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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A1Z9L3 | DHX8_DROME | MDELQKLEYLSLVSKICTELDNHLGINDKDLAEFIIDLENKNRTYDTFRKALLDNGAEFPDSLVQNLQRIINLMRPSRPGGASQEKTVGDKKEDKKSQLLKMFPGLALPNDTYSKKEESDDDEKVKAKPEKHSETHKKTDMSDVDAAMMELEALAPGEGATLVRPHKEVSSRDRHKRRSRDRDTKRRSRSREDRHSDRRRSRSRDKERRRRSRSRDNRRRSRSREDRDRDRDRRHKSSSSRDHHERRRRSRSRSTERRDRRDRSRDCSEKMPPPSAAMTDDPEAGKIYSGKIANIVPFGCFVQLFGLRKRWEGLVHISQL... | 3.6.4.13 | null | chromatin organization [GO:0006325]; chromosome condensation [GO:0030261]; mRNA splicing, via spliceosome [GO:0000398]; oogenesis [GO:0048477]; regulation of alternative mRNA splicing, via spliceosome [GO:0000381]; spliceosomal complex disassembly [GO:0000390]; ventral cord development [GO:0007419] | catalytic step 2 spliceosome [GO:0071013]; nucleus [GO:0005634]; precatalytic spliceosome [GO:0071011]; spliceosomal complex [GO:0005681] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; RNA binding [GO:0003723]; RNA helicase activity [GO:0003724] | PF21010;PF04408;PF00271;PF07717;PF00575; | 1.20.120.1080;2.40.50.140;3.40.50.300; | DEAD box helicase family, DEAH subfamily, DDX8/PRP22 sub-subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18981222}. | 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:0000250|UniProtKB:P24384}; | null | null | null | null | FUNCTION: Involved in pre-mRNA splicing as component of the spliceosome (PubMed:18981222, PubMed:24244416). Facilitates nuclear export of spliced mRNA by releasing the RNA from the spliceosome (By similarity). Before and after egg-chamber formation, required for nurse-cell chromatin dispersal (NCCD) probably by playing... | Drosophila melanogaster (Fruit fly) |
A1Z9P3 | SHRM_DROME | MKMRNHKENGNGSEMGESTKSLAKMEPENNNKISVVSVSKLLLKDSNGANSRSSNSNASFSSASVAGSVQDDLPHHNSSSSQLGQQHGSSLDQCGLTQAGLEEYNNRSSSYYDQTAFHHQKQPSYAQSEGYHSYVSSSDSTSATPFLDKLRQESDLLSRQSHHWSENDLSSVCSNSVAPSPIPLLARQSHSHSHSHAHSHSNSHGHSHGHAHSASSSSSSNNNSNGSATNNNNNNSSESTSSTETLKWLGSMSDISEASHATGYSAISESVSSSQRIVHSSRVPTPKRHHSESVLYLHNNEEQGDSSPTASNSSQMMISE... | null | null | actin cytoskeleton organization [GO:0030036]; actin filament organization [GO:0007015]; actomyosin structure organization [GO:0031032]; apical constriction [GO:0003383]; cell migration [GO:0016477]; cell morphogenesis [GO:0000902]; embryonic morphogenesis [GO:0048598]; establishment of planar polarity of embryonic epit... | adherens junction [GO:0005912]; apical junction complex [GO:0043296]; apical plasma membrane [GO:0016324]; bicellular tight junction [GO:0005923]; cell-cell junction [GO:0005911]; cortical actin cytoskeleton [GO:0030864]; cytoskeleton [GO:0005856]; microtubule [GO:0005874]; plasma membrane [GO:0005886] | actin binding [GO:0003779]; actin filament binding [GO:0051015]; kinase binding [GO:0019900]; protein homodimerization activity [GO:0042803] | PF08687; | 6.10.250.3120; | Shroom family | null | SUBCELLULAR LOCATION: [Isoform D]: Cell junction, adherens junction {ECO:0000269|PubMed:20549743, ECO:0000269|PubMed:22493320, ECO:0000269|PubMed:24535826}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16684770, ECO:0000269|PubMed:20549743}. Note=In adherens junctions, enriched in discrete spots and in tricellular junct... | null | null | null | null | null | FUNCTION: Binds to Rho-kinase Rok and targets it to the apical cell cortex where it mediates apical constriction (PubMed:20549743, PubMed:22493320). During embryogenic axis elongation, required for the localization to adherens junctions and the establishment of planar polarization of both Rho-kinase Rok and myosin regu... | Drosophila melanogaster (Fruit fly) |
A1Z9S1 | BL1S1_DROME | MLTSMVKEHHKEQAKRKQEQEVRRKEAIEASNELTQSLVDTLNVGVAQAYLNQKRLDAEAKQLHLGATNFAKQTHQWLQLIDQFSTALKDLGDVENWARSIEGDMHTINQTLELAYKASRATQTSSGAGTSLEASTSASASANPSAT | null | null | autophagosome-lysosome fusion [GO:0061909]; endosomal transport [GO:0016197]; eye pigment granule organization [GO:0008057]; neuromuscular synaptic transmission [GO:0007274]; olfactory learning [GO:0008355]; regulation of synaptic vesicle cycle [GO:0098693]; synapse organization [GO:0050808]; synaptic vesicle recycling... | BLOC-1 complex [GO:0031083]; neuromuscular junction [GO:0031594]; presynapse [GO:0098793] | null | PF06320; | null | BLOC1S1 family | null | null | null | null | null | null | null | FUNCTION: Component of the biogenesis of lysosome-related organelles complex-1 (BLOC-1) involved in pigment granule biogenesis and membrane trafficking in synapses (PubMed:20015953, PubMed:28317021). In response to high synaptic activity at neuromuscular junctions, stabilizes Pldn protein levels and, together with Pldn... | Drosophila melanogaster (Fruit fly) |
A1Z9X0 | APKC_DROME | MQKMPSQILNDGSSVSLNSASMNMANTPNSITVKTAYNGQIIITTINKNISYEELCYEIRNICRFPLDQPFTIKWVDEENDPCTISTKMELDEAIRLYEMNFDSQLVIHVFPNVPQAPGLSCDGEDRSIYRRGARRWRKLYRVNGHIFQAKRFNRRAFCAYCQDRIWGLGRQGFKCIQCKLLVHKKCHKLVQKHCTDQPEPLVKERAEESSDPIPVPLPPLPYEAMSGGAEACETHDHAHIVAPPPPEDPLEPGTQRQYSLNDFELIRVIGRGSYAKVLMVELRRTRRIYAMKVIKKALVTDDEDIDWVQTEKHVFETAS... | 2.7.11.13 | null | adherens junction organization [GO:0034332]; apical protein localization [GO:0045176]; asymmetric neuroblast division [GO:0055059]; asymmetric protein localization involved in cell fate determination [GO:0045167]; branching involved in open tracheal system development [GO:0060446]; cell-cell junction assembly [GO:00070... | apical cortex [GO:0045179]; apical junction complex [GO:0043296]; apical plasma membrane [GO:0016324]; apicolateral plasma membrane [GO:0016327]; cell cortex [GO:0005938]; nucleus [GO:0005634]; subapical complex [GO:0035003] | ATP binding [GO:0005524]; diacylglycerol-dependent serine/threonine kinase activity [GO:0004697]; metal ion binding [GO:0046872]; myosin binding [GO:0017022]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674] | PF00130;PF00564;PF00069;PF00433; | 3.30.60.20;1.10.510.10; | Protein kinase superfamily, AGC Ser/Thr protein kinase family, PKC subfamily | null | SUBCELLULAR LOCATION: Cytoplasm, cell cortex {ECO:0000269|PubMed:10995441, ECO:0000269|PubMed:11734648, ECO:0000269|PubMed:15302858, ECO:0000269|PubMed:18614576, ECO:0000269|PubMed:20434988, ECO:0000269|PubMed:24830287}. Apicolateral cell membrane {ECO:0000269|PubMed:10995441, ECO:0000269|PubMed:11734648, ECO:0000269|P... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.13; Evidence={ECO:0000305}; CATALYTIC ACTIVITY: Reac... | null | null | null | null | FUNCTION: Serine/threonine protein kinase which is required for apico-basal cell polarity in the germ line as well as in epithelial and neural precursor cells, for epithelial planar cell polarity and for cell proliferation. During oocyte development, required for the posterior translocation of oocyte specification fact... | Drosophila melanogaster (Fruit fly) |
A1ZA47 | ZASP_DROME | MAQPQLLQIKLSRFDAQPWGFRLQGGTDFAQPLLVQKVNAGSLSEQAGLQPGDAVVKINDVDVFNLRHKDAQDIVVRSGNNFVITVQRGGSTWRPHVTPTGNVPQPNSPYLQTVTKTSLAHKQQDSQHIGCGYNNAARPFSNGGDGGVKSIVNKQYNTPVGIYSDESIAETLSAQAEVLAGGVLGVNFKKNEKEYQGDRSEVLKFLREEETGQSTPAFGNSHYEHDAPQQLQQPQQQYNQHQQHYHQQQQQQQSSTTRHVSAPVNSPKPPSTGGLPTGQNICTECERLITGVFVRIKDKNLHVECFKCATCGTSLKNQGY... | null | null | actin cytoskeleton organization [GO:0030036]; heart development [GO:0007507]; muscle structure development [GO:0061061]; myofibril assembly [GO:0030239]; regulation of cell-matrix adhesion [GO:0001952] | actin cytoskeleton [GO:0015629]; adherens junction [GO:0005912]; apical part of cell [GO:0045177]; basal part of cell [GO:0045178]; basolateral plasma membrane [GO:0016323]; cell leading edge [GO:0031252]; filamentous actin [GO:0031941]; focal adhesion [GO:0005925]; muscle tendon junction [GO:0005927]; stress fiber [GO... | actin binding [GO:0003779]; actinin binding [GO:0042805]; metal ion binding [GO:0046872]; muscle alpha-actinin binding [GO:0051371] | PF15936;PF00412;PF00595; | 2.30.42.10;2.10.110.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:18166658}. Note=Regulates or strengthens the link of integrins to the actin cytoskeleton. {ECO:0000269|PubMed:18166658}. | null | null | null | null | null | FUNCTION: Regulator of cell matrix adhesion having two related functions, one upstream of Actn organizing the Z line and the other downstream of integrins regulating assembly of integrin adhesion sites. Also required for the formation of myotendinous junctions in muscles. {ECO:0000269|PubMed:18166658}. | Drosophila melanogaster (Fruit fly) |
A1ZA55 | CGLR1_DROME | MAMNLENIVNQATAQYVKIKEHREPYTAHYNALKDKVYSEWKSSAVLGKLLKGSTLCGGYGDKLKVSIPDEFDLLIHLVFPENDKIIVKADASKPGNVILDMTKVMEIIGSQEHNKPVFDRLQKIVNNKKQLLEDKLNSFLESIMTQTLNKMGNQIEVAGRISHLQYKKCGPAHTIFVKGSCKYSVDFVPAIRLSAAQVVLAPEQRIHFGETLYWDAIPKPMKPAKTDNTSFTSSFYEAERRLLYGKQFLKPAIRLMKQNRNVKNKANLKSYHIKTLFLWQVIQQDPSYWSNSPKDIFIEMLGKLADSLALTPKKGKLPF... | 2.7.7.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:34261127}; Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000269|PubMed:34261127}; | cellular response to virus [GO:0098586]; cGAS/STING signaling pathway [GO:0140896]; defense response to virus [GO:0051607]; immune response involved in response to exogenous dsRNA [GO:1902615]; innate immune response [GO:0045087]; response to exogenous dsRNA [GO:0043330] | cytosol [GO:0005829] | 2',3'-cyclic GMP-AMP synthase activity [GO:0061501]; 3',2'-cyclic GMP-AMP synthase activity [GO:0140700]; ATP binding [GO:0005524]; double-stranded RNA binding [GO:0003725]; GTP binding [GO:0005525]; metal ion binding [GO:0046872] | PF03281;PF20266; | 1.10.1410.40;3.30.460.90; | Mab-21 family | null | null | CATALYTIC ACTIVITY: Reaction=ATP + GTP = 3',2'-cGAMP + 2 diphosphate; Xref=Rhea:RHEA:68344, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:37565, ChEBI:CHEBI:177334; Evidence={ECO:0000269|PubMed:34261127, ECO:0000269|PubMed:34261128}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:68345; Evidence={ECO:0000269|... | null | null | null | null | FUNCTION: Nucleotidyltransferase that catalyzes the formation of cyclic GMP-AMP (3',2'-cGAMP) from ATP and GTP and plays a key role in antiviral innate immunity (PubMed:34261127, PubMed:34261128). Synthesizes 3',2'-cGAMP in a two-step reaction through production of the linear intermediate pppA(2'-5')pG (PubMed:34261127... | Drosophila melanogaster (Fruit fly) |
A1ZAB5 | CLU_DROME | MALETEAKNSNATATGDATATATKASGKAKENNNTAGGKKNLNPNSNQQNSNQNLVNGNGTAADGPAAKKKGKKNRNKSPTEPTTEAVLSNGHAEKPTVVDAVEDNADTNANVEKPQEGGAPDAEADGDDIDLDALQDIGITVNISSPGADLLCVQLSSMELVQEIHQLLMDREETCHRTCFSLQLDNVTLDNFAELKSINNLEQGSTIKVVEEPYTMREARIHVRHVRDLLKNLDPADAYNGIDCTSLTYLNTITQGDLLDKKRTRPDSVDCTPPEYVTPGVSDPPILPLHPNVKNAKGPQALKVLTTSAWNPPPGPRK... | null | null | asymmetric neuroblast division [GO:0055059]; intracellular distribution of mitochondria [GO:0048312]; mitochondrion localization [GO:0051646] | cytoplasm [GO:0005737]; endoplasmic reticulum [GO:0005783]; extrinsic component of mitochondrial outer membrane [GO:0031315]; Golgi apparatus [GO:0005794]; mitochondrion [GO:0005739]; mitotic spindle [GO:0072686]; outer mitochondrial membrane protein complex [GO:0098799] | mRNA binding [GO:0003729]; ribosome binding [GO:0043022] | PF13236;PF15044;PF12807;PF05303;PF13374;PF13424; | 3.30.2280.10;1.25.40.10; | CLU family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03013, ECO:0000269|PubMed:19638420}. | null | null | null | null | null | FUNCTION: mRNA-binding protein involved in proper cytoplasmic distribution of mitochondria. {ECO:0000255|HAMAP-Rule:MF_03013, ECO:0000269|PubMed:19638420}. | Drosophila melanogaster (Fruit fly) |
A1ZAJ2 | KIF1A_DROME | MSSVKVAVRVRPFNSREIARESKCIIEMAGATTAITNPKVPPNTSDSVKRFNFDYSYWSHDHHDADFSTQSMVYKDIGEEMLQHSFDGYNVCIFAYGQTGAGKSYTMMGRQEEQQEGIIPMICKDLFTRIQDTETDDLKYSVEVSYMEIYCERVRDLLNPKNKGNLRVREHPLLGPYVEDLSKLAVTDYQDIHDLIDEGNKARTVAATNMNETSSRSHAVFTIFFTQRRHDLMTNLTTEKVSKISLVDLAGSERADSTGAKGTRLKEGANINKSLTTLGKVISALAEVASKKKNTKKADFIPYRDSALTWLLRENLGGNS... | null | null | anterograde axonal transport [GO:0008089]; anterograde synaptic vesicle transport [GO:0048490]; axo-dendritic transport [GO:0008088]; axonal transport [GO:0098930]; cytoskeleton-dependent intracellular transport [GO:0030705]; filopodium assembly [GO:0046847]; larval locomotory behavior [GO:0008345]; microtubule-based m... | axon [GO:0030424]; axon cytoplasm [GO:1904115]; axon terminus [GO:0043679]; dendrite [GO:0030425]; kinesin complex [GO:0005871]; microtubule [GO:0005874]; microtubule associated complex [GO:0005875] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; GTP-dependent protein binding [GO:0030742]; microtubule binding [GO:0008017]; plus-end-directed microtubule motor activity [GO:0008574] | PF12473;PF00498;PF12423;PF00225;PF16183;PF00169; | 2.60.200.20;6.10.250.2520;3.40.850.10;2.30.29.30; | TRAFAC class myosin-kinesin ATPase superfamily, Kinesin family, Unc-104 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17643120}. Cell projection, axon {ECO:0000269|PubMed:30174114}. Note=Microtubule-associated. {ECO:0000269|PubMed:17643120}. | null | null | null | null | null | FUNCTION: Required for presynaptic maturation, has a role in axonal transport of dense-core vesicles carrying synaptic vesicle precursors, components required for the morphological transformation of axonal growth cones to mature boutons. {ECO:0000269|PubMed:17643120, ECO:0000269|PubMed:30174114}. | Drosophila melanogaster (Fruit fly) |
A1ZAU8 | PTRO_DROME | MDVETQEIRQARQRASVKWLLSKAFNNRVPDNLKEPFYRDHENQERLKPQIIVELGNATLYCQTLANLYSDPNYQSMNHWSIIQTLARKGVPVAESADMPITETVLIQTNPLRINAHMSVIESLMVLYAKEISSGDRVMAAIRRISGNNYQAPTGQSYEQALLGWISHACAALKKRIIKEVDAGLPDDNGSRLQTPDIPPVRDFQDLCDGICLALLISYYCPKVVPWTSVRINYLPAVEDSIHNILLVCNFSQKHLPYTVMHMTPEDVTYMRGSMKLNLVVLLTDLFNLFEIHPAKCVCYPGMDGQVPHSNSFGGGLNRR... | null | null | asymmetric protein localization involved in cell fate determination [GO:0045167]; centrosome duplication [GO:0051298]; cortical microtubule organization [GO:0043622]; cytoplasmic microtubule organization [GO:0031122]; establishment of mitotic spindle asymmetry [GO:0061867]; microtubule cytoskeleton organization [GO:000... | anterior cell cortex [GO:0061802]; centrosome [GO:0005813]; lateral cell cortex [GO:0097575]; microtubule [GO:0005874]; microtubule minus-end [GO:0036449]; midbody [GO:0030496]; mitotic spindle [GO:0072686]; perinuclear region of cytoplasm [GO:0048471]; spindle [GO:0005819]; subapical part of cell [GO:0120219] | calmodulin binding [GO:0005516]; microtubule binding [GO:0008017]; microtubule minus-end binding [GO:0051011]; spectrin binding [GO:0030507] | PF17095;PF11971;PF08683; | 3.10.20.360; | CAMSAP1 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, spindle pole body {ECO:0000269|PubMed:24100293}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:20946984}. Cytoplasm, cytoskeleton, microtubule organizing center {ECO:0000269|PubMed:32066907}. Cytoplasm... | null | null | null | null | null | FUNCTION: Key microtubule-organizing protein that specifically binds the minus-end of microtubules and regulates their dynamics and organization (PubMed:17412918, PubMed:20946984, PubMed:24100293, PubMed:26246606, PubMed:32066907). Involved in mitotic spindle assembly (PubMed:17412918, PubMed:26246606). Regulates micro... | Drosophila melanogaster (Fruit fly) |
A1ZAW0 | DCR2_DROME | MEDVEIKPRGYQLRLVDHLTKSNGIVYLPTGSGKTFVAILVLKRFSQDFDKPIESGGKRALFMCNTVELARQQAMAVRRCTNFKVGFYVGEQGVDDWTRGMWSDEIKKNQVLVGTAQVFLDMVTQTYVALSSLSVVIIDECHHGTGHHPFREFMRLFTIANQTKLPRVVGLTGVLIKGNEITNVATKLKELEITYRGNIITVSDTKEMENVMLYATKPTEVMVSFPHQEQVLTVTRLISAEIEKFYVSLDLMNIGVQPIRRSKSLQCLRDPSKKSFVKQLFNDFLYQMKEYGIYAASIAIISLIVEFDIKRRQAETLSVK... | 3.1.26.3 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:35768513}; COFACTOR: Name=ATP; Xref=ChEBI:CHEBI:30616; Evidence={ECO:0000269|PubMed:15066283, ECO:0000269|PubMed:15550672, ECO:0000269|PubMed:24488111, ECO:0000269|PubMed:29269422, ECO:0000269|PubMed:29550490, ECO:0000269|PubMed:35768513}; | apoptotic DNA fragmentation [GO:0006309]; cellular response to virus [GO:0098586]; defense response to virus [GO:0051607]; detection of virus [GO:0009597]; dosage compensation by hyperactivation of X chromosome [GO:0009047]; dsRNA transport [GO:0033227]; global gene silencing by mRNA cleavage [GO:0098795]; heterochroma... | cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; nucleus [GO:0005634]; perinuclear region of cytoplasm [GO:0048471]; RISC complex [GO:0016442]; RISC-loading complex [GO:0070578] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent activity, acting on RNA [GO:0008186]; bidentate ribonuclease III activity [GO:0016443]; deoxyribonuclease I activity [GO:0004530]; helicase activity [GO:0004386]; mRNA 3'-UTR binding [GO:0003730]; ribonuclease III activity [GO:0004525]; RNA b... | PF00270;PF03368;PF20931;PF00035;PF00271;PF02170;PF00636; | 3.30.160.20;3.30.160.380;3.40.50.300;2.170.260.10;1.10.1520.10; | Helicase family, Dicer subfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:26257286}. Cytoplasm {ECO:0000269|PubMed:26257286}. Cytoplasm, Cytoplasmic ribonucleoprotein granule {ECO:0000269|PubMed:26257286}. | CATALYTIC ACTIVITY: Reaction=Endonucleolytic cleavage to 5'-phosphomonoester.; EC=3.1.26.3; Evidence={ECO:0000269|PubMed:15066283, ECO:0000269|PubMed:21419681, ECO:0000269|PubMed:24488111, ECO:0000269|PubMed:27872309, ECO:0000269|PubMed:28416567, ECO:0000269|PubMed:28874570, ECO:0000269|PubMed:29269422, ECO:0000269|Pub... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=6 nM for 515 bp dsRNA {ECO:0000269|PubMed:21419681}; KM=2 nM for 515 bp dsRNA (in the presence of r2d2) {ECO:0000269|PubMed:21419681}; KM=0.4 nM for 515 bp dsRNA (in the presence of loqs isoform PD) {ECO:0000269|PubMed:21419681}; KM=14000 nM for ATP (in the presenc... | null | null | null | FUNCTION: Double-stranded RNA (dsRNA) endoribonuclease which cleaves endogenous (endo), exogenous (exo), and viral dsRNAs to produce short interfering RNAs (siRNAs) (PubMed:15066283, PubMed:16554838, PubMed:18953338, PubMed:19635780, PubMed:21419681, PubMed:23063653, PubMed:24009507, PubMed:24488111, PubMed:25891075, P... | Drosophila melanogaster (Fruit fly) |
A1ZAY1 | DLISH_DROME | MAFLCPVRMRRDKKKATNASIERDLPAVGVLGMGRITGSSSIETLVRVGIEKEHGLSPDSKMVVLHDFTPCVDDELEVKRGQLVNILYRENDWVYVIGQDSRQEGFIPFSYCAPCNTQLADLAVKKKLPREQCPEQPIEENIPLLGTDNKLDVLCDETLNPGSANSIENTLLVEPECTPFVKEPSGRCIVLYTFIARDENDLSVERGEFVTVLNREDPDWFWIMRSDGQEGFVPASFIYPADSVRVLQQQKATLNAMETILQQGQQGQQSQQQQQPQLGLGTDDLRYHGTELVMLYDYKAQAPDDLYLSVRRGDWIYADL... | null | null | establishment of epithelial cell planar polarity [GO:0090163]; establishment of planar polarity [GO:0001736]; negative regulation of hippo signaling [GO:0035331]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; protein localization involved in establishment of planar polar... | apical cortex [GO:0045179]; apicolateral plasma membrane [GO:0016327]; cilium [GO:0005929]; cytoplasm [GO:0005737]; subapical part of cell [GO:0120219] | cadherin binding [GO:0045296] | PF07653;PF14604; | 2.30.30.40; | null | PTM: Palmitoylated by app. {ECO:0000269|PubMed:27692068}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27692068}. Cytoplasm, cell cortex {ECO:0000269|PubMed:27692068}. Note=Low levels are found diffusely in the cytoplasm with high levels concentrated at the subapical cell cortex. {ECO:0000269|PubMed:27692068}. | null | null | null | null | null | FUNCTION: Required for the apical cell cortex localization, total cellular level and full activity of dachs. {ECO:0000269|PubMed:27692068}. | Drosophila melanogaster (Fruit fly) |
A1ZBD6 | MCTP_DROME | MSRIQYVDQVDQVELDQQQQPGSSSTVSGSTPPLQISPHGSPSLQQSQRLGKHLSKSASELNGHDCHLSESPHISPKRAKSAVAQQLAGVSSGGVASGVGVLQKTHGFFNNLRHRWSRAKSKDRLGRKSPSDFLEESTDYAADYSSEGSSVTHSPRHRSTTIGGSPLAREFRATAKMAQVIQRFGGSMEGRIDEHPENGSAGCSPPELSTQQQLEALQANELRRKREAQLRQFVFFQLRVHLKSGSDLVAMDKNGLSDPYVKFKVGGRLLHKSRTIHRDLNPVWDEVFIVPIEDPFQPIIVKVFDYDWGLQDDFMGSAKL... | null | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041, ECO:0000269|PubMed:28485711}; Note=Binds Ca(2+) via the C2 domains in absence of phospholipids. {ECO:0000269|PubMed:28485711}; | regulation of neuronal synaptic plasticity [GO:0048168]; regulation of neurotransmitter secretion [GO:0046928]; synaptic vesicle exocytosis [GO:0016079] | endoplasmic reticulum membrane [GO:0005789]; membrane [GO:0016020]; neuromuscular junction [GO:0031594]; synaptic vesicle membrane [GO:0030672] | calcium ion binding [GO:0005509] | PF00168;PF08372; | 2.60.40.150; | null | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:28485711}; Multi-pass membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Calcium sensor which is essential for the stabilization of normal baseline neurotransmitter release and for the induction and long-term maintenance of presynaptic homeostatic plasticity (PubMed:28485711). {ECO:0000269|PubMed:28485711}. | Drosophila melanogaster (Fruit fly) |
