ID SMCA4_HUMAN Reviewed; 1647 AA. AC P51532; B1A8Z4; B1A8Z5; B1A8Z6; B1A8Z7; E9PBR8; O95052; Q9HBD3; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 2. DT 02-SEP-2026, entry version 256. DE RecName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4 {ECO:0000305}; DE Short=SMARCA4 {ECO:0000303|PubMed:18386774}; DE EC=3.6.4.- {ECO:0000269|PubMed:30339381}; DE AltName: Full=BRG1-associated factor 190A; DE Short=BAF190A; DE AltName: Full=Mitotic growth and transcription activator; DE AltName: Full=Protein BRG-1; DE AltName: Full=Protein brahma homolog 1; DE AltName: Full=SNF2-beta; DE AltName: Full=Transcription activator BRG1; GN Name=SMARCA4 {ECO:0000312|HGNC:HGNC:11100}; GN Synonyms=BAF190A, BRG1 {ECO:0000303|PubMed:15075294, GN ECO:0000303|PubMed:18386774, ECO:0000303|PubMed:8232556}, SNF2B, GN SNF2L4; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=8232556; DOI=10.1038/366170a0; RA Khavari P.A., Peterson C.L., Tamkun J.W., Mendel D.B., Crabtree G.R.; RT "BRG1 contains a conserved domain of the SWI2/SNF2 family necessary for RT normal mitotic growth and transcription."; RL Nature 366:170-174(1993). RN [2] RP SEQUENCE REVISION. RA Khavari P.A., Peterson C.L., Tamkun J.W., Mendel D.B., Crabtree G.R.; RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Fetal brain; RX PubMed=8208605; DOI=10.1093/nar/22.10.1815; RA Chiba H., Muramatsu M., Nomoto A., Kato H.; RT "Two human homologues of Saccharomyces cerevisiae SWI2/SNF2 and Drosophila RT brahma are transcriptional coactivators cooperating with the estrogen RT receptor and the retinoic acid receptor."; RL Nucleic Acids Res. 22:1815-1820(1994). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=11085541; RA Wong A.K.C., Shanahan F., Chen Y., Lian L., Ha P., Hendricks K., RA Ghaffari S., Iliev D., Penn B., Woodland A.-M., Smith R., Salada G., RA Carillo A., Laity K., Gupte J., Swedlund B., Tavtigian S.V., Teng D.H.-F., RA Lees E.; RT "BRG1, a component of the SWI-SNF complex, is mutated in multiple human RT tumor cell lines."; RL Cancer Res. 60:6171-6177(2000). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5). RC TISSUE=Lung; RX PubMed=18386774; DOI=10.1002/humu.20730; RA Medina P.P., Romero O.A., Kohno T., Montuenga L.M., Pio R., Yokota J., RA Sanchez-Cespedes M.; RT "Frequent BRG1/SMARCA4-inactivating mutations in human lung cancer cell RT lines."; RL Hum. Mutat. 29:617-622(2008). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [8] RP INTERACTION WITH NR3C1 AND PGR. RX PubMed=9590696; DOI=10.1038/30032; RA Fryer C.J., Archer T.K.; RT "Chromatin remodelling by the glucocorticoid receptor requires the BRG1 RT complex."; RL Nature 393:88-91(1998). RN [9] RP INTERACTION WITH IKZF1. RX PubMed=10204490; DOI=10.1016/s1074-7613(00)80034-5; RA Kim J., Sif S., Jones B., Jackson A., Koipally J., Heller E., Winandy S., RA Viel A., Sawyer A., Ikeda T., Kingston R., Georgopoulos K.; RT "Ikaros DNA-binding proteins direct formation of chromatin remodeling RT complexes in lymphocytes."; RL Immunity 10:345-355(1999). RN [10] RP IDENTIFICATION IN THE BAF53 COMPLEX WITH BAF53A; RUVBL1 AND TRRAP, AND RP FUNCTION. RX PubMed=11839798; DOI=10.1128/mcb.22.5.1307-1316.2002; RA Park J., Wood M.A., Cole M.D.; RT "BAF53 forms distinct nuclear complexes and functions as a critical c-Myc- RT interacting nuclear cofactor for oncogenic transformation."; RL Mol. Cell. Biol. 22:1307-1316(2002). RN [11] RP INTERACTION WITH NR3C1 AND SMARD1. RX PubMed=12917342; DOI=10.1128/mcb.23.17.6210-6220.2003; RA Hsiao P.W., Fryer C.J., Trotter K.W., Wang W., Archer T.K.; RT "BAF60a mediates critical interactions between nuclear receptors and the RT BRG1 chromatin-remodeling complex for transactivation."; RL Mol. Cell. Biol. 23:6210-6220(2003). RN [12] RP FUNCTION, AND INTERACTION WITH TOPBP1. RX PubMed=15075294; DOI=10.1101/gad.1180204; RA Liu K., Luo Y., Lin F.-T., Lin W.-C.; RT "TopBP1 recruits Brg1/Brm to repress E2F1-induced apoptosis, a novel pRb- RT independent and E2F1-specific control for cell survival."; RL Genes Dev. 18:673-686(2004). RN [13] RP INTERACTION WITH ZMIM2. RX PubMed=16051670; DOI=10.1210/me.2005-0097; RA Huang C.-Y., Beliakoff J., Li X., Lee J., Li X., Sharma M., Lim B., Sun Z.; RT "hZimp7, a novel PIAS-like protein, enhances androgen receptor-mediated RT transcription and interacts with SWI/SNF-like BAF complexes."; RL Mol. Endocrinol. 19:2915-2929(2005). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-11 AND SER-1452, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [15] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [16] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [17] RP IDENTIFICATION IN THE BAF COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=18765789; DOI=10.1101/gad.471408; RA Lange M., Kaynak B., Forster U.B., Toenjes M., Fischer J.J., Grimm C., RA Schlesinger J., Just S., Dunkel I., Krueger T., Mebus S., Lehrach H., RA Lurz R., Gobom J., Rottbauer W., Abdelilah-Seyfried S., Sperling S.; RT "Regulation of muscle development by DPF3, a novel histone acetylation and RT methylation reader of the BAF chromatin remodeling complex."; RL Genes Dev. 22:2370-2384(2008). RN [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-613; SER-1382; SER-1452; RP SER-1570; SER-1575 AND SER-1586, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [19] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [20] RP INTERACTION WITH TERT, AND FUNCTION. RX PubMed=19571879; DOI=10.1038/nature08137; RA Park J.I., Venteicher A.S., Hong J.Y., Choi J., Jun S., Shkreli M., RA Chang W., Meng Z., Cheung P., Ji H., McLaughlin M., Veenstra T.D., RA Nusse R., McCrea P.D., Artandi S.E.; RT "Telomerase modulates Wnt signalling by association with target gene RT chromatin."; RL Nature 460:66-72(2009). RN [21] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-353; THR-609; SER-610; RP SER-613; SER-695; SER-1570; SER-1575 AND SER-1627, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [22] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-188, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [23] RP INVOLVEMENT IN RTPS2. RX PubMed=20137775; DOI=10.1016/j.ajhg.2010.01.013; RA Schneppenheim R., Fruhwald M.C., Gesk S., Hasselblatt M., Jeibmann A., RA Kordes U., Kreuz M., Leuschner I., Martin Subero J.I., Obser T., Oyen F., RA Vater I., Siebert R.; RT "Germline nonsense mutation and somatic inactivation of SMARCA4/BRG1 in a RT family with rhabdoid tumor predisposition syndrome."; RL Am. J. Hum. Genet. 