDVSQLLSDPLVLPYLISIHCDLGRIEPPPTDKRKPSASLSSRLRTYPTQSTLRPYSLSSNAPTT... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q9HC98}; | molting cycle [GO:0042303]; phosphorylation [GO:0016310]; positive regulation of endocytosis [GO:0045807] | cytoplasm [GO:0005737] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00069; | 1.10.510.10; | Protein kinase superfamily, NEK Ser/Thr protein kinase family, NIMA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:25523392}. Note=In hyp7 syncytium, localizes in puncta and small tubules near the plasma membrane apical region. Does not co-localize with nekl-3. {ECO:0000269|PubMed:25523392}. | 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:0000250|UniProtKB:Q9HC98}; CATALYTI... | null | null | null | null | FUNCTION: Probable serine/threonine-protein kinase required for the completion of molting. May play a role in endocytosis in the hypodermis syncytium. {ECO:0000269|PubMed:25523392}. | Caenorhabditis elegans |
O01789 | SMC1_CAEEL | MRGGSSLDSFPGKGTLHTLEIENFKSYKGKHTIGPFTRFTAIIGPNGSGKSNLMDAISFVLGEKPSSLRVRKYADLIHGAPINKPVAKKCRVTMNYKYSDGKVKAFTRGVNNGTSEHLLDGQTVTSAAYSQEMESINIFIKARNFLVYQGAIENIAMKTPKERTQLFEELSRSHEFQAEYERLKVEMTKAEDDTQHNMNKRRGIAQEKREAKMEKDEAEKYQTMKNELAAKSTMLFLHQLFHCERTIDESKEEINAQKKTIASLEATRSKEEAKIAAVHQEHRKALREVQKMTRKLDQKETDLAEKQQNMLTLKVSVAHE... | null | null | cell division [GO:0051301]; chromosome segregation [GO:0007059]; DNA repair [GO:0006281]; embryo development ending in birth or egg hatching [GO:0009792]; establishment of mitotic sister chromatid cohesion [GO:0034087]; mitotic sister chromatid cohesion [GO:0007064]; response to UV [GO:0009411]; response to X-ray [GO:0... | chromatin [GO:0000785]; cohesin complex [GO:0008278]; meiotic cohesin complex [GO:0030893]; MIS12/MIND type complex [GO:0000444]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DNA binding [GO:0003677] | PF06470;PF02463; | 1.20.1060.20;3.30.70.1620;3.40.50.300; | SMC family, SMC1 subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12827206, ECO:0000269|PubMed:21856158}. Chromosome {ECO:0000269|PubMed:12827206, ECO:0000269|PubMed:21856158}. Note=Has diffuse nuclear appearance at interphase during mitosis in somatic and germline tissues (PubMed:12827206). Colocalizes with rec-8 along synapsed chrom... | null | null | null | null | null | FUNCTION: Involved in chromosome cohesion during cell cycle and in DNA repair (By similarity). Required for chromosome segregation during mitosis (PubMed:12808038, PubMed:12827206). Central component of cohesin complex (PubMed:12827206). The cohesin complex is required for the cohesion of sister chromatids after DNA re... | Caenorhabditis elegans |
O01798 | SPE8_CAEEL | MRSKSSEGDLQPEDTQSREDKETTATYSEDTKPETQKERNAALDNLAKTPIQLVVQPTPLTPAITPCEAPPPPPPPKPSSDNNNSKRLKVKDQLIEVPSDEVGRVENNIDNFPFYHGFMGRNECEAMLSNHGDFLIRMTEIGKRVAYVISIKWKYQNIHVLVKRTKTKKLYWTKKYAFKSICELIAYHKRNHKPIYEGMTLICGLARHGWQLNNEQVTLNKKLGEGQFGEVHKGSLKTSVFAAPVTVAVKTLHQNHLSANEKILFLREANVMLTLSHPNVIKFYGVCTMKEPIMIVMEFCDGKSLEDALLSKEEKVSAED... | 2.7.10.2 | null | cell differentiation [GO:0030154]; innate immune response [GO:0045087]; phosphorylation [GO:0016310]; spermatid development [GO:0007286]; transmembrane receptor protein tyrosine kinase signaling pathway [GO:0007169] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; non-membrane spanning protein tyrosine kinase activity [GO:0004715]; signaling receptor binding [GO:0005102] | PF07714;PF00017; | 3.30.505.10;1.10.510.10; | Protein kinase superfamily, Tyr protein kinase family, Fes/fps subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:25022984}; Peripheral membrane protein {ECO:0000269|PubMed:25022984}. Cytoplasm {ECO:0000269|PubMed:25022984}. Note=Localizes mainly in the cytoplasm of stage I spermatocytes and at the cell membrane of stage II spermatocytes and spermatids. {ECO:0000269|PubMed:25... | CATALYTIC ACTIVITY: Reaction=ATP + L-tyrosyl-[protein] = ADP + H(+) + O-phospho-L-tyrosyl-[protein]; Xref=Rhea:RHEA:10596, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620, ChEBI:CHEBI:456216; EC=2.7.10.2; | null | null | null | null | FUNCTION: Probable non-receptor tyrosine-protein kinase which plays a role in spermatid activation (spermiogenesis) in hermaphrodites. {ECO:0000269|PubMed:25022984, ECO:0000269|PubMed:3197956}. | Caenorhabditis elegans |