A2A259 | PK2L1_MOUSE | MNSMESPKNQELQTLGNRAWDNPAYSDPPSPNRTLRICTVSSVALPETQPKKPEVRCQEKTQRTLVSSCCLHICRSIRGLWGTTLTENTAENRELYVKTTLRELVVYIVFLVDICLLTYGMTSSSAYYYTKVMSELFLHTPSDSGVSFQTISSMSDFWDFAQGPLLDSLYWTKWYNNQSLGRGSHSFIYYENLLLGAPRLRQLRVRNDSCVVHEDFREDILNCYDVYSPDKEDQLPFGPQNGTAWTYHSQNELGGSSHWGRLTSYSGGGYYLDLPGSRQASAEALQGLQEGLWLDRGTRVVFIDFSVYNANINLFCILRL... | null | null | cellular response to acidic pH [GO:0071468]; cellular response to pH [GO:0071467]; detection of chemical stimulus involved in sensory perception of sour taste [GO:0001581]; detection of chemical stimulus involved in sensory perception of taste [GO:0050912]; detection of mechanical stimulus [GO:0050982]; inorganic catio... | actin cytoskeleton [GO:0015629]; calcium channel complex [GO:0034704]; cation channel complex [GO:0034703]; ciliary membrane [GO:0060170]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; membrane [GO:0016020]; non-motile cilium [GO:0097730]; plasma membrane [GO:0005886]; rece... | calcium channel activity [GO:0005262]; calcium ion binding [GO:0005509]; calcium-activated potassium channel activity [GO:0015269]; identical protein binding [GO:0042802]; monoatomic cation channel activity [GO:0005261]; muscle alpha-actinin binding [GO:0051371]; sodium channel activity [GO:0005272]; transmembrane tran... | PF18109;PF08016;PF20519; | 1.10.287.70;1.20.5.340;1.10.238.10;1.20.120.350; | Polycystin family | PTM: Palmitoylation is important for expression at the cell membrane and for channel activity. {ECO:0000250|UniProtKB:Q9P0L9}. | SUBCELLULAR LOCATION: Cell projection, cilium membrane {ECO:0000269|PubMed:24336288, ECO:0000269|PubMed:24336289}; Multi-pass membrane protein {ECO:0000269|PubMed:29567962}. Cell membrane {ECO:0000269|PubMed:15548533, ECO:0000269|PubMed:16891422, ECO:0000269|PubMed:18535624, ECO:0000269|PubMed:19464260, ECO:0000269|Pub... | null | null | null | null | null | FUNCTION: Pore-forming subunit of a heteromeric, non-selective cation channel that is permeable to Ca(2+) (PubMed:15548533, PubMed:16891422, PubMed:19464260, PubMed:20538909, PubMed:21185261, PubMed:22420714, PubMed:25820328, PubMed:28904867, PubMed:29567962). Pore-forming subunit of a calcium-permeant ion channel form... | Mus musculus (Mouse) |
A2A288 | ZC12D_HUMAN | MEHPSKMEFFQKLGYDREDVLRVLGKLGEGALVNDVLQELIRTGSRPGALEHPAAPRLVPRGSCGVPDSAQRGPGTALEEDFRTLASSLRPIVIDGSNVAMSHGNKETFSCRGIKLAVDWFRDRGHTYIKVFVPSWRKDPPRADTPIREQHVLAELERQAVLVYTPSRKVHGKRLVCYDDRYIVKVAYEQDGVIVSNDNYRDLQSENPEWKWFIEQRLLMFSFVNDRFMPPDDPLGRHGPSLSNFLSRKPKPPEPSWQHCPYGKKCTYGIKCKFYHPERPHHAQLAVADELRAKTGARPGAGAEEQRPPRAPGGSAGARA... | 3.1.-.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305}; | 3'-UTR-mediated mRNA destabilization [GO:0061158]; negative regulation of cell growth [GO:0030308]; negative regulation of G1/S transition of mitotic cell cycle [GO:2000134] | cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; P-body [GO:0000932] | metal ion binding [GO:0046872]; mRNA binding [GO:0003729]; RNA endonuclease activity [GO:0004521] | PF11977;PF18039; | 3.40.50.11980; | ZC3H12 family | null | SUBCELLULAR LOCATION: Cytoplasm, P-body {ECO:0000269|PubMed:26134560}. Note=Colocalizes with ZC3H12A in GW bodies (GWBs) (PubMed:26134560). {ECO:0000269|PubMed:26134560}.; SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm. Note=Localized as discrete granules. Colocalized with mRNA-processing body markers, AGO2 and DCP1A, bu... | null | null | null | null | null | FUNCTION: May regulate cell growth likely by suppressing RB1 phosphorylation (PubMed:19531561). May function as RNase and regulate the levels of target RNA species (Potential). In association with ZC3H12A enhances the degradation of interleukin IL-6 mRNA level in activated macrophages (PubMed:26134560). Serve as a tumo... | Homo sapiens (Human) |
A2A2Y4 | FRMD3_HUMAN | MFASCHCVPRGRRTMKMIHFRSSSVKSLSQEMRCTIRLLDDSEISCHIQRETKGQFLIDHICNYYSLLEKDYFGIRYVDPEKQRHWLEPNKSIFKQMKTHPPYTMCFRVKFYPHEPLKIKEELTRYLLYLQIKRDIFHGRLLCSFSDAAYLGACIVQAELGDYDPDEHPENYISEFEIFPKQSQKLERKIVEIHKNELRGQSPPVAEFNLLLKAHTLETYGVDPHPCKDSTGTTTFLGFTAAGFVVFQGNKRIHLIKWPDVCKLKFEGKTFYVIGTQKEKKAMLAFHTSTPAACKHLWKCGVENQAFYKYAKSSQIKTVS... | null | null | actomyosin structure organization [GO:0031032] | cytoskeleton [GO:0005856]; membrane [GO:0016020] | cytoskeletal protein binding [GO:0008092] | PF08736;PF09380;PF00373;PF09379; | 1.20.80.10;2.30.29.30; | null | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. | null | null | null | null | null | FUNCTION: Putative tumor suppressor gene that may be implicated in the origin and progression of lung cancer. {ECO:0000269|PubMed:17260017}. | Homo sapiens (Human) |
A2A432 | CUL4B_MOUSE | MSRSTRSKERRENDTDSEDNSSETSNQERRRCRQGPPRPPYPPLLPPVFPPPTPPPQVRRTRGLQDLGAMKSVCPGTSGFSSPNPSAASAAAQEVRSATDGNTSTTPPTSAKKRKLNSSSSSSNSSNEREDFDSTSSSSTPPQPRDSASPSTSSFCLGVPVATSSHVPIQKKLRFEDTLEFVGIDTKMAEESSSSSSSSSPTAATSQQQQQQQLKTKSILISSVASVHHANGLAKSSTAVSSFANSKPGSAKKLVIKNFKDKPKLPENYTDETWQKLKEAVEAIQNSTSIKYNLEELYQAVENLCSHKISANLYKQLRQI... | null | null | astrocyte differentiation [GO:0048708]; cell cycle [GO:0007049]; cellular response to UV [GO:0034644]; DNA damage response [GO:0006974]; gene expression [GO:0010467]; neuron projection development [GO:0031175]; positive regulation of G1/S transition of mitotic cell cycle [GO:1900087]; positive regulation of protein cat... | Cul4A-RING E3 ubiquitin ligase complex [GO:0031464]; Cul4B-RING E3 ubiquitin ligase complex [GO:0031465]; cytosol [GO:0005829]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | damaged DNA binding [GO:0003684]; ubiquitin protein ligase binding [GO:0031625] | PF00888;PF10557; | 1.20.1310.10;1.10.10.10; | Cullin family | PTM: Neddylated. Deneddylated via its interaction with the COP9 signalosome (CSN) complex (By similarity). {ECO:0000250|UniProtKB:Q13620}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24357321}. Nucleus {ECO:0000269|PubMed:24357321}. Note=More concentrated in nuclei than in cytoplasm in germinal vesicle (GV) stage oocytes, zygotes and the 2-cell stage, but distributed in the cytoplasm at the MII-stage oocytes. {ECO:0000269|PubMed:24357321}. | null | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:35197566}. | null | null | FUNCTION: Core component of multiple cullin-RING-based E3 ubiquitin-protein ligase complexes which mediate the ubiquitination and subsequent proteasomal degradation of target proteins (PubMed:35197566). The functional specificity of the E3 ubiquitin-protein ligase complex depends on the variable substrate recognition s... | Mus musculus (Mouse) |
A2A5K6 | ZN335_MOUSE | MEENEVESSSDAAPRPGQPEEPSESGLGVCTSEAVSADSSDAATVPGLTEADDSGVGQSSDGGNHSVEEVSESISTDPLPHGCLPDSSSVSRGPVAEMPGGPPALVHSSVLPDPSMLVSDCTASSSDLGSAIDKIIESTIGPDLIQSCITVTSGEEGGAETTQYLILQGPDDGAPMASSMSTSTLANSLAAIEALADGPTSTSACLEPPEEPQGDPSSVAQQPPAPVTEELDLQSLEAMMEVVVVQQFKCKMCQYRSSTKATLLRHMRERHFRPALAAAAAATGKRGRVRKWGTSTKTTEEDRPEEEEEDDDIVDAGAID... | null | null | brain development [GO:0007420]; brain morphogenesis [GO:0048854]; cerebral cortex neuron differentiation [GO:0021895]; epigenetic regulation of gene expression [GO:0040029]; in utero embryonic development [GO:0001701]; neuron projection morphogenesis [GO:0048812]; positive regulation of lymphocyte proliferation [GO:005... | histone methyltransferase complex [GO:0035097]; nucleus [GO:0005634] | histone methyltransferase binding [GO:1990226]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; transcription cis-regulatory region binding [GO:0000976] | PF00096;PF13912;PF13909; | 3.30.160.60; | Krueppel C2H2-type zinc-finger protein family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23178126}. | null | null | null | null | null | FUNCTION: Component or associated component of some histone methyltransferase complexes may regulate transcription through recruitment of those complexes on gene promoters (By similarity). Enhances ligand-dependent transcriptional activation by nuclear hormone receptors (By similarity). Plays an important role in neura... | Mus musculus (Mouse) |
A2A5N8 | LMBL1_MOUSE | MEGHTDMEILRTVKGSSTGEVNVHLVARDSAGPHPQLPTTAFIIPTNAATLGLPSTALDVPYPREPVHVGALERVAGSEPVTATILPQLSTGTGTNSTVRLLDWTGVSAPLPGSGMRFRINEYAPLNMIGVERPRSPEQRHEGGMARRDAGIQHPDVHQDRQDITSLEPPVDASSCKCQACGPQQSSGLDVGSSGDRCSQPFQKRSVIVENSGCTIASELLKPMKKRKHKEYQSPSEESEPEAVKQGEGKDAEREPTPSTPENEEWSRSQLVSSEKKDGWSWESYLEEQKAVTAPVSLFQDSQAVTHNKNGFKLGMKLEG... | null | null | chromatin organization [GO:0006325]; epigenetic regulation of gene expression [GO:0040029]; hemopoiesis [GO:0030097]; heterochromatin formation [GO:0031507]; negative regulation of DNA-templated transcription [GO:0045892]; regulation of megakaryocyte differentiation [GO:0045652]; regulation of mitotic nuclear division ... | chromatin [GO:0000785]; chromatin lock complex [GO:0061793]; condensed chromosome [GO:0000793]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | chromatin binding [GO:0003682]; histone binding [GO:0042393]; methylated histone binding [GO:0035064]; nucleosome binding [GO:0031491]; zinc ion binding [GO:0008270] | PF02820;PF00536;PF01530; | 2.30.30.140;4.10.320.30;1.10.150.50; | null | PTM: Ubiquitinated in a VCP/p97-dependent way following DNA damage, leading to its removal from DNA damage sites, promoting accessibility of H4K20me2 mark for DNA repair protein TP53BP1, which is then recruited to DNA damage sites. {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Note=Excluded from the nucleolus. Does not colocalize with the PcG protein BMI1, suggesting that these two proteins do not belong to the same complex (By similarity). {ECO:0000250}. | null | null | null | null | null | FUNCTION: Polycomb group (PcG) protein that specifically recognizes and binds mono- and dimethyllysine residues on target proteins, therey acting as a 'reader' of a network of post-translational modifications. PcG proteins maintain the transcriptionally repressive state of genes: acts as a chromatin compaction factor b... | Mus musculus (Mouse) |
A2A5R2 | BIG2_MOUSE | MQESQTKSMFVSRALEKILADKEVKRPQHSQLRRACQVALDEIKAELEKQRLGAAAPPKANFIEADKYFLPFELACQSKSPRVVSTSLDCLQKLIAYGHITGNAPDSGAPGKRLIDRIVETICNCFQGPQTDEGVQLQIIKALLTAVTSPHIEIHEGTILQTVRTCYNIYLASKNLINQTTAKATLTQMLNVIFTRMENQVLQEARELEKPMQSKPQSPVIQATAGSPKFSRLKQSQAQSKPTTPEKAELPNGDHAQSGLGKVSLENGEAPRERGSPVSGRAEPSRGTDSGAQEVVKDILEDVVTSAVKEAAEKHGLPEP... | null | null | endomembrane system organization [GO:0010256]; endosome organization [GO:0007032]; exocytosis [GO:0006887]; Golgi to plasma membrane transport [GO:0006893]; intracellular signal transduction [GO:0035556]; positive regulation of tumor necrosis factor production [GO:0032760]; protein transport [GO:0015031]; receptor recy... | asymmetric synapse [GO:0032279]; axonemal microtubule [GO:0005879]; centrosome [GO:0005813]; cytoplasmic vesicle [GO:0031410]; cytosol [GO:0005829]; dendritic spine [GO:0043197]; GABA-ergic synapse [GO:0098982]; glutamatergic synapse [GO:0098978]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; microtubule organizi... | GABA receptor binding [GO:0050811]; guanyl-nucleotide exchange factor activity [GO:0005085]; myosin binding [GO:0017022]; protein kinase A regulatory subunit binding [GO:0034237] | PF20252;PF16213;PF01369;PF09324;PF12783; | 1.10.220.20;1.10.1000.11; | null | PTM: In vitro phosphorylated by PKA reducing its GEF activity and dephosphorylated by phosphatase PP1. {ECO:0000250}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Membrane {ECO:0000250}. Golgi apparatus {ECO:0000250}. Cytoplasm, perinuclear region {ECO:0000250}. Golgi apparatus, trans-Golgi network {ECO:0000250}. Endosome {ECO:0000250}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250}. Cell projection... | null | null | null | null | null | FUNCTION: Promotes guanine-nucleotide exchange on ARF1 and ARF3 and to a lower extent on ARF5 and ARF6. Promotes the activation of ARF1/ARF5/ARF6 through replacement of GDP with GTP. Involved in the regulation of Golgi vesicular transport. Required for the integrity of the endosomal compartment. Involved in trafficking... | Mus musculus (Mouse) |
A2A5Z6 | SMUF2_MOUSE | MSNPGGRRNGPVKLRLTVLCAKNLVKKDFFRLPDPFAKVVVDGSGQCHSTDTVKNTLDPKWNQHYDLYIGKSDSVTISVWNHKKIHKKQGAGFLGCVRLLSNAINRLKDTGYQRLDLCKLGPNDNDTVRGQIVVSLQSRDRIGTGGQVVDCSRLFDNDLPDGWEERRTASGRIQYLNHITRTTQWERPTRPASEYSSPGRPLSCFVDENTPITGTNGATCGHSSDPRLAERRVRSQRHRNYMSRTHLHTPPDLPEGYEQRTTQQGQVYFLHTQTGVSTWHDPRVPRDLSNINCEELGPLPPGWEIRNTATGRVYFVDHNN... | 2.3.2.26 | null | negative regulation of BMP signaling pathway [GO:0030514]; negative regulation of transforming growth factor beta receptor signaling pathway [GO:0030512]; positive regulation of trophoblast cell migration [GO:1901165]; proteasome-mediated ubiquitin-dependent protein catabolic process [GO:0043161]; protein polyubiquitin... | cytoplasm [GO:0005737]; cytosol [GO:0005829]; membrane raft [GO:0045121]; nuclear speck [GO:0016607]; plasma membrane [GO:0005886]; ubiquitin ligase complex [GO:0000151] | identical protein binding [GO:0042802]; SMAD binding [GO:0046332]; transforming growth factor beta receptor binding [GO:0005160]; ubiquitin protein ligase activity [GO:0061630] | PF00168;PF00632;PF00397; | 2.20.70.10;2.60.40.150;3.30.2160.10;3.30.2410.10;3.90.1750.10; | null | PTM: Auto-ubiquitinated and ubiquitinated in the presence of RNF11 and UBE2D1 (By similarity). Ubiquitinated by the SCF(FBXL15) complex and TTC3, leading to its degradation by the proteasome (By similarity). 'Lys-48'-linked polyubiquitination mediated by TRAF4 at Lys-119 leads to SMURF2 proteasomal degradation (By simi... | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9HAU4}. Cytoplasm {ECO:0000250|UniProtKB:Q9HAU4}. Cell membrane {ECO:0000250|UniProtKB:Q9HAU4}. Membrane raft {ECO:0000250|UniProtKB:Q9HAU4}. Note=Cytoplasmic in the presence of SMAD7. Colocalizes with CAV1, SMAD7 and TGF-beta receptor in membrane rafts. {ECO:000025... | 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=2.3.2.26; Evidence={ECO:0000250|UniProtKB:Q9HAU4}; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfers the ubiquitin to targeted substrates. Interacts with SMAD7 to trigger SMAD7-mediated transforming growth factor beta/TGF-beta receptor ubiquitin-dependent degradat... | Mus musculus (Mouse) |
A2A6C4 | SPP2C_MOUSE | MACLGSLHPLGSLLLLFLLLLLSPEARGEYGLVRVVSKNWSKDYCVLYSSDYVNLPRDLHHAPLLSLHDGTKTPWCPDEDSFHQAQDSSPRQRPLHQTTTMVTRGNCSFYAKGWLAQDQGAQGLLIVSRARNQQCSDTISKPQDPSKPWPALTIPVAVLRYTDMLDIVSHTYGDTDVRVAMFAPLEPVTDYNMAIIFILAVGTVAAGGYWAGLMEANKLQRRQAQRGGGLGGHNQQQTVAAERSQRAWEDDDFEDAPMDFTPAMTGAVVTMSCSIMILLYFFYDCFVYVMIGIFSLGASTGLYSCLAPILCHLPLWRYQW... | 3.4.23.- | null | acrosome assembly [GO:0001675]; intracellular calcium ion homeostasis [GO:0006874]; membrane protein intracellular domain proteolysis [GO:0031293]; membrane protein proteolysis [GO:0033619] | cytoplasmic side of endoplasmic reticulum membrane [GO:0098554]; endoplasmic reticulum membrane [GO:0005789]; Golgi-associated vesicle membrane [GO:0030660]; lumenal side of endoplasmic reticulum membrane [GO:0098553]; lysosomal membrane [GO:0005765] | aspartic endopeptidase activity, intramembrane cleaving [GO:0042500]; molecular adaptor activity [GO:0060090]; protein homodimerization activity [GO:0042803] | PF02225;PF04258; | 3.50.30.30; | Peptidase A22B family | PTM: Glycosylated. {ECO:0000250|UniProtKB:P49768}. | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:30733280, ECO:0000269|PubMed:30733281, ECO:0000269|PubMed:35960805}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q8IUH8}; Lumenal side {ECO:0000269|PubMed:30733280}. | null | null | null | null | null | FUNCTION: Sperm-specific intramembrane-cleaving aspartic protease (I-CLiP) that cleaves distinct tail-anchored proteins and SNARE proteins (PubMed:30733280, PubMed:30733281, PubMed:35960805). In elongated spermatids, modulates intracellular Ca(2+) homeostasis by controlling PLN abundance through proteolytic cleavage (P... | Mus musculus (Mouse) |
A2A6Q5 | CDC27_MOUSE | MTVLQEPVQAAIWQALNHYAYRDAVFLAERLYAEVHSEEALFLLATCYYRSGKAYKAYRLLKGHSCTTPQCKYLLAKCCVDLSKLAEGEQILSGGVFNKQKSHDDLVTEFGDSACFTLSLLGHVYCKTDRLAKGSECYQKSLSLNPFLWSPFESLCEIGEKPDPDQTFKLTSLQNFSSCLPNTCTTLVSNHSLSHRQPETVLTETPQDTIELNRLNLESSNSKYSLNTDSSVSYIDSTVISPDNVPLGPGTAILSKQVQNKPKTGRSLLGGPTALSPLTPSFGILPLETPSPGDGSYLQNYTNTPSVIDVAPTGAPTKKS... | null | null | anaphase-promoting complex-dependent catabolic process [GO:0031145]; cell division [GO:0051301]; metaphase/anaphase transition of mitotic cell cycle [GO:0007091]; protein K11-linked ubiquitination [GO:0070979]; protein ubiquitination [GO:0016567] | anaphase-promoting complex [GO:0005680]; centrosome [GO:0005813]; cytoplasm [GO:0005737]; mitotic spindle [GO:0072686]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle [GO:0005819] | protein phosphatase binding [GO:0019903] | PF12895;PF00515;PF13181; | 1.25.40.10; | APC3/CDC27 family | PTM: Phosphorylated. Phosphorylation on Ser-427 and Thr-447 occurs specifically during mitosis (By similarity). {ECO:0000250}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:P30260}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:P30260}. | null | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: Component of the anaphase promoting complex/cyclosome (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls progression through mitosis and the G1 phase of the cell cycle. The APC/C complex acts by mediating ubiquitination and subsequent degradation of target proteins: it mainly mediates the forma... | Mus musculus (Mouse) |
A2A7Q9 | RN19B_MOUSE | MGSEKDSESPRSTSLHAAAPDPKCRSGGRRRRLTFHSVFSASARGRRARTKPQAEPPPPAAPPPPPPPAPAPVEAQAPPVEALPSEPAAEAEAEAVAAGPEEDEAAEGGGAEEVECPLCLVRLPPERAPRLLSCPHRSCRDCLRHYLRLEISESRVPISCPECSERLNPHDIRLLLADPPLMHKYEEFMLRRYLASDPDCRWCPAPDCGYAVIAYGCASCPKLTCEREGCQTEFCYHCKQIWHPNQTCDMARQQRAQTLRVRTKHTSGLSYGQESGPADDIKPCPRCSAYIIKMNDGSCNHMTCAVCGCEFCWLCMKEIS... | 2.3.2.31 | null | adaptive immune response [GO:0002250]; natural killer cell mediated cytotoxicity [GO:0042267]; positive regulation of proteasomal ubiquitin-dependent protein catabolic process [GO:0032436]; protein autoubiquitination [GO:0051865]; protein polyubiquitination [GO:0000209]; ubiquitin-dependent protein catabolic process [G... | cytolytic granule [GO:0044194]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; ubiquitin ligase complex [GO:0000151] | ubiquitin binding [GO:0043130]; ubiquitin conjugating enzyme binding [GO:0031624]; ubiquitin protein ligase activity [GO:0061630]; zinc ion binding [GO:0008270] | PF01485; | 1.20.120.1750;2.20.25.20;3.30.40.10; | RBR family, RNF19 subfamily | null | SUBCELLULAR LOCATION: Cytoplasmic granule membrane {ECO:0000250|UniProtKB:Q6ZMZ0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q6ZMZ0}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q6ZMZ0}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q6ZMZ0}. | 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:O60260}; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: E3 ubiquitin-protein ligase which accepts ubiquitin from E2 ubiquitin-conjugating enzymes UBE2L3 and UBE2L6 in the form of a thioester and then directly transfers the ubiquitin to targeted substrates, such as UCKL1. Involved in the cytolytic activity of natural killer cells and cytotoxic T-cells. Protects aga... | Mus musculus (Mouse) |
A2A825 | CPLN2_MOUSE | MARPPMHGSVIVPDWHETVEGKEYLACILRKNRRREFGLLERPVLPPSVVIDTASYKIFVSGKSGVGKTALVAKLAGLEVPIVHHETTGIQTTVVFWPAKLKASDCVVMFRFEFWDCGESALKKFDHMLPACKENADAFLFLFSFTDRASFEDLPGQLTRVAGEAPGLVKIVIGSKFDQYMHTDVPARDLTAFRQAWELPLFRVKSVPGRRLADGRTLDGRAGLADTAHVLNGLAEQLWHQDQVAAGLLPSSPESAPG | null | null | axoneme assembly [GO:0035082]; cilium assembly [GO:0060271]; cranial skeletal system development [GO:1904888]; endocardial cushion fusion [GO:0003274]; exocytosis [GO:0006887]; limb development [GO:0060173]; protein localization [GO:0008104]; protein processing [GO:0016485]; protein transport [GO:0015031]; regulation o... | centriole [GO:0005814]; ciliary basal body [GO:0036064]; ciliary base [GO:0097546]; ciliary transition zone [GO:0035869]; cytoplasm [GO:0005737] | GTP binding [GO:0005525]; GTPase activity [GO:0003924] | PF00071; | 3.40.50.300; | Small GTPase superfamily, Rab family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000250|UniProtKB:Q6GNL4}. | null | null | null | null | null | FUNCTION: Potential effector of the planar cell polarity signaling pathway. Plays a role in targeted membrane trafficking most probably at the level of vesicle fusion with membranes. Involved in cilium biogenesis by regulating the transport of cargo proteins to the basal body and to the apical tips of cilia. More gener... | Mus musculus (Mouse) |