86:279-284(2010). RN [24] RP INTERACTION WITH DEPF2. RX PubMed=20460684; DOI=10.1074/jbc.m109.087783; RA Tando T., Ishizaka A., Watanabe H., Ito T., Iida S., Haraguchi T., RA Mizutani T., Izumi T., Isobe T., Akiyama T., Inoue J., Iba H.; RT "Requiem protein links RelB/p52 and the Brm-type SWI/SNF complex in a RT noncanonical NF-kappaB pathway."; RL J. Biol. Chem. 285:21951-21960(2010). RN [25] RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ZEB1, AND TISSUE RP SPECIFICITY. RX PubMed=20418909; DOI=10.1038/onc.2010.102; RA Sanchez-Tillo E., Lazaro A., Torrent R., Cuatrecasas M., Vaquero E.C., RA Castells A., Engel P., Postigo A.; RT "ZEB1 represses E-cadherin and induces an EMT by recruiting the SWI/SNF RT chromatin-remodeling protein BRG1."; RL Oncogene 29:3490-3500(2010). RN [26] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-695; SER-699; SER-1570 AND RP SER-1575, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [27] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [28] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-613; SER-695; SER-699; RP SER-1382; SER-1627 AND SER-1631, AND IDENTIFICATION BY MASS SPECTROMETRY RP [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [29] RP INTERACTION WITH ADNP2. RX PubMed=23071114; DOI=10.1074/jbc.m112.387027; RA Dresner E., Malishkevich A., Arviv C., Leibman Barak S., Alon S., Ofir R., RA Gothilf Y., Gozes I.; RT "Novel evolutionary-conserved role for the activity-dependent RT neuroprotective protein (ADNP) family that is important for RT erythropoiesis."; RL J. Biol. Chem. 287:40173-40185(2012). RN [30] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-695; SER-699 AND SER-1452, RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [31] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-613 AND SER-1631, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [32] RP SUBCELLULAR LOCATION. RX PubMed=25593309; DOI=10.1101/gad.252189.114; RA Gong F., Chiu L.Y., Cox B., Aymard F., Clouaire T., Leung J.W., RA Cammarata M., Perez M., Agarwal P., Brodbelt J.S., Legube G., Miller K.M.; RT "Screen identifies bromodomain protein ZMYND8 in chromatin recognition of RT transcription-associated DNA damage that promotes homologous RT recombination."; RL Genes Dev. 29:197-211(2015). RN [33] RP INTERACTION WITH ACTL6A. RX PubMed=28649782; DOI=10.1002/humu.23282; RA Marom R., Jain M., Burrage L.C., Song I.W., Graham B.H., Brown C.W., RA Stevens S.J.C., Stegmann A.P.A., Gunter A.T., Kaplan J.D., Gavrilova R.H., RA Shinawi M., Rosenfeld J.A., Bae Y., Tran A.A., Chen Y., Lu J.T., RA Gibbs R.A., Eng C., Yang Y., Rousseau J., de Vries B.B.A., Campeau P.M., RA Lee B.; RT "Heterozygous variants in ACTL6A, encoding a component of the BAF complex, RT are associated with intellectual disability."; RL Hum. Mutat. 38:1365-1371(2017). RN [34] RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1365, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; DOI=10.1038/nsmb.3366; RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C., RA Nielsen M.L.; RT "Site-specific mapping of the human SUMO proteome reveals co-modification RT with phosphorylation."; RL Nat. Struct. Mol. Biol. 24:325-336(2017). RN [35] RP REVIEW ON SWI/SNF CHROMATIN REMODELING COMPLEXES. RX PubMed=22952240; DOI=10.1074/jbc.r111.309302; RA Euskirchen G., Auerbach R.K., Snyder M.; RT "SWI/SNF chromatin-remodeling factors: multiscale analyses and diverse RT functions."; RL J. Biol. Chem. 287:30897-30905(2012). RN [36] RP REVIEW ON SWI/SNF CHROMATIN REMODELING COMPLEXES. RX PubMed=26601204; DOI=10.1126/sciadv.1500447; RA Kadoch C., Crabtree G.R.; RT "Mammalian SWI/SNF chromatin remodeling complexes and cancer: Mechanistic RT insights gained from human genomics."; RL Sci. Adv. 1:E1500447-E1500447(2015). RN [37] RP FUNCTION, AND IDENTIFICATION IN THE GBAF COMPLEX. RX PubMed=29374058; DOI=10.1074/jbc.ra117.001065; RA Alpsoy A., Dykhuizen E.C.; RT "Glioma tumor suppressor candidate region gene 1 (GLTSCR1) and its paralog RT GLTSCR1-like form SWI/SNF chromatin remodeling subcomplexes."; RL J. Biol. Chem. 293:3892-3903(2018). RN [38] RP INTERACTION WITH HDGFL2 AND DPF3, AND FUNCTION. RX PubMed=32459350; DOI=10.1093/nar/gkaa441; RA Zhu X., Lan B., Yi X., He C., Dang L., Zhou X., Lu Y., Sun Y., Liu Z., RA Bai X., Zhang K., Li B., Li M.J., Chen Y., Zhang L.; RT "HRP2-DPF3a-BAF complex coordinates histone modification and chromatin RT remodeling to regulate myogenic gene transcription."; RL Nucleic Acids Res. 48:6563-6582(2020). RN [39] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=30339381; DOI=10.1021/acs.jmedchem.8b01318; RA Papillon J.P.N., Nakajima K., Adair C.D., Hempel J., Jouk A.O., Karki R.G., RA Mathieu S., Moebitz H., Ntaganda R., Smith T., Visser M., Hill S.E., RA Hurtado F.K., Chenail G., Bhang H.C., Bric A., Xiang K., Bushold G., RA Gilbert T., Vattay A., Dooley J., Costa E.A., Park I., Li A., Farley D., RA Lounkine E., Yue Q.K., Xie X., Zhu X., Kulathila R., King D., Hu T., RA Vulic K., Cantwell J., Luu C., Jagani Z.; RT "Discovery of Orally Active Inhibitors of Brahma Homolog (BRM)/SMARCA2 RT ATPase Activity for the Treatment of Brahma Related Gene 1 (BRG1)/SMARCA4- RT