ID E9Q9V7_MOUSE Unreviewed; 936 AA. AC E9Q9V7; DT 05-APR-2011, integrated into UniProtKB/TrEMBL. DT 05-APR-2011, sequence version 1. DT 27-MAR-2024, entry version 80. DE SubName: Full=Snf2-related CREBBP activator protein {ECO:0000313|Ensembl:ENSMUSP00000063817.6}; GN Name=Srcap {ECO:0000313|Ensembl:ENSMUSP00000063817.6, GN ECO:0000313|MGI:MGI:2444036}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|Ensembl:ENSMUSP00000063817.6, ECO:0000313|Proteomes:UP000000589}; RN [1] {ECO:0000313|Ensembl:ENSMUSP00000063817.6, ECO:0000313|Proteomes:UP000000589} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000063817.6, RC ECO:0000313|Proteomes:UP000000589}; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S., RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., RA Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of the RT mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] {ECO:0007829|PubMed:21183079} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001; RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R., RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.; RT "A tissue-specific atlas of mouse protein phosphorylation and expression."; RL Cell 143:1174-1189(2010). RN [3] {ECO:0000313|Ensembl:ENSMUSP00000063817.6} RP IDENTIFICATION. RC STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000063817.6}; RG Ensembl; RL Submitted (NOV-2023) to UniProtKB. CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR AlphaFoldDB; E9Q9V7; -. DR SMR; E9Q9V7; -. DR IntAct; E9Q9V7; 1. DR MINT; E9Q9V7; -. DR jPOST; E9Q9V7; -. DR MaxQB; E9Q9V7; -. DR PeptideAtlas; E9Q9V7; -. DR ProteomicsDB; 369471; -. DR Ensembl; ENSMUST00000066582.12; ENSMUSP00000063817.6; ENSMUSG00000053877.13. DR UCSC; uc009jvy.1; mouse. DR AGR; MGI:2444036; -. DR MGI; MGI:2444036; Srcap. DR VEuPathDB; HostDB:ENSMUSG00000053877; -. DR GeneTree; ENSGT00940000157457; -. DR HOGENOM; CLU_000315_12_1_1; -. DR TreeFam; TF106424; -. DR ChiTaRS; Srcap; mouse. DR Proteomes; UP000000589; Chromosome 7. DR Bgee; ENSMUSG00000053877; Expressed in undifferentiated genital tubercle and 181 other cell types or tissues. DR ExpressionAtlas; E9Q9V7; baseline and differential. DR GO; GO:0005794; C:Golgi apparatus; ISO:MGI. DR GO; GO:0016604; C:nuclear body; ISO:MGI. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0005634; C:nucleus; ISO:MGI. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI. DR GO; GO:0032991; C:protein-containing complex; ISO:MGI. DR GO; GO:0000812; C:Swr1 complex; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0016887; F:ATP hydrolysis activity; IBA:GO_Central. DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro. DR GO; GO:0042393; F:histone binding; IBA:GO_Central. DR CDD; cd18003; DEXQc_SRCAP; 1. DR Gene3D; 1.20.120.850; SWI2/SNF2 ATPases, N-terminal domain; 1. DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR014012; HSA_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR038718; SNF2-like_sf. DR InterPro; IPR000330; SNF2_N. DR PANTHER; PTHR45685:SF1; HELICASE SRCAP; 1. DR PANTHER; PTHR45685; HELICASE SRCAP-RELATED; 1. DR Pfam; PF07529; HSA; 1. DR Pfam; PF00176; SNF2-rel_dom; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00573; HSA; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51204; HSA; 1. PE 1: Evidence at protein level; KW Reference proteome {ECO:0000313|Proteomes:UP000000589}. FT DOMAIN 105..177 FT /note="HSA" FT /evidence="ECO:0000259|PROSITE:PS51204" FT DOMAIN 622..787 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000259|PROSITE:PS51192" FT REGION 1..50 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 228..397 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 438..572 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..35 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 228..257 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 268..291 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 292..314 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 381..397 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 443..469 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 478..540 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 541..556 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" SQ SEQUENCE 936 AA; 106320 MW; 7345C78F7D1DAFDF CRC64; MQSSPSTAHP QLPILQTQMV SDGMTGISPQ HIAQDSSLDG PPGPQDGTTV PLEGFSLSHA ADLVNRGQKW EKSHAEIAEQ AKHEAEIETR IAELRKEGFW SLKRLPKVPE PPRPKGHWDY LCEEMQWLSA DFAQERRWKR GVARKVVRMV IRHHEEQRQK EERARREEQA KLRRIASTMA KDVRQFWSNV EKVVQFKQQS RLEEKRKKAL DLHLDFIVGQ TEKYSDLLSQ SLNQPPASSK AGSSPCLGSS SAASSPPPPV SRLDDEDGDF QPQEEEEEDD EETIEVEEQQ EGNDAETQRR EIELLRHEGE LPLEELLRSL PPQLLGGPFS PSQTPSHDSD TQDGPEENIE EEPSQDLEVH PPSSAVTQCN KQRWHPDEDD EEFTANEDEE DEEDTIAAEE QLEGEVDHAM ELSELAREGE LSMEELLQQY AGAYACDASA PASGDSEDED EVEANSSDGE LEETVEEAAQ EDSSSQSDSA EECSEDEEDE HSEEEMSGSS QSEESESDES EDAQSQSQAD EEQDDEGEDD DVDDDDDDGF GVEYLLARDD ERSEVDGGSG PPTPGPTTTL GPKKEITDIA AAAESLQPKG YTLATTQVKT PIPLLLRGQL REYQHIGLDW LVTMYEKKLN GILADEMGLG KTIQTISLLA HLACEKGNWG PHLIIVPTSV MLNWEMELKR WCPSFKILTY YGAQKERKLK RQGWTKPNAF HVCITSYKLV LQDHQAFRRK NWRYLILDEA QNIKNFKSQR WQSLLNFNSQ RRLLLTGTPL QNSLMELWSL MHFLMPHVFQ SHREFKEWFS NPLTGMIEGS QEYNEGLVKR LHKVLRPFLL RRVKVDVEKQ MPKKYEHVIR CRLSKRQRCL YDDFMAQTTT KETLATGHFM SVINILMQLR KVCNHPNLFD PRPVTSPFIT PGICFSTASL VLRATEVHPL QVCSYP //