A2A863 | ITB4_MOUSE | MAGPCCSPWVKLLLLAAMLSASLPGDLANRCKKAQVKSCTECIRVDKSCAYCTDELFKERRCNTQAELLAAGCRGESILVMESSLEITENTQIDTSLHRSQVSPQGLQVRLRPGEERSFVFQVFEPLESPVDLYILMDFSNSMSDDLDNLKQMGQNLAKILRQLTSDYTIGFGKFVDKVSVPQTDMRPEKLKEPWPNSDPPFSFKNVISLTENVEEFWNKLQGERISGNLDAPEGGFDAILQTAVCTRDIGWRADSTHLLVFSTESAFHYEADGANVLAGIMNRNDEKCHLDASGAYTQYKTQDYPSVPTLVRLLAKHNI... | null | null | autophagy [GO:0006914]; cell adhesion [GO:0007155]; cell adhesion mediated by integrin [GO:0033627]; cell motility [GO:0048870]; cell-cell adhesion [GO:0098609]; cell-matrix adhesion [GO:0007160]; filopodium assembly [GO:0046847]; hemidesmosome assembly [GO:0031581]; integrin-mediated signaling pathway [GO:0007229]; me... | basal plasma membrane [GO:0009925]; basement membrane [GO:0005604]; cell cortex [GO:0005938]; cell leading edge [GO:0031252]; cell surface [GO:0009986]; focal adhesion [GO:0005925]; glutamatergic synapse [GO:0098978]; hemidesmosome [GO:0030056]; integrin complex [GO:0008305]; nuclear membrane [GO:0031965]; nucleolus [G... | G protein-coupled receptor binding [GO:0001664]; insulin-like growth factor I binding [GO:0031994]; integrin binding [GO:0005178]; metal ion binding [GO:0046872]; neuregulin binding [GO:0038132] | PF03160;PF00041;PF18372;PF07965;PF00362;PF17205; | 2.60.40.2030;4.10.1240.30;2.60.40.10;2.10.25.10;3.30.1680.10;2.60.40.1510;3.40.50.410; | Integrin beta chain family | PTM: Palmitoylated by DHHC3 at several cysteines of the membrane-proximal region, enhancing stability and cell surface expression. Palmitoylation also promotes secondary association with tertaspanins (By similarity). {ECO:0000250|UniProtKB:P16144}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Single-pass type I membrane protein {ECO:0000250}. Cell membrane {ECO:0000250}; Lipid-anchor {ECO:0000250}. Cell junction, hemidesmosome {ECO:0000250}. Note=Colocalizes with DST at the leading edge of migrating keratinocytes. {ECO:0000250}. | null | null | null | null | null | FUNCTION: Integrin alpha-6/beta-4 is a receptor for laminin. It plays a critical structural role in the hemidesmosome of epithelial cells. Is required for the regulation of keratinocyte polarity and motility. ITGA6:ITGB4 binds to NRG1 (via EGF domain) and this binding is essential for NRG1-ERBB signaling. ITGA6:ITGB4 b... | Mus musculus (Mouse) |
A2A884 | ZEP3_MOUSE | MDPDQSIKGTKKADGSPRKRLTKGEAIQTSVSSSAPYPGSGTTAPSESATQELLATQPFSGPSQEKTGQQQKPARRPSIEASVHISQLPQHPLTPAFMSPGKPEHLLEGSTWQLVDPMRPGPSGSFVAPGLHPQSQLLPSHASILPPEELPGIPKVFVPRPSQVSLKPAEEAHKKERKPQKPGKYICQYCSRPCAKPSVLQKHIRSHTGERPYPCGPCGFSFKTKSNLYKHRKSHAHRIKAGLASGSSSEMYPPGLEMERIPGEEFEEPTEGESTDSEEETGAASGPSTDVLPKPKHPLLSSSLYSSGSHGSSQERCSLS... | null | null | positive regulation of DNA-templated transcription [GO:0045893]; regulation of transcription by RNA polymerase II [GO:0006357]; skeletal muscle cell differentiation [GO:0035914] | cytosol [GO:0005829]; nucleus [GO:0005634] | DNA binding [GO:0003677]; DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978] | PF00096; | 3.30.160.60; | null | PTM: Phosphorylated on threonine and serine residues. Phosphorylation by cyclin-dependent kinase CDK1 decreases HIVEP3 DNA binding affinity, and by epidermal growth factor receptor kinase increases its DNA binding affinity. {ECO:0000269|PubMed:9862992}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11804591}. Nucleus {ECO:0000269|PubMed:11804591}. | null | null | null | null | null | FUNCTION: Plays a role of transcription factor; binds to recognition signal sequences (Rss heptamer) for somatic recombination of immunoglobulin and T-cell receptor gene segments; Binds also to the kappa-B motif of gene such as S100A4, involved in cell progression and differentiation. Kappa-B motif is a gene regulatory... | Mus musculus (Mouse) |
A2A891 | CMTA1_MOUSE | MWRAEGKWLPKTSRKSVSQSVFCGTSTYCVLNTVPPIEDDHGNSNSSHVKIFLPKKLLECLPKCSSLPKERHRWNTNEEIAAYLITFEKHEEWLTTSPKTRPQNGSMILYNRKKVKYRKDGYCWKKRKDGKTTREDHMKLKVQGVECLYGCYVHSSIIPTFHRRCYWLLQNPDIVLVHYLNVPAIEDCGKPCGPILCSINTDKKEWAKWTKEELIGQLKPMFHGIKWTCSNGNSSSGFSVEQLVQQILDSHQTKPQPRTHNCLCTGSLGAGSSVHHKCNSAKHRIISPKVEPRAGGYGGHSEVQHNDVSEGKHEPSHGRS... | null | null | neuromuscular process controlling balance [GO:0050885]; positive regulation of calcineurin-NFAT signaling cascade [GO:0070886]; positive regulation of protein dephosphorylation [GO:0035307]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of transcription by RNA polymerase II [GO:0006... | cytosol [GO:0005829]; nucleolus [GO:0005730]; nucleus [GO:0005634] | double-stranded DNA binding [GO:0003690]; sequence-specific DNA binding [GO:0043565]; transcription coregulator activity [GO:0003712] | PF12796;PF03859;PF01833; | 1.20.5.190;1.25.40.20;2.60.40.10; | CAMTA family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9Y6Y1, ECO:0000255|PROSITE-ProRule:PRU00767}. Cytoplasm {ECO:0000250|UniProtKB:Q9Y6Y1}. | null | null | null | null | null | FUNCTION: Transcriptional activator. {ECO:0000250}. | Mus musculus (Mouse) |
A2A8L1 | CHD5_MOUSE | MRGPLGTEEELPRLFAEEMENEEEMSEEEDGGLEGFEDFFPAEPVSLPKKKPKKLKESKSSKGKRKKKEGSNDEMSDNEEDLEEKSESEGSDYSPTKKKKKKLKEKKEKKEKKEKRKKRGEDEDDNDDGGLKEPKSSGQLMAEWGLDDVDYLFSEDDYHTLTNYKAFSQFLRPLIAKKNPKIPMSKMMTVLGAKWREFSANNPFKGSSAAAAAAAVAAAVETVTIAPPLAISPQQVPQTLPIRKAKTKEGKGPGVRKKNKGAKDSKKKGRGKRVAGLKFRFGGISKRKKGSSSEEDEREDSDLDNASIHSSSVRSECSAA... | 3.6.4.12 | null | cerebral cortex neuron differentiation [GO:0021895]; chromatin remodeling [GO:0006338]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of transcription by RNA polymerase II [GO:0000122]; positive regulation of signal transduction by p53 class mediator [GO:1901798]; regulation of ... | chromatin [GO:0000785]; heterochromatin [GO:0000792]; nucleus [GO:0005634]; NuRD complex [GO:0016581] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent chromatin remodeler activity [GO:0140658]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; H3K27me3 modified histone binding [GO:0061628]; helicase activity [GO:0004386]; histone binding [GO:0042393]; histone deacetylase binding [GO... | PF08074;PF06461;PF08073;PF00385;PF06465;PF00271;PF00628;PF00176; | 2.40.50.40;1.10.10.60;3.40.50.300;3.40.50.10810;3.30.40.10; | SNF2/RAD54 helicase family | PTM: Methylated at Gln-1392 by N6AMT1. {ECO:0000250|UniProtKB:Q8TDI0}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23318260, ECO:0000269|PubMed:23948251}. Chromosome {ECO:0000269|PubMed:27806305}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; | null | null | null | null | FUNCTION: Chromatin-remodeling protein that binds DNA through histones and regulates gene transcription (PubMed:23318260). May specifically recognize and bind trimethylated 'Lys-27' (H3K27me3) and non-methylated 'Lys-4' of histone H3 (PubMed:23318260, PubMed:23948251). Acts as a component of the histone deacetylase NuR... | Mus musculus (Mouse) |
A2A8L5 | PTPRF_MOUSE | MAPEPAPGRRMVPLVPALVMLGLMAGAHGDSKPVFVKVPEDQTGLSGGVASFVCQATGEPKPRITWMKKGKKVSSQRFEVIEFDDGAGSVLRIQPLRVQRDEAIYECTATNSLGEINTSAKLSVLEEDQLPSGFPTIDMGPQLKVVEKGRTATMLCAAGGNPDPEISWFKDFLPVDPAASNGRIKQLRSGALQIESSEESDQGKYECVATNSAGTRYSAPANLYVRVRRVAPRFSIPPSSQEVMPGGSVNLTCVAVGAPMPYVKWMMGAEELTKEDEMPVGRNVLELSNVMRSANYTCVAISSLGMIEATAQVTVKALPK... | 3.1.3.48 | null | cell migration [GO:0016477]; homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; negative regulation of cell population proliferation [GO:0008285]; negative regulation of cell projection organization [GO:0031345]; negative regulation of cytokine-mediated signaling pathway [GO:0001960]; negativ... | endosome [GO:0005768]; excitatory synapse [GO:0060076]; growth cone [GO:0030426]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; postsynaptic density membrane [GO:0098839]; receptor complex [GO:0043235] | cell adhesion molecule binding [GO:0050839]; chondroitin sulfate proteoglycan binding [GO:0035373]; heparin binding [GO:0008201]; insulin receptor binding [GO:0005158]; phosphate ion binding [GO:0042301]; phosphoprotein phosphatase activity [GO:0004721]; protein tyrosine phosphatase activity [GO:0004725]; protein-conta... | PF00041;PF07679;PF00102; | 2.60.40.10;3.90.190.10; | Protein-tyrosine phosphatase family, Receptor class 2A subfamily | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane protein {ECO:0000305}. | CATALYTIC ACTIVITY: Reaction=H2O + O-phospho-L-tyrosyl-[protein] = L-tyrosyl-[protein] + phosphate; Xref=Rhea:RHEA:10684, Rhea:RHEA-COMP:10136, Rhea:RHEA-COMP:10137, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:46858, ChEBI:CHEBI:82620; EC=3.1.3.48; Evidence={ECO:0000255|PROSITE-ProRule:PRU10044}; | null | null | null | null | FUNCTION: Possible cell adhesion receptor. It possesses an intrinsic protein tyrosine phosphatase activity (PTPase) and dephosphorylates EPHA2 regulating its activity (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
A2A8U2 | TM201_MOUSE | MEGVSALLASCPTAGLAGGLGVTACAAAGVVLYRIARRVKPTHTMVNCWFCNHDTLVPYGNRNCWDCPHCEQYNGFQENGDYNKPIPAQYMEHLNHVVSSVPSPRDPAQPQQWVSSQVLLCRRCSHHQTTKIKQLAAFTPREEGRYDEEIEVYRHHLEQMYKLCRPCQAAVEYYIKHQNRQLRALLLSHQFRRREADQAHGQSFSSSAVKAPFQVILLRALAFLACAFLLFTTLYGPSEPFTPGAALPPALPPGGNSSAASDNTTSQAEGWQQLLGLLPEHATEKLHEAWAFGQSHQTSIVAVGLLTCLLAMLLAGRIRL... | null | null | fibroblast migration [GO:0010761]; nuclear migration [GO:0007097]; nuclear migration along microtubule [GO:0030473] | nuclear inner membrane [GO:0005637]; nuclear membrane [GO:0031965] | actin filament binding [GO:0051015]; lamin binding [GO:0005521] | PF10476;PF09779; | null | TMEM201 family | null | SUBCELLULAR LOCATION: [Isoform 2]: Nucleus inner membrane {ECO:0000250|UniProtKB:Q5SNT2}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q5SNT2}. Note=The C-terminal of isoform 2 is located on the nucleoplasmic side. During interphase, isoform 2 is distributed in the inner nuclear membrane and during mitosis, it is... | null | null | null | null | null | FUNCTION: Involved in nuclear movement during fibroblast polarization and migration (PubMed:22349700). May recruit Ran GTPase to the nuclear periphery (By similarity). {ECO:0000250|UniProtKB:Q5SNT2, ECO:0000269|PubMed:22349700}.; FUNCTION: [Isoform 2]: May define a distinct membrane domain in the vicinity of the mitoti... | Mus musculus (Mouse) |
A2A935 | PRD16_MOUSE | MRSKARARKLAKSDGDVVNNMYEPDPDLLAGQSAEEETEDGILSPIPMGPPSPFPTSEDFTPKEGSPYEAPVYIPEDIPIPPDFELRESSIPGAGLGIWAKRKMEIGERFGPYVVTPRAALKEADFGWEMLTDTEVSSQESCIKKQISEDLGSEKFCVDANQAGSGSWLKYIRVACSCDDQNLAMCQINEQIYYKVIKDIEPGEELLVHVKEGAYSLGVMAPSLDEDPTFRCDECDELFQCRLDLRRHKKYACSSAGAQLYEGLGEELKPEGLGVGSDGQAHECKDCERMFPNKYSLEQHMIVHTEEREYKCDQCPKAFN... | 2.1.1.367 | null | brown fat cell differentiation [GO:0050873]; heterochromatin organization [GO:0070828]; methylation [GO:0032259]; negative regulation of DNA-templated transcription [GO:0045892]; negative regulation of granulocyte differentiation [GO:0030853]; negative regulation of transcription by RNA polymerase II [GO:0000122]; nega... | cytoplasm [GO:0005737]; nucleus [GO:0005634]; transcription regulator complex [GO:0005667]; transcription repressor complex [GO:0017053] | DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; histone H3K9 methyltransferase activity [GO:0046974]; histone H3K9 monomethyltransferase activity [GO:0140948]; histone H3K9me2 methyltransferase activity [GO:0140947]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory... | PF21549;PF00096; | 3.30.160.60;2.170.270.10; | PRDM16 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18483224}. Cytoplasm {ECO:0000250|UniProtKB:Q9HAZ2}. | CATALYTIC ACTIVITY: Reaction=L-lysyl(9)-[histone H3] + S-adenosyl-L-methionine = H(+) + N(6)-methyl-L-lysyl(9)-[histone H3] + S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:60280, Rhea:RHEA-COMP:15542, Rhea:RHEA-COMP:15546, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:61929; EC=2.1... | null | null | null | null | FUNCTION: Binds DNA and functions as a transcriptional regulator (PubMed:18483224). Displays histone methyltransferase activity and monomethylates 'Lys-9' of histone H3 (H3K9me1) in vitro (PubMed:22939622). Probably catalyzes the monomethylation of free histone H3 in the cytoplasm which is then transported to the nucle... | Mus musculus (Mouse) |
A2A974 | CP4CB_MOUSE | MSASALSSIRFPGSISEYLQVASVLSLLLLLFKTAQLYLHRQWLLSSTQQFPSPPSHWLFGHKILKDQDLQDILTRIKNFPSACPQWLWGSKVRIQVYDPDYMKLILGRSDPKAHGSYRFLAPWIGRGLLLLDGQTWFQHRRMLTPAFHYDILKPYTEIMADSVHVMLDKWEQIVGQDSTLEIFQHITLMTLDTIMKCAFSHEGSVQLDRKYKSYIQAVEDLNNLFFLRVRNIFHQNDIIYRVSSNGCLANSACQLAHDHTDQVIKSRRSQLQDEEELEKLKKKRRLDFLDILLFARMENGKSLSDKDLRAEVDTFMFEG... | 1.14.14.1 | COFACTOR: Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250|UniProtKB:P20817}; | arachidonic acid metabolic process [GO:0019369]; fatty acid metabolic process [GO:0006631]; icosanoid biosynthetic process [GO:0046456]; kidney development [GO:0001822]; lauric acid metabolic process [GO:0048252]; linoleic acid metabolic process [GO:0043651]; omega-hydroxylase P450 pathway [GO:0097267] | endoplasmic reticulum membrane [GO:0005789]; intracellular membrane-bounded organelle [GO:0043231] | alkane 1-monooxygenase activity [GO:0018685]; arachidonic acid monooxygenase activity [GO:0008391]; arachidonic acid omega-hydroxylase activity [GO:0052869]; aromatase activity [GO:0070330]; fatty acid omega-hydroxylase activity [GO:0120250]; heme binding [GO:0020037]; iron ion binding [GO:0005506]; monooxygenase activ... | PF00067; | 1.10.630.10; | Cytochrome P450 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17112342}; Peripheral membrane protein. Microsome membrane {ECO:0000269|PubMed:17112342}; Peripheral membrane protein. | CATALYTIC ACTIVITY: Reaction=an organic molecule + O2 + reduced [NADPH--hemoprotein reductase] = an alcohol + H(+) + H2O + oxidized [NADPH--hemoprotein reductase]; Xref=Rhea:RHEA:17149, Rhea:RHEA-COMP:11964, Rhea:RHEA-COMP:11965, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:30879, ChEBI:CHEBI:57... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=2 uM for dodecanoic acid {ECO:0000269|PubMed:17112342}; KM=43 uM for (5Z,8Z,11Z,14Z)-eicosatetraenoic acid (without cytochrome b5) {ECO:0000269|PubMed:17112342}; KM=72 uM for (5Z,8Z,11Z,14Z)-eicosatetraenoic acid (with cytochrome b5) {ECO:0000269|PubMed:17112342}; ... | PATHWAY: Lipid metabolism; fatty acid metabolism. {ECO:0000305|PubMed:17112342}. | null | null | FUNCTION: A cytochrome P450 monooxygenase involved in the metabolism of fatty acids and their oxygenated derivatives (oxylipins) (PubMed:17112342). Mechanistically, uses molecular oxygen inserting one oxygen atom into a substrate, and reducing the second into a water molecule, with two electrons provided by NADPH via c... | Mus musculus (Mouse) |
A2A9A2 | DMTA2_MOUSE | MELRSELPSVPGAATAAATATGPPVASVASVAAAAAAAASLPVSVAGGLLRAPPLLLRAAEKYPRTPKCARCRNHGVVSALKGHKRYCRWKDCLCAKCTLIAERQRVMAAQVALRRQQAQEENEARELQLLYGTAEGLALAAANGIIPPRPAYEVFGSVCATDGGGPGAGAPAGSAGGAGGAEAKLQKFDLFPKTLLQAGRPDSPQPPPGKPLSPDGADSGPRTSSPEVRPGSGSENGDGESFSGSPLARASKEAGGSCPGSAGAGGGGEEDSPGSSSPLGSESGSEADKEEAEAAPTPGLGGGPGPRQRTPLDILTRVF... | null | null | cerebral cortex regionalization [GO:0021796]; dopaminergic neuron differentiation [GO:0071542]; germ cell development [GO:0007281]; neuroblast proliferation [GO:0007405]; neuron fate specification [GO:0048665]; positive regulation of neuroblast proliferation [GO:0002052]; regulation of transcription by RNA polymerase I... | nucleus [GO:0005634] | DNA-binding transcription factor activity, RNA polymerase II-specific [GO:0000981]; identical protein binding [GO:0042802]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; sequence-specific DNA binding [GO:0043565] | PF00751;PF03474;PF20624; | 4.10.1040.10; | DMRT family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00070}. | null | null | null | null | null | FUNCTION: May be involved in sexual development. | Mus musculus (Mouse) |
A2A9C3 | SZT2_MOUSE | MASERPEPEVEEAGQVFLLMKKDYRISRNVRLAWFLNHLHQTVQATPQELLLQSEQELEVLSVLPPGWQPDEPVVPRPFLLVPSTRVTFLAWQYRFVIELDLSPSTGIVDDSTGEILFDEVFHALSRCLGGLLRPFRVPGSCINFQPEIYVTIQAYSSIIGLQSHQVLVQGCLLDPSQREAFLQQVYEQLCLFEDKVATMLQQQYEPQGQAEDQSPESGESLGRKVGVSMVTADLGLVSMIRQGILALQLLPSNSSAGIIVITDGVTSVPDVAVCETLLNQLRSGTVACSFVQVGGVYSYDCSFGHVPNVELMKFIAMAT... | null | null | cellular response to amino acid starvation [GO:0034198]; cellular response to glucose starvation [GO:0042149]; central nervous system development [GO:0007417]; corpus callosum morphogenesis [GO:0021540]; negative regulation of TORC1 signaling [GO:1904262]; pigmentation [GO:0043473]; post-embryonic development [GO:00097... | GATOR1 complex [GO:1990130]; GATOR2 complex [GO:0061700]; KICSTOR complex [GO:0140007]; lysosomal membrane [GO:0005765]; peroxisome [GO:0005777] | null | null | null | null | null | SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q5T011}. Peroxisome {ECO:0000269|PubMed:20045724}. Note=Localization to lysosomes is amino acid-independent. {ECO:0000250|UniProtKB:Q5T011}. | null | null | null | null | null | FUNCTION: As part of the KICSTOR complex functions in the amino acid-sensing branch of the TORC1 signaling pathway. Recruits, in an amino acid-independent manner, the GATOR1 complex to the lysosomal membranes and allows its interaction with GATOR2 and the RAG GTPases. Functions upstream of the RAG GTPases and is requir... | Mus musculus (Mouse) |
A2A9F4 | KDF1_MOUSE | MPRPGQPRPSSGPPRLGPWERPSELCLETNDERSQPPPGRRTRRPDPKDPGHHGPESITFISGSAEPANEPPTCCLLWRPWGWDWCRAAFCFRRCRDCLQRCGACVRGCSPCLSAGDPIEGSAEAAWAKEHNGVPPSPDRAPPSRRDGQRLKTSMGSSFSYPDVKLKGIPVYPYRHATSPVPDVDSCCKEPLAEPPPTRHSLPSTFTNSPRGSEEYYSFHESDLDLPEMGSGSMSSREIDVLIFKKLTELFSVHQIDELAKCTSDTVFLEKTSKISDLISSITQDYHLDEQDAEGRLVRGIIRISTRKSRSRPQTSEGRS... | null | null | developmental growth [GO:0048589]; establishment of skin barrier [GO:0061436]; keratinocyte development [GO:0003334]; keratinocyte proliferation [GO:0043616]; limb epidermis development [GO:0060887]; morphogenesis of embryonic epithelium [GO:0016331]; negative regulation of keratinocyte proliferation [GO:0010839]; nega... | anchoring junction [GO:0070161]; cell cortex [GO:0005938]; cell junction [GO:0030054]; cell leading edge [GO:0031252]; cytoplasm [GO:0005737] | null | PF15551; | null | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:24075906}. Cell junction {ECO:0000269|PubMed:24075906}. Note=Localized at cell borders in single layered keratinocytes. Localized at cell borders in the basal and spinous layers but is more diffusely localized in the granular layer. Colocalized with actin near the cel... | null | null | null | null | null | FUNCTION: Plays a role in the regulation of the epidermis formation during early development. Required both as an inhibitor of basal cell proliferation and a promoter of differentiation of basal progenitor cell progeny. {ECO:0000269|PubMed:24075906}. | Mus musculus (Mouse) |
A2AA28 | MET23_MOUSE | MDSVRPRAPWAPPPDPASLDSPTCEPGLMAGTQLFRFREEPVPGGNRAVLEVRVPQVLHVQYGMYVWPCAVVLAQYLWFHRRSLPGKAVLEVGAGVSLPGILAAKCGAKVILSDSSEFPHCLDICRQSCQMNNLPQVEVVGLTWGHISKDILSLPPQDIILGSDVFFEPEDFESILATVYFLMQKNPKVQFWSTYQVRSADWSLEGLLYKWDMKCVHIPLESFDADKEDIAESTLPGRHTVEMLIISFAKDSF | 2.1.1.319 | null | cognition [GO:0050890]; epigenetic programing of male pronucleus [GO:0044727]; epigenetic programming in the zygotic pronuclei [GO:0044725]; methylation [GO:0032259]; positive regulation of transcription by RNA polymerase II [GO:0045944] | cytoplasm [GO:0005737]; female pronucleus [GO:0001939]; male pronucleus [GO:0001940]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; protein-containing complex [GO:0032991] | DNA-binding transcription factor binding [GO:0140297]; heat shock protein binding [GO:0031072]; histone H3R17 methyltransferase activity [GO:0035642]; histone methyltransferase activity [GO:0042054]; protein-arginine omega-N asymmetric methyltransferase activity [GO:0035242]; protein-lysine N-methyltransferase activity... | PF10294; | 3.40.50.150; | Methyltransferase superfamily, METTL23 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:28930672}. Cytoplasm {ECO:0000269|PubMed:28930672}. Note=Localizes in male and female zygote pronucleus and cytoplasm. {ECO:0000269|PubMed:28930672}. | CATALYTIC ACTIVITY: Reaction=L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) + N(omega),N(omega)-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-homocysteine; Xref=Rhea:RHEA:48096, Rhea:RHEA-COMP:10532, Rhea:RHEA-COMP:11991, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856, ChEBI:CHEBI:59789, ChEBI:CHEBI:... | null | null | null | null | FUNCTION: Histone methyltransferase that dimethylates histone H3 at 'Arg-17', forming asymmetric dimethylarginine (H3R17me2a), leading to activate transcription via chromatin remodeling (PubMed:28930672). Maternal factor involved in epigenetic chromatin reprogramming of the paternal genome in the zygote: mediates H3R17... | Mus musculus (Mouse) |
A2AAE1 | BLTP1_MOUSE | MDQRKNDSIVPSITQLEDFLTEHNSNVVWLLVATILSCGWIIYLTYYNSRNVGLILTLVLNRLYKHGYIHIGSFSFSVLSGKVMVREIYYITEDMSIRIQDGFIIFRWWKMYNPKQKQHDPKAETRLYITVNDFEFHVYNRSDLYGRLQELFGLEPTIIPPKKDDDKTRENGRTRTQSKIERVKVKTESQDPTSSWRSLIPVIKVNVSTGRLAFGNHYQPQTLCINFDDAFLTYTTKPPSSHLDQFMHIVKGKLENVRVMLVPSPRYVGLQNDEPPRLMGEGFVVLQSNDVDLYYYMDEPGLVPEETEESTEGDISSEDC... | null | null | adipose tissue development [GO:0060612]; endocytic recycling [GO:0032456]; endosomal transport [GO:0016197]; fat cell differentiation [GO:0045444]; intermembrane lipid transfer [GO:0120009]; lipid metabolic process [GO:0006629]; lipid storage [GO:0019915]; nucleus localization [GO:0051647]; phagocytosis [GO:0006909]; r... | endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum-plasma membrane contact site [GO:0140268]; mitochondrial membrane [GO:0031966]; nucleus [GO:0005634]; plasma membrane [GO:0005886]; presynapse [GO:0098793] | phosphatidylethanolamine transfer activity [GO:1904121] | PF10479;PF21677;PF20413; | null | null | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q12150}; Single-pass membrane protein {ECO:0000255}. Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q12150}; Single-pass membrane protein {ECO:0000255}. Mitochondrion membrane {ECO:0000250|UniProtKB:Q12150}; Single-pass membrane protein {ECO:0000255}. No... | null | null | null | null | null | FUNCTION: Tube-forming lipid transport protein which provides phosphatidylethanolamine for glycosylphosphatidylinositol (GPI) anchor synthesis in the endoplasmic reticulum. Plays a role in endosomal trafficking and endosome recycling. Also involved in the actin cytoskeleton and cilia structural dynamics. Acts as a regu... | Mus musculus (Mouse) |