O01803 | RB11A_CAEEL | MGSRDDEYDYLFKVVLIGDSGVGKSNLLSRFTRNEFNLESKSTIGVEFATRSISVEGKTVKAQIWDTAGQERYRAITSAYYRGAVGALLVYDIAKHVTYENVERWLKELRDHADQNIVIMLVGNKSDLRHLRAVPTDEAKIYAERNQLSFIETSALDSTNVEAAFTNILTEIYKSVSNKHVGTDRQGYGGGSGTIIPSPASDPPKKQCCIP | null | null | cortical granule exocytosis [GO:0060471]; eggshell formation [GO:0030703]; embryo development ending in birth or egg hatching [GO:0009792]; exocytosis [GO:0006887]; membrane addition at site of mitotic cytokinesis [GO:0061796]; mitotic cytokinesis [GO:0000281]; protein transport [GO:0015031]; receptor-mediated endocyto... | apical plasma membrane [GO:0016324]; centrosome [GO:0005813]; cortical granule [GO:0060473]; cytosol [GO:0005829]; Golgi apparatus [GO:0005794]; Golgi membrane [GO:0000139]; Golgi trans cisterna membrane [GO:1990676]; recycling endosome [GO:0055037]; recycling endosome membrane [GO:0055038]; spindle [GO:0005819]; trans... | GTP binding [GO:0005525]; GTPase activity [GO:0003924] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Rab family | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle {ECO:0000269|PubMed:18765566, ECO:0000269|PubMed:20116245, ECO:0000269|PubMed:22992455}. Endosome {ECO:0000269|PubMed:19158384}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:18385514, ECO:0000269|PubMed:19158384}. Cytoplasm, cytoskeleton, microtubule ... | null | null | null | null | null | FUNCTION: The small GTPases Rab are key regulators of intracellular membrane trafficking, from the formation of transport vesicles to their fusion with membranes (PubMed:21320697, PubMed:24843160). Rabs cycle between an inactive GDP-bound form and an active GTP-bound form that is able to recruit to membranes different ... | Caenorhabditis elegans |
O01811 | MEC6_CAEEL | MGLQSAAAHFINRFIIWITIFMVACFLLRLLVVLDLNKRVYNHTPGPCRVLTDNYKGTAGMTYVESQKRVYITLGYGRAHDLKTKTGIAFYKTNRTDGRSQQEMYDLIEMTINWNGYEYKKEFIPTGIDSYSSSNGRVLLYVINAHPNHQCIHFFQIVESSKLNHRKAICDPSFSSLQDIAVVGPDRLFVTNMAAFGRGWAQILEFSLQTGQGAVYYYDGSKLSTAASSLIAPTGIGYDAKRRILYVGSMIRESIFAYKVAKDTTLELLYEMMLLTSPIGVFVESKTGDIWIAAHPVIHESAWHYTHPENQNIHSPSQIL... | null | null | detection of mechanical stimulus involved in sensory perception of touch [GO:0050976]; mechanosensory behavior [GO:0007638]; positive regulation of detection of mechanical stimulus involved in sensory perception of touch [GO:1905789]; positive regulation of mechanosensory behavior [GO:1905792]; potassium ion transport ... | axon [GO:0030424]; plasma membrane [GO:0005886] | arylesterase activity [GO:0004064]; sodium channel activity [GO:0005272] | PF01731; | 2.120.10.30; | Paraoxonase family | PTM: Glycosylated. {ECO:0000269|PubMed:12478294}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12478294}; Single-pass membrane protein {ECO:0000269|PubMed:12478294}. Cell projection, axon {ECO:0000269|PubMed:12478294}. Note=Co-localizes with mec-4 in puncta along the axons of touch cell receptor neurons and in muscles. {ECO:0000269|PubMed:12478294}. | null | null | null | null | null | FUNCTION: Subunit of an amiloride-sensitive cation channel (degenerin channel complex) permeable for sodium, potassium, lithium and N-methylglucamine, and required for mechanosensory transduction (touch sensitivity) (PubMed:12478294). Interacts with degenerin channel proteins and stabilizes the channel (PubMed:12478294... | Caenorhabditis elegans |
O01822 | BL1S6_CAEEL | MSNTEHNVESKNVTDTLDEILRLQEDIQARIGSSNHNLETNFESIKDFVSRAHAYIPILNQISKDMIEICERTQALKKKTSQLELSDTNIEDGSTTSTPTTTNKSQ | null | null | endosomal transport [GO:0016197]; positive regulation of gut granule assembly [GO:1904757]; positive regulation of intracellular protein transport [GO:0090316] | BLOC complex [GO:0031082]; BLOC-1 complex [GO:0031083]; cytoplasm [GO:0005737]; endosome [GO:0005768] | protein homodimerization activity [GO:0042803] | null | null | BLOC1S6 family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:22916203}. Endosome {ECO:0000269|PubMed:22916203}. | null | null | null | null | null | FUNCTION: Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1) involved in gut granule biogenesis. {ECO:0000269|PubMed:22916203}. | Caenorhabditis elegans |