Mutant Cancers."; RL J. Med. Chem. 61:10155-10172(2018). RN [40] RP STRUCTURE BY NMR OF 1452-1570 IN COMPLEX WITH ACETYLATED HISTONES, AND RP MUTAGENESIS OF VAL-1484; PHE-1539 AND ASN-1540. RX PubMed=17274598; DOI=10.1021/bi0611208; RA Shen W., Xu C., Huang W., Zhang J., Carlson J.E., Tu X., Wu J., Shi Y.; RT "Solution structure of human Brg1 bromodomain and its specific binding to RT acetylated histone tails."; RL Biochemistry 46:2100-2110(2007). RN [41] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1448-1575 IN COMPLEX WITH RP ACETYLATED HISTONE 3. RX PubMed=17582821; DOI=10.1002/cbic.200600562; RA Singh M., Popowicz G.M., Krajewski M., Holak T.A.; RT "Structural ramification for acetyl-lysine recognition by the bromodomain RT of human BRG1 protein, a central ATPase of the SWI/SNF remodeling RT complex."; RL ChemBioChem 8:1308-1316(2007). RN [42] {ECO:0007744|PDB:6BGH} RP STRUCTURE BY NMR OF 1591-1602 IN COMPLEX WITH BRD3, INTERACTION WITH BRD3, RP AND DOMAIN. RX PubMed=29567837; DOI=10.1074/jbc.ra117.000678; RA Wai D.C.C., Szyszka T.N., Campbell A.E., Kwong C., Wilkinson-White L.E., RA Silva A.P.G., Low J.K.K., Kwan A.H., Gamsjaeger R., Chalmers J.D., RA Patrick W.M., Lu B., Vakoc C.R., Blobel G.A., Mackay J.P.; RT "The BRD3 ET domain recognizes a short peptide motif through a mechanism RT that is conserved across chromatin remodelers and transcriptional RT regulators."; RL J. Biol. Chem. 293:7160-7175(2018). RN [43] RP VARIANTS CSS4 LYS-546 DEL; MET-859; CYS-885; PHE-921; THR-1011 AND RP GLY-1157. RX PubMed=22426308; DOI=10.1038/ng.2219; RA Tsurusaki Y., Okamoto N., Ohashi H., Kosho T., Imai Y., Hibi-Ko Y., RA Kaname T., Naritomi K., Kawame H., Wakui K., Fukushima Y., Homma T., RA Kato M., Hiraki Y., Yamagata T., Yano S., Mizuno S., Sakazume S., Ishii T., RA Nagai T., Shiina M., Ogata K., Ohta T., Niikawa N., Miyatake S., Okada I., RA Mizuguchi T., Doi H., Saitsu H., Miyake N., Matsumoto N.; RT "Mutations affecting components of the SWI/SNF complex cause Coffin-Siris RT syndrome."; RL Nat. Genet. 44:376-378(2012). RN [44] RP INVOLVEMENT IN OTSC12, VARIANT OTSC12 LYS-1578, AND CHARACTERIZATION OF RP VARIANT OTSC12 LYS-1578. RX PubMed=37399313; DOI=10.1136/jmg-2023-109264; RA Drabkin M., Jean M.M., Noy Y., Halperin D., Yogev Y., Wormser O., RA Proskorovski-Ohayon R., Dolgin V., Levaot N., Brumfeld V., Ovadia S., RA Kishner M., Kazenell U., Avraham K.B., Shelef I., Birk O.S.; RT "SMARCA4 mutation causes human otosclerosis and a similar phenotype in RT mice."; RL J. Med. Genet. 61:117-124(2024). CC -!- FUNCTION: ATPase involved in transcriptional activation and repression CC of select genes by chromatin remodeling (alteration of DNA-nucleosome CC topology). Component of SWI/SNF chromatin remodeling complexes that CC carry out key enzymatic activities, changing chromatin structure by CC altering DNA-histone contacts within a nucleosome in an ATP-dependent CC manner (PubMed:15075294, PubMed:29374058, PubMed:30339381, CC PubMed:32459350). Component of the CREST-BRG1 complex, a multiprotein CC complex that regulates promoter activation by orchestrating the CC calcium-dependent release of a repressor complex and the recruitment of CC an activator complex. In resting neurons, transcription of the c-FOS CC promoter is inhibited by SMARCA4-dependent recruitment of a phospho- CC RB1-HDAC repressor complex. Upon calcium influx, RB1 is CC dephosphorylated by calcineurin, which leads to release of the CC repressor complex. At the same time, there is increased recruitment of CC CREBBP to the promoter by a CREST-dependent mechanism, which leads to CC transcriptional activation. The CREST-BRG1 complex also binds to the CC NR2B promoter, and activity-dependent induction of NR2B expression CC involves the release of HDAC1 and recruitment of CREBBP (By CC similarity). Belongs to the neural progenitors-specific chromatin CC remodeling complex (npBAF complex) and the neuron-specific chromatin CC remodeling complex (nBAF complex). During neural development, a switch CC from a stem/progenitor to a postmitotic chromatin remodeling mechanism CC occurs as neurons exit the cell cycle and become committed to their CC adult state. The transition from proliferating neural stem/progenitor CC cells to postmitotic neurons requires a switch in subunit composition CC of the npBAF and nBAF complexes. As neural progenitors exit mitosis and CC differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A CC and PHF10/BAF45A, are exchanged for homologous alternative CC ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron- CC specific complexes (nBAF). The npBAF complex is essential for the self- CC renewal/proliferative capacity of the multipotent neural stem cells. CC The nBAF complex along with CREST plays a role regulating the activity CC of genes essential for dendrite growth. SMARCA4/BAF190A may promote CC neural stem cell self-renewal/proliferation by enhancing Notch- CC dependent proliferative signals, while concurrently making the neural CC stem cell insensitive to SHH-dependent differentiating cues (By CC similarity). Acts as a corepressor of ZEB1 to regulate E-cadherin CC transcription and is required for induction of epithelial-mesenchymal CC transition (EMT) by ZEB1 (PubMed:20418909). Binds via DLX1 to enhancers CC located in the intergenic region between DLX5 and DLX6 and this binding CC is stabilized by the long non-coding RNA (lncRNA) Evf2 (By similarity). CC Binds to RNA in a promiscuous manner (By similarity). In brown adipose CC tissue, involved in the regulation of thermogenic genes expression (By CC similarity). {ECO:0000250|UniProtKB:Q3TKT4, CC ECO:0000250|UniProtKB:Q8K1P7, ECO:0000269|PubMed:15075294, CC ECO:0000269|PubMed:19571879, ECO:0000269|PubMed:20418909, CC ECO:0000269|PubMed:29374058, ECO:0000269|PubMed:30339381, CC ECO:0000269|PubMed:32459350, ECO:0000303|PubMed:22952240, CC ECO:0000303|PubMed:26601204}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + phosphate + H(+); Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; CC Evidence={ECO:0000269|PubMed:30339381}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066; CC Evidence={ECO:0000305|PubMed:30339381}; CC -!