A2AAJ9 | OBSCN_MOUSE | MDHSFSGAPRFLTRPKAFVVSVGKDATLSCQIVGNPTPHVSWEKDRQPVEAGARFRLAQDGDVYRLTILDLALGDSGQYVCRARNAIGEAFAAVGLRVDSEGTCAEQAPHFLLRPTSIRVREGADATFRCRVGGSPQPAVSWSKDGRRLGPPDAPHVRVEEHGESSALRIRSARPRDGGTYEVRAENPLGSASAAAALVVDSDAEVAGPPGTSTATLLAHLQQRREAMRAEGIPPSPPGAGTRTCTVTEGKHARLSCFVTGEPKPETVWKKDGQLVTEGRRHVVYEDEQENFVLKILFCKQSDRGLYTCTASNLVGQTYS... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000269|PubMed:23392350}; | cell differentiation [GO:0030154]; negative regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction [GO:0051898]; protein autophosphorylation [GO:0046777]; protein phosphorylation [GO:0006468] | cytosol [GO:0005829]; extracellular space [GO:0005615]; intercalated disc [GO:0014704]; M band [GO:0031430]; nuclear body [GO:0016604]; plasma membrane [GO:0005886]; sarcolemma [GO:0042383]; sarcomere [GO:0030017]; striated muscle myosin thick filament [GO:0005863]; Z disc [GO:0030018] | ankyrin binding [GO:0030506]; ATP binding [GO:0005524]; cadherin binding [GO:0045296]; calmodulin binding [GO:0005516]; guanyl-nucleotide exchange factor activity [GO:0005085]; metal ion binding [GO:0046872]; phosphatidylinositol bisphosphate binding [GO:1902936]; phosphatidylinositol-3,4,5-trisphosphate binding [GO:00... | PF00041;PF07679;PF00047;PF00612;PF00169;PF00069;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 | PTM: Autophosphorylated by protein kinase domain 1 and 2. {ECO:0000269|PubMed:23392350}.; PTM: Two small isoforms, one probably containing protein kinase domain 2 and a partial protein kinase domain 1 and one containing only protein kinase domain 2, are glycosylated. {ECO:0000269|PubMed:23392350}. | SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere, M line {ECO:0000269|PubMed:23392350}. Cytoplasm, myofibril, sarcomere, Z line {ECO:0000269|PubMed:23392350}. Cell membrane, sarcolemma {ECO:0000269|PubMed:23392350}. Nucleus {ECO:0000269|PubMed:23392350}. Secreted {ECO:0000269|PubMed:23392350}. Note=Colocalizes wit... | CATALYTIC ACTIVITY: Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-[protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616, ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1; Evidence={ECO:0000269|PubMed:23392350}; CATALYTIC... | null | null | null | null | FUNCTION: Structural component of striated muscles which plays a role in myofibrillogenesis. Probably involved in the assembly of myosin into sarcomeric A bands in striated muscle (By similarity). Has serine/threonine protein kinase activity and phosphorylates N-cadherin CDH2 and sodium/potassium-transporting ATPase su... | Mus musculus (Mouse) |
A2AAY5 | SPD2B_MOUSE | MPPRRSIVEVKVLDVQKRRVPNKHYVYIIRVTWSSGATEAIYRRYSKFFDLQMQMLDKFPMEGGQKDPKQRIIPFLPGKILFRRSHIRDVAVKRLIPIDEYCKALIQLPPYISQCDEVLQFFETRPEDLNPPKEEHIGKKKSGNDPTSVDPMVLEQYVVVADYQKQESSEISLSVGQVVDIIEKNESGWWFVSTAEEQGWVPATCLEGQDGVQDEFSLQPEEEEKYTVIYPYTARDQDEMNLERGAVVEVVQKNLEGWWKIRYQGKEGWAPASYLKKNSGEPLPPKLGPSSPAHSGALDLDGVSRHQNAMGREKELLNNQ... | null | null | adipose tissue development [GO:0060612]; bone development [GO:0060348]; cranial skeletal system development [GO:1904888]; eye development [GO:0001654]; heart development [GO:0007507]; osteoblast fate commitment [GO:0002051]; podosome assembly [GO:0071800]; positive regulation of adipose tissue development [GO:1904179];... | anchoring junction [GO:0070161]; cell projection [GO:0042995]; cytoplasm [GO:0005737]; podosome [GO:0002102] | phosphatidylinositol-3,5-bisphosphate binding [GO:0080025]; phosphatidylinositol-3-phosphate binding [GO:0032266]; phosphatidylinositol-4-phosphate binding [GO:0070273]; phosphatidylinositol-5-phosphate binding [GO:0010314]; SH2 domain binding [GO:0042169]; superoxide-generating NADPH oxidase activator activity [GO:001... | PF00787;PF00018;PF07653; | 3.30.1520.10;2.30.30.40; | SH3PXD2 family | PTM: Phosphorylated in SRC-transformed cells. {ECO:0000269|PubMed:19144821}. | SUBCELLULAR LOCATION: Cytoplasm. Cell projection, podosome. Note=Cytoplasmic in normal cells and localizes to podosomes in SRC-transformed cells. | null | null | null | null | null | FUNCTION: Adapter protein involved in invadopodia and podosome formation and extracellular matrix degradation. Binds matrix metalloproteinases (ADAMs), NADPH oxidases (NOXs) and phosphoinositides. Acts as an organizer protein that allows NOX1- or NOX3-dependent reactive oxygen species (ROS) generation and ROS localizat... | Mus musculus (Mouse) |
A2ABV5 | MED14_MOUSE | MAPVQLDNHQLIPPGGGGGSSGGGGSSSGSASAPAPPPPAAAVAAAAAAAASPGYRLSTLIEFLLHRAYSELMVLTDLLPRKSDVERKIEIVQFASRTRQLFVRLLALVKWANDAGKVEKCAMISSFLDQQAILFVDTADRLASLARDALVHARLPSFAIPYAIDVLTTGSYPRLPTCIRDKIIPPDPITKIEKQATLHQLNQILRHRLVTTDLPPQLANLTVANGRVKFRVEGEFEATLTVMGDDPEVPWRLLKLEILVEDKETGDGRALVHSMQIDFIHQLVQSRLFADEKPLQDMYNCLHCFCLSLQLEVLHSQTLM... | null | null | positive regulation of transcription by RNA polymerase II [GO:0045944]; positive regulation of transcription elongation by RNA polymerase II [GO:0032968]; positive regulation of transcription initiation by RNA polymerase II [GO:0060261]; regulation of transcription by RNA polymerase II [GO:0006357]; RNA polymerase II p... | core mediator complex [GO:0070847]; mediator complex [GO:0016592]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | transcription coactivator activity [GO:0003713]; transcription coregulator activity [GO:0003712] | PF08638; | null | Mediator complex subunit 14 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to... | Mus musculus (Mouse) |
A2AC93 | DNAI2_MOUSE | MEIVYVYLKKRSEFGKQCNFSDRQAELNIDILPNPELAALYVERNPVDTGIQCSASMSEHEANTERFEMESCGVNHVEGGWPKDVNPQELEQTIRFRKKVEKDENYINAVMQLGSIMEHCIKQNNAIDIYEEYFDDEEAVEVTEEAPSAKTINVFRDPQEIKRTATHLSWHPDGNRKLAVAYSCLKFQRAPMSMNYDSYIWDLENPNRPEIALKPLSPLVTLEYNPKDSHVLLGGCYNGQIACWDTRKGSLVAELSTIEFSHRDPVYGTIWLQSKTGTECFSASTDGQVMWWDIRKISEPIEVVIMDISRKEQLENALGA... | null | null | cilium assembly [GO:0060271]; cilium movement [GO:0003341]; determination of left/right symmetry [GO:0007368]; outer dynein arm assembly [GO:0036158] | 9+2 motile cilium [GO:0097729]; axonemal dynein complex [GO:0005858]; axoneme [GO:0005930]; cilium [GO:0005929]; cytoplasm [GO:0005737]; dynein axonemal particle [GO:0120293]; external side of plasma membrane [GO:0009897]; microtubule [GO:0005874]; outer dynein arm [GO:0036157]; sperm flagellum [GO:0036126] | dynein heavy chain binding [GO:0045504]; dynein light chain binding [GO:0045503]; microtubule motor activity [GO:0003777] | PF00400; | 2.130.10.10; | Dynein intermediate chain family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:Q9GZS0}. Dynein axonemal particle {ECO:0000250|UniProtKB:Q4QR00}. Note=Located in the proximal region of respiratory cilia. {ECO:0000250|UniProtKB:Q9GZS0}. | null | null | null | null | null | FUNCTION: Part of the dynein complex of respiratory cilia. {ECO:0000250}. | Mus musculus (Mouse) |
A2AD83 | FRMD7_MOUSE | MLHLKVQFLDDSQKIFVVDQKSSGKALFNLSCGHLNLAEKEYFGLEFCSHSGNNVWLELLKPITKQVKNPKEVVFKFMVKFFPVDPGHLREELTRYLFTLQIKKDLALGRLPCSDNCTALMVSHILQSELGDFHEETVRKHLVQTQYLPSQASLESKIMQFHQQHIGRSPAESDILLLDIARKLDMYGIRPQPASDGEGMQIHLAVAHMGVLVLRGNTKINTFNWAKIRKLSFKRKHFLIKLHANILVLCKDTLEFTMASRDACKAFWKTCVEYHAFFRLSEEPKSKPKTLLCSKGSSFRYSGRTQRQLLEYGKKGRLKS... | null | null | negative regulation of stress fiber assembly [GO:0051497]; nervous system development [GO:0007399]; positive regulation of lamellipodium assembly [GO:0010592]; positive regulation of small GTPase mediated signal transduction [GO:0051057]; regulation of neuron projection development [GO:0010975] | cytoskeleton [GO:0005856]; cytosol [GO:0005829]; growth cone [GO:0030426]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886] | guanyl-nucleotide exchange factor activity [GO:0005085] | PF08736;PF09380;PF00373;PF09379; | 1.20.80.10;2.30.29.30; | null | null | SUBCELLULAR LOCATION: Cell projection, neuron projection {ECO:0000269|PubMed:19892780}. Cell projection, growth cone {ECO:0000269|PubMed:19892780}. Note=In undifferentiated neurons, located in the actin-rich regions of the cell body. In differentiated neurons, located in the actin-rich regions of the cell body and prim... | null | null | null | null | null | FUNCTION: Plays a role in neurite development, may be through the activation of the GTPase RAC1. Plays a role in the control of eye movement and gaze stability. {ECO:0000250|UniProtKB:Q6ZUT3, ECO:0000269|PubMed:19892780}. | Mus musculus (Mouse) |
A2AF47 | DOC11_MOUSE | MAEVRKFTKRLSKPGTAAELRQSVSEAVRGSVVLEKAKLVEPLDYENVITQRKTQIYSDPLRDLLMFPMEDISISVIGRQRRTVQSTVPEDAEKRAQSLFVKECIKTYSTDWHVVNYKYEDFSGDFRMLPCKSLRPEKIPNHVFEIDEDCEKDEDSSSLCSQKGGVIKQGWLHKANVNSTITVTMKVFKRRYFYLTQLPDGSYILNSYKDEKNSKESKGCIYLDACIDVVQCPKMRRHAFELKMLDKYSHYLAAETEQEMEEWLIMLKKIIQINTDSLVQEKKDTVEAIQEEETSSQGKAENIMASLERSMHPELMKYGR... | null | null | B cell homeostasis [GO:0001782]; marginal zone B cell differentiation [GO:0002315]; positive regulation of filopodium assembly [GO:0051491]; positive regulation of GTPase activity [GO:0043547]; small GTPase-mediated signal transduction [GO:0007264] | null | guanyl-nucleotide exchange factor activity [GO:0005085]; small GTPase binding [GO:0031267] | PF06920;PF20422;PF20421;PF14429;PF11878;PF00169; | 1.20.58.740;1.25.40.410;2.60.40.150;2.30.29.30; | DOCK family | null | null | null | null | null | null | null | FUNCTION: Guanine nucleotide-exchange factor (GEF) that activates CDC42 by exchanging bound GDP for free GTP (PubMed:15710388, PubMed:16968698, PubMed:25851601). Required for marginal zone (MZ) B-cell development, is associated with early bone marrow B-cell development, MZ B-cell formation, MZ B-cell number and margina... | Mus musculus (Mouse) |
A2AG06 | MEIOC_MOUSE | MEVSGGDTCRPRHPQGLREGPEPKVAAAAAAFRGSANRCWNLSVDTSNRLSDVFNSMMLTGSAPFYDCYKSQNEDNVDLRQTCTPLSSSTEYASSIDSSLFYAPWSTYGDDIKQPPSSQISVKNRIQTERNDYGSETDLYGLVSNILEEQDKSQPYFAEGTCSSNLKSVWPMNTSRFVDHHDLLTEPKRPVDTSISQQAFYSGESVSAVEKQYLHNSSLTPQQKIDELYHGYTGLDLEEQWLYLSRSDHSNCYNSQANDTVKATFQEYPFVKNCFTPQTGLSDIMKESGIDTYAYGREKICTKGLETPLQHKRAEIFLSQ... | null | null | chromosome organization involved in meiotic cell cycle [GO:0070192]; double-strand break repair [GO:0006302]; female meiosis I [GO:0007144]; germline cell cycle switching, mitotic to meiotic cell cycle [GO:0051729]; male meiosis I [GO:0007141]; metaphase chromosome alignment [GO:0051310]; mRNA stabilization [GO:0048255... | cytoplasm [GO:0005737]; nucleus [GO:0005634] | null | PF15189; | null | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:26742488, ECO:0000269|PubMed:28380054}. Nucleus {ECO:0000269|PubMed:28380054}. Note=at late pachytene a fraction is nuclear. {ECO:0000269|PubMed:28380054}. | null | null | null | null | null | FUNCTION: Is required for meiosis completion in both male and female germ cells. Confers stability to numerous meiotic mRNAs in gonads allowing proper initiation and progression into meiosis prophase I. The function may involve YTHDC2 and is independent of induction by retinoic acid (RA). Maintains an extended meiotic ... | Mus musculus (Mouse) |
A2AGH6 | MED12_MOUSE | MAAFGILSYEHRPLKRLRLGPPDVYPQDPKQKEDELTALNVKQGFNNQPAVSGDEHGSAKNVNFNPAKISSNFSSIIAEKLRCNTLSDTGRRKSLMNQKDNFWLVTARSQSAINTWFTDLAGTKPLTHLAKKVPIFSKKEEVFGYLAKYTVPVMRAAWLIKMTCAYYAAMSETKVKKKNTADPFTEWTQIITKYLWEQLQKMAEYYRPGPAGSGGCGSTIGPLPHDVEMAIRQWDYNEKLALFMFQDGMLDRHEFLTWVLECFEKIRPGEDELLKLLLPLLLRYSGEFVQSAYLSRRLAYFCTRRLALQLDGVSSHSSHV... | null | null | axis elongation involved in somitogenesis [GO:0090245]; embryonic brain development [GO:1990403]; embryonic neurocranium morphogenesis [GO:0048702]; embryonic organ development [GO:0048568]; endoderm development [GO:0007492]; heart development [GO:0007507]; neural tube closure [GO:0001843]; neural tube development [GO:... | CKM complex [GO:1990508]; mediator complex [GO:0016592]; nucleoplasm [GO:0005654]; ubiquitin ligase complex [GO:0000151] | beta-catenin binding [GO:0008013]; chromatin binding [GO:0003682]; nuclear thyroid hormone receptor binding [GO:0046966]; RNA polymerase II cis-regulatory region sequence-specific DNA binding [GO:0000978]; transcription coactivator activity [GO:0003713]; ubiquitin protein ligase activity [GO:0061630] | PF09497;PF12145;PF12144; | null | Mediator complex subunit 12 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000305}. | null | null | null | null | null | FUNCTION: Component of the Mediator complex, a coactivator involved in the regulated transcription of nearly all RNA polymerase II-dependent genes. Mediator functions as a bridge to convey information from gene-specific regulatory proteins to the basal RNA polymerase II transcription machinery. Mediator is recruited to... | Mus musculus (Mouse) |
A2AGL3 | RYR3_MOUSE | MAEAGEGGEDEIQFLRTEDEVVLQCIANIHKEQRKFCLAAEGLGNRLCFLEPTSEAKYIPPDLCVCNFVLEQSLSVRALQEMLANTVENGGEGAAQGGGHRTLLYGHAILLRHSFSGMYLTCLTTSRSQTDKLAFDVGLREHATGEACWWTIHPASKQRSEGEKVRIGDDLILVSVSSERYLHLSISNGSIQVDASFMQTLWNVHPTCSGSSIEEGYLLGGHVVRLFHGHDECLTIPSTDQNDSQHRRVFYEAGGAGTRARSLWRVEPLRISWSGSNIRWGQAFRLRHLTTGHYLALTEDQGLLLQDRGKSDTKSTAFSF... | null | null | calcium ion transmembrane transport [GO:0070588]; cellular response to ATP [GO:0071318]; cellular response to caffeine [GO:0071313]; cellular response to calcium ion [GO:0071277]; cellular response to magnesium ion [GO:0071286]; intracellular calcium ion homeostasis [GO:0006874]; negative regulation of cytosolic calciu... | calcium channel complex [GO:0034704]; cytoplasmic side of plasma membrane [GO:0009898]; junctional membrane complex [GO:0030314]; membrane [GO:0016020]; perinuclear region of cytoplasm [GO:0048471]; sarcolemma [GO:0042383]; sarcoplasmic reticulum membrane [GO:0033017]; smooth endoplasmic reticulum [GO:0005790]; Z disc ... | calcium ion binding [GO:0005509]; calcium-induced calcium release activity [GO:0048763]; calmodulin binding [GO:0005516]; ryanodine-sensitive calcium-release channel activity [GO:0005219] | PF08709;PF00520;PF02815;PF08454;PF06459;PF01365;PF21119;PF02026;PF00622; | 1.10.287.70;1.10.490.160;2.60.120.920;2.80.10.50;6.20.350.10;1.10.238.10;1.25.10.30; | Ryanodine receptor (TC 1.A.3.1) family, RYR3 subfamily | null | SUBCELLULAR LOCATION: Sarcoplasmic reticulum membrane {ECO:0000269|PubMed:9582272}; 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:8702664, ECO:0000269|PubMed:9582272}; | null | null | null | null | FUNCTION: Cytosolic calcium-activated calcium channel that mediates the release of Ca(2+) from the sarcoplasmic reticulum into the cytoplasm in muscle and thereby plays a role in triggering muscle contraction. May regulate Ca(2+) release by other calcium channels. Calcium channel that mediates Ca(2+)-induced Ca(2+) rel... | Mus musculus (Mouse) |
A2AGT5 | CKAP5_MOUSE | MGDDSEWLKLPVDQKCEHKLWKARLSGYEEALKIFQKIKDEKSPEWSKYLGLIKKFVTDSNAVVQLKGLEAALVYVENAHVAGKTTGEVVSGVVSKVFNQPKAKAKELGIEICLMYVEIEKGESVQEELLKGLDNKNPKIIVACIETLRKALSEFGSKIISLKPIIKVLPKLFESRDKAVRDEAKLFAIEIYRWNRDAVKHTLQNINSVQLKELEEEWVKLPTGAPKPSRFLRSQQELEAKLEQQQSAGGDAEGGGDDGDEVPQVDAYELLDAVEILSKLPKDFYDKIEAKKWQERKEALEAVEVLVKNPKLEAGDYADL... | null | null | cell division [GO:0051301]; central nervous system myelin formation [GO:0032289]; centrosome cycle [GO:0007098]; centrosome duplication [GO:0051298]; cytoplasmic translation [GO:0002181]; dendritic spine maintenance [GO:0097062]; establishment or maintenance of microtubule cytoskeleton polarity [GO:0030951]; excitatory... | centrosome [GO:0005813]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; kinetochore [GO:0000776]; microtubule plus-end [GO:0035371]; neuronal ribonucleoprotein granule [GO:0071598]; perikaryon [GO:0043204]; postsynapse [GO:0098794]; protein-containing complex [GO:0032991]; spindle pole [GO:0000922] | microtubule binding [GO:0008017]; microtubule plus end polymerase [GO:0061863]; microtubule plus-end binding [GO:0051010]; ribonucleoprotein complex binding [GO:0043021] | PF12348;PF21041; | 1.25.10.10; | TOG/XMAP215 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q14008}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q14008}. Cytoplasm, cytoskeleton, spindle {ECO:0000250|UniProtKB:Q14008}. Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q1400... | null | null | null | null | null | FUNCTION: Binds to the plus end of microtubules and regulates microtubule dynamics and microtubule organization. Acts as a processive microtubule polymerase. Promotes cytoplasmic microtubule nucleation and elongation. Plays a major role in organizing spindle poles. In spindle formation protects kinetochore microtubules... | Mus musculus (Mouse) |
A2AH22 | AMRA1_MOUSE | MKVVPEKNAVRILWGRERGTRAMGAQRLLQELVEDKTRWMKWEGKRVELPDSPRSTFLLAFSPDRTLLASTHVNHNIYITEVKTGKCVHSLIGHRRTPWCVTFHPTISGLIASGCLDGEVRIWDLHGGSESWFTDSNNAIASLAFHPTAQLLLIATANEIHFWDWSRREPFAVVKTASEMERVRLVRFDPLGHYLLTAIVNPSNQQGDDEPEIPIDGTELSHYRQRALLQSQPVRRTPLLHNFLHMLSSRSSGIQVGEQSTVQDSATPSPPPPPPQPSTERPRTSAYIRLRQRVSYPTTVECCQHPGILCLCSRCAGTRV... | null | null | autophagosome assembly [GO:0000045]; autophagy [GO:0006914]; cell cycle [GO:0007049]; cell differentiation [GO:0030154]; cellular response to starvation [GO:0009267]; mitophagy [GO:0000423]; negative regulation of cardiac muscle cell apoptotic process [GO:0010667]; negative regulation of cell population proliferation [... | autophagosome [GO:0005776]; axoneme [GO:0005930]; Cul4-RING E3 ubiquitin ligase complex [GO:0080008]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; endoplasmic reticulum [GO:0005783]; focal adhesion [GO:0005925]; intracellular membrane-bounded organelle [GO:0043231]; mitochondrion [GO:0005739]; nucleus [GO:0005634]; ph... | GTPase binding [GO:0051020]; protein phosphatase binding [GO:0019903]; ubiquitin ligase-substrate adaptor activity [GO:1990756]; ubiquitin protein ligase binding [GO:0031625] | PF00400; | 2.130.10.10; | WD repeat AMBRA1 family | PTM: Phosphorylation at Ser-52 by MTOR inhibits its ability to regulate autophagy and mediate ubiquitination of ULK1. Phosphorylation by ULK1 in response to autophagy induction abolishes interaction with DYNLL1 and DYNLL2, releasing AMBRA1 from the cytoskeletal docking site to induce autophagosome nucleation. Phosphory... | SUBCELLULAR LOCATION: Endoplasmic reticulum {ECO:0000250|UniProtKB:Q9C0C7}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q9C0C7}. Cytoplasmic vesicle, autophagosome {ECO:0000305|PubMed:17589504, ECO:0000305|PubMed:24089209, ECO:0000305|PubMed:28362576, ECO:0000305|PubMed:32616651}. Mitochondrion {ECO:0000250|UniProtK... | null | null | PATHWAY: Protein modification; protein ubiquitination. {ECO:0000269|PubMed:23974797, ECO:0000269|PubMed:33854232, ECO:0000269|PubMed:33854235, ECO:0000269|PubMed:33854239}. | null | null | FUNCTION: Substrate-recognition component of a DCX (DDB1-CUL4-X-box) E3 ubiquitin-protein ligase complex involved in cell cycle control and autophagy (PubMed:17589504, PubMed:33854232, PubMed:33854235, PubMed:33854239). The DCX(AMBRA1) complex specifically mediates the polyubiquitination of target proteins such as BECN... | Mus musculus (Mouse) |
A2AHC3 | CAMP1_MOUSE | MVDAGGRCAAEGWRRMEAPPEGADLVPLDRYDAARAKIAANLQWICAKAYGLDNIPEDLRDPFYIDQYEQEHIKPPVIKLLLSSELYCRVCSLILKGDQVATLQGHQSVIQALSRKGIYVMESDDTPVTDADLSQAPIKMSGHMAMVDALMMAYTVEMISIEKVVASVKRFSTFSASKELPYDLEDAMVFWINKVNLKMREITEKEVKLKQQPLESPAHQKVRYRREHLSARQSPYFPLLEDLMRDGSDGAALLAVVHYYCPEQMKLDDICLKEVPSMADSLYNIRLLREFSNEHLNKCFYLTLEDMLYAPLVLKPNVMV... | null | null | cytoplasmic microtubule organization [GO:0031122]; cytoskeleton organization [GO:0007010]; microtubule cytoskeleton organization [GO:0000226]; negative regulation of microtubule depolymerization [GO:0007026]; neuron projection development [GO:0031175]; regulation of cell morphogenesis [GO:0022604]; regulation of microt... | cytoplasm [GO:0005737]; microtubule [GO:0005874]; microtubule minus-end [GO:0036449] | calmodulin binding [GO:0005516]; microtubule binding [GO:0008017]; microtubule minus-end binding [GO:0051011]; spectrin binding [GO:0030507] | PF17095;PF11971;PF08683; | 3.10.20.360; | CAMSAP1 family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q5T5Y3}. Note=Associates with the minus-end of microtubules. In contrast to CAMSAP2 and CAMSAP3, does not form stretches of decorated microtubule minus-ends. {ECO:0000250|UniProtKB:Q5T5Y3}. | null | null | null | null | null | FUNCTION: Key microtubule-organizing protein that specifically binds the minus-end of non-centrosomal microtubules and regulates their dynamics and organization. Specifically recognizes growing microtubule minus-ends and stabilizes microtubules. Acts on free microtubule minus-ends that are not capped by microtubule-nuc... | Mus musculus (Mouse) |