O01836 | GLH3_CAEEL | MDKSPTKTSIRTKFARHQPISDVDTTEQSSSCIKKDDRGLSSFGVQSSVFSRRSCRMSELEAKPTIISEDQRIAVRSEIGGSFSGFDDKVDNVFHSNNNLHGSPSTTELECPGIMNPRFLVGRSLNSRSRAVTRGSKRTSNVKENEGSIHRSDDQVSTENCSAKDEERDRDSGGVSSYGNKRSDEFCGTSPILEAKGFGISNTCFNCKKYGHRATECSAPQRECANCGDPNHRANECASWSKNGVQEPTKVTYVPVVDKMEEVFSMLKINAGDFFDKFFDASVQLVSRGQPVTIQPCKSFSDSDIPQSMRRNVERAGYTR... | 3.6.4.13 | null | cell differentiation [GO:0030154]; gamete generation [GO:0007276]; germ cell development [GO:0007281] | nucleus [GO:0005634]; P granule [GO:0043186] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; DEAD/H-box RNA helicase binding [GO:0017151]; JUN kinase binding [GO:0008432]; mRNA binding [GO:0003729]; protein self-association [GO:0043621]; RNA helicase activity [GO:0003724]; zinc ion binding [GO:0008270] | PF00270;PF00271;PF00098; | 3.40.50.300;4.10.60.10; | DEAD box helicase family, DDX4/VASA subfamily | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21402787}. | 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: Probable ATP-binding RNA helicase. | Caenorhabditis elegans |
O01839 | VPS51_CAEEL | MSSVLDVTKPDFDVEAFVVKLLREKSLDGLVKEEEEMVSAVRRLDSDVHQIVYENYNKFLTATNTVRKIQDEFTQLDSEMKSLSRSMSTISTLIGNLDGVLGEKRDDILQLGSSYKVVNSLKHIFDLPHVLRSEFDERNYGEVLRMFKLAEESLSQYKDVPTVQLVLQKSKKIYDMTENQLMDQLRNPASGAELVSEAVDLLLTIGRDEDEVQKVLLTCSEQSLRVDLKELSANHSDVLDLVDKASESFIPNLTLIATTHDRLFEDKREDLITVLKTEMNSLHALVSKVFLSSSDAKDCSIVVRALDRYFRKISTCRYVI... | null | null | endocytic recycling [GO:0032456]; Golgi organization [GO:0007030]; Golgi vesicle transport [GO:0048193]; lysosomal transport [GO:0007041]; negative regulation of dense core granule transport [GO:1904810]; positive regulation of dense core granule transport [GO:1904811]; positive regulation of locomotion involved in loc... | cytosol [GO:0005829]; EARP complex [GO:1990745]; GARP complex [GO:0000938]; membrane [GO:0016020] | syntaxin binding [GO:0019905] | PF08700; | null | VPS51 family | null | SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network {ECO:0000269|PubMed:21613545}. | null | null | null | null | null | FUNCTION: Acts as a component of the GARP complex that is involved in retrograde transport from early and late endosomes to the trans-Golgi network (TGN) (PubMed:21613545). The GARP complex facilitates tethering as well as SNARE complex assembly at the Golgi (PubMed:21613545). Plays a role in the trafficking of cargo t... | Caenorhabditis elegans |
O01887 | TRYL5_CAEEL | MRPRIIVFLFQVLVVIKGTKLKYYNDELCGRQSTYTSFMLTDAAGNTGNPTHLAPWAVQIRVKARKGDFEVICGGTLITLKHVLTAAHCFQKHFGAKKEGGEENSMSGRYCESNQRFTDSEILTRTVVTVGAMCTRLEQKYGCVNEKQNGKTLKISRFAIGDFYKTHCEQGNDIVILELESTIDDVEGANYACLPFLPEVNIQSGANVTSFGWGSDPGKGFDNAAFPMIQVLTLATETLATCEENWGTSIPFDSFCTAEEEDKNVCSGDSGGGLTFHQSDSAREFIIAIVSYGSDCVQLIGGSEPRSQINTDVRKHQKFI... | 3.4.21.- | null | proteolysis [GO:0006508]; spermatid development [GO:0007286] | extracellular space [GO:0005615]; secretory vesicle [GO:0099503] | serine-type endopeptidase activity [GO:0004252] | PF00089; | 2.40.10.10; | Peptidase S1 family | null | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:22125495, ECO:0000269|PubMed:30470702}. Cytoplasmic vesicle, secretory vesicle lumen {ECO:0000269|PubMed:22125495, ECO:0000269|PubMed:30470702}. Note=In males, partially colocalizes with swm-1 in vesicles near the apical membrane of cuboidal cells (PubMed:22125495, Pub... | null | null | null | null | null | FUNCTION: Serine protease which, in males, acts as a promoting signal during mating to activate sperm. {ECO:0000269|PubMed:22125495}. | Caenorhabditis elegans |
O01901 | WASC3_CAEEL | MNASSRTKPAIDLNKVPPIDHHRTAVTFNCLIMKMTEMLNNFGNKMEDILEKAEQSLDTADRKLRLMESKLAGMSLEDKSTTATPSSAPEIDEIHESNPSSSQIVEETVEEKPEEHTTTVLIKDDPAYSKYFKMLKLGVLEAGVIQKMKSEGVDPSILKRGDEPSRPQAQTSRNYESSGESTASFSDSD | null | null | actin filament polymerization [GO:0030041]; cytoplasmic sequestering of protein [GO:0051220]; determination of adult lifespan [GO:0008340]; exocytosis [GO:0006887]; regulation of gene expression [GO:0010468] | cytoplasm [GO:0005737]; WASH complex [GO:0071203] | null | PF10152; | null | CCDC53 family | PTM: Phosphorylated (PubMed:22265419). Phosphorylation on Thr-182 may promote DHIC complex dissociation and consequently the activation of heat-shock transcription factor hsf-1 (PubMed:22265419). Phosphorylation is modulated by the Insulin/IGF-1-like signaling (IIS) mediated pathway (PubMed:22265419). {ECO:0000269|PubM... | null | null | null | null | null | null | FUNCTION: Acts as a component of the WASH core complex that functions as a nucleation-promoting factor (NPF) at the surface of endosomes, where it recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of tubules that serve as transport intermediates during endosome ... | Caenorhabditis elegans |
