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
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)