A2AHL1 | ANO3_MOUSE | MVHHSGSIQSFKQQKGMNISKSEITTEASLKPSRRSLPCLAQSYAHSKSLSQSASLFQSTESESQAPTSVTFLSADKPEHVTSEESRKDSTLKCSFADLSDFCLALGKDKDYLDESEHANYDRSRLLNDFVTKDKPASKTKLSKNDMSYIASSGLLFKDGKKRIDYILVYRKTNIQYDKRNTFEKNLRAEGLMLEKEPAIANPDIMFIKIHIPWDTLCKYAERLNIRVPFRKKCYYTDQKNKSKSRVQNYFKRIKKWMSQNPMVLDKSAFPELEESDCYTGPFSRARIHHFIINNKDTFFSNATRSRIVYHMLERTKYEN... | null | null | calcium activated galactosylceramide scrambling [GO:0061591]; calcium activated phosphatidylcholine scrambling [GO:0061590]; chloride transmembrane transport [GO:1902476]; detection of mechanical stimulus [GO:0050982]; detection of temperature stimulus [GO:0016048]; establishment of localization in cell [GO:0051649] | plasma membrane [GO:0005886] | chloride channel activity [GO:0005254]; phospholipid scramblase activity [GO:0017128]; protein dimerization activity [GO:0046983] | PF16178;PF04547; | null | Anoctamin family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000255}. Note=Shows an intracellular localization. {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571, ChEBI:CHEBI:57643; Evidence={ECO:0000269|PubMed:23532839}; PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:38573; Evidence={ECO:0000305|PubMed:23532839}; CATALYTIC ACTIVI... | null | null | null | null | FUNCTION: Has calcium-dependent phospholipid scramblase activity; scrambles phosphatidylcholine and galactosylceramide (PubMed:23532839). Does not exhibit calcium-activated chloride channel (CaCC) activity (PubMed:23532839). Seems to act as potassium channel regulator and may inhibit pain signaling; can facilitate KCNT... | Mus musculus (Mouse) |
A2AI05 | NDOR1_MOUSE | MQVPQLLVLFGSQTGTAQDEAERLGREARRRRLGCRVQALDSYSVANLIREPLVIFVCATTGQGDPPDNMKNFWRFIFRKSLPSSSLCQMDFAVLGLGDSSYAKFNFVAKKLHRRLLQLGGSALLPPCLGDDQHELGPDAAIDPWVGDLWEKIMVMYPVPLDIPEIPHGVPLPSKFIFQFLQEVPSIGAEELNIASSAPQTPPSELQPFLAPVITNQRVTGPQHFQDVRLIEFDITDSNISFAAGDVVFILPSNSEAHTQQFCQVLCLDPNQFFTLKPREPGVPDPPGLPQPCTVWNLVSQYLDIASVPRRSFFELLACL... | 1.18.1.- | COFACTOR: Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000255|HAMAP-Rule:MF_03178}; COFACTOR: Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000255|HAMAP-Rule:MF_03178}; | electron transport chain [GO:0022900]; iron-sulfur cluster assembly [GO:0016226] | cytosol [GO:0005829]; intermediate filament cytoskeleton [GO:0045111]; nucleoplasm [GO:0005654]; perinuclear region of cytoplasm [GO:0048471] | electron transfer activity [GO:0009055]; FAD binding [GO:0071949]; flavin adenine dinucleotide binding [GO:0050660]; FMN binding [GO:0010181]; NADPH binding [GO:0070402]; NADPH-hemoprotein reductase activity [GO:0003958]; oxidoreductase activity [GO:0016491]; oxidoreductase activity, acting on iron-sulfur proteins as d... | PF00667;PF00258;PF00175; | 3.40.50.360;3.40.50.80;2.40.30.10; | NADPH-dependent diflavin oxidoreductase NDOR1 family; Flavodoxin family; Flavoprotein pyridine nucleotide cytochrome reductase family | null | SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000255|HAMAP-Rule:MF_03178}. Note=Concentrated in perinuclear structure. {ECO:0000255|HAMAP-Rule:MF_03178}. | CATALYTIC ACTIVITY: Reaction=NADPH + 2 oxidized [2Fe-2S]-[protein] = H(+) + NADP(+) + 2 reduced [2Fe-2S]-[protein]; Xref=Rhea:RHEA:67716, Rhea:RHEA-COMP:17327, Rhea:RHEA-COMP:17328, ChEBI:CHEBI:15378, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349; Evidence={ECO:0000255|HAMAP-Rule:MF_03178};... | null | null | null | null | FUNCTION: NADPH-dependent reductase which is a central component of the cytosolic iron-sulfur (Fe-S) protein assembly (CIA) machinery. Transfers electrons from NADPH via its FAD and FMN prosthetic groups to the [2Fe-2S] cluster of CIAPIN1, another key component of the CIA machinery. In turn, this reduced cluster provid... | Mus musculus (Mouse) |
A2AI08 | TPRN_MOUSE | MAGLGRLDPGPRTVMPAWKREILERRRAKLAALSGGQGSGAAPDGPNERLVLAESLGPLSQNPFMRLESERRRGTRPAQQLLELYCRVPGVRTIRADNILIIESAPGFPPAVPPAAGIRAAEVVVYEAPQPGRVSRLLEKFDSPAAPCRRGSPERFRPALPQLPVASASAATRTPTNRSLAPASPVRLSQPAPPISPVPVAQRAGQRSACCEPAHPDGTAGPGARRSDFLQKTGSNSFTVHPRGLPRSAVNRSLSNGPMTQESPTGPANGLSGSPPVPGKWKPKVESKEPSLHPPPSPGTPSATSVGPPAFPAPSPASAT... | null | null | auditory receptor cell stereocilium organization [GO:0060088]; sensory perception of sound [GO:0007605]; stereocilium maintenance [GO:0120045] | cytoplasm [GO:0005737]; cytosol [GO:0005829]; microvillus [GO:0005902]; nucleoplasm [GO:0005654]; stereocilium [GO:0032420]; stereocilium base [GO:0120044] | actin binding [GO:0003779]; protein phosphatase 1 binding [GO:0008157]; protein phosphatase binding [GO:0019903]; protein serine/threonine phosphatase inhibitor activity [GO:0004865] | PF13914;PF13916; | null | Taperin family | null | SUBCELLULAR LOCATION: Cell projection, stereocilium {ECO:0000269|PubMed:20170899, ECO:0000269|PubMed:24285636, ECO:0000269|PubMed:30159668, ECO:0000269|PubMed:30380417, ECO:0000269|PubMed:35752427, ECO:0000269|PubMed:37952086}. Cell projection, microvillus {ECO:0000269|PubMed:24285636}. Nucleus, nucleoplasm {ECO:000025... | null | null | null | null | null | FUNCTION: Essential for hearing (PubMed:30380417, PubMed:35752427, PubMed:37952086). Required for maintenance of stereocilia on both inner and outer hair cells (PubMed:27693694). Necessary for the integrity of the stereociliary rootlet (PubMed:30159668). May act as an actin cytoskeleton regulator involved in the regula... | Mus musculus (Mouse) |
A2AIR5 | NMD3A_MOUSE | MRRLSLWWLLSRVCLLLPPPCALVLAGVPSSSSHPQPCQILKRIGHAVRVGAVHLQPWTTAPRAASRAQDGGRAGAQRDEPESGTWRPPAPSQGARWLGSALHGRGPPGSRKLGEGAGTETLWPRDALLFAVENLNRVEGLLPYNLSLEVVMAIEAGLGDLPLMPFSSPSSPWSSDPFSFLQSVCHTVVVQGVSALLAFPQSQGEMMELDLVSSVLHIPVLSIVRHEFPRESQNPLHLQLSLENSLSSDADVTVSILTMNNWYNFSLLLCQEDWNITDFLLLTENNSKFHLESIINITANLSSTKDLLSFLQVQLENIRN... | null | null | calcium ion transport [GO:0006816]; dendrite development [GO:0016358]; ionotropic glutamate receptor signaling pathway [GO:0035235]; modulation of chemical synaptic transmission [GO:0050804]; negative regulation of dendritic spine development [GO:0061000]; prepulse inhibition [GO:0060134]; presynaptic modulation of che... | cytoplasm [GO:0005737]; glutamatergic synapse [GO:0098978]; neuron projection [GO:0043005]; neuronal cell body [GO:0043025]; NMDA selective glutamate receptor complex [GO:0017146]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839]; postsynaptic membrane [GO:0045211]; presynapse [GO:0098793] | calcium channel activity [GO:0005262]; glutamate receptor activity [GO:0008066]; glutamate-gated receptor activity [GO:0004970]; glycine binding [GO:0016594]; identical protein binding [GO:0042802]; NMDA glutamate receptor activity [GO:0004972]; protein phosphatase 2A binding [GO:0051721]; transmitter-gated monoatomic ... | PF00060;PF10613;PF00497; | 3.40.50.2300;3.40.190.10; | Glutamate-gated ion channel (TC 1.A.10.1) family, NR3A/GRIN3A subfamily | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9R1M7}; Multi-pass membrane protein {ECO:0000250|UniProtKB:Q9R1M7}. Postsynaptic cell membrane {ECO:0000250|UniProtKB:Q9R1M7}. Postsynaptic density {ECO:0000250|UniProtKB:Q9R1M7}. Note=Enriched in postsynaptic plasma membrane and postsynaptic densities. Requir... | null | null | null | null | null | FUNCTION: NMDA receptor subtype of glutamate-gated ion channels with reduced single-channel conductance, low calcium permeability and low voltage-dependent sensitivity to magnesium. Mediated by glycine. During the development of neural circuits, plays a role in the synaptic refinement period, restricting spine maturati... | Mus musculus (Mouse) |
A2AIV2 | VIR_MOUSE | MAVDSSMELLFLDTFKHPSAEQSSHIDVVRFPCVVYINEVRVIPPGVRAHSGLPDNRAYGETSPHTFQLDLFFNNVSKPSAPVFDRLGSLEYDENTSIIFRPNSKVNTDGLVLRGWYNCLTLAIYGSVDRVISHDRDSPPPPPPPPPPPQPQPTLKRNLKHADGEKEDQFNGSPPRPQPRGPRTPPGPPPPDDDEDDPMSLPVSGDKEEDVPHREDYFEPISPDRNSVPQEGQYSDEGEVEEEPQEEGEDDEDDVDVEEEEDEDEDDCHTVDSIPDDEEEDEEEEGEEDEEGEGDDGYEQISSDEDGIADLERETFKYPN... | null | null | mRNA alternative polyadenylation [GO:0110104]; mRNA methylation [GO:0080009]; RNA splicing [GO:0008380] | cytoplasm [GO:0005737]; nuclear speck [GO:0016607]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; RNA N6-methyladenosine methyltransferase complex [GO:0036396] | RNA binding [GO:0003723] | PF15912; | null | Vir family | null | SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000250|UniProtKB:Q69YN4}. Nucleus, nucleoplasm {ECO:0000269|PubMed:29547716}. Cytoplasm {ECO:0000269|PubMed:29547716}. Note=Mainly nuclear with some fraction located in the cytoplasm (PubMed:29547716). ZC3H13 is required to anchor component of the MACOM subcomplex, such as VI... | null | null | null | null | null | FUNCTION: Associated component of the WMM complex, a complex that mediates N6-methyladenosine (m6A) methylation of RNAs, a modification that plays a role in the efficiency of mRNA splicing and RNA processing. Acts as a key regulator of m6A methylation by promoting m6A methylation of mRNAs in the 3'-UTR near the stop co... | Mus musculus (Mouse) |
A2AIV8 | CARD9_MOUSE | MSDYENDDECWSTLESFRVKLISVIDPSRITPYLRQCKVLNPDDEEQVLSDPNLVIRKRKVGVLLDILQRTGHKGYVAFLESLELYYPQLYRKVTGKEPARVFSMIIDASGESGLTQLLMTEVMKLQKKVQDLTALLSSKDDFIKELRVKDSLLRKHQERVQRLKEECELSSAELKRCKDENYELAMCLAHLSEEKGAALMRNRDLQLEVDRLRHSLMKAEDDCKVERKHTLKLRHAMEQRPSQELLWELQQEKDLLQARVQELQVSVQEGKLDRNSPYIQVLEEDWRQALQEHQKQVSTIFSLRKDLRQAETLRARCTE... | null | null | antifungal innate immune response [GO:0061760]; defense response to Gram-positive bacterium [GO:0050830]; defense response to virus [GO:0051607]; host-mediated regulation of intestinal microbiota composition [GO:0048874]; immunoglobulin mediated immune response [GO:0016064]; JNK cascade [GO:0007254]; neutrophil mediate... | CBM complex [GO:0032449]; cytoplasm [GO:0005737]; cytosol [GO:0005829] | CARD domain binding [GO:0050700]; metal ion binding [GO:0046872]; protein homodimerization activity [GO:0042803]; protein self-association [GO:0043621] | PF00619; | 1.10.533.10; | null | PTM: Phosphorylated at Thr-231 by PRKCD downstream of C-type lectin receptors activation: phosphorylation promotes interaction with BCL10, followed by activation of NF-kappa-B and MAP kinase p38 pathways (PubMed:22265677). Phosphorylated at Thr-531 and Thr-531 by CK2 following interaction with VHL, leading to inhibit t... | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9H257}. | null | null | null | null | null | FUNCTION: Adapter protein that plays a key role in innate immune response against fungi by forming signaling complexes downstream of C-type lectin receptors (PubMed:16862125, PubMed:20538615, PubMed:26679537, PubMed:29080677). CARD9-mediated signals are essential for antifungal immunity against a subset of fungi from t... | Mus musculus (Mouse) |
A2AIW0 | ENTR1_MOUSE | MSGYARRQGAPPLSRTRSLVVPDAPAFYERRSCLPQLDCERPHGGDLHPHLFGFRPTFMCYVPSPVLASVGDTGFGYGKGKCTNQGPSGAPETRFGGDKLEDLEEANPFSFKEFLKTKNLSLSKEDTTTSRIYPKEASRHPLGLEHSSPASQLMGYGLESQQPFFEDPTRASNLEEDEDDGWNITYLPSAVDQTHSSRDTQDSPPCDTYLSFFSNSSELACPESLPPWTLSDTDSRISPASPAGSPNADFAAHEESLGDRHLRTLQISYEALKDENSKLRRKLNEVQSFSETQTEMVRTLERKLEAKMIKEESDFHDLES... | null | null | cell cycle [GO:0007049]; cell division [GO:0051301]; cell projection organization [GO:0030030]; endocytic recycling [GO:0032456]; positive regulation of cilium assembly [GO:0045724]; positive regulation of protein localization to cilium [GO:1903566]; protein transport [GO:0015031]; regulation of cytokinesis [GO:0032465... | centrosome [GO:0005813]; ciliary basal body [GO:0036064]; early endosome [GO:0005769]; midbody [GO:0030496]; recycling endosome [GO:0055037]; retromer complex [GO:0030904] | null | null | null | ENTR1 family | PTM: Phosphorylated. {ECO:0000250|UniProtKB:Q96C92}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16332174}. Early endosome {ECO:0000250|UniProtKB:Q96C92}. Endosome {ECO:0000250|UniProtKB:Q96C92}. Recycling endosome {ECO:0000250|UniProtKB:Q96C92}. Midbody {ECO:0000250|UniProtKB:Q96C92}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:000025... | null | null | null | null | null | FUNCTION: May be involved in modulation of TNF response. May be involved in presentation of TNFRSF1A on the cell surface (PubMed:16332174). Involved in the endosome-to-plasma membrane trafficking and recycling of SNX27-retromer-dependent cargo proteins, such as GLUT1. Involved in the regulation of cytokinesis; the func... | Mus musculus (Mouse) |
A2AJ15 | MA1B1_MOUSE | MYPPPAPPPAPHRDFISVTLSLGESYDNSKSRRRRSCWRKWKQLSRLQRNVILFVLGFLILCGFLYSLHTADQWKALSGRPAEVEKMKQEVLPVLPAPQKESAEQEGFADILSQKRQRHFRRGPPHLQIRPPNTVSKDGMQDDAKEREAALGKAQQEENTQRTVISWRGAVIEPEQATELPYKRAEASIKPLVLASKIWKEPAPPNERQKGVIEAFLHAWKGYQKFAWGHDELKPVSKTFSEWFGLGLTLIDALDTMWILGLKQEFKQARKWVSENLDFQKNVDVNLFESTIRILGGLLSTYHLSGDSLFLTKAEDFGKR... | 3.2.1.113 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250|UniProtKB:P45700}; | carbohydrate metabolic process [GO:0005975]; ERAD pathway [GO:0036503]; mannoprotein catabolic process [GO:0006058]; protein glycosylation [GO:0006486] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; endoplasmic reticulum quality control compartment [GO:0044322]; endosome [GO:0005768]; membrane [GO:0016020]; trans-Golgi network [GO:0005802] | calcium ion binding [GO:0005509]; mannosyl-oligosaccharide 1,2-alpha-mannosidase activity [GO:0004571] | PF01532; | 1.50.10.10; | Glycosyl hydrolase 47 family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type II membrane protein. | CATALYTIC ACTIVITY: Reaction=4 H2O + N(4)-(alpha-D-Man-(1->2)-alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-(1->2)-alpha-D-Man-(1->6)]-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc)-L-asparaginyl-[protein] (N-glucan mannose isomer 9A1,2,3B1,2,3) = 4... | null | PATHWAY: Protein modification; protein glycosylation. {ECO:0000250|UniProtKB:P32906}. | null | null | FUNCTION: Involved in glycoprotein quality control targeting of misfolded glycoproteins for degradation. It primarily trims a single alpha-1,2-linked mannose residue from Man(9)GlcNAc(2) to produce Man(8)GlcNAc(2), but at high enzyme concentrations, as found in the ER quality control compartment (ERQC), it further trim... | Mus musculus (Mouse) |
A2AJ76 | HMCN2_MOUSE | MTPGAQLLPLLVAISTAVAAVVTSDAPTKTLSPATGDATLAFVFDVTGSMWDDLMQVIDGASRILERSLSSRSRVIANYALVPFHDPDIGPVTLTADPVVFQRELRELYVQGGGDCPEMSVGAIKAAVEVANPGSFIYVFSDARAKDYHKKKELLQLLQLKQSQVVFVLTGDCGDRTHPGYLVFEEIASTSSGQVFQLDKQQVSEVLKWVESAIQASKVHLLSADHEEEGEHTWRIPFDPSLKEVTIALSGPGPEIEVRDPLGRVLQTDEGLNVLLNIPDSAKVVAFKPEHPGLWAIKVYSSGRHSVRISGISNINFRAG... | null | null | homophilic cell adhesion via plasma membrane adhesion molecules [GO:0007156]; response to stimulus [GO:0050896]; synapse organization [GO:0050808] | axon [GO:0030424]; basement membrane [GO:0005604]; cell cortex [GO:0005938]; cell junction [GO:0030054]; cleavage furrow [GO:0032154]; collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886] | axon guidance receptor activity [GO:0008046]; calcium ion binding [GO:0005509] | PF12662;PF07645;PF07474;PF07679;PF13927; | 2.40.155.10;2.60.40.10;2.10.25.10;3.40.50.410; | null | PTM: Reported to be phosphorylated; however as this position is extracellular, the in vivo relevance is unsure. | SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:17015624}. Cleavage furrow {ECO:0000269|PubMed:21215633}. Note=The antibody used in PubMed:17015624 and PubMed:21215633 to determine subcellular location does not distinguish between HMCN1 and HMCN2. {ECO:0000269|PubMed:170156... | null | null | null | null | null | null | Mus musculus (Mouse) |
A2AJ77 | PRD12_MOUSE | MMGSVLPAEALVLKTGLKAPGLALAEVITSDILHSFLYGRWRNVLGEQLLEDKSHHASPKTAFTAEVLAQSFSGEVQKLSSLVLPVEVIIAQSSIPGEGLGIFSKTWIKAGTEMGPFTGRVIAPEHVDICKNNNLMWEVFNEDGTVRYFIDASQEDHRSWMTYIKCARNEQEQNLEVVQIGTSIFYKAIEMIPPDQELLVWYGNSHNTFLGIPGVPGLEEEQKKNKHEDFHPADSATGTAGRMRCVICHRGFNSRSNLRSHMRIHTLDKPFVCRFCNRRFSQSSTLRNHVRLHTGERPYKCQVCQSAYSQLAGLRAHQKS... | 2.1.1.- | null | detection of temperature stimulus involved in sensory perception of pain [GO:0050965]; methylation [GO:0032259]; negative regulation of transcription by RNA polymerase II [GO:0000122]; neurogenesis [GO:0022008]; neuron projection development [GO:0031175]; regulation of gene expression [GO:0010468]; sensory perception o... | nucleoplasm [GO:0005654]; nucleus [GO:0005634] | DNA binding [GO:0003677]; histone chaperone activity [GO:0140713]; histone methyltransferase binding [GO:1990226]; metal ion binding [GO:0046872]; methyltransferase activity [GO:0008168] | PF21549;PF00096; | 3.30.160.60;2.170.270.10; | Class V-like SAM-binding methyltransferase superfamily | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9H4Q4}. | null | null | null | null | null | FUNCTION: Involved in the positive regulation of histone H3-K9 dimethylation. {ECO:0000269|PubMed:26005867}. | Mus musculus (Mouse) |
A2AJ88 | PLPL7_MOUSE | MQNEEDACLEAGYCLGTTLSSWRLHFMEEQSQSTMLMGIGIGALLTLAFVGITFFFVYRRVRRLRRAEPTPQYRFRKRDKVMFYGRKIMRKVTTLPHTLVGNTSAPRQRVRKRTKVLSLAKRILRFKKEYPTLQPKEPPPSLLEADLTEFDVKNSHLPSEVLYMLKNVRVLGHFEKPLFLELCKHMVFVQLQEGEHVFQPGEPDISIYVVQDGRLEVCIQDADGTEVVVKEVLPGDSVHSLLSILDVITGHTAPYKTVSARAAVSSTVLWLPAAAFQGVFEKYPETLVRVVQIIMVRLQRVTFLALHNYLGLTTELFNPE... | 3.1.1.-; 3.1.1.5 | null | phosphatidylcholine catabolic process [GO:0034638] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; lipid droplet [GO:0005811] | lysophospholipase activity [GO:0004622]; phosphatidyl phospholipase B activity [GO:0102545] | PF00027;PF01734; | 3.40.1090.10;2.60.120.10; | NTE family | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:18086666, ECO:0000269|PubMed:28887301}; Single-pass type III membrane protein {ECO:0000269|PubMed:28887301}. Lipid droplet {ECO:0000269|PubMed:18086666, ECO:0000269|PubMed:28887301}.; SUBCELLULAR LOCATION: [Isoform 1]: Endoplasmic reticulum membra... | CATALYTIC ACTIVITY: Reaction=a 1-acyl-sn-glycero-3-phosphocholine + H2O = a fatty acid + H(+) + sn-glycerol 3-phosphocholine; Xref=Rhea:RHEA:15177, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16870, ChEBI:CHEBI:28868, ChEBI:CHEBI:58168; EC=3.1.1.5; Evidence={ECO:0000269|PubMed:18086666, ECO:0000269|PubMed:2888730... | null | null | BIOPHYSICOCHEMICAL PROPERTIES: pH dependence: Optimum pH is 8.5. {ECO:0000269|PubMed:18086666}; | null | FUNCTION: Lysophospholipase which preferentially deacylates unsaturated lysophosphatidylcholine (C18:1), generating glycerophosphocholine (PubMed:18086666, PubMed:28887301). Can also deacylate, to a lesser extent, lysophosphatidylethanolamine (C18:1), lysophosphatidyl-L-serine (C18:1) and lysophosphatidic acid (C16:0) ... | Mus musculus (Mouse) |
A2AJB7 | LCN5_MOUSE | MCSVARHMESIMLFTLLGLCVGLAAGTEAAVVKDFDVNKFLGFWYEIALASKMGAYGLAHKEEKMGAMVVELKENLLALTTTYYNEGHCVLEKVAATQVDGSAKYKVTRISGEKEVVVVATDYMTYTVIDITSLVAGAVHRAMKLYSRSLDNNGEALNNFQKIALKHGFSETDIHILKHDLTCVNALQSGQI | null | null | retinoic acid metabolic process [GO:0042573] | extracellular space [GO:0005615] | retinoid binding [GO:0005501]; small molecule binding [GO:0036094] | PF00061; | 2.40.128.20; | Calycin superfamily, Lipocalin family | PTM: 2 different forms with differently processed N-termini exist. | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1591332, ECO:0000269|PubMed:2393684}. Note=Synthesized by the mid and distal caput of the epididymis and secreted into the epididymal lumen. {ECO:0000269|PubMed:1591332, ECO:0000269|PubMed:2393684}. | null | null | null | null | null | FUNCTION: Associates with spermatozoa in the epididymal fluid but does not bind tightly to them. Binds both all-trans and 13-cis retinoic acid. May act as a retinoid carrier protein which is required for epididymal function and/or sperm maturation. {ECO:0000269|PubMed:1591332, ECO:0000269|PubMed:1591333}. | Mus musculus (Mouse) |
A2AJK6 | CHD7_MOUSE | MADPGMMSLFGEDGSLFSEGLEGLGECGYPENPVNPMGQQMPIDQGFPSLQPSLHHPSPNQNQTKLTHFDHYSQYEQKMHLMDQPNRMMGSAPGNGLASPHSQYHTPPVPQVPHGGGGGGQMGVYPGIQNERHGQSFVDGGSMWGPRAVQVPDQIRAPYQQQQPQPAPSGPPAQGHPQHMQQMGSYLARGDFSMQQHGQPQQRMGQFSQGQEGLSQGSPFIATSGPGHLSHMPQQSPSMAPSLRHPVQQQFHHHPAALHGESVAHSPRFSPNPPQQGAVRPQTLNFSSRNQTVPSPTVNNSGQYSRYPYSNLNQGLVNST... | 3.6.4.12 | null | adult heart development [GO:0007512]; adult walking behavior [GO:0007628]; aorta development [GO:0035904]; aorta morphogenesis [GO:0035909]; artery morphogenesis [GO:0048844]; atrioventricular canal development [GO:0036302]; blood circulation [GO:0008015]; blood vessel development [GO:0001568]; blood vessel remodeling ... | chromatin [GO:0000785]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | ATP binding [GO:0005524]; ATP hydrolysis activity [GO:0016887]; ATP-dependent chromatin remodeler activity [GO:0140658]; chromatin binding [GO:0003682]; DNA binding [GO:0003677]; helicase activity [GO:0004386]; histone binding [GO:0042393]; promoter-specific chromatin binding [GO:1990841]; RNA polymerase II cis-regulat... | PF07533;PF00385;PF00271;PF00176; | 2.40.50.40;3.40.5.120;1.10.10.60;3.40.50.300;3.40.50.10810; | SNF2/RAD54 helicase family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9P2D1}. | CATALYTIC ACTIVITY: Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; | null | null | null | null | FUNCTION: Probable transcription regulator. Maybe involved in the in 45S precursor rRNA production (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