- ACTIVITY REGULATION: Binding to RNAs including lncRNA Evf2 leads to CC inhibition of SMARCA4 ATPase and chromatin remodeling activities. CC {ECO:0000250|UniProtKB:Q3TKT4}. CC -!- SUBUNIT: Component of the multiprotein chromatin-remodeling complexes CC SWI/SNF: SWI/SNF-A (BAF), SWI/SNF-B (PBAF) and related complexes. The CC canonical complex contains a catalytic subunit (either CC SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B) and at least SMARCE1, CC ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and SMARCB1/SNF5/BAF47. CC Other subunits specific to each of the complexes may also be present CC permitting several possible developmental- and tissue-specific CC combinations (PubMed:22952240, PubMed:26601204). Component of the BAF CC complex, which includes at least actin (ACTB), ARID1A/BAF250A, CC ARID1B/BAF250B, SMARCA2/BRM, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, CC ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170, CC SMARCB1/SNF5/INI1, and one or more SMARCD1/BAF60A, SMARCD2/BAF60B, or CC SMARCD3/BAF60C. In muscle cells, the BAF complex also contains DPF3 CC (PubMed:18765789). Component of neural progenitors-specific chromatin CC remodeling complex (npBAF complex) composed of at least, ARID1A/BAF250A CC or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, CC SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, CC SMARCC2/BAF170, PHF10/BAF45A, ACTL6A/BAF53A and actin. Component of CC neuron-specific chromatin remodeling complex (nBAF complex) composed of CC at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, CC SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, CC SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, CC DPF1/BAF45B, DPF3/BAF45C, ACTL6B/BAF53B and actin. Component of the CC SWI/SNF-B (PBAF) chromatin remodeling complex, at least composed of CC SMARCA4/BRG1, SMARCB1/BAF47/SNF5, ACTL6A/BAF53A or ACTL6B/BAF53B, CC SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B, perhaps SMARCD3/BAF60C, CC SMARCC1/BAF155, SMARCC2/BAF170, PBRM1/BAF180, ARID2/BAF200 and actin CC (PubMed:26601204). Component of SWI/SNF (GBAF) subcomplex, which CC includes at least BICRA or BICRAL (mutually exclusive), BRD9, SS18, CC SMARCA2/BRM, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, SMARCC1/BAF155, and CC SMARCD1/BAF60A (PubMed:29374058). Component of the BAF53 complex, at CC least composed of BAF53A, RUVBL1, SMARCA4/BRG1/BAF190A, and TRRAP, CC which preferentially acetylates histone H4 (and H2A) within nucleosomes CC (PubMed:11839798). Component of the CREST-BRG1 complex, at least CC composed of SMARCA4/BRG1/BAF190A, SS18L1/CREST, HDAC1, RB1 and SP1 (By CC similarity). Interacts with PHF10/BAF45A (By similarity). Interacts CC with MYOG (By similarity). Interacts directly with IKFZ1; the CC interaction associates IKFZ1 with the BAF complex (PubMed:10204490). CC Interacts with ZEB1 (via N-terminus) (PubMed:20418909). Interacts with CC NR3C1, PGR, SMARD1, TOPBP1 and ZMIM2/ZIMP7 (PubMed:12917342, CC PubMed:15075294, PubMed:16051670, PubMed:9590696). Interacts with (via CC the bromodomain) with TERT; the interaction regulates Wnt-mediated CC signaling (PubMed:19571879). Interacts with TBX21 in a KDM6B-dependent CC manner (By similarity). Interacts with KDM6A and KDM6B (By similarity). CC Interacts with HNRNPU; this interaction occurs in embryonic stem cells CC and stimulates global Pol II-mediated transcription (By similarity). CC Interacts with ACTL6A (PubMed:28649782). Interacts with DLX1 (By CC similarity). Interacts with DPF2 (PubMed:20460684). Interacts with CC DPF3a (isoform 2 of DPF3/BAF45C) and with HDGFL2 in a DPF3a-dependent CC manner (PubMed:32459350). May interact with ADNP2 (PubMed:23071114). CC Interacts with LETMD1 (via C-terminal); the interaction regulates CC transcriptional expression of thermogenic genes in brown adipose tissue CC (By similarity). Interacts (via KIKL motif) with BRD3 (via NET domain) CC (PubMed:29567837). {ECO:0000250|UniProtKB:Q3TKT4, CC ECO:0000269|PubMed:10204490, ECO:0000269|PubMed:11839798, CC ECO:0000269|PubMed:12917342, ECO:0000269|PubMed:15075294, CC ECO:0000269|PubMed:16051670, ECO:0000269|PubMed:17274598, CC ECO:0000269|PubMed:17582821, ECO:0000269|PubMed:18765789, CC ECO:0000269|PubMed:19571879, ECO:0000269|PubMed:20418909, CC ECO:0000269|PubMed:20460684, ECO:0000269|PubMed:28649782, CC ECO:0000269|PubMed:29374058, ECO:0000269|PubMed:29567837, CC ECO:0000269|PubMed:32459350, ECO:0000269|PubMed:9590696, CC ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}. CC -!- INTERACTION: CC P51532; O14497: ARID1A; NbExp=28; IntAct=EBI-302489, EBI-637887; CC P51532; Q8NFD5: ARID1B; NbExp=5; IntAct=EBI-302489, EBI-679921; CC P51532; Q68CP9: ARID2; NbExp=10; IntAct=EBI-302489, EBI-637818; CC P51532; P24385: CCND1; NbExp=5; IntAct=EBI-302489, EBI-375001; CC P51532; O75461: E2F6; NbExp=5; IntAct=EBI-302489, EBI-749694; CC P51532; P16104: H2AX; NbExp=9; IntAct=EBI-302489, EBI-494830; CC P51532; P52333: JAK3; NbExp=5; IntAct=EBI-302489, EBI-518246; CC P51532; Q86U86: PBRM1; NbExp=7; IntAct=EBI-302489, EBI-637807; CC P51532; P37231: PPARG; NbExp=5; IntAct=EBI-302489, EBI-781384; CC P51532; Q06330: RBPJ; NbExp=2; IntAct=EBI-302489, EBI-632552; CC P51532; Q13127: REST; NbExp=2; IntAct=EBI-302489, EBI-926706; CC P51532; P51532: SMARCA4; NbExp=5; IntAct=EBI-302489, EBI-302489; CC P51532; Q12824: SMARCB1; NbExp=43; IntAct=EBI-302489, EBI-358419; CC P51532; Q92922: SMARCC1; NbExp=29; IntAct=EBI-302489, EBI-355653; CC P51532; Q96GM5: SMARCD1; NbExp=15; IntAct=EBI-302489, EBI-358489; CC P51532; Q969G3-2: SMARCE1; NbExp=2; IntAct=EBI-302489, EBI-455096; CC P51532; A4PIV7: SYT-SSX1; NbExp=14; IntAct=EBI-302489, EBI-6901002; CC P51532; O14746: TERT; NbExp=8; IntAct=EBI-302489, EBI-1772203; CC P51532; P06536: Nr3c1; Xeno; NbExp=3; IntAct=EBI-302489, EBI-1187143; CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00549, CC ECO:0000269|PubMed:20418909, ECO:0000269|PubMed:25593309}. CC Note=Colocalizes with long non-coding RNA Evf2 in nuclear RNA clouds CC (By similarity). Localizes to sites of DNA damage (PubMed:25593309). CC {ECO:0000250|UniProtKB:Q3TKT4, ECO:0000269|PubMed:25593309}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=P51532-1; Sequence=Displayed; CC Name=2; CC IsoId=P51532-2; Sequence=VSP_043137; CC Name=3; CC IsoId=P51532-3; Sequence=VSP_043137, VSP_043677, VSP_043678; CC Name=4; CC IsoId=P51532-4; Sequence=VSP_043137, VSP_043677; CC Name=5; CC IsoId=P51532-5; Sequence=VSP_043137, VSP_043678; CC -!- TISSUE SPECIFICITY: Colocalizes with ZEB1 in E-cadherin-negative cells CC from established lines, and stroma of normal colon as well as in de- CC differentiated epithelial cells at the invasion front of colorectal CC carcinomas (at protein level). {ECO:0000269|PubMed:20418909}. CC -!- DOMAIN: The KIKL motif recognizes and binds the NET domain of BRD3. CC {ECO:0000269|PubMed:29567837}. CC -!- DISEASE: Rhabdoid tumor predisposition syndrome 2 (RTPS2) [MIM:613325]: CC A familial cancer syndrome predisposing to renal or extrarenal CC malignant rhabdoid tumors and to a variety of tumors of the central CC nervous system, including choroid plexus carcinoma, medulloblastoma, CC and central primitive neuroectodermal tumors. Rhabdoid tumors are the CC most aggressive and lethal malignancies occurring in early childhood. CC {ECO:0000269|PubMed:20137775}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Coffin-Siris syndrome 4 (CSS4) [MIM:614609]: A form of Coffin- CC Siris syndrome, a congenital multiple malformation syndrome with broad CC phenotypic and genetic variability. Cardinal features are intellectual CC disability, coarse facial features, hypertrichosis, and hypoplastic or CC absent fifth digit nails or phalanges. Additional features include CC malformations of the cardiac, gastrointestinal, genitourinary, and/or CC central nervous systems. Sucking/feeding difficulties, poor growth, CC ophthalmologic abnormalities, hearing impairment, and spinal anomalies CC are common findings. Both autosomal dominant and autosomal recessive CC inheritance patterns have been reported. {ECO:0000269|PubMed:22426308}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- DISEASE: Otosclerosis 12 (OTSC12) [MIM:620792]: A form of otosclerosis, CC a pathological condition of the ear characterized by formation of CC spongy bone in the labyrinth capsule, especially in front of and CC posterior to the footplate of the stapes, resulting in conductive CC hearing impairment. Cochlear otosclerosis may also develop, resulting CC in sensorineural hearing loss. OTSC12 is an autosomal dominant form CC with incomplete penetrance. {ECO:0000269|PubMed:37399313}. Note=The CC disease is caused by variants affecting the gene represented in this CC entry. CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}. CC -!- CAUTION: Like other proteins within the SNF2 family, they do not CC possess helicase activity but instead remodel chromatin via an ATP- CC dependent translocation mechanism. {ECO:0000303|PubMed:22952240, CC ECO:0000303|PubMed:26601204}. CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and CC Haematology; CC URL="https://atlasgeneticsoncology.org/gene/42333/smarca4"; CC -!- WEB RESOURCE: Name=Mendelian genes SWI/SNF related, matrix associated, CC actin dependent regulator of chromatin, subfamily a, member 4 CC (SMARCA4); Note=Leiden Open Variation Database (LOVD); CC URL="https://databases.lovd.nl/shared/genes/SMARCA4"; 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 EMBL; U29175; AAB40977.1; -; mRNA. DR EMBL; D26156; BAA05143.1; -; mRNA. DR EMBL; AF254822; AAG24789.1; -; Genomic_DNA. DR EMBL; EU430756; ACA09750.1; -; mRNA. DR EMBL; EU430757; ACA09751.1; -; mRNA. DR EMBL; EU430758; ACA09752.1; -; mRNA. DR EMBL; EU430759; ACA09753.1; -; mRNA. DR EMBL; AC006127; AAC97986.1; -; Genomic_DNA. DR EMBL; AC006127; AAC97987.1; -; Genomic_DNA. DR EMBL; AC011442; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC011485; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471106; EAW84167.1; -; Genomic_DNA. DR CCDS; CCDS12253.1; -. [P51532-1] DR CCDS; CCDS45972.1; -. [P51532-4] DR CCDS; CCDS45973.1; -. [P51532-3] DR CCDS; CCDS54217.1; -. [P51532-2] DR CCDS; CCDS54218.1; -. [P51532-5] DR PIR; S45252; S45252. DR RefSeq; NP_001122316.1; NM_001128844.3. [P51532-1] DR RefSeq; NP_001122317.1; NM_001128845.2. [P51532-4] DR RefSeq; NP_001122318.1; NM_001128846.2. [P51532-3] DR RefSeq; NP_001122319.1; NM_001128847.4. [P51532-2] DR RefSeq; NP_001122320.1; NM_001128848.2. [P51532-5] DR RefSeq; NP_001361386.1; NM_001374457.1. [P51532-2] DR RefSeq; NP_003063.2; NM_003072.5. [P51532-1] DR RefSeq; XP_024307435.1; XM_024451667.2. [P51532-5] DR RefSeq; XP_047295200.1; XM_047439244.1. [P51532-1] DR RefSeq; XP_047295203.1; XM_047439247.1. [P51532-2] DR RefSeq; XP_047295204.1; XM_047439248.1. [P51532-2] DR RefSeq; XP_047295205.1; XM_047439249.1. [P51532-5] DR RefSeq; XP_047295206.1; XM_047439250.1. [P51532-5] DR RefSeq; XP_047295207.1; XM_047439251.1. [P51532-5] DR RefSeq; XP_054177792.1; XM_054321817.1. [P51532-1] DR RefSeq; XP_054177796.1; XM_054321821.1. [P51532-2] DR RefSeq; XP_054177797.1; XM_054321822.1. [P51532-2] DR RefSeq; XP_054177798.1; XM_054321823.1. [P51532-5] DR RefSeq; XP_054177799.1; XM_054321824.1. [P51532-5] DR