O01925 | MBOA5_CAEEL | MGVVGALSEVTSASEDALRLLISVLAGYPLAVVHRTFFYNKPAQHQHLFFVIVGLSLWMFNCGSSVIHPILSIFGAFFITNFMAGTDASIYAAHIVFLGHLLIGYWFHETDTYDITWTTPFCIMTLRFIGLVMDVYDGAQKPEHLKPDQKLTAISDKPGLLEIAAFGLFFQGTLVGPQFTLSKFRSFVNGDWLDSDGQPPKSAFLPSIGRFLAGCTYMVLHQWGQFWIPDQYFNSDAYNNLSFFWRWSWVTLWFRLTMYKYCAMWLITEGASILSGLGHNGKDAEGNDRWDGVRDLHIIKWETGHDYNSVVESFNCGTNT... | 2.3.1.-; 2.3.1.23; 2.3.1.n6; 2.3.1.n7 | null | lipid modification [GO:0030258]; nematode larval development [GO:0002119]; phosphatidylcholine biosynthetic process [GO:0006656]; phosphatidylethanolamine biosynthetic process [GO:0006646]; phosphatidylserine biosynthetic process [GO:0006659]; positive regulation of growth rate [GO:0040010]; post-embryonic body morphog... | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020] | 1-acylglycerophosphocholine O-acyltransferase activity [GO:0047184]; 1-acylglycerophosphoethanolamine O-acyltransferase activity [GO:0106262]; 1-acylglycerophosphoserine O-acyltransferase activity [GO:0106263]; lysophospholipid acyltransferase activity [GO:0071617]; O-acyltransferase activity [GO:0008374] | PF03062; | null | Membrane-bound acyltransferase family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + an acyl-CoA = a 1,2-diacyl-sn-glycero-3-phosphocholine + CoA; Xref=Rhea:RHEA:12937, ChEBI:CHEBI:57287, ChEBI:CHEBI:57643, ChEBI:CHEBI:58168, ChEBI:CHEBI:58342; EC=2.3.1.23; Evidence={ECO:0000269|PubMed:18782225}; CATALYTIC ACTIVITY: Reaction=a 1-acyl-s... | null | PATHWAY: Lipid metabolism; phospholipid metabolism. {ECO:0000269|PubMed:18782225}. | null | null | FUNCTION: Probable acyltransferase which may mediate the conversion of lysophosphatidylcholine (1-acyl-sn-glycero-3-phosphocholine or LPC) into phosphatidylcholine (1,2-diacyl-sn-glycero-3-phosphocholine or PC) (LPCAT activity). May also catalyze the conversion of lysophosphatidylethanolamine (1-acyl-2-hydroxy-sn-glyce... | Caenorhabditis elegans |
O01965 | ARI11_CAEEL | MSSDDEINMDDSDSSQGEIDDGCMSDDDGIVLESREQNSSDYKDNGEPDNEVLNHDSLEAEMKKTITDVQAVLQVKTGVCRILLHKYKWNKESLLERFYEHPDTTTFLIDAHVIPRRQERLPAGDAECDICCSLGELSGLSCNHRACTQCWKAYLTNKIANNAQSEIECMAPNCKLLIEDEKVMFYITDPTVIATYRKLIVASYVETNRLLKWCPGIDCGKAVRVSHWEPRLVVCSCGSRFCFSCGHDWHEPVNCRLLKLWLKKCNDDSETSNWINANTKECPKCMITIEKDGGCNHMTCKNTACRFEFCWMCLGPWEPH... | 2.3.2.31 | null | positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; protein polyubiquitination [GO:0000209]; ubiquitin-dependent protein catabolic process [GO:0006511] | cytoplasm [GO:0005737]; nucleus [GO:0005634]; ubiquitin ligase complex [GO:0000151] | ubiquitin conjugating enzyme binding [GO:0031624]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270] | PF21235;PF19422;PF01485; | 1.20.120.1750;3.30.40.10; | RBR family, Ariadne subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16457801}. Cytoplasm {ECO:0000269|PubMed:16457801}. | CATALYTIC ACTIVITY: Reaction=[E2 ubiquitin-conjugating enzyme]-S-ubiquitinyl-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-N(6)-ubiquitinyl-L-lysine.; EC=2.3.2.31; Evidence={ECO:0000250|UniProtKB:Q9Y4X5}; | null | null | null | null | FUNCTION: E3 ubiquitin-protein transferase, which catalyzes ubiquitination of target proteins together with ubiquitin-conjugating enzyme E2 ubc-18 (By similarity). Acts with ubc-18 to regulate pharyngeal development (PubMed:16457801, PubMed:19521497). {ECO:0000250|UniProtKB:Q9Y4X5, ECO:0000269|PubMed:16457801, ECO:0000... | Caenorhabditis elegans |