A2AJN7 | S4A11_MOUSE | MSQNEHCQDSGEYFSAGTQGYFKNNMEDNLEVREDSLGDEVFDTVNSSIVSGESIRFFVNVNLEVQPSKSDLEAATGGCVLLHTSRKYLKLKNFEEEVRAHRDLDGFLAQASIILNETATSLDDVLRTMLNRFALDPNHAEPDCDLDLLMAKLFTDAGAPMESKVHLLSDTIQGVTATVRGVQYEQSWLCIICTMKTLQKRHVCISRLVRPQNWGENSCEVRFVILVLAPPKMKSTKTAMEVARTFATMFSDITFRQKLLKTRTEEEFKEALVHQRQLLTMMMPRAAGHSMSSLHTHRHPQPPKCKDFFPFGKGIWMDIM... | null | null | cellular hypotonic response [GO:0071476]; cellular response to oxidative stress [GO:0034599]; fluid transport [GO:0042044]; intracellular monoatomic cation homeostasis [GO:0030003]; monoatomic anion transport [GO:0006820]; monoatomic ion homeostasis [GO:0050801]; regulation of mesenchymal stem cell differentiation [GO:... | apical plasma membrane [GO:0016324]; basolateral plasma membrane [GO:0016323]; plasma membrane [GO:0005886]; vesicle membrane [GO:0012506] | active borate transmembrane transporter activity [GO:0046715]; bicarbonate transmembrane transporter activity [GO:0015106]; borate efflux transmembrane transporter activity [GO:0080139]; protein dimerization activity [GO:0046983]; proton channel activity [GO:0015252]; proton transmembrane transporter activity [GO:00150... | PF00955; | 1.10.287.570; | Anion exchanger (TC 2.A.31) family | PTM: Glycosylated. {ECO:0000250|UniProtKB:Q8NBS3}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q8NBS3}; Multi-pass membrane protein {ECO:0000255}. Basolateral cell membrane {ECO:0000250|UniProtKB:Q8NBS3}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=2 Na(+)(in) + tetrahydroxoborate(in) = 2 Na(+)(out) + tetrahydroxoborate(out); Xref=Rhea:RHEA:66816, ChEBI:CHEBI:29101, ChEBI:CHEBI:41132; Evidence={ECO:0000250|UniProtKB:Q8NBS3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66817; Evidence={ECO:0000250|UniProtKB:Q8NBS3}; | null | null | null | null | FUNCTION: Multifunctional transporter with an impact in cell morphology and differentiation (PubMed:20185830). In the presence of borate B(OH)4(-), acts as a voltage-dependent electrogenic Na(+)-coupled B(OH)4(-) cotransporter controlling boron homeostasis (By similarity). At early stages of stem cell differentiation, ... | Mus musculus (Mouse) |
A2AJX4 | MALR1_MOUSE | MFLPKAAVSAFSMHGSLCFLWTVCLSISPLSQQGVQAFQCSNGVSLPSDYVCDFTDHCGDNSEEQQCWSYGRCNFEDRLCSMTEDQTLQPGWTRRSGIISNSPPFWDHNGNISAHFLALVSRVDSISSNLRSRIFLPTNDQQVCQITFYNFSSNQNGKLIAGLQTLCGDPIEHLWQKTEILQSRWERNVITVQSSQQFQVIFQAQMLATHGQEEVIAIDDISFSSGCLPADVCQTCGFDLDTCGLATEASAGRTSWMCTKVREIPSLDSVPWQDQRGHDEGSFVWMRAGHASVSRLVESSAYLNSSVCHCMDGNCRLQFN... | null | null | cholesterol homeostasis [GO:0042632]; negative regulation of bile acid biosynthetic process [GO:0070858] | cytoplasm [GO:0005737]; cytoplasmic vesicle membrane [GO:0030659]; Golgi apparatus [GO:0005794] | null | PF00057;PF00629; | 2.60.120.200;2.10.25.10;4.10.400.10; | null | null | SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:23747249}; Single-pass type I membrane protein {ECO:0000255}. | null | null | null | null | null | FUNCTION: Enhances production and/or transport of FGF15 and thus has a role in regulation of bile acid synthesis. {ECO:0000269|PubMed:23747249}. | Mus musculus (Mouse) |
A2AKK5 | ACNT1_MOUSE | MMIKLIATPSNALVDEPVSIRATGLPPSQIVTIKATVKDENDNVFQSQAFYKTNEAGEVDLEKTPALGGDYVGVHPMGLFFSLKPKKAFHRLMKKDVMNSPFCICLDLYDSVNWLETVRIPSKASQRVQRWFVGPGVKREQIQEGRVRGALFLPPGKGPFPGIIDLFGVIGGLVEFRASLLASHGFAVLALAYFAYKDLPEKLQEVDLEYFEEAANFLLSHPKIQQPGIGVISTSKGAEIGLAMACYLKQVIATVCINGATTTTAVPLRYQDLVVTPIQQALERMEVHVSGAVCFRHTTQYLQNKNILPVEKAQGKILFI... | 2.3.1.- | null | acyl-CoA metabolic process [GO:0006637]; fatty acid metabolic process [GO:0006631] | peroxisome [GO:0005777] | fatty acyl-CoA hydrolase activity [GO:0047617]; N-acyltransferase activity [GO:0016410] | PF08840;PF04775; | 2.60.40.2240;3.40.50.1820; | C/M/P thioester hydrolase family | null | SUBCELLULAR LOCATION: Peroxisome {ECO:0000269|PubMed:17116739}. | CATALYTIC ACTIVITY: Reaction=taurine + tetracosanoyl-CoA = CoA + H(+) + N-tetracosanoyl-taurine; Xref=Rhea:RHEA:50120, ChEBI:CHEBI:15378, ChEBI:CHEBI:57287, ChEBI:CHEBI:65052, ChEBI:CHEBI:132049, ChEBI:CHEBI:507393; Evidence={ECO:0000269|PubMed:17116739}; CATALYTIC ACTIVITY: Reaction=eicosanoyl-CoA + taurine = CoA + H(... | BIOPHYSICOCHEMICAL PROPERTIES: Kinetic parameters: KM=11 uM for C16:0-coenzyme A {ECO:0000269|PubMed:17116739}; Vmax=159.5 nmol/min/mg enzyme {ECO:0000269|PubMed:17116739}; | null | null | null | FUNCTION: Acyltransferase which efficiently conjugates very long-chain and long-chain fatty acids to taurine (PubMed:17116739). Shows no conjugation activity in the presence of glycine (PubMed:17116739). {ECO:0000269|PubMed:17116739}. | Mus musculus (Mouse) |
A2AKQ0 | S35D1_MOUSE | MAEVHRRQHAPVKGEAPAKSSTHRDEEELGMAPAETLTVFLKLLAAGFYGVSSFLIVVVNKSVLTNYRFPSSLCVGLGQMVATVAVLWVGKTLRVVKFPDFDRNVPRKTFPLPLLYFGNQITGLFSTKKLNLPMFTVLRRFSILFTMFAEGALLKKTFSWGIKMTVFAMIIGAFVAASSDLAFDLEGYVFILINDVLTAANGAYVKQKLDSKELGKYGLLYYNALFMILPTLAIAYFTGDAQKAMEFEGWADTLFLLQFTLSCVMGFILMYATVLCTQYNSALTTTIVGCIKNILITYIGMVFGGDYIFTWTNFIGLNIS... | null | null | chondroitin sulfate biosynthetic process [GO:0030206]; embryonic skeletal system development [GO:0048706]; pyrimidine nucleotide-sugar transmembrane transport [GO:0090481] | endoplasmic reticulum [GO:0005783]; endoplasmic reticulum membrane [GO:0005789]; Golgi apparatus [GO:0005794] | antiporter activity [GO:0015297]; GDP-fucose transmembrane transporter activity [GO:0005457]; pyrimidine nucleotide-sugar transmembrane transporter activity [GO:0015165]; UDP-glucuronic acid transmembrane transporter activity [GO:0005461]; UDP-N-acetylgalactosamine transmembrane transporter activity [GO:0005463]; UDP-N... | PF03151; | null | TPT transporter family, SLC35D subfamily | null | SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:17952091}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=UDP-alpha-D-glucuronate(out) + UDP-N-acetyl-alpha-D-glucosamine(in) = UDP-alpha-D-glucuronate(in) + UDP-N-acetyl-alpha-D-glucosamine(out); Xref=Rhea:RHEA:73703, ChEBI:CHEBI:57705, ChEBI:CHEBI:58052; Evidence={ECO:0000250|UniProtKB:Q9NTN3}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHE... | null | null | null | null | FUNCTION: Antiporter that transports nucleotide sugars across the endoplasmic reticulum (ER) membrane in exchange for either their cognate nucleoside monophosphate or another nucleotide sugar (By similarity). Transports various UDP-sugars including UDP-N-acetyl-alpha-D-glucosamine (UDP-GlcNAc), UDP-N-acetyl-alpha-D-gal... | Mus musculus (Mouse) |
A2AKX3 | SETX_MOUSE | MSTCCWCTPGGSSTIDVLKRYASSTGSSEFQTADEDLCYCLECVAEYHRARDEVPFLHEVLWELETLRLVSHFEKSMKAEAEDDDDLYIVDNNGEEQLFDCSGQDFENKLRVPLFEILKYPYLLLHERVNELCVEALCRMEQNNCSFQVFDKYPGIYLFLVHPNEMVRRWAILTARNLGKVDRDDYYDLQEVLTCLFKVIELGLLESPDIYTSSVLEKGKLILLPAHMYDTTNYKNYWLGICMLLTILEEQAMDSLLLGSDKQNDFMQSILHTMEKQSDDDSMDPFWPALHCFMVILDRLGSKVWGQLIDPIEAFQTIIN... | 3.6.4.- | null | cell differentiation [GO:0030154]; cellular response to fibroblast growth factor stimulus [GO:0044344]; cellular response to hydrogen peroxide [GO:0070301]; cellular response to oxidative stress [GO:0034599]; cellular response to retinoic acid [GO:0071300]; circadian rhythm [GO:0007623]; DNA damage response [GO:0006974... | axon [GO:0030424]; chromosome, telomeric region [GO:0000781]; cytoplasm [GO:0005737]; growth cone [GO:0030426]; intercellular bridge [GO:0045171]; nuclear body [GO:0016604]; nuclear chromosome [GO:0000228]; nucleolus [GO:0005730]; nucleoplasm [GO:0005654]; nucleus [GO:0005634] | ATP binding [GO:0005524]; helicase activity [GO:0004386]; hydrolase activity [GO:0016787]; identical protein binding [GO:0042802]; RNA binding [GO:0003723]; transcription termination site sequence-specific DNA binding [GO:0001147] | PF13086;PF13087; | 3.40.50.300; | DNA2/NAM7 helicase family | PTM: Ubiquitinated. {ECO:0000250|UniProtKB:Q7Z333}.; PTM: Sumoylated preferentially with SUMO2 or SUMO3. {ECO:0000250|UniProtKB:Q7Z333}. | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q7Z333}. Nucleus, nucleoplasm {ECO:0000269|PubMed:16644229}. Nucleus, nucleolus {ECO:0000269|PubMed:16644229}. Cytoplasm {ECO:0000269|PubMed:16644229}. Chromosome {ECO:0000269|PubMed:23593030}. Chromosome, telomere {ECO:0000250|UniProtKB:Q7Z333}. Cell projection, axo... | null | null | null | null | null | FUNCTION: Probable RNA/DNA helicase involved in diverse aspects of RNA metabolism and genomic integrity. Plays a role in transcription regulation by its ability to modulate RNA Polymerase II (Pol II) binding to chromatin and through its interaction with proteins involved in transcription. Contributes to the mRNA splici... | Mus musculus (Mouse) |
A2AL36 | CNTRL_MOUSE | MKKGSERRLSKAKMPLSSHFPGPSSLRSSMRSRSLSPLIGSETQPLHPGGQWPAQAELTDESTVPLEPQQRKGAESYVGVRYITEALIKKLTKQDNLALVKSLNLSLSKDGGKKFRYIENLEKCVKLEVLNLSYNLIVKIEKVDKLLRLRELNLSYNKISKIEGLENMCNLQKLNLAGNEIEHIPVWFAKKLKSLRVLNLKGNKISSLQDVSKLKPLQDLTSLVLIDNPVVALPHYLQFIIFHLRSLESLEGQPVTTQDRQEAFERFSLEEIERLEKDLEKKTVETEELKNKQTKFLEEIKNQDKLNKSLKEEAMLQKQS... | null | null | aorta development [GO:0035904]; axoneme assembly [GO:0035082]; cardiac septum development [GO:0003279]; cell cycle [GO:0007049]; coronary vasculature development [GO:0060976]; female germ-line stem cell asymmetric division [GO:0048132]; kidney development [GO:0001822]; ventricular septum development [GO:0003281] | axoneme [GO:0005930]; centriolar satellite [GO:0034451]; centriolar subdistal appendage [GO:0120103]; centrosome [GO:0005813]; cytosol [GO:0005829]; Flemming body [GO:0090543]; meiotic spindle [GO:0072687]; meiotic spindle pole [GO:0090619]; mitotic spindle pole [GO:0097431]; perinuclear region of cytoplasm [GO:0048471... | dynein complex binding [GO:0070840] | PF14580; | 3.80.10.10; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q7Z7A1}. Midbody, Midbody ring {ECO:0000250|UniProtKB:Q7Z7A1}. | null | null | null | null | null | FUNCTION: Involved in cell cycle progression and cytokinesis. During the late steps of cytokinesis, anchors exocyst and SNARE complexes at the midbody, thereby allowing secretory vesicle-mediated abscission (By similarity). {ECO:0000250}. | Mus musculus (Mouse) |
A2ALS5 | RPGP1_MOUSE | MIEKMQGSRMDEQRCSFPPPLKTEEDYIPYPSVHEVLGREGPFPLILLPQFGGYWIEGTNHEISSLPETEPLQSPTTKVKLECNPTARIYRKHFLGKEHFNYYSLDTALGHLVFSLKYDVIGDQEHLRLLLRTKCRTHHDVIPISCLTEFPNVVQMAKLVCEDVNVDRFYPVLYPKASRLIVTFDEHVISNNFKFGVIYQKLGQTSEEELFSTNEESPAFVEFLEFLGQKVKLQDFKGFRGGLDVTHGQTGTESVYCNFRNKEIMFHVSTKLPYTEGDAQQLQRKRHIGNDIVAVVFQDENTPFVPDMIASNFLHAYVVV... | null | null | cell-cell adhesion [GO:0098609]; cellular response to glial cell derived neurotrophic factor [GO:1990792]; establishment of localization in cell [GO:0051649]; negative regulation of neuron differentiation [GO:0045665]; negative regulation of thyroid gland epithelial cell proliferation [GO:1904442]; phagocytosis [GO:000... | axon [GO:0030424]; cytoplasm [GO:0005737]; dendrite [GO:0030425]; early endosome [GO:0005769]; Golgi membrane [GO:0000139]; membrane [GO:0016020]; neuronal cell body [GO:0043025] | GTPase activator activity [GO:0005096] | PF02188;PF21022;PF02145; | 6.10.140.210;3.40.50.11210; | null | null | SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}. | null | null | null | null | null | FUNCTION: GTPase activator for the nuclear Ras-related regulatory protein RAP-1A (KREV-1), converting it to the putatively inactive GDP-bound state. {ECO:0000250}. | Mus musculus (Mouse) |
A2ALU4 | SHRM2_MOUSE | MEGAEPRARPERLAEAEAPATDGVRLVEVQLSGGAPWGFTLKGGREHGEPLVITKIEEGSKAAAVDKLLAGDEIVAINDVSLSGFRQEAICLVKGSHKTLKLVVKRKSDPSWRPHSWHATKYFDVHPEPAASLFLNTSGSPSWKSQHQASSSSHDLSGSWEHTSLQRTSDHFSSMGSIDSLDHSSQLYPSGHLSSAKSNSSIDHLGGHSKRDSAYGSFSTCSSTPDHTLPKADASSTENILYKVGLWEASRPGSSRQSQSTGDPQGLQDRPSCFIPRVPGNSSKSPRPEDNVEPKIATHGRSNFGPVWYVPDKKKAPSPP... | null | null | actin filament organization [GO:0007015]; apical protein localization [GO:0045176]; brain development [GO:0007420]; camera-type eye development [GO:0043010]; camera-type eye morphogenesis [GO:0048593]; cell migration [GO:0016477]; cell-cell junction maintenance [GO:0045217]; cellular pigment accumulation [GO:0043482]; ... | adherens junction [GO:0005912]; apical junction complex [GO:0043296]; apical plasma membrane [GO:0016324]; bicellular tight junction [GO:0005923]; cell cortex [GO:0005938]; cell-cell junction [GO:0005911]; cortical actin cytoskeleton [GO:0030864]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; microtubule [GO:00058... | actin binding [GO:0003779]; actin filament binding [GO:0051015]; beta-catenin binding [GO:0008013]; protein domain specific binding [GO:0019904] | PF08688;PF08687;PF00595; | 2.30.42.10;6.10.250.3120; | Shroom family | null | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:16684770}. Cell junction, tight junction {ECO:0000269|PubMed:16684770}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:16684770}. Note=Associates with cortical F-actin. | null | null | null | null | null | FUNCTION: May be involved in endothelial cell morphology changes during cell spreading. In the retinal pigment epithelium, may regulate the biogenesis of melanosomes and promote their association with the apical cell surface by inducing gamma-tubulin redistribution. {ECO:0000269|PubMed:16684770, ECO:0000269|PubMed:1698... | Mus musculus (Mouse) |
A2ALV5 | SHOC1_MOUSE | MALNGRTMFPAFKYYAIDYLQEDIIKERLYRDALLLQIPSCLNQDKNIIDDKYRTPWTRAIPVQEMEDNSVLEQWRTRFCVEGVPEKKTVTGVMINGTFEEIVPSSNPNSPPGIENDKLFPSKDYVDDFIPVKCSLYYPGVKAEHQGLLIDEEMIFMNKAMDNHLPTVNGLLSRLKLYLVKDPFLDFKEELSGKDNFTEYFSVQECSEPFVRDFHMAEETFCKKKLPSVFPSGFKSLISTNPKQEILILPPSKLKKPLNSIPKIMDSVDESECFKGDITSKHEFDTEDIKCNSTENLTFASLCEPECSEPGDLEMPPTHL... | 3.6.-.- | null | reciprocal meiotic recombination [GO:0007131]; resolution of meiotic recombination intermediates [GO:0000712]; synaptonemal complex assembly [GO:0007130] | chromosome [GO:0005694]; condensed nuclear chromosome [GO:0000794] | ATP hydrolysis activity [GO:0016887]; single-stranded DNA binding [GO:0003697] | PF17825; | null | XPF family | null | SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:29742103, ECO:0000269|PubMed:30272023, ECO:0000269|PubMed:30746471}. Note=Localizes to meiotic chromosomes; associates with mid-stage meiotic recombination intermediates (PubMed:29742103). Localization requires meiotic double-strand breaks (DSBs) recombination interm... | null | null | null | null | null | FUNCTION: ATPase required during meiosis for the formation of crossover recombination intermediates (PubMed:29742103). Binds DNA: preferentially binds to single-stranded DNA and DNA branched structures (By similarity). Does not show nuclease activity in vitro, but shows ATPase activity, which is stimulated by the prese... | Mus musculus (Mouse) |
A2AM29 | AF9_MOUSE | MASSCAVQVKLELGHRAQVRKKPTVEGFTHDWMVFVRGPEHSNIQHFVEKVVFHLHESFPRPKRVCKDPPYKVEESGYAGFILPIEVYFKNKEEPKKVRFDYDLFLHLEGHPPVNHLRCEKLTFNNPTEDFRRKLLKAGGDPNRSIHTSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSSTSFSKPHKLMKEHKEKPSKDSREHKSAFKEPSRDHNKSSKDSSKKPKENKPLKEEKIVPKMAFKEPKPMSKEPKADSNLLTVTSGQQDKKAPSKRPPASDSEELSAKKRKKSSSEALFKSFSSAPPLILT... | null | null | anterior/posterior pattern specification [GO:0009952]; gene expression [GO:0010467]; hematopoietic stem cell differentiation [GO:0060218]; negative regulation of canonical Wnt signaling pathway [GO:0090090]; positive regulation of DNA-templated transcription [GO:0045893]; positive regulation of Wnt signaling pathway, p... | chromosome [GO:0005694]; cytosol [GO:0005829]; nucleus [GO:0005634]; transcription elongation factor complex [GO:0008023] | chromatin binding [GO:0003682]; DNA binding [GO:0003677]; histone binding [GO:0042393]; lysine-acetylated histone binding [GO:0070577]; modification-dependent protein binding [GO:0140030] | PF17793;PF03366; | 1.20.1270.290;2.60.40.1970; | null | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00376, ECO:0000269|PubMed:11439343}. Chromosome {ECO:0000250|UniProtKB:P42568}. Note=Colocalizes with acylated histone H3. H3 Colocalizes with histone H3 crotonylated at 'Lys-18' (H3K18cr). {ECO:0000250|UniProtKB:P42568}. | null | null | null | null | null | FUNCTION: Chromatin reader component of the super elongation complex (SEC), a complex required to increase the catalytic rate of RNA polymerase II transcription by suppressing transient pausing by the polymerase at multiple sites along the DNA. Specifically recognizes and binds acylated histone H3, with a preference fo... | Mus musculus (Mouse) |
A2AMM0 | CAVN4_MOUSE | MEHNGSASNAGKIHQNRLSSVTEDEDQDAALTIVTVLDRVASVVDSVQASQKRIEERHREMGNAIKSVQIDLLKLSQSHSNTGYVVNKLFEKTRKVSAHIKDVKARVEKQQVRVTKVETKQEEIMKKNKFRVVIFQEDIPCPASLSVVKDRSLPENQEEAEEVFDPPIELSSDEEYYVEESRSARLRKSGKEHIDHIKKAFSRENMQKTRQTLDKKVSGIRTRIVTPERRERLRQSGERLRQSGERLRQSGERFKKSISSAAPSKEAFKIRSLRKAKDPKAEGQEVDRGMGVDIISGSLALGPIHEFHSDEFSETEKEVT... | null | null | cardiac myofibril assembly [GO:0055003]; muscle organ development [GO:0007517]; positive regulation of transcription by RNA polymerase II [GO:0045944]; regulation of gene expression [GO:0010468]; Rho protein signal transduction [GO:0007266] | caveola [GO:0005901]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; plasma membrane [GO:0005886]; sarcolemma [GO:0042383]; sarcoplasm [GO:0016528]; Z disc [GO:0030018] | GTPase activator activity [GO:0005096] | PF15237; | null | CAVIN family | null | SUBCELLULAR LOCATION: Cytoplasm, myofibril, sarcomere {ECO:0000269|PubMed:18332105}. Cytoplasm {ECO:0000269|PubMed:18332105}. Cytoplasm, cytosol {ECO:0000269|PubMed:19546242}. Membrane, caveola {ECO:0000269|PubMed:19546242, ECO:0000269|PubMed:24567387}. Cell membrane, sarcolemma {ECO:0000269|PubMed:19546242}. Cell memb... | null | null | null | null | null | FUNCTION: Modulates the morphology of formed caveolae in cardiomyocytes, but is not required for caveolar formation. Facilitates the recruitment of MAPK1/3 to caveolae within cardiomyocytes and regulates alpha-1 adrenergic receptor-induced hypertrophic responses in cardiomyocytes through MAPK1/3 activation (PubMed:2456... | Mus musculus (Mouse) |
A2AMT1 | BFSP1_MOUSE | MYRRSYVFQARQERYERAQPAGPAAQPGGTAPGLAALQALGERVAVQVQRARALQQRHAGLRRQLDAFQRLGEQPGPEDALARHVEANLQRARDLTAEHARLERQEAEAQRALDEFRSKYENECECQLVLKEMLERLNKEADEALLRNLHLQLEAQFLQADISVAKDRYKKNLLEIQTYITVLQQIVQTAPQVSLVTGMRESGLLMQEKLFTEREVAALQNQLEEGREAVTHLQAQKAELQAQTTALEQAIKHAHECYDEELQLYNEQIENLRKEIEEAERSLERSSYDCRQLAVAQQTLRNELDRYHRIIEIEGSRLSS... | null | null | cell maturation [GO:0048469]; intermediate filament organization [GO:0045109]; lens fiber cell development [GO:0070307] | cell cortex [GO:0005938]; cytoplasm [GO:0005737]; intermediate filament [GO:0005882]; plasma membrane [GO:0005886] | structural constituent of eye lens [GO:0005212] | PF00038; | 1.20.5.170;1.20.5.1160; | Intermediate filament family | PTM: Proteolytically cleaved during lens cell fiber differentiation with increased fragmentation as fiber cell age increases. {ECO:0000250|UniProtKB:Q06002}.; PTM: [Filensin C-terminal fragment]: Myristoylated at Gly-432 following proteolytic cleavage at Asp-431. {ECO:0000250|UniProtKB:Q06002}.; PTM: [Filensin N-termin... | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19029034}; Peripheral membrane protein {ECO:0000250|UniProtKB:Q06002}; Cytoplasmic side {ECO:0000250|UniProtKB:Q06002}. Cytoplasm {ECO:0000269|PubMed:19029034, ECO:0000269|PubMed:27559293}. Cytoplasm, cytoskeleton {ECO:0000250|UniProtKB:Q06002}. Cytoplasm, cell co... | null | null | null | null | null | FUNCTION: Required for the correct formation of lens intermediate filaments as part of a complex composed of BFSP1, BFSP2 and CRYAA (PubMed:27559293). Involved in altering the calcium regulation of MIP water permeability (By similarity). {ECO:0000250|UniProtKB:Q12934, ECO:0000269|PubMed:27559293}. | Mus musculus (Mouse) |
A2AN08 | UBR4_MOUSE | MATSGGEEAAAAAPAPGAPATGQDTTPGWEVAVRPLLSASYSAFEMKELPQLVASVIESESEILHHEKQYEPFYSSFVALSTHYITTVCSLIPRNQLQSVAAACKVLIEFSLLRLENPDEACAVSQKHLILLIKGLCTGCSRLDRTEIITFTAMMKSAKLPQTVKTLSDVEDQKELASPVSPELRQKEVQMNFLNQLTSVFNPRTVPSPPISPQALVEGENDEQSSPDQVSAAKTKSVFIAQNVASLQELGGSEKLLRVCLNLPYFLRYINRFQDAVVANSFFIMPATVADATAVRNGFHSLVIDVTMALDTLSLPVLEP... | 2.3.2.27 | null | negative regulation of fatty acid biosynthetic process [GO:0045717]; protein ubiquitination [GO:0016567]; ubiquitin-dependent protein catabolic process [GO:0006511] | centrosome [GO:0005813]; cytosol [GO:0005829]; membrane [GO:0016020]; nucleoplasm [GO:0005654] | calmodulin binding [GO:0005516]; ubiquitin protein ligase activity [GO:0061630]; ubiquitin-protein transferase activity [GO:0004842]; zinc ion binding [GO:0008270] | PF13764;PF19423;PF02207; | null | UBR4 family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane protein {ECO:0000305}. Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton {ECO:0000250}. Nucleus {ECO:0000250}. Note=Concentrates at the leading edge of membrane structures involved in actin motility. {ECO:0000250}. | 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; | null | PATHWAY: Protein modification; protein ubiquitination. | null | null | FUNCTION: E3 ubiquitin-protein ligase which is a component of the N-end rule pathway. Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation. Together with clathrin, forms meshwork structures in... | Mus musculus (Mouse) |