RefSeq; XP_054177800.1; XM_054321825.1. [P51532-5] DR RefSeq; XP_054177801.1; XM_054321826.1. [P51532-5] DR PDB; 2GRC; X-ray; 1.50 A; A=1448-1575. DR PDB; 2H60; NMR; -; A=1452-1570. DR PDB; 3UVD; X-ray; 1.85 A; A=1448-1569. DR PDB; 5DKD; X-ray; 2.00 A; A/B=1451-1569. DR PDB; 5EA1; X-ray; 2.00 A; A/B/C=1451-1580. DR PDB; 6BGH; NMR; -; B=1591-1602. DR PDB; 6HR2; X-ray; 1.76 A; A/E=1449-1568. DR PDB; 6LTH; EM; 3.00 A; I=1-1647. DR PDB; 6LTJ; EM; 3.70 A; I=1-1647. DR PDB; 6SY2; NMR; -; A=610-658. DR PDB; 6ZS2; X-ray; 1.57 A; A/B=1451-1569. DR PDB; 7TAB; X-ray; 1.16 A; A=1448-1575. DR PDB; 7TD9; X-ray; 1.61 A; AAA/BBB/CCC=1448-1575. DR PDB; 7VDT; EM; 2.80 A; A=160-1647. DR PDB; 7VDV; EM; 3.40 A; A=160-1647. DR PDB; 7VRB; X-ray; 2.39 A; A/B/C/D=172-213. DR PDB; 7Y8R; EM; 4.40 A; I=1-1647. DR PDB; 8EB1; NMR; -; A=874-878. DR PDB; 8G1Q; X-ray; 3.73 A; H=1447-1569. DR PDB; 8QJR; X-ray; 3.17 A; G/H=1451-1569. DR PDB; 9DTX; X-ray; 2.11 A; D=1448-1569. DR PDB; 9RL4; EM; 3.50 A; I=1-1647. DR PDB; 9RMC; EM; 4.20 A; I=1-1647. DR PDB; 9RN1; EM; 5.90 A; I=1-1647. DR PDB; 9RN2; EM; 4.10 A; I=1-1647. DR PDB; 9UX9; EM; 3.05 A; K=2-1647. DR PDB; 9WBZ; EM; 2.90 A; A=1-1647. DR PDB; 9WC1; EM; 3.40 A; D=1-1647. DR AlphaFoldDB; P51532; -. DR EMDB; EMD-0974; -. DR EMDB; EMD-31925; -. DR EMDB; EMD-31926; -. DR EMDB; EMD-33684; -. DR EMDB; EMD-54030; -. DR EMDB; EMD-54056; -. DR EMDB; EMD-54077; -. DR EMDB; EMD-54078; -. DR EMDB; EMD-64577; -. DR EMDB; EMD-65851; -. DR EMDB; EMD-65854; -. DR SMR; P51532; -. DR BioGRID; 112481; 868. DR ComplexPortal; CPX-1195; Embryonic stem cell-specific SWI/SNF ATP-dependent chromatin remodeling complex. DR ComplexPortal; CPX-1196; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B variant. DR ComplexPortal; CPX-1199; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A variant. DR ComplexPortal; CPX-1204; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant. DR ComplexPortal; CPX-1206; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant. DR ComplexPortal; CPX-1209; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant. DR ComplexPortal; CPX-1211; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant. DR ComplexPortal; CPX-1212; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant. DR ComplexPortal; CPX-1215; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant. DR ComplexPortal; CPX-1216; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant. DR ComplexPortal; CPX-1218; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant. DR ComplexPortal; CPX-1219; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant. DR ComplexPortal; CPX-1221; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant. DR ComplexPortal; CPX-1222; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant. DR ComplexPortal; CPX-1224; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant. DR ComplexPortal; CPX-1226; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant. DR ComplexPortal; CPX-1228; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant. DR ComplexPortal; CPX-4206; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA4 variant. DR ComplexPortal; CPX-4207; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA4 variant. DR ComplexPortal; CPX-4225; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRA-SMARCA4 variant. DR ComplexPortal; CPX-4226; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRAL-SMARCA4 variant. DR CORUM; P51532; -. DR DIP; DIP-24249N; -. DR FunCoup; P51532; 2542. DR IntAct; P51532; 455. DR MINT; P51532; -. DR NDEx; IQUERY-CP-SMARCA4; 13 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000343896; -. DR BindingDB; P51532; -. DR ChEMBL; CHEMBL3085620; -. DR GuidetoPHARMACOLOGY; 2740; -. DR CarbonylDB; P51532; -. DR GlyGen; P51532; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; P51532; -. DR MetOSite; P51532; -. DR PhosphoSitePlus; P51532; -. DR SwissPalm; P51532; -. DR BioMuta; SMARCA4; -. DR DMDM; 116242792; -. DR CPTAC; CPTAC-1367; -. DR jPOST; P51532; -. DR MassIVE; P51532; -. DR PaxDb; 9606-ENSP00000343896; -. DR PeptideAtlas; P51532; -. DR ProteomicsDB; 56327; -. [P51532-1] DR ProteomicsDB; 56328; -. [P51532-2] DR ProteomicsDB; 56329; -. [P51532-3] DR ProteomicsDB; 56330; -. [P51532-4] DR ProteomicsDB; 56331; -. [P51532-5] DR Pumba; P51532; -. DR ABCD; P51532; 4 sequenced antibodies. DR Antibodypedia; 3778; 615 antibodies from 49 providers. DR DNASU; 6597; -. DR Ensembl; ENST00000344626.10; ENSP00000343896.4; ENSG00000127616.23. [P51532-1] DR Ensembl; ENST00000429416.8; ENSP00000395654.1; ENSG00000127616.23. [P51532-1] DR Ensembl; ENST00000444061.8; ENSP00000392837.2; ENSG00000127616.23. [P51532-5] DR Ensembl; ENST00000541122.6; ENSP00000445036.2; ENSG00000127616.23. [P51532-4] DR Ensembl; ENST00000589677.5; ENSP00000464778.1; ENSG00000127616.23. [P51532-3] DR Ensembl; ENST00000590574.6; ENSP00000466963.1; ENSG00000127616.23. [P51532-2] DR Ensembl; ENST00000643296.1; ENSP00000496635.1; ENSG00000127616.23. [P51532-4] DR Ensembl; ENST00000644737.1; ENSP00000495548.1; ENSG00000127616.23. [P51532-4] DR Ensembl; ENST00000645460.1; ENSP00000494463.1; ENSG00000127616.23. [P51532-5] DR Ensembl; ENST00000646484.1; ENSP00000495536.1; ENSG00000127616.23. [P51532-2] DR Ensembl; ENST00000646510.1; ENSP00000494772.1; ENSG00000127616.23. [P51532-2] DR Ensembl; ENST00000647230.1; ENSP00000494676.1; ENSG00000127616.23. [P51532-2] DR Ensembl; ENST00000896342.1; ENSP00000566401.1; ENSG00000127616.23. [P51532-3] DR Ensembl; ENST00000924715.1; ENSP00000594774.1; ENSG00000127616.23. [P51532-1] DR Ensembl; ENST00000924716.1; ENSP00000594775.1; ENSG00000127616.23. [P51532-5] DR Ensembl; ENST00000924718.1; ENSP00000594777.1; ENSG00000127616.23. [P51532-3] DR Ensembl; ENST00000924724.1; ENSP00000594783.1; ENSG00000127616.23. [P51532-5] DR