O01971 | EMR1_CAEEL | MDVSQLTDAELRDSLKSHGVSVGPIVATTRKLYEKKLIKLSDGSINNQSNLNDSQFNEDSLIISSSPKKSPPQRVFQNVSAATAAATTSPESDSDDCEESMRYLTEEEMAADRASARQAQSNKGGFLGSTITFTILFVFIAVFAYFLIENAEQLKLVAETNPEDTI | null | null | chromosome segregation [GO:0007059]; mitotic cytokinesis [GO:0000281]; nuclear envelope organization [GO:0006998]; response to X-ray [GO:0010165] | nuclear envelope [GO:0005635]; nuclear inner membrane [GO:0005637] | lamin binding [GO:0005521] | PF03020; | 1.10.720.40; | null | null | SUBCELLULAR LOCATION: Nucleus inner membrane {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:11870211, ECO:0000269|PubMed:12490171}; Single-pass membrane protein {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:11870211, ECO:0000269|PubMed:12490171}; Nucleoplasmic side {ECO:0000269|PubMed:10982402, ECO:0000269|PubMed:... | null | null | null | null | null | FUNCTION: Nuclear lamina-associated inner nuclear membrane protein that is involved in cell division, nuclear structure organization, maintenance of nuclear envelope integrity and nuclear envelope reformation after mitosis (PubMed:11870211, PubMed:12684533, PubMed:22171324). Involved in chromosome segregation and cell ... | Caenorhabditis elegans |
O01991 | EF2K_CAEEL | MTIDTTNESDNSPTNSPGLEASARTFSLNASKMVRITDDYADEVFIEQNDVVIEKPRMDPLHVRKLMETWRKAARRARTNYIDPWDEFNIHEYPVQRAKRYRYSAIRKQWTEDIVDVRLHPDSFARGAMRECYRLKKCSKHGTSQDWSSNYVAKRYICQVDRRVLFDDVRLQMDAKLWAEEYNRYNPPKKIDIVQMCVIEMIDVKGSPLYHLEHFIEGKYIKYNSNSGFVSNAARLTPQAFSHFTFERSGHQMMVVDIQGVGDLYTDPQIHTVVGTDYGDGNLGTRGMALFFHSHRCNDICETMDLSNFELSPPEIEATE... | 2.7.11.20 | null | myosin II filament disassembly [GO:0031037]; phosphorylation [GO:0016310]; response to differentiation-inducing factor 1 [GO:1903013] | actomyosin contractile ring [GO:0005826] | ATP binding [GO:0005524]; calcium ion binding [GO:0005509]; calmodulin binding [GO:0005516]; elongation factor-2 kinase activity [GO:0004686]; myosin heavy chain kinase activity [GO:0016905] | PF02816; | 3.20.200.10;1.25.40.10; | Protein kinase superfamily, Alpha-type protein kinase family | null | null | CATALYTIC ACTIVITY: Reaction=[translation elongation factor 2] + ATP = [translation elongation factor 2]-phosphate + ADP + H(+); Xref=Rhea:RHEA:21436, Rhea:RHEA-COMP:11268, Rhea:RHEA-COMP:11269, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43176, ChEBI:CHEBI:68546, ChEBI:CHEBI:456216; EC=2.7.11.20; Evidence={ECO:0... | null | null | null | null | FUNCTION: Phosphorylates elongation factor-2 (eEF-2) at two threonine residues that are conserved in all eukaryotes and are located within a GTP-binding domain (PubMed:9144159). Calcium(2+)/calmodulin dependent activity (PubMed:9144159). Inactivates eEF-2 by catalyzing its phosphorylation (PubMed:9144159). eEF-2 cataly... | Caenorhabditis elegans |
O02002 | CASP1_DROME | MTDECVTRNYGVGIRSPNGSENRGSFIMADNTDAKGCTPESLVVGGATAASPLPANKFVARMPVERYASEYNMSHKHRGVALIFNHEFFDIPSLKSRTGTNVDAQELKKAFENLGFAVSVHKDCKLRDILKHVGKAAELDHTDNDCLAVAILSHGEHGYLYAKDTQYKLDNIWHYFTATFCPSLAGKPKLFFIQACQGDRLDGGITLEKGVTETDGESSTSYKIPIHADFLFSYSTIPGYFSWRNINNGSWYMQSLIRELNANGKKYDLLTLLTFVNQRVALDFESNVPATPMMDRQKQIPCLTSMLTRILRFGDKPNGN... | 3.4.22.- | null | apoptotic process [GO:0006915]; cellular response to starvation [GO:0009267]; execution phase of apoptosis [GO:0097194]; negative regulation of neuromuscular synaptic transmission [GO:1900074]; negative regulation of Toll signaling pathway [GO:0045751]; neuron remodeling [GO:0016322]; nurse cell apoptotic process [GO:0... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; mitochondrion [GO:0005739]; neuronal cell body [GO:0043025]; neuronal ribonucleoprotein granule [GO:0071598] | BIR domain binding [GO:1990525]; cysteine-type endopeptidase activity [GO:0004197]; cysteine-type endopeptidase activity involved in apoptotic signaling pathway [GO:0097199]; cysteine-type endopeptidase activity involved in execution phase of apoptosis [GO:0097200] | PF00656; | 3.40.50.1460; | Peptidase C14A family | null | null | null | null | null | null | null | FUNCTION: Involved in the activation cascade of caspases responsible for apoptosis execution (By similarity). Proteolytically cleaves poly(ADP-ribose) polymerase (PARP). Loss of zygotic DCP-1 function causes larval lethality and melanotic tumors. {ECO:0000250}. | Drosophila melanogaster (Fruit fly) |