A2ANU3 | SYNG1_MOUSE | MDGIIEQKSVLVHSKISDAGKRNGLINTRNFMAESRDGLVSVYPAPQYQSHRLVASAAPGSLEGGRSEPVQQLLDPNTLQQSVESHYRPNIILYSDGVLRSWGDGVATDCCETTFIEDRSPTKDSLEYPDGKFIDLSGDDIKIHTLSYDVEEEEELQELESDYSSDTESEDNFLMMPPRDHLGLSVFSMLCCFWPLGIAAFYLSHETNKAVAKGDFHQASTSSRRALFLAVLSITIGTGIYVGVAVALIAYLSKNNHL | null | null | intracellular protein transport [GO:0006886]; positive regulation of synapse assembly [GO:0051965]; synaptic vesicle clustering [GO:0097091] | cell body [GO:0044297]; dendritic shaft [GO:0043198]; dendritic spine [GO:0043197]; early endosome membrane [GO:0031901]; excitatory synapse [GO:0060076]; intracellular membrane-bounded organelle [GO:0043231]; plasma membrane [GO:0005886]; postsynaptic density [GO:0014069]; postsynaptic density membrane [GO:0098839]; s... | glutamate receptor binding [GO:0035254]; protein homodimerization activity [GO:0042803] | PF04505; | null | CD225/Dispanin family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20152115}; Single-pass type II membrane protein {ECO:0000269|PubMed:20152115}. Early endosome membrane {ECO:0000269|PubMed:20152115}; Single-pass type II membrane protein {ECO:0000269|PubMed:20152115}. Postsynaptic density membrane {ECO:0000269|PubMed:20152115}. S... | null | null | null | null | null | FUNCTION: May regulate AMPA receptor content at nascent synapses, and have a role in postsynaptic development and maturation. {ECO:0000250}. | Mus musculus (Mouse) |
A2AP18 | PLCH2_MOUSE | MGGLAWGPSRAAGSSWVNASGTWEQPLRGFSGLQGGRRRGRGEKGIPEEPLCQLTPQLGLSLRVPFGLGDYGLDMPGPQPSAASQTTGAVACLAEVLLWVGGSVVVSPRWQLSLVVERCMSAMQEGTQMVKLRGSSKGLVRFYYLDEHRSCLRWRPSRKNEKAKISIDSIQEVSEGRQSEIFQRYPDSSFDPNCCFSIYHGSHRESLDLVSPSSEEARTWVTGLRYLMAGISDEDSLARRQRTRDQWLKQTFDEADKNGDGSLSISEVLQLLHKLNVNLPRQRVKQMFREADTDDHQGTLGFEEFCAFYKMMSTRRDLYL... | 3.1.4.11 | COFACTOR: Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000255|PROSITE-ProRule:PRU00041}; | lipid catabolic process [GO:0016042]; phosphatidylinositol metabolic process [GO:0046488]; phosphatidylinositol-mediated signaling [GO:0048015]; phospholipase C-activating G protein-coupled receptor signaling pathway [GO:0007200]; release of sequestered calcium ion into cytosol [GO:0051209] | cytoplasm [GO:0005737]; plasma membrane [GO:0005886] | calcium ion binding [GO:0005509]; phosphatidylinositol phospholipase C activity [GO:0004435]; phospholipase C activity [GO:0004629] | PF00168;PF09279;PF16457;PF00388;PF00387; | 2.60.40.150;1.10.238.10;3.20.20.190;2.30.29.30; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15899900}. Cell membrane {ECO:0000269|PubMed:15899900}. Note=Localized predominantly at the plasma membrane. {ECO:0000269|PubMed:15899900}. | CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-4,5-bisphosphate) + H2O = 1D-myo-inositol 1,4,5-trisphosphate + a 1,2-diacyl-sn-glycerol + H(+); Xref=Rhea:RHEA:33179, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17815, ChEBI:CHEBI:58456, ChEBI:CHEBI:203600; EC=3.1.4.11; Evidence={EC... | null | null | null | null | FUNCTION: The production of the second messenger molecules diacylglycerol (DAG) and inositol 1,4,5-trisphosphate (IP3) is mediated by activated phosphatidylinositol-specific phospholipase C enzymes. This phospholipase activity is very sensitive to calcium. May be important for formation and maintenance of the neuronal ... | Mus musculus (Mouse) |
A2APB8 | TPX2_MOUSE | MSQVPTTYSFDAPTDFINFSSLDAEEDTENIDSWFDEKANLENKFLRQRGIGEPFQGKNSLRKAKLQQGFVTPLKAVDNTYHKETEKENLQKQSIPSNDCSSLDAKRAVSGNTPVQPQRRSIRLSAQKDLEQKEKNHVASVEMKAKRCVAPATDCPPQKRMKVSHKKKLEEEEEGSAPATSRKNERETLEKAKGKHTVPGVPPAREKVLKSTEEQEIEKRLRMQQEVVELRRKNEEFKKLALAGPGQPVKKSTSQVTKTVDFHFLTDERIKQHPKNQEEYKEVNFMSELRKHSSTPARGTRGCTIIKPFNLSKGKKRTFD... | null | null | activation of protein kinase activity [GO:0032147]; apoptotic process [GO:0006915]; cell division [GO:0051301]; microtubule nucleation [GO:0007020]; mitotic spindle assembly [GO:0090307]; negative regulation of microtubule depolymerization [GO:0007026]; regulation of mitotic spindle organization [GO:0060236]; spindle a... | aster [GO:0005818]; axon hillock [GO:0043203]; cytoplasm [GO:0005737]; intercellular bridge [GO:0045171]; mitotic spindle [GO:0072686]; nuclear microtubule [GO:0005880]; nucleoplasm [GO:0005654]; nucleus [GO:0005634]; spindle [GO:0005819]; spindle pole [GO:0000922] | importin-alpha family protein binding [GO:0061676]; microtubule binding [GO:0008017]; molecular adaptor activity [GO:0060090]; protein kinase activator activity [GO:0030295]; protein kinase binding [GO:0019901] | PF09041;PF06886;PF12214; | null | TPX2 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9ULW0}. Cytoplasm, cytoskeleton, spindle {ECO:0000269|PubMed:27753540}. Cytoplasm, cytoskeleton, spindle pole {ECO:0000250|UniProtKB:Q9ULW0}. Note=During mitosis it is strictly associated with the spindle pole and with the mitotic spindle, whereas during S and G2, i... | null | null | null | null | null | FUNCTION: Spindle assembly factor required for normal assembly of mitotic spindles. Required for normal assembly of microtubules during apoptosis. Required for chromatin and/or kinetochore dependent microtubule nucleation. Mediates AURKA localization to spindle microtubules. Activates AURKA by promoting its autophospho... | Mus musculus (Mouse) |
A2APC3 | TTLL9_MOUSE | MSRQKNQNSKGHGVSKGKEREQRTLIRFKTTLMNTLMDVLRHRPGWVEVKDEGEWDFYWCDVSWLRENFDHTYMDEHVRISHFRNHYELTRKNYMVKNLKRFRKYLERESGKTEAAKCDFFPKTFEMPCEYHLFVEEFRKNPGITWIMKPVARSQGKGIFLFRRLKDIMDWRKGTSGKKPTGVETQPARANMNPSGSHDTRSSDDQKDDLPVENYVAQRYVENPYLIGGRKFDLRVYVLVMSYIPLRAWLYRDGFARFSNTRFTLNSIDDHYVHLTNVAVQKTSPDYHLKKGCKWMLQRFRQYLASKHGPKAVETLFSDM... | 6.3.2.- | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:A4Q9E8}; | flagellated sperm motility [GO:0030317]; microtubule cytoskeleton organization [GO:0000226]; protein modification process [GO:0036211] | ciliary basal body [GO:0036064]; cilium [GO:0005929]; cytoplasm [GO:0005737]; microtubule [GO:0005874]; motile cilium [GO:0031514] | ATP binding [GO:0005524]; metal ion binding [GO:0046872]; tubulin binding [GO:0015631]; tubulin-glutamic acid ligase activity [GO:0070740] | PF03133; | 3.30.1490.20;3.30.470.20; | Tubulin--tyrosine ligase family | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium basal body {ECO:0000269|PubMed:17499049}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:17499049}. Cytoplasm, cytoskeleton, flagellum axoneme {ECO:0000305|PubMed:27257088}. | CATALYTIC ACTIVITY: Reaction=(L-glutamyl)(n)-gamma-L-glutamyl-L-glutamyl-[protein] + ATP + L-glutamate = (L-glutamyl)(n+1)-gamma-L-glutamyl-L-glutamyl-[protein] + ADP + H(+) + phosphate; Xref=Rhea:RHEA:60148, Rhea:RHEA-COMP:15519, Rhea:RHEA-COMP:15675, ChEBI:CHEBI:15378, ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEB... | null | null | null | null | FUNCTION: Probable tubulin polyglutamylase that generates side chains of glutamate on the gamma-carboxyl group of specific glutamate residues within the C-terminal tail of target proteins (PubMed:27257088). Similar to TTLL1, may acquire enzymatic activity only in complex with other proteins as it is most likely lacking... | Mus musculus (Mouse) |
A2APF3 | CTCFL_MOUSE | MAAAEVPVPSGYFTQIKEQKLKPGDLEEEKEEDGVQRVEAQEGVVKEVEAENSCLLLEARAPVESDRRILTLQTVHLESQDVHLQGLGWLSVPHSEELSGTVPEAEGILQLPSVLWLDPEPQLSLQHCVTVSIPEELYPPEELQRIHFHLLRENVLMAEENPELTPDLDESTALKKPEEDEKDQLPPQGETDKREERLLLLEMKPKEGKDDEIVLTISHLSLEEQQDPPAANQTSVPGAKAAKPKRRRQTKGKPQSFQCDTCPFTSSKLSTFNRHIKIHSNERPHLCHLCLKAFRTVTLLRNHVNTHTGTRPHKCRDCDM... | null | null | establishment of protein localization to chromatin [GO:0071169]; genomic imprinting [GO:0071514]; regulation of transcription by RNA polymerase II [GO:0006357]; transcription initiation-coupled chromatin remodeling [GO:0045815] | chromosome [GO:0005694]; cytoplasm [GO:0005737]; cytosol [GO:0005829]; nuclear body [GO:0016604]; nucleus [GO:0005634] | chromatin insulator sequence binding [GO:0043035]; DNA-binding transcription activator activity, RNA polymerase II-specific [GO:0001228]; DNA-binding transcription repressor activity, RNA polymerase II-specific [GO:0001227]; histone binding [GO:0042393]; metal ion binding [GO:0046872]; RNA polymerase II cis-regulatory ... | PF00096; | 3.30.160.60; | CTCF zinc-finger protein family | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000269|PubMed:17048991}. | null | null | null | null | null | FUNCTION: Testis-specific DNA binding protein responsible for insulator function, nuclear architecture and transcriptional control, which probably acts by recruiting epigenetic chromatin modifiers. Plays a key role in gene imprinting in male germline, by participating in the establishment of differential methylation at... | Mus musculus (Mouse) |
A2APX8 | SCN1A_MOUSE | MEQTVLVPPGPDSFNFFTRESLAAIERRIAEEKAKNPKPDKKDDDENGPKPNSDLEAGKNLPFIYGDIPPEMVSEPLEDLDPYYINKKTFIVLNKGKAIFRFSATSALYILTPFNPLRKIAIKILVHSLFSMLIMCTILTNCVFMTMSNPPDWTKNVEYTFTGIYTFESLIKIIARGFCLEDFTFLRDPWNWLDFTVITFAYVTEFVDLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCVQWPPTNASLEEHSIEKNITMDYNGTLVNETVFEFDWKSYIQD... | null | null | adult walking behavior [GO:0007628]; cardiac muscle cell action potential involved in contraction [GO:0086002]; detection of mechanical stimulus involved in sensory perception of pain [GO:0050966]; determination of adult lifespan [GO:0008340]; establishment of localization in cell [GO:0051649]; membrane depolarization ... | axon [GO:0030424]; axon initial segment [GO:0043194]; intercalated disc [GO:0014704]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; node of Ranvier [GO:0033268]; nuclear body [GO:0016604]; presynaptic membrane [GO:0042734]; sodium channel complex [GO:0034706]; T-tubule [GO:0030315]; voltage-gated sodium chann... | sodium ion binding [GO:0031402]; voltage-gated monoatomic ion channel activity involved in regulation of presynaptic membrane potential [GO:0099508]; voltage-gated sodium channel activity [GO:0005248] | PF00520;PF06512;PF11933; | 1.10.287.70;1.10.238.10;1.20.5.1190;1.20.120.350; | Sodium channel (TC 1.A.1.10) family, Nav1.1/SCN1A subfamily | PTM: Phosphorylation at Ser-1516 by PKC in a highly conserved cytoplasmic loop slows inactivation of the sodium channel and reduces peak sodium currents. {ECO:0000250|UniProtKB:P04775}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27281198}; Multi-pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}. | CATALYTIC ACTIVITY: Reaction=Na(+)(in) = Na(+)(out); Xref=Rhea:RHEA:34963, ChEBI:CHEBI:29101; Evidence={ECO:0000269|PubMed:27281198}; | null | null | null | null | FUNCTION: Mediates the voltage-dependent sodium ion permeability of excitable membranes (PubMed:16921370, PubMed:17928448, PubMed:27281198). Assuming opened or closed conformations in response to the voltage difference across the membrane, the protein forms a sodium-selective channel through which Na(+) ions may pass i... | Mus musculus (Mouse) |
A2AQ07 | TBB1_MOUSE | MREIVHIQIGQCGNQIGAKFWEVIGEEHGIDCAGSYCGTSALQLERISVYYNEAYGKKYVPRAVLVDLEPGTMDSIRSSRLGVLFQPDSFVHGNSGAGNNWAKGHYTEGAELIENVMDVVRRESESCDCLQGFQIVHSLGGGTGSGMGTLLMNKIREEYPDRILNSFSVMPSPKVSDTVVEPYNAVLSIHQLIENTDACFCIDNEALYDICFRTLRLTTPTYGDLNHLVSLTMSGITTSLRFPGQLNADLRKLAVNMVPFPRLHFFMPGFAPLTAQGSQQYRALSVAELTQQMFDARNIMAACDPRRGRYLTVACIFRGK... | null | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:P68363}; | microtubule cytoskeleton organization [GO:0000226]; microtubule polymerization [GO:0046785]; microtubule-based process [GO:0007017]; mitotic cell cycle [GO:0000278]; platelet aggregation [GO:0070527]; platelet formation [GO:0030220]; spindle assembly [GO:0051225]; thyroid gland development [GO:0030878]; thyroid hormone... | cytoplasm [GO:0005737]; intercellular bridge [GO:0045171]; microtubule [GO:0005874]; mitotic spindle [GO:0072686] | GTP binding [GO:0005525]; GTPase activity [GO:0003924]; metal ion binding [GO:0046872]; structural constituent of cytoskeleton [GO:0005200] | PF00091;PF03953; | 1.10.287.600;3.30.1330.20;3.40.50.1440; | Tubulin family | PTM: Some glutamate residues at the C-terminus are polyglycylated, resulting in polyglycine chains on the gamma-carboxyl group. Glycylation is mainly limited to tubulin incorporated into axonemes (cilia and flagella) whereas glutamylation is prevalent in neuronal cells, centrioles, axonemes, and the mitotic spindle. Bo... | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. | null | null | null | null | null | FUNCTION: Tubulin is the major constituent of microtubules, a cylinder consisting of laterally associated linear protofilaments composed of alpha- and beta-tubulin heterodimers. Microtubules grow by the addition of GTP-tubulin dimers to the microtubule end, where a stabilizing cap forms. Below the cap, tubulin dimers a... | Mus musculus (Mouse) |
A2AQ19 | RTF1_MOUSE | MRGRLCVGRAAAVAAAVAAAAVAVPLAGGQEGSQGGVRRGSRGTTMVKKRKGRVVIDSDTEDSGSDENLDQELLSLAKRKRSDSEEKEPPVSQPAASSDSETSDSDDEWTFGSNKNKKKGKTRKVEKKGAMKKQANKAASSGSSDRDSSAESSAPEEGEVSDSESSSSSSSSDSDSSSEDEEFHDGYGEDLMGDEEDRARLEQMTEKEREQELFNRIEKREVLKRRFEIKKKLKTAKKKEKKEKKKKQEEEQEKKKLTQIQESQVTSHNKERRSKRDEKLDKKSQAMEELKAEREKRKNRTAELLAKKQPLKTSEVYSDD... | null | null | blastocyst growth [GO:0001832]; chromatin organization [GO:0006325]; endodermal cell fate commitment [GO:0001711]; negative regulation of transcription by RNA polymerase II [GO:0000122]; stem cell population maintenance [GO:0019827]; transcription elongation by RNA polymerase II [GO:0006368]; Wnt signaling pathway [GO:... | Cdc73/Paf1 complex [GO:0016593]; nucleolus [GO:0005730] | RNA polymerase II C-terminal domain phosphoserine binding [GO:1990269]; single-stranded DNA binding [GO:0003697] | PF03126; | 3.90.70.200; | null | null | SUBCELLULAR LOCATION: Nucleus, nucleoplasm {ECO:0000250}. | null | null | null | null | null | FUNCTION: Component of the PAF1 complex (PAF1C) which has multiple functions during transcription by RNA polymerase II and is implicated in regulation of development and maintenance of embryonic stem cell pluripotency. PAF1C associates with RNA polymerase II through interaction with POLR2A CTD non-phosphorylated and 'S... | Mus musculus (Mouse) |
A2AQ25 | SKT_MOUSE | MEESEGQKCEPNLPPSGDSRQMPQQGRSNLHVTSQEDAACRRPRERLSNGNARAQVSKPARNIPRRHTLGGPRSSKEILGMQPSEMDRKREAFLEHLKQKYPHHATAIMGHQERLRDQTKSPKLSHSPQPPNLGDPVEHLSETSGDSLEAMSEGEVPSPFARGSRTRASLPVVRSANQTKERSLGVLYLQYGDETKQLRMPNEVTSTDTIRALFVSAFPQQLTMKMLESPSVAIYIKDDSRNVYYELNDVRNIQDRSLLKVYNKDPSHAFNHMTKAVNGDMRMQREIVYARGDGLVAPRPGSVAHPPHVIPNSPPSTPVP... | null | null | embryonic skeletal system development [GO:0048706] | centrosome [GO:0005813]; cytoplasm [GO:0005737] | null | PF03915; | 1.20.58.1540; | null | null | SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000250|UniProtKB:Q5T5P2}. Cytoplasm {ECO:0000269|PubMed:16204209}. | null | null | null | null | null | FUNCTION: Required for normal development of intervertebral disks. {ECO:0000269|PubMed:16204209}. | Mus musculus (Mouse) |
A2AR95 | LRAD3_MOUSE | MWLLGPLCLLLSSTAESQLLPGNNFTNECNIPGNFMCSNGRCIPGAWQCDGLPDCFDKSDEKECPKAKSKCGPTFFPCASGIHCIIGRFRCNGFEDCPDGSDEENCTANPLLCSTARYHCRNGLCIDKSFICDGQNNCQDNSDEESCESSLEPGSGQVFVTSENQLVYYPSITYAIIGSSVIFVLVVALLALVLHHQRKRNNLMTLPVHRLQHPVLLSRLVVLDHPHHCNVTYNVNNGVQYVATQAEQNASEVGSPPSYSEALLDQRPAWYDLPPPPYSSDTESLNQADLPPYRSRSGSAYSASSQAASSLLSVEASSHN... | null | null | receptor-mediated endocytosis [GO:0006898]; regulation of protein processing [GO:0070613] | membrane [GO:0016020]; plasma membrane [GO:0005886] | amyloid-beta binding [GO:0001540] | PF00057; | 4.10.400.10; | LDLR family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21795536}; Single-pass type I membrane protein {ECO:0000269|PubMed:21795536}. | null | null | null | null | null | FUNCTION: May influence APP processing, resulting in a decrease in sAPP-alpha production and increased amyloidogenic P3 peptide production (PubMed:21795536). May regulate ITCH and NEDD4 E3 ligase activity and degradation (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q86YD5, ECO:0000269|PubMed:21795536}. | Mus musculus (Mouse) |
A2ARA8 | ITA8_MOUSE | MSAGTHCGPPGNRAPPFARLCCVSAALGMLWSPACLAFNLDVDKLTVYSGPEGSYFGYSLDFYIPDARTASVLVGAPKANTSQPDIVEGGAVYYCPWPSERSAQCKQIPFDTTNNRKIRVNGTKEPIEFKSNQWFGATVRAHKGKVVACAPLYHWRTLKPNPAKDPVGTCYVAIQNFSAYAEHSPCRNSNADPEGQGYCQAGFSLDFYKNGDLIVGGPGSFYWQGQVITVSIADIIANYSFKDILRKLAAEKQTDVAPASYDDSYLGYSVAAGEFTGDSQQELVAGIPRGAQNFGYVSIINSTDMTFIQNFTGEQMASYF... | null | null | cell adhesion mediated by integrin [GO:0033627]; cell projection organization [GO:0030030]; cell-cell adhesion [GO:0098609]; cell-matrix adhesion [GO:0007160]; establishment of protein localization [GO:0045184]; extracellular matrix organization [GO:0030198]; inner ear morphogenesis [GO:0042472]; integrin-mediated sign... | apical part of cell [GO:0045177]; dendritic spine membrane [GO:0032591]; endoplasmic reticulum [GO:0005783]; external side of plasma membrane [GO:0009897]; glutamatergic synapse [GO:0098978]; integrin complex [GO:0008305]; perikaryon [GO:0043204]; plasma membrane [GO:0005886]; postsynaptic density membrane [GO:0098839] | integrin binding [GO:0005178]; metal ion binding [GO:0046872] | PF01839;PF08441;PF20805;PF20806;PF00357; | 1.20.5.930;2.130.10.130;2.60.40.1460;2.60.40.1510;2.60.40.1530; | Integrin alpha chain family | null | SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:10742111}; Single-pass type I membrane protein {ECO:0000269|PubMed:10742111}. Cell membrane {ECO:0000250}. | null | null | null | null | null | FUNCTION: Integrin alpha-8/beta-1 functions in the genesis of kidney and probably of other organs by regulating the recruitment of mesenchymal cells into epithelial structures. It recognizes the sequence R-G-D in a wide array of ligands including TNC, FN1, SPP1 TGFB1, TGFB3 and VTN. NPNT is probably its functional liga... | Mus musculus (Mouse) |
A2ARI4 | LGR4_MOUSE | MPGPLRLLCFFALGLLGSAGPSGAAPPLCAAPCSCDGDRRVDCSGKGLTAVPEGLSAFTQALDISMNNITQLPEDAFKNFPFLEELQLAGNDLSFIHPKALSGLKELKVLTLQNNQLKTVPSEAIRGLSALQSLRLDANHITSVPEDSFEGLVQLRHLWLDDNILTEVPVRPLSNLPTLQALTLALNNISSIPDFAFTNLSSLVVLHLHNNKIKSLSQHCFDGLDNLETLDLNYNNLDEFPQAIKALPSLKELGFHSNSISVIPDGAFAGNPLLRTIHLYDNPLSFVGNSAFHNLSDLHSLVIRGASLVQWFPNLAGTVH... | null | null | adenylate cyclase-activating G protein-coupled receptor signaling pathway [GO:0007189]; axon guidance [GO:0007411]; bone mineralization [GO:0030282]; bone remodeling [GO:0046849]; circadian regulation of gene expression [GO:0032922]; circadian rhythm [GO:0007623]; digestive tract development [GO:0048565]; epithelial ce... | plasma membrane [GO:0005886] | heparin binding [GO:0008201]; protein-hormone receptor activity [GO:0016500]; Roundabout binding [GO:0048495]; transmembrane signaling receptor activity [GO:0004888] | PF00001;PF13855;PF01462; | 1.20.1070.10;3.80.10.10; | G-protein coupled receptor 1 family | null | SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21693646}; Multi-pass membrane protein {ECO:0000269|PubMed:21693646}. | null | null | null | null | null | FUNCTION: Receptor for R-spondins that potentiates the canonical Wnt signaling pathway and is involved in the formation of various organs. Upon binding to R-spondins (RSPO1, RSPO2, RSPO3 or RSPO4), associates with phosphorylated LRP6 and frizzled receptors that are activated by extracellular Wnt receptors, triggering t... | Mus musculus (Mouse) |
A2ARP1 | VIP1_MOUSE | MWSLTANEDESTTAHFFLGAGDEGLGTCGIGMRTEESDSELLEDEEDEVPPEPQIIVGICAMTKKSKSKPMTQILERLCRFDYLTVVILGEDVILNEPVENWPSCHCLISFHSKGFPLDKAVAYSKLRNPFLINDLAMQYYIQDRREVYRILQEEGIDLPRYAVLNRDPACPEECSLIEGEDQVEVNGAVFPKPFVEKPVSAEDHNVYIYYPSSAGGGSQRLFRKIGSRSSVYSPESSVRKTGSYIYEEFMPTDGTDVKVYTVGPDYAHAEARKSPALDGKVERDSEGKEVRYPVMLTAMEKLVARKVCVAFKQTVCGFD... | 2.7.4.24 | null | inositol metabolic process [GO:0006020]; inositol phosphate biosynthetic process [GO:0032958]; phosphorylation [GO:0016310] | cytosol [GO:0005829]; plasma membrane [GO:0005886] | ATP binding [GO:0005524]; diphosphoinositol-pentakisphosphate kinase activity [GO:0033857]; inositol heptakisphosphate kinase activity [GO:0000829]; inositol hexakisphosphate 1-kinase activity [GO:0052723]; inositol hexakisphosphate 3-kinase activity [GO:0052724]; inositol hexakisphosphate 5-kinase activity [GO:0000832... | PF00328;PF18086; | 3.40.50.11950;3.30.470.20;3.40.50.1240; | Histidine acid phosphatase family, VIP1 subfamily | null | SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q6PFW1}. Cell membrane {ECO:0000250|UniProtKB:Q6PFW1}. Note=Relocalizes to the plasma membrane upon activation of the PtdIns 3-kinase pathway. {ECO:0000250|UniProtKB:Q6PFW1}. | CATALYTIC ACTIVITY: Reaction=1D-myo-inositol hexakisphosphate + ATP = 1-diphospho-1D-myo-inositol 2,3,4,5,6-pentakisphosphate + ADP; Xref=Rhea:RHEA:37459, ChEBI:CHEBI:30616, ChEBI:CHEBI:58130, ChEBI:CHEBI:74946, ChEBI:CHEBI:456216; EC=2.7.4.24; Evidence={ECO:0000250|UniProtKB:Q6PFW1}; PhysiologicalDirection=left-to-rig... | null | null | null | null | FUNCTION: Bifunctional inositol kinase that acts in concert with the IP6K kinases IP6K1, IP6K2 and IP6K3 to synthesize the diphosphate group-containing inositol pyrophosphates diphosphoinositol pentakisphosphate, PP-InsP5, and bis-diphosphoinositol tetrakisphosphate, (PP)2-InsP4. PP-InsP5 and (PP)2-InsP4, also respecti... | Mus musculus (Mouse) |
A2ARP9 | CTSR2_MOUSE | MAQEQGHFQLLRADAIRSKLIDTFSLIEHLQGLSQAVPRHTLREILDPSYQQKLMSGDQEQLVRFSIKPRRMGHITHSRRLLSRLRVRCSRMPPLSLWAGWVLDSSVFSKFIISLIFLNTFVLMVEIELMESTNTALWPVKLALEVADWFILLSFIVEILLMWLASFSLFWKDAWNVFDFFVTLLSLLPELVVLLGVPAHSVWLQLLRVCRVLRSLKLFARFRQIKVILLALVRALKSMTFLLMLLLIFFYIFAVTGVYFFREYSRSTIEGLEYNMFFSDLLNSLVTVFILFTLDHWYAVLQDIWKVPESSRVFSSIYVI... | null | null | fertilization [GO:0009566]; flagellated sperm motility [GO:0030317]; sperm capacitation [GO:0048240] | CatSper complex [GO:0036128]; sperm flagellum [GO:0036126] | calcium channel activity [GO:0005262]; calcium-activated cation channel activity [GO:0005227] | PF00520; | 1.10.287.70;1.20.120.350; | Cation channel sperm-associated (TC 1.A.1.19) family | null | SUBCELLULAR LOCATION: Cell projection, cilium, flagellum membrane {ECO:0000269|PubMed:11675491}; Multi-pass membrane protein {ECO:0000269|PubMed:34225353}. | CATALYTIC ACTIVITY: Reaction=Ca(2+)(in) = Ca(2+)(out); Xref=Rhea:RHEA:29671, ChEBI:CHEBI:29108; Evidence={ECO:0000305|PubMed:21412339}; | null | null | null | null | FUNCTION: Pore-forming subunit of the CatSper complex, a sperm-specific voltage-gated calcium channel that plays a central role in sperm cell hyperactivation. Controls calcium entry to mediate the hyperactivated motility, a step needed for sperm motility which is essential late in the preparation of sperm for fertiliza... | Mus musculus (Mouse) |
A2ARV4 | LRP2_MOUSE | MERGAAAAAWMLLLAIAACLAPVSGQECGSGNFRCDNGYCIPASWRCDGTRDCLDDTDEIGCPPRSCGSGFFLCPAEGTCIPSSWVCDQDKDCSDGADEQQNCPGTTCSSQQLTCSNGQCVPIEYRCDHVSDCPDGSDERNCYYPTCDQLTCANGACYNTSQKCDHKVDCRDSSDEANCTTLCSQKEFQCGSGECILRAYVCDHDNDCEDNSDEHNCNYDTCGGHQFTCSNGQCINQNWVCDGDDDCQDSGDEDGCESNQRHHTCYPREWACPGSGRCISMDKVCDGVPDCPEGEDENNATSGRYCGTGLCSILNCEYQC... | null | null | amyloid-beta clearance [GO:0097242]; aorta development [GO:0035904]; cell population proliferation [GO:0008283]; cellular response to growth factor stimulus [GO:0071363]; chemoattraction of axon [GO:0061642]; coronary artery morphogenesis [GO:0060982]; coronary vasculature development [GO:0060976]; diol metabolic proce... | apical part of cell [GO:0045177]; apical plasma membrane [GO:0016324]; axon [GO:0030424]; axonal growth cone [GO:0044295]; brush border [GO:0005903]; brush border membrane [GO:0031526]; cell surface [GO:0009986]; clathrin-coated pit [GO:0005905]; dendrite [GO:0030425]; endocytic vesicle [GO:0030139]; endoplasmic reticu... | calcium ion binding [GO:0005509]; hemoglobin binding [GO:0030492]; hormone binding [GO:0042562]; insulin-like growth factor I binding [GO:0031994]; low-density lipoprotein particle receptor binding [GO:0050750]; nuclear receptor binding [GO:0016922]; PDZ domain binding [GO:0030165]; protein transporter activity [GO:014... | PF12662;PF07645;PF14670;PF00057;PF00058; | 2.10.25.10;4.10.400.10;2.120.10.30; | LDLR family | PTM: A fraction undergoes proteolytic cleavage of the extracellular domain at the cell membrane to generate a cytoplasmic tail fragment. This is internalized into the early endosome from where it trafficks in an LDLRAP1/ARH-dependent manner to the endocytic recycling compartment (ERC). In the ERC, it is further cleaved... | SUBCELLULAR LOCATION: Apical cell membrane {ECO:0000269|PubMed:16143106, ECO:0000269|PubMed:20460439, ECO:0000269|PubMed:22340494, ECO:0000269|PubMed:22354480}; Single-pass type I membrane protein {ECO:0000255}. Endosome lumen {ECO:0000250|UniProtKB:P98158}. Membrane, coated pit {ECO:0000269|PubMed:22340494}. Cell proj... | null | null | null | null | null | FUNCTION: Multiligand endocytic receptor. Acts together with CUBN to mediate endocytosis of high-density lipoproteins (PubMed:10766831). Mediates receptor-mediated uptake of polybasic drugs such as aprotinin, aminoglycosides and polymyxin B (By similarity). In the kidney, mediates the tubular uptake and clearance of le... | Mus musculus (Mouse) |
A2AS55 | ANR16_MOUSE | MALPGDPRRLCRLVQEGRLRDLQEELAVARGCRGPAGDTLLHCAARHGRQDILAYLVEAWSMDIEATNRDYKRPLHEAASMGHRDCVRYLLGRGAVVDSLKKADWTPLMMACTRKNLDVIQDLVEHGANPLLKNKDGWNSFHIASREGHPVILRYLLTVCPDAWKTESNIRRTPLHTAAMHGCLEAVQVLLERCHYEPDCRDNCGVTPFMDAIQCGHVSIAKLLLEQHKACSSAADSMGAQALHRAAVTGQDEAIRFLVCGLGIDVDVRAKSSQLTALHYAAKEGQTNTVQTLLSLGADINSTDERNRSVLHLACAGQHV... | null | null | tRNA modification [GO:0006400] | cytoplasm [GO:0005737]; nucleus [GO:0005634] | null | PF12796;PF13637; | 1.25.40.20; | null | null | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:29769718}. Nucleus {ECO:0000269|PubMed:29769718}. | null | null | null | null | null | FUNCTION: Required to prevent the misactivation of serine (Ser) with tRNA(Ala) by promoting the hydrolysis of Ser-mischarged tRNA(Ala), thereby playing a role in translational fidelity (PubMed:29769718). Binds directly to the catalytic domain of AARS/AlaRS and captures Ser that is misactivated by AARS/AlaRS, preventing... | Mus musculus (Mouse) |
A2AS89 | GDAH_MOUSE | MLRLLRSSWARGLGSGVATWRPSAGLFRPGCPGIRQASGASDTPHHQSPSSESPVQPVGVGVCSMMRLPLQSSPEGLDAAFIGVPLDTGTSNRPGARFGPCRIREESLMLGAVNPSTGALPFQSLRVADLGNVNVNLYNLQDSCLLIREAYQNVLAAGCIPLTLGGDQTITYPILQAVAKEHGPVGLVHVGAHTNTTDKPREEKVYHRTPFRRSVDEGLLDSKRVVQIGIRGSSRTLDPYRYSRSQGFRVVLAEDCWMKSLVPLMAEVRQQMGGKPLYISFAIDALDPAYAPGTGTPEIAGLTPSQALEIIRGCQGLNVV... | 3.5.3.-; 3.5.3.1; 3.5.3.17; 3.5.3.7 | COFACTOR: Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000255|PROSITE-ProRule:PRU00742}; | putrescine biosynthetic process from arginine, using agmatinase [GO:0033389]; urea cycle [GO:0000050] | mitochondrion [GO:0005739] | agmatinase activity [GO:0008783]; arginase activity [GO:0004053]; guanidinobutyrase activity [GO:0047971]; guanidinopropionase activity [GO:0047972]; metal ion binding [GO:0046872] | PF00491; | 3.40.800.10; | Arginase family, Agmatinase subfamily | null | SUBCELLULAR LOCATION: Mitochondrion {ECO:0000250}. | CATALYTIC ACTIVITY: Reaction=3-guanidinopropanoate + H2O = beta-alanine + urea; Xref=Rhea:RHEA:16029, ChEBI:CHEBI:15377, ChEBI:CHEBI:16199, ChEBI:CHEBI:57593, ChEBI:CHEBI:57966; EC=3.5.3.17; Evidence={ECO:0000250|UniProtKB:Q9BSE5}; PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16030; Evidence={ECO:0000250|UniPro... | null | PATHWAY: Nitrogen metabolism; urea cycle; L-ornithine and urea from L-arginine: step 1/1. {ECO:0000250|UniProtKB:Q9BSE5}. | null | null | FUNCTION: Hydrolyzes linear guanidino acids to form urea and the corresponding amines. Displays specificity for substrates having a negatively charged head group and short chains including taurocyamine, guanidino propanoic and butanoic acids. May protect cells by detoxifying potentially harmful amounts of guanidino aci... | Mus musculus (Mouse) |
A2ASI5 | SCN3A_MOUSE | MAQALLVPPGPESFRLFTRESLAAIEKRAAEEKAKKPKKEQDIDDENKPKPNSDLEAGKNLPFIYGDIPPEMVSEPLEDLDPYYVSKKTFVVLNKGKAIFRFSATSALYILTPLNPVRKIAIKILVHSLFSMLIMCTILTNCVFMTLSNPPDWTKNVEYTFTGIYTFESLIKILARGFCLEDFTFLRDPWNWLDFSVIVMAYVTEFVDLGNVSALRTFRVLRALKTISVIPGLKTIVGALIQSVKKLSDVMILTVFCLSVFALIGLQLFMGNLRNKCLQWPPSDSAFEINTTSYFNGTMDSNGTFVNVTMSTFNWKDYIA... | null | null | behavioral response to pain [GO:0048266]; cellular response to antibiotic [GO:0071236]; membrane depolarization during action potential [GO:0086010]; neuronal action potential [GO:0019228]; response to pyrethroid [GO:0046684]; sodium ion transmembrane transport [GO:0035725] | axon [GO:0030424]; basal plasma membrane [GO:0009925]; membrane [GO:0016020]; neuronal cell body [GO:0043025]; plasma membrane [GO:0005886]; sarcoplasm [GO:0016528]; voltage-gated sodium channel complex [GO:0001518] | calmodulin binding [GO:0005516]; sodium channel activity [GO:0005272]; sodium ion binding [GO:0031402]; voltage-gated sodium channel activity [GO:0005248] | PF00520;PF06512;PF11933; | 1.10.287.70;1.10.238.10;1.20.5.1190;1.20.120.350; | Sodium channel (TC 1.A.1.10) family, Nav1.3/SCN3A subfamily | PTM: May be ubiquitinated by NEDD4L; which would promote its endocytosis. {ECO:0000250|UniProtKB:Q9NY46}.; PTM: Phosphorylation at Ser-1453 in a highly conserved cytoplasmic loop slows inactivation of the channel and reduces peak sodium currents. {ECO:0000250}. | SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9NY46}; Multi-pass membrane protein {ECO:0000250|UniProtKB:D0E0C2}. Basal cell membrane {ECO:0000269|PubMed:29142310}. Note=In enterochromaffin cells, localized highly asymmetrically, almost exclusively at the basal side. {ECO:0000269|PubMed:29142310}. | null | null | null | null | null | FUNCTION: Mediates the voltage-dependent sodium ion permeability of excitable membranes. Assuming opened or closed conformations in response to the voltage difference across the membrane, forms a sodium-selective channel through which Na(+) ions may pass in accordance with their electrochemical gradient (PubMed:2914231... | Mus musculus (Mouse) |
A2ASQ1 | AGRIN_MOUSE | MPPLPLEHRPRQQPGASVLVRYFMIPCNICLILLATSTLGFAVLLFLSNYKPGIHFTAAPSMPPDVCRGMLCGFGAVCEPSVEDPGRASCVCKKNVCPAMVAPVCGSDASTYSNECELQRAQCNQQRRIRLLRQGPCGSRDPCANVTCSFGSTCVPSADGQTASCLCPTTCFGAPDGTVCGSDGVDYPSECQLLRHACANQEHIFKKFDGPCDPCQGSMSDLNHICRVNPRTRHPEMLLRPENCPAQHTPICGDDGVTYENDCVMSRIGAARGLLLQKVRSGQCQTRDQCPETCQFNSVCLSRRGRPHCSCDRVTCDGAY... | null | null | cell differentiation [GO:0030154]; chemical synaptic transmission [GO:0007268]; circadian rhythm [GO:0007623]; enzyme-linked receptor protein signaling pathway [GO:0007167]; motor neuron apoptotic process [GO:0097049]; negative regulation of P-type sodium:potassium-exchanging transporter activity [GO:1903407]; negative... | axonal growth cone [GO:0044295]; basement membrane [GO:0005604]; cell surface [GO:0009986]; collagen-containing extracellular matrix [GO:0062023]; extracellular region [GO:0005576]; extracellular space [GO:0005615]; glutamatergic synapse [GO:0098978]; Golgi lumen [GO:0005796]; sarcolemma [GO:0042383]; synapse [GO:00452... | acetylcholine receptor regulator activity [GO:0030548]; ATPase inhibitor activity [GO:0042030]; BMP binding [GO:0036122]; calcium ion binding [GO:0005509]; chondroitin sulfate binding [GO:0035374]; dystroglycan binding [GO:0002162]; heparan sulfate proteoglycan binding [GO:0043395]; receptor ligand activity [GO:0048018... | PF00008;PF00050;PF07648;PF00053;PF00054;PF01390; | 2.60.120.200;3.30.60.30;2.10.25.10;3.30.70.960; | null | PTM: Contains heparan and chondroitin sulfate chains and alpha-dystroglycan as well as N-linked and O-linked oligosaccharides. Heparin and heparin sulfate binding in the G3 domain is independent of calcium ions. Binds heparin with a stoichiometry of 2:1. Binds sialic acid with a stoichiometry of 1:1 and binding require... | SUBCELLULAR LOCATION: Synapse {ECO:0000269|PubMed:10402191, ECO:0000269|PubMed:12796478, ECO:0000269|PubMed:17611272, ECO:0000269|PubMed:18230682, ECO:0000269|PubMed:8653787}. Cell membrane {ECO:0000269|PubMed:11018052, ECO:0000269|PubMed:11161480}; Single-pass type II membrane protein {ECO:0000269|PubMed:11018052, ECO... | null | null | null | null | null | FUNCTION: [Isoform 1]: Heparan sulfate basal lamina glycoprotein that plays a central role in the formation and the maintenance of the neuromuscular junction (NMJ) and directs key events in postsynaptic differentiation. This neuron-specific (z+) isoform is a component of the AGRN-LRP4 receptor complex that induces the ... | Mus musculus (Mouse) |
A2ASS6 | TITIN_MOUSE | MTTQAPMFTQPLQSVVVLEGSTATFEAHVSGSPVPEVSWFRDGQVISTSTLPGVQISFSDGRARLMIPAVTKANSGRYSLRATNGSGQATSTAELLVTAETAPPNFSQRLQSMTVRQGSQVRLQVRVTGIPTPVVKFYRDGAEIQSSLDFQISQEGDLYSLLIAEAYPEDSGTYSVNATNSVGRATSTAELVVQGEEVVPAKKTKTIVSTAQISETRQTRIEKKIEAHFDARSIATVEMVIDGATGQLPHKTPPRIPPKPKSRSPTPPSIAAKAQLARQQSPSPIRHSPSPVRHVRAPTPSPVRSVSPAGRISTSPIRSV... | 2.7.11.1 | COFACTOR: Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250|UniProtKB:Q8WZ42}; | adult heart development [GO:0007512]; cardiac muscle tissue development [GO:0048738]; cardiac muscle tissue morphogenesis [GO:0055008]; cardiac myofibril assembly [GO:0055003]; detection of muscle stretch [GO:0035995]; forward locomotion [GO:0043056]; heart development [GO:0007507]; heart growth [GO:0060419]; heart mor... | A band [GO:0031672]; I band [GO:0031674]; M band [GO:0031430]; muscle myosin complex [GO:0005859]; nucleus [GO:0005634]; sarcomere [GO:0030017]; Z disc [GO:0030018] | ankyrin binding [GO:0030506]; ATP binding [GO:0005524]; calmodulin binding [GO:0005516]; metal ion binding [GO:0046872]; protein serine kinase activity [GO:0106310]; protein serine/threonine kinase activity [GO:0004674]; protein tyrosine kinase activity [GO:0004713]; structural constituent of cytoskeleton [GO:0005200];... | PF00041;PF07679;PF00069;PF02818;PF18362;PF09042; | 2.60.40.10;1.10.510.10; | Protein kinase superfamily, CAMK Ser/Thr protein kinase family | PTM: Autophosphorylated. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Nucleus {ECO:0000250|UniProtKB:Q8WZ42}. | 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:Q8WZ42}; CATALYTI... | null | null | null | null | FUNCTION: Key component in the assembly and functioning of vertebrate striated muscles. By providing connections at the level of individual microfilaments, it contributes to the fine balance of forces between the two halves of the sarcomere. The size and extensibility of the cross-links are the main determinants of sar... | Mus musculus (Mouse) |
A2ASZ8 | SCMC2_MOUSE | MLCLCLYVPIAGAAQTEFQYFESKGLPAELKSIFKLSVFIPSQEFSTYRQWKQKIVQAGDKDLDGQLDFEEFVHYLQDHEKKLRLVFKSLDKKNDGRIDAQEIMQSLRDLGVKISEQQAEKILKSMDKNGTMTIDWNEWRDYHLLHPVENIPEIILYWKHSTIFDVGENLTVPDEFTVEERQTGMWWRHLVAGGGAGAVSRTCTAPLDRLKVLMQVHASRSNNMCIVGGFTQMIREGGAKSLWRGNGINVLKIAPESAIKFMAYEQMKRLVGSDQETLRIHERLVAGSLAGAIAQSSIYPMEVLKTRMALRKTGQYSGML... | null | null | adipose tissue development [GO:0060612]; ADP transport [GO:0015866]; ATP metabolic process [GO:0046034]; ATP transport [GO:0015867]; calcium ion transmembrane transport [GO:0070588]; camera-type eye development [GO:0043010]; cellular respiration [GO:0045333]; multicellular organism growth [GO:0035264]; response to acti... | mitochondrial inner membrane [GO:0005743]; mitochondrion [GO:0005739] | ATP transmembrane transporter activity [GO:0005347]; ATP:inorganic phosphate antiporter activity [GO:0140987]; calcium ion binding [GO:0005509] | PF13499;PF13833;PF00153; | 1.10.238.10;1.50.40.10; | Mitochondrial carrier (TC 2.A.29) family | null | SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000305|PubMed:15054102}; Multi-pass membrane protein {ECO:0000255}. | CATALYTIC ACTIVITY: Reaction=ATP(out) + Mg(2+)(out) + phosphate(in) = ATP(in) + Mg(2+)(in) + phosphate(out); Xref=Rhea:RHEA:65840, ChEBI:CHEBI:18420, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474; Evidence={ECO:0000250|UniProtKB:Q6KCM7}; | null | null | null | null | FUNCTION: Electroneutral antiporter that most probably mediates the transport of adenyl nucleotides through the inner mitochondrial membrane. Originally identified as an ATP-magnesium/inorganic phosphate antiporter, it could have a broader specificity for adenyl nucleotides. By regulating the mitochondrial matrix adeny... | Mus musculus (Mouse) |
A2AT37 | RENT2_MOUSE | MPAERKKSASMEEKESLLNNKEKDCSERRPVSSKEKPRDDLKVTAKKEVSKVPEDKKKRLEEDKRKKEDKERKKKEEEKVKAEEELKKKEEEEKKKQEEEERKKQEEQAKRQQEEAAAQLKEKEESLQLHQEAWERHQLRKELRSKNQNAPDNRPEENFFSRLDSSLKKNTAFVKKLKTITEQQRDSLSHDFNGLNLSKYIAEAVASIVEAKLKLSDVNCAAHLCSLFHQRYSDFAPSLLQVWKKHFEARKEEKTPNITKLRTDLRFIAELTIVGIFTDKEGLSLIYEQLKSIINADRESHTHVSVVISFCRHCGDDIAG... | null | null | animal organ regeneration [GO:0031100]; liver development [GO:0001889]; nuclear-transcribed mRNA catabolic process, nonsense-mediated decay [GO:0000184]; response to unfolded protein [GO:0006986] | cytoplasm [GO:0005737]; cytoplasmic ribonucleoprotein granule [GO:0036464]; cytosol [GO:0005829]; exon-exon junction complex [GO:0035145]; perinuclear region of cytoplasm [GO:0048471] | RNA binding [GO:0003723]; telomeric DNA binding [GO:0042162] | PF02854;PF04050; | 1.25.40.180;4.10.80.160;6.10.250.770; | null | null | SUBCELLULAR LOCATION: Cytoplasm, perinuclear region {ECO:0000250|UniProtKB:Q9HAU5}. Cytoplasm {ECO:0000269|PubMed:27149095}. | null | null | null | null | null | FUNCTION: Involved in nonsense-mediated decay (NMD) of mRNAs containing premature stop codons by associating with the nuclear exon junction complex (EJC). Recruited by UPF3B associated with the EJC core at the cytoplasmic side of the nuclear envelope and the subsequent formation of an UPF1-UPF2-UPF3 surveillance comple... | Mus musculus (Mouse) |
A2AU37 | RD21L_MOUSE | MFYTHVLMSKRGPLAKIWLAAHWEKKLTKAHVFECNLEITIQKIISPKVKIALRTSGHLLLGVVRIYNRKAKYLLADCSEAFLKMKMTFRPGLVDLPKENFEAAYNTITLPEEFHDFEIYNINEIDISEPLAQNQSRPEEITLREEYSNDLLFQAGSFGDEPEILRRHSFFDDNILMNSSGLVVEHSSGSFAEEKSLFFDNGDGFGDEGAAGEMIDNLLQDESTFLEEAYLNKEVSLPPELPSSIMVEPGNSDDQCIPEDEEINEITLLSNEDEGFTLDPIDDLDIADRRRRKKRRLLVDPVKEISSKAMHRQLASFMDT... | null | null | double-strand break repair [GO:0006302]; double-strand break repair via homologous recombination [GO:0000724]; fertilization [GO:0009566]; homologous chromosome pairing at meiosis [GO:0007129]; meiotic attachment of telomere to nuclear envelope [GO:0070197]; replication-born double-strand break repair via sister chroma... | chromosome [GO:0005694]; cohesin complex [GO:0008278]; condensed nuclear chromosome [GO:0000794]; lateral element [GO:0000800]; meiotic cohesin complex [GO:0030893]; nucleus [GO:0005634] | chromatin binding [GO:0003682] | PF04824;PF04825; | 1.10.10.580; | Rad21 family | null | SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:21242291, ECO:0000269|PubMed:21274006, ECO:0000269|PubMed:21527826, ECO:0000269|PubMed:21743440}. Chromosome {ECO:0000269|PubMed:21242291, ECO:0000269|PubMed:21274006, ECO:0000269|PubMed:21527826, ECO:0000269|PubMed:21743440}. Note=In meiotic chromosomes, localized alon... | null | null | null | null | null | FUNCTION: Meiosis-specific component of some cohesin complex required during the initial steps of prophase I in male meiosis. Probably required during early meiosis in males for separation of sister chromatids and homologous chromosomes. Replaces RAD21 in premeiotic S phase (during early stages of prophase I), while RA... | Mus musculus (Mouse) |
A2AU72 | ARMC3_MOUSE | MGKKIKKEVEPPPKDVFDPITIESKKAATVVLMLKSPEEDILAKACEAIYKFALKGEENKATLLELGAVEPLTKLLTHEDKTVRRNAMMIFGILASNSDVKKLLRELEVMNSVIAQLSPEEEVVIHEFASLCLANMSVEYTGKVQIFEHGGLEPLIRLLSSSDPDVKKNSIECIYNLVQDFQCRTTLQELNAIPPILELLRSEYPIIQLLALKTLGVITCDKEARTMLKENQGLDHLTKILETKELNDLHVEALSVIANCLEDMDTMVLMQQTGSLKKVLSFAESSTIPDIQKNAAKAIAKAAYDPENRKVFHEQEVEKC... | null | null | flagellated sperm motility [GO:0030317]; ribophagy [GO:0034517]; spermatid development [GO:0007286] | null | null | PF00514;PF14381; | 1.25.10.10; | null | PTM: Palmitoylation is important for its function in autophagy. {ECO:0000269|PubMed:34428398}. | null | null | null | null | null | null | FUNCTION: Essential for male fertility and sperm motility. During spermatogenesis, promotes the autophagic degradation of excessive ribosomes, providing energy resources for mitochondria and thus ensuring sperm flagellar motility. {ECO:0000269|PubMed:34428398}. | Mus musculus (Mouse) |
A2AUC9 | KLH41_MOUSE | MDSQRELAEELRLYQSTLLQDGLKDLLEEKKFIDCTLKAGDKSFPCHRLILSACSPYFREYFLSEIEEEKKKEVALDNVDPAILDLIIKYLYSASIDLNDGNVQDIFALSSRFQIPSVFTVCVSYLQKRLAPGNCLAILRLGLLLDCPRLAISAREFVSDRFVQICKEEDFMQLSPQELISVISNDSLNVEKEEVVFEAVMKWVRTDKENRAKNLSEVFDCIRFRLMAEKYFKDHVEKDDIIKSNPEVQKKIKVLKDAFAGKLPEPSKNAEKAGAGEVNGDVGDEDLLPGYLNDIPRHGMFVKDLILLVNDTAAVAYDPM... | null | null | myofibril assembly [GO:0030239]; protein ubiquitination [GO:0016567]; pseudopodium assembly [GO:0031269]; regulation of myoblast differentiation [GO:0045661]; regulation of myoblast proliferation [GO:2000291]; regulation of skeletal muscle cell differentiation [GO:2001014]; skeletal muscle cell differentiation [GO:0035... | Cul3-RING ubiquitin ligase complex [GO:0031463]; cytoplasm [GO:0005737]; cytoskeleton [GO:0005856]; cytosol [GO:0005829]; endoplasmic reticulum membrane [GO:0005789]; M band [GO:0031430]; nucleoplasm [GO:0005654]; plasma membrane [GO:0005886]; pseudopodium [GO:0031143]; ruffle [GO:0001726]; sarcoplasmic reticulum membr... | null | PF07707;PF00651;PF01344; | 1.25.40.420;2.120.10.80; | null | PTM: Ubiquitinated by E3 ubiquitin ligase complex formed by CUL3 and RBX1 and probably targeted for proteasome-independent degradation. Quinone-induced oxidative stress increases its ubiquitination. {ECO:0000250|UniProtKB:O60662}. | SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:18178185, ECO:0000269|PubMed:22562206}. Cytoplasm, cytoskeleton {ECO:0000269|PubMed:18178185}. Cell projection, pseudopodium {ECO:0000250|UniProtKB:Q9ER30}. Cell projection, ruffle {ECO:0000250|UniProtKB:Q9ER30}. Cytoplasm, myofibril, sarcomere, M line {ECO:0000269|Pu... | null | null | null | null | null | FUNCTION: Involved in skeletal muscle development and differentiation. Regulates proliferation and differentiation of myoblasts and plays a role in myofibril assembly by promoting lateral fusion of adjacent thin fibrils into mature, wide myofibrils. Required for pseudopod elongation in transformed cells. {ECO:0000269|P... | Mus musculus (Mouse) |
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