O02100 | HOP1_CAEEL | MPRTKRVYSGKTITGVLYPVAICMLFVAINVKLSQPEQQEQSKVVYGLFHSYDTADSGTITLYLIGFLILTTSLGVFCYQMKFYKAIKVYVLANSIGILLVYSVFHFQRIAEAQSIPVSVPTFFFLILQFGGLGITCLHWKSHRRLHQFYLIMLAGLTAIFILNILPDWTVWMALTAISFWDIVAVLTPCGPLKMLVETANRRGDDKFPAILYNSSSYVNEVDSPDTTRSNSTPLTEFNNSSSSRLLESDSLLRPPVIPRQIREVREVEGTIRLGMGDFVFYSLMLGNTVQTCPLPTVVACFVSNLVGLTITLPIVTLSQ... | null | null | amyloid-beta formation [GO:0034205]; calcium ion transport [GO:0006816]; egg-laying behavior [GO:0018991]; embryo development ending in birth or egg hatching [GO:0009792]; gonad development [GO:0008406]; membrane protein ectodomain proteolysis [GO:0006509]; negative regulation of apoptotic process [GO:0043066]; nematod... | apical plasma membrane [GO:0016324]; cell cortex [GO:0005938]; cell surface [GO:0009986]; ciliary rootlet [GO:0035253]; dendritic shaft [GO:0043198]; endoplasmic reticulum membrane [GO:0005789]; gamma-secretase complex [GO:0070765]; Golgi membrane [GO:0000139]; growth cone [GO:0030426]; lysosomal membrane [GO:0005765];... | aspartic endopeptidase activity, intramembrane cleaving [GO:0042500]; endopeptidase activity [GO:0004175] | PF01080; | 1.10.472.100; | Peptidase A22A family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. | null | null | null | null | null | FUNCTION: Probable catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptors (lin-12 or glp-1). Probably works redundantly of lin-12, which provides more presenilin function. {ECO:0000269|PubMed:10051671}. | Caenorhabditis elegans |
O02101 | SWIC2_CAEEL | MHSQQRPNPQMNRHPYGTPGSAPQMRRPGGFAGQPPQMHGPRMVAPPAAPLPKKKKYADKCIHPKIRELEPDAENYMALLASEQKLDSTLSRKKLDIQEALKRPSKVKKRLRIYISHTFIEEKQPEKDTDEASLPMWELRVEGRLLDEQPPAPAIPGQRPVPKRKFSSFFKSLVIELDKEMYGPDQHLVEWHRTPQTNETDGFQVKRAGDRPVKCRILLLLDNHPAKFKLHPRLAKVLGIATETRPKIIEALWQYIKTHGLQDPQERDIINCDTFLSQCFGVNRMRFMEVPNKLHQLLQQTDPLEFNHIIQRPKEGQEQV... | null | null | chromatin remodeling [GO:0006338]; positive regulation of double-strand break repair [GO:2000781]; regulation of G1/S transition of mitotic cell cycle [GO:2000045]; regulation of mitotic metaphase/anaphase transition [GO:0030071]; regulation of nucleotide-excision repair [GO:2000819]; regulation of transcription by RNA... | condensed chromosome [GO:0000793]; nuclear envelope [GO:0005635]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; SWI/SNF complex [GO:0016514] | RNA polymerase II-specific DNA-binding transcription factor binding [GO:0061629]; transcription coregulator activity [GO:0003712] | PF02201; | 1.10.245.10; | SMARCD family | null | SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000269|PubMed:26739451}. Chromosome {ECO:0000269|PubMed:26739451}. Nucleus envelope {ECO:0000269|PubMed:26739451}. Note=Localizes to mitotic chromosomes in the early embryo. {ECO:0000269|PubMed:26739451}. | null | null | null | null | null | FUNCTION: Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Component of SWI/SNF chromatin remodeling complexes that carry out key enzymatic activities, changing chromatin structure by altering DNA-histone contacts within a nucleosome ... | Caenorhabditis elegans |
O02151 | NHR14_CAEEL | MDFLISTSLSESTSTSADFCVVCGDKAIGKHYGAVACNGCKGFFRRSVWQNLQYTCRFNKQCNIDKDHRNACRYCRFQKCLADGMKPEAIQNERDRIGSTKRRKRSGANSENNSDSEGTPSPKIEVMGNSVSRKLIEMLLDIEHRLASNQSMNALLRDESEMKNSRQRAVNYLIGWTNMLHPLPEVPLADKVLLLKKFSSAFTLLGTLQRSMALPHFVLPNDQVLSISASHPPELFEALTRIIDELLTPLRRLRTDHAEFSCLKALLLLNPDVVGISNNTRERIREARDALLKTLFAYMSNTQNSIDASLRVSSLLMIIP... | null | null | cell differentiation [GO:0030154]; defense response to Gram-negative bacterium [GO:0050829]; negative regulation of protein localization to nucleus [GO:1900181]; regulation of innate immune response [GO:0045088]; regulation of transcription by RNA polymerase II [GO:0006357] | nucleus [GO:0005634] | nuclear receptor activity [GO:0004879]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; steroid hormone binding [GO:1990239]; zinc ion binding [GO:0008270] | PF00104;PF00105; | 3.30.50.10;1.10.565.10; | Nuclear hormone receptor family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407}. | null | null | null | null | null | FUNCTION: Orphan nuclear receptor (PubMed:10022975). Transcriptional repressor of intestinal metal transporter smf-3 and genes of the innate immune response (PubMed:31532389). Inhibits nuclear localization of transcription factor pqm-1; in response to pathogen stress, may facilitate translocation of pqm-1, leading to t... | Caenorhabditis elegans |
O02193 | MOF_DROME | MSEAELEQTPSAGHVQEQPIEEEHEPEQEPTDAYTIGGPPRTPVEDAAAELSASLDVSGSDQSAEQSLDLSGVQAEAAAESEPPAKRQHRDISPISEDSTPASSTSTSSTRSSSSSRYDDVSEAEEAPPEPEPEQPQQQQQEEKKEDGQDQVKSPGPVELEAQEPAQPQKQKEVVDQEIETEDEPSSDTVICVADINPYGSGSNIDDFVMDPDAPPNAIITEVVTIPAPLHLKGTQQLGLPLAAPPPPPPPPAAEQVPETPASPTDDGEEPPAVYLSPYIRSRYMQESTPGLPTRLAPRDPRQRNMPPPAVVLPIQTVLS... | 2.3.1.48 | null | DNA damage response, signal transduction by p53 class mediator [GO:0030330]; DNA repair-dependent chromatin remodeling [GO:0140861]; dosage compensation by hyperactivation of X chromosome [GO:0009047]; negative regulation of DNA-templated transcription [GO:0045892]; positive regulation of DNA-templated transcription [G... | MSL complex [GO:0072487]; NSL complex [GO:0044545]; NuA4 histone acetyltransferase complex [GO:0035267]; nuclear chromosome [GO:0000228]; nucleus [GO:0005634]; polytene chromosome interband [GO:0005705]; transcription regulator complex [GO:0005667]; X chromosome [GO:0000805]; X chromosome located dosage compensation co... | chromatin binding [GO:0003682]; histone acetyltransferase activity [GO:0004402]; histone H4K16 acetyltransferase activity [GO:0046972]; lncRNA binding [GO:0106222]; metal ion binding [GO:0046872]; transcription coregulator activity [GO:0003712] | PF01853;PF11717;PF17772; | 2.30.30.140;3.40.630.30;3.30.60.60;1.10.10.10; | MYST (SAS/MOZ) family | PTM: Autoacetylation at Lys-638 is required for binding histone H4 with high affinity and for proper function. {ECO:0000250|UniProtKB:Q9H7Z6}.; PTM: Ubiquitinated by msl-2. {ECO:0000269|PubMed:23084834, ECO:0000269|PubMed:28510597}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20620954}. Chromosome {ECO:0000269|PubMed:11014199, ECO:0000269|PubMed:18510926, ECO:0000269|PubMed:20620954, ECO:0000269|PubMed:22421046, ECO:0000269|PubMed:28510597}. Note=When part of MSL complex, specifically localizes to many sites on the male X chromosome: display... | CATALYTIC ACTIVITY: Reaction=acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L-lysyl-[histone]; Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845, Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48; Evidence={ECO:0000269|PubMed:10882077, EC... | null | null | null | null | FUNCTION: Histone acetyltransferase that catalyzes the formation of the majority of histone H4 acetylation at 'Lys-16' (H4K16ac), an epigenetic mark that prevents chromatin compaction and constitutes the only acetylation mark intergenerationally transmitted (PubMed:10882077, PubMed:18510926, PubMed:20620953, PubMed:224... | Drosophila melanogaster (Fruit fly) |
O02194 | PSN_DROME | MAAVNLQASCSSGLASEDDANVGSQIGAAERLERPPRRQQQRNNYGSSNQDQPDAAILAVPNVVMREPCGSRPSRLTGGGGGSGGPPTNEMEEEQGLKYGAQHVIKLFVPVSLCMLVVVATINSISFYNSTDVYLLYTPFHEQSPEPSVKFWSALANSLILMSVVVVMTFLLIVLYKKRCYRIIHGWLILSSFMLLFIFTYLYLEELLRAYNIPMDYPTALLIMWNFGVVGMMSIHWQGPLRLQQGYLIFVAALMALVFIKYLPEWTAWAVLAAISIWDLIAVLSPRGPLRILVETAQERNEQIFPALIYSSTVVYALVN... | 3.4.23.- | null | amyloid-beta formation [GO:0034205]; apoptotic process [GO:0006915]; calcium ion transport [GO:0006816]; membrane protein ectodomain proteolysis [GO:0006509]; negative regulation of apoptotic process [GO:0043066]; Notch receptor processing [GO:0007220]; Notch receptor processing, ligand-dependent [GO:0035333]; Notch si... | apical plasma membrane [GO:0016324]; cell cortex [GO:0005938]; cell surface [GO:0009986]; ciliary rootlet [GO:0035253]; dendritic shaft [GO:0043198]; endoplasmic reticulum membrane [GO:0005789]; gamma-secretase complex [GO:0070765]; Golgi membrane [GO:0000139]; growth cone [GO:0030426]; lysosomal membrane [GO:0005765];... | aspartic endopeptidase activity, intramembrane cleaving [GO:0042500]; endopeptidase activity [GO:0004175] | PF01080; | 1.10.472.100; | Peptidase A22A family | PTM: Cleaved. The cleavage, which probably takes place between the 6th and the 7th transmembrane regions, may be required for activation of the gamma-secretase activity. {ECO:0000269|PubMed:10662508}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. Golgi apparatus membrane {ECO:0000250}; Multi-pass membrane protein {ECO:0000250}. | null | null | null | null | null | FUNCTION: Probable catalytic subunit of the gamma-secretase complex, an endoprotease complex that catalyzes the intramembrane cleavage of integral membrane proteins such as Notch receptor. Required for S3 cleavage of Notch, which releases activated Notch protein from the cell membrane. Involved in the patterning of the... | Drosophila melanogaster (Fruit fly) |
O02213 | SER2_CAEEL | MFRNYTDSVQEMVLRAIDSIRDSVINASSAVSTTTLPPLDIPMTSMKPPSIIPTVELVLGTITYLVIIAMTVVGNTLVVVAVFSYRPLKKVQNYFLVSLAASDLAVAIFVMPLHVVTFLAGGKWLLGVTVCQFFTTADILLCTSSILNLCAIALDRYWAIHNPINYAQKRTTKFVCIVIVIVWILSMLISVPPIIGWNNWQENMMEDSCGLSTEKAFVVFSAAGSFFLPLLVMVVVYVKIFISARQRIRTNRGRSALMRIQNAEGDDDYRKMSIKRASVESARTSSRVGEKTPLVIADGQTTVTTLAAHSTDGGSLPKDE... | null | null | adenylate cyclase-activating adrenergic receptor signaling pathway [GO:0071880]; dopamine receptor signaling pathway [GO:0007212]; octopamine or tyramine signaling pathway [GO:0007211] | membrane [GO:0016020]; plasma membrane [GO:0005886] | G protein-coupled amine receptor activity [GO:0008227]; octopamine receptor activity [GO:0004989]; tyramine receptor activity [GO:0008226] | PF00001; | 1.20.1070.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. | null | null | null | null | null | FUNCTION: G-protein coupled receptor for tyramine, a known neurotransmitter and neuromodulator and direct precursor of octopamine. The rank order of potency is tyramine > octopamine > dopamine > serotonin > epinephrine = norepinephrine. {ECO:0000269|PubMed:12354282}. | Caenorhabditis elegans |
O02217 | P2R31_CAEEL | MPTDEPSKRKSILPTIPTSLMLKKSNEALSDFERTFNDRVMDIFAENRRIDVEEFKKNAECFLNIIRSNKIDLNWGEGGESRYVTITRLMKILKTSPQSIKDLLPHNTVSNFVKITNYNLTIDITLLEELVRTVIHAEESYIKLLPFSENSTEISSYSLQDFVATHFIPIMIEEPENPVYYTAYAVGTIFFLLGARRRDCVYLKDLLASTLLLQLEECIHAENHCLSPPKIDVFTVAQFRTTLSEFRFLDSQRKGLLAPADLKFFRDGIFNEVFTKRIFEISITYEDGRIDFKAFVDFVTALKFRHTTASAKYHFEILDL... | null | null | cortical cytoskeleton organization [GO:0030865]; embryo development ending in birth or egg hatching [GO:0009792]; microtubule cytoskeleton organization [GO:0000226]; mitotic spindle assembly [GO:0090307]; mitotic spindle organization [GO:0007052]; positive regulation of B cell differentiation [GO:0045579]; protein loca... | centrosome [GO:0005813]; cytoplasm [GO:0005737]; protein phosphatase type 2A complex [GO:0000159]; spindle [GO:0005819] | protein phosphatase 2A binding [GO:0051721] | null | 1.10.238.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17218259, ECO:0000269|PubMed:23336080}. | null | null | null | null | null | FUNCTION: Regulatory subunit of phosphatase let-92 which recruits let-92/paa-1 complex to the centrosomes, thereby regulating microtubule outgrowth from centrosomes and mitotic spindle assembly ensuring the stability of kinetochore microtubules. {ECO:0000269|PubMed:17218259, ECO:0000269|PubMed:23336080}. | Caenorhabditis elegans |
O02219 | AHA1_CAEEL | MAQDIFMDPWQSATSFAMEDEDMGMPSGKYARMEDEMGENKERFARENHSEIERRRRNKMTHYINELAEMVPQCASLGRKPDKLTILRMAVSHMKGIRGHTAQDETSYKPSFLTDQELKHLILEAANGFLFVVCCQTGKVLYVADSITPVLNLKQEDWLQRNLNELIHPDDQDKIRDQLCGSEVSVNKVLDLKSGSVKREGASTRVHMSCRRGFICRMRVGALEPLHRLRNRRPLFQHAGQNYVVMHCTGYIKNAPPQGINAPASSCLVAIARLQVASMPVCADPTSTNQFSVRVSEDGKMTFIDARVSDLIGLSSDQLI... | null | null | cell fate specification [GO:0001708]; determination of adult lifespan [GO:0008340]; intracellular receptor signaling pathway [GO:0030522]; neurogenesis [GO:0022008]; positive regulation of transcription by RNA polymerase II [GO:0045944]; protein maturation by protein folding [GO:0022417]; regulation of transcription by... | aryl hydrocarbon receptor complex [GO:0034751]; cytoplasm [GO:0005737]; nucleus [GO:0005634]; protein folding chaperone complex [GO:0101031]; RNA polymerase II transcription regulator complex [GO:0090575] | DNA binding [GO:0003677]; DNA-binding transcription factor activity [GO:0003700]; 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]; RNA polymerase II-specific... | PF00010;PF00989;PF14598; | 4.10.280.10;3.30.450.20; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00981, ECO:0000269|PubMed:11427734}. Note=Nuclear location dependent on hif-1 expression in intestinal tissue but not in neuronal cells. {ECO:0000269|PubMed:11427734}. | null | null | null | null | null | FUNCTION: Transcription factor (PubMed:17628356). Efficient DNA binding requires dimerization with another bHLH protein, such as cky-1 or ahr-1 (PubMed:17628356, PubMed:9501178). Regulates transcription of target genes, probably acting in complex with cky-1 (PubMed:17628356). Has a role in cellular differentiation (Pub... | Caenorhabditis elegans |
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