Ensembl; ENST00000924734.1; ENSP00000594793.1; ENSG00000127616.23. [P51532-4] DR Ensembl; ENST00000924739.1; ENSP00000594798.1; ENSG00000127616.23. [P51532-2] DR Ensembl; ENST00000924740.1; ENSP00000594799.1; ENSG00000127616.23. [P51532-5] DR Ensembl; ENST00000924746.1; ENSP00000594805.1; ENSG00000127616.23. [P51532-2] DR Ensembl; ENST00000924749.1; ENSP00000594808.1; ENSG00000127616.23. [P51532-4] DR Ensembl; ENST00000924751.1; ENSP00000594810.1; ENSG00000127616.23. [P51532-3] DR Ensembl; ENST00000924752.1; ENSP00000594811.1; ENSG00000127616.23. [P51532-5] DR Ensembl; ENST00000924754.1; ENSP00000594813.1; ENSG00000127616.23. [P51532-1] DR GeneID; 6597; -. DR KEGG; hsa:6597; -. DR MANE-Select; ENST00000344626.10; ENSP00000343896.4; NM_003072.5; NP_003063.2. DR UCSC; uc002mqf.5; human. [P51532-1] DR AGR; HGNC:11100; -. DR CIViC; 6597; 15 evidence items across 7 molecular profiles. DR ClinPGx; PA35950; -. DR CTD; 6597; -. DR DisGeNET; 6597; -. DR GeneCards; SMARCA4; -. DR GeneReviews; SMARCA4; -. DR HGNC; HGNC:11100; SMARCA4. DR HPA; ENSG00000127616; Low tissue specificity. DR MalaCards; SMARCA4; -. DR MIM; 603254; gene. DR MIM; 613325; phenotype. DR MIM; 614609; phenotype. DR MIM; 620792; phenotype. DR OpenTargets; ENSG00000127616; -. DR Orphanet; 1465; Coffin-Siris syndrome. DR Orphanet; 231108; Rhabdoid tumor predisposition syndrome. DR Orphanet; 370396; Small cell carcinoma of the ovary. DR Orphanet; 466962; SMARCA4-deficient sarcoma of thorax. DR VEuPathDB; HostDB:ENSG00000127616; -. DR eggNOG; KOG0386; Eukaryota. DR GeneTree; ENSGT00940000156887; -. DR HOGENOM; CLU_000315_15_0_1; -. DR InParanoid; P51532; -. DR OMA; YGPGHKL; -. DR OrthoDB; 6017at2759; -. DR PAN-GO; P51532; 7 GO annotations based on evolutionary models. DR PhylomeDB; P51532; -. DR PathwayCommons; P51532; -. DR Reactome; R-HSA-1266695; Interleukin-7 signaling. DR Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex. DR Reactome; R-HSA-3214858; RMTs methylate histone arginines. DR Reactome; R-HSA-3247509; Chromatin modifying enzymes. DR Reactome; R-HSA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known. DR Reactome; R-HSA-9619665; EGR2 and SOX10-mediated initiation of Schwann cell myelination. DR Reactome; R-HSA-9764725; Negative Regulation of CDH1 Gene Transcription. DR Reactome; R-HSA-9824585; Regulation of MITF-M-dependent genes involved in pigmentation. DR Reactome; R-HSA-9845323; Regulation of endogenous retroelements by Piwi-interacting RNAs (piRNAs). DR Reactome; R-HSA-9933937; Formation of the canonical BAF (cBAF) complex. DR Reactome; R-HSA-9933939; Formation of the polybromo-BAF (pBAF) complex. DR Reactome; R-HSA-9933946; Formation of the embryonic stem cell BAF (esBAF) complex. DR Reactome; R-HSA-9933947; Formation of the non-canonical BAF (ncBAF) complex. DR Reactome; R-HSA-9934037; Formation of neuronal progenitor and neuronal BAF (npBAF and nBAF). DR Reactome; R-HSA-9976102; Differentiation of naive CD4+ T cells to T helper 2 cells (Th2 cells). DR SignaLink; P51532; -. DR SIGNOR; P51532; -. DR Agora; ENSG00000127616; -. DR BioGRID-ORCS; 6597; 222 hits in 1208 CRISPR screens. DR CD-CODE; 1A18FFC4; Paraspeckle. DR CD-CODE; 804901D1; Nuclear speckle. DR CD-CODE; 91857CE7; Nucleolus. DR CD-CODE; B5B9A610; PML body. DR ChiTaRS; SMARCA4; human. DR EvolutionaryTrace; P51532; -. DR GeneWiki; SMARCA4; -. DR GenomeRNAi; 6597; -. DR Pharos; P51532; Tchem. DR PRO; PR:P51532; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; P51532; protein. DR Bgee; ENSG00000127616; Expressed in ganglionic eminence and 200 other cell types or tissues. DR ExpressionAtlas; P51532; baseline and differential. DR GO; GO:0140092; C:bBAF complex; NAS:ComplexPortal. DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL. DR GO; GO:0000791; C:euchromatin; IEA:Ensembl. DR GO; GO:0005576; C:extracellular region; HDA:UniProtKB. DR GO; GO:0001650; C:fibrillar center; IDA:HPA. DR GO; GO:0140288; C:GBAF complex; NAS:ComplexPortal. DR GO; GO:0000776; C:kinetochore; NAS:ComplexPortal. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0071565; C:nBAF complex; ISS:UniProtKB. DR GO; GO:0071564; C:npBAF complex; IDA:BHF-UCL. DR GO; GO:0016363; C:nuclear matrix; NAS:ComplexPortal. DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0005726; C:perichromatin fibrils; IEA:Ensembl. DR GO; GO:0032991; C:protein-containing complex; HDA:UniProtKB. DR GO; GO:0016586; C:RSC-type complex; NAS:ComplexPortal. DR GO; GO:0016514; C:SWI/SNF complex; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0016887; F:ATP hydrolysis activity; EXP:UniProtKB. DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IGI:BHF-UCL. DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IDA:BHF-UCL. DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl. DR GO; GO:0070182; F:DNA polymerase binding; IPI:BHF-UCL. DR GO; GO:0004386; F:helicase activity; TAS:ProtInc. DR GO; GO:0042393; F:histone binding; IEA:InterPro. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0106222; F:lncRNA binding; IEA:Ensembl. DR GO; GO:0050681; F:nuclear androgen receptor binding; IPI:BHF-UCL. DR GO; GO:0002039; F:p53 binding; IPI:BHF-UCL. DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IEA:Ensembl. DR GO; GO:0030957; F:Tat protein binding; IPI:BHF-UCL. DR GO; GO:0003713; F:transcription coactivator activity; IDA:BHF-UCL. DR GO; GO:0001221; F:transcription coregulator binding; IPI:UniProtKB. DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB. DR GO; GO:0006338; P:chromatin remodeling; IDA:BHF-UCL. DR GO; GO:0043923; P:host-mediated activation of viral transcription; IMP:BHF-UCL. DR GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; IMP:BHF-UCL. DR GO; GO:0045596; P:negative regulation of cell differentiation; NAS:ComplexPortal. DR GO; GO:0030308; P:negative regulation of cell growth; IMP:BHF-UCL. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:BHF-UCL. DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; TAS:BHF-UCL. DR GO; GO:0007399; P:nervous system development; IEA:Ensembl. DR GO; GO:0003407; P:neural retina development; IEP:BHF-UCL. DR GO; GO:0045597; P:positive regulation of cell differentiation; NAS:ComplexPortal. DR GO; GO:0008284; P:positive regulation of cell population proliferation; NAS:ComplexPortal. DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:UniProt. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IMP:BHF-UCL. DR GO; GO:2000781; P:positive regulation of double-strand break repair; NAS:ComplexPortal. DR GO; GO:1902661; P:positive regulation of glucose mediated signaling pathway; IDA:UniProtKB. DR GO; GO:1902895; P:positive regulation of miRNA transcription; IMP:BHF-UCL. DR GO; GO:0045663; P:positive regulation of myoblast differentiation; NAS:ComplexPortal. DR GO; GO:1901798; P:positive regulation of signal transduction by p53 class mediator; IDA:BHF-UCL. DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; NAS:ComplexPortal. DR GO; GO:0045582; P:positive regulation of T cell differentiation; NAS:ComplexPortal. DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL. DR GO; GO:1901838; P:positive regulation of transcription of nucleolar large rRNA by RNA polymerase I; IMP:UniProtKB. DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IMP:BHF-UCL. DR GO; GO:0070316; P:regulation of G0 to G1 transition; NAS:ComplexPortal. DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; NAS:ComplexPortal. DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; NAS:ComplexPortal. DR GO; GO:2000819; P:regulation of nucleotide-excision repair; NAS:ComplexPortal. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; NAS:BHF-UCL. DR GO; GO:0001188; P:RNA polymerase I preinitiation complex assembly; IEA:GOC. DR GO; GO:0045815; P:transcription initiation-coupled chromatin remodeling; ISS:UniProt. DR CDD; cd05516; Bromo_SNF2L2; 1. DR CDD; cd18062; DEXHc_SMARCA4; 1. DR CDD; cd18793; SF2_C_SNF; 1. DR FunFam; 3.40.50.10810:FF:000008; Chromatin structure-remodeling complex subunit snf21; 1. DR FunFam; 1.20.920.10:FF:000004; probable global transcription activator SNF2L2 isoform X1; 1. DR FunFam; 3.40.5.120:FF:000001; probable global transcription activator SNF2L2 isoform X1; 1. DR FunFam; 3.40.50.300:FF:000116; probable global transcription activator SNF2L2 isoform X1; 1. DR FunFam; 1.20.5.170:FF:000089; Putative global transcription activator SNF2L2; 1. DR Gene3D; 1.20.5.170; -; 1. DR Gene3D; 3.40.5.120; -; 1. DR Gene3D; 1.20.920.10; Bromodomain-like; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1. DR InterPro; IPR030100; BRG1_ATP-bd. DR InterPro; IPR006576; BRK_domain. DR InterPro; IPR037259; BRK_sf. DR InterPro; IPR001487; Bromodomain. DR InterPro; IPR036427; Bromodomain-like_sf. DR InterPro; IPR018359; Bromodomain_CS. DR InterPro; IPR014978; Gln-Leu-Gln_QLQ. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C-like. DR InterPro; IPR014012; HSA_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR029295; SnAC. DR InterPro; IPR038718; SNF2-like_sf. DR InterPro; IPR049730; SNF2/RAD54-like_C. DR InterPro; IPR000330; SNF2_N. DR PANTHER; PTHR10799; SNF2/RAD54 HELICASE FAMILY; 1. DR Pfam; PF07533; BRK; 1. DR Pfam; PF00439; Bromodomain; 1. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF07529; HSA; 1. DR Pfam; PF08880; QLQ; 1. DR Pfam; PF14619; SnAC; 1. DR Pfam; PF00176; SNF2-rel_dom; 1. DR PRINTS; PR00503; BROMODOMAIN. DR SMART; SM00592; BRK; 1. DR SMART; SM00297; BROMO; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SMART; SM00573; HSA; 1. DR SMART; SM00951; QLQ; 1. DR SMART; SM01314; SnAC; 1. DR SUPFAM; SSF160481; BRK domain-like; 1. DR SUPFAM; SSF47370; Bromodomain; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR PROSITE; PS00633; BROMODOMAIN_1; 1. DR PROSITE; PS50014; BROMODOMAIN_2; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR PROSITE; PS51204; HSA; 1. DR PROSITE; PS51666; QLQ; 1. DR PDBsum; 2GRC; -. DR PDBsum; 2H60; -. DR PDBsum; 3UVD; -. DR PDBsum; 5DKD; -. DR PDBsum; 5EA1; -. DR PDBsum; 6BGH; -. DR PDBsum; 6HR2; -. DR PDBsum; 6LTH; -. DR PDBsum; 6LTJ; -. DR PDBsum; 6SY2; -. DR PDBsum; 6ZS2; -. DR PDBsum; 7TAB; -. DR PDBsum; 7TD9; -. DR PDBsum; 7VDT; -. DR PDBsum; 7VDV; -. DR PDBsum; 7VRB; -. DR PDBsum; 7Y8R; -. DR PDBsum; 8EB1; -. DR PDBsum; 8G1Q; -. DR PDBsum; 8QJR; -. DR PDBsum; 9DTX; -. DR PDBsum; 9RL4; -. DR PDBsum; 9RMC; -. DR PDBsum; 9RN1; -. DR PDBsum; 9RN2; -. DR PDBsum; 9UX9; -. DR PDBsum; 9WBZ; -. DR PDBsum; 9WC1; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Activator; Alternative splicing; ATP-binding; KW Bromodomain; Chromatin regulator; Deafness; Disease variant; Hydrolase; KW Intellectual disability; Isopeptide bond; Neurogenesis; Nucleotide-binding; KW Nucleus; Phosphoprotein; Proteomics identification; Reference proteome; KW Repressor; RNA-binding; Transcription; Transcription regulation; KW Ubl conjugation. FT CHAIN 1..1647 FT /note="SWI/SNF-related matrix-associated actin-dependent FT regulator of chromatin subfamily A member 4" FT /id="PRO_0000074353" FT DOMAIN 171..206 FT /note="QLQ" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01001" FT DOMAIN 460..532 FT /note="HSA" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549" FT DOMAIN 766..931 FT /note="Helicase ATP-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT DOMAIN 1084..1246 FT /note="Helicase C-terminal" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542" FT DOMAIN 1453..1564 FT /note="Bromo" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035" FT REGION 1..282 FT /note="Necessary for interaction with SS18L1/CREST" FT /evidence="ECO:0000250" FT REGION 1..177 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 198..352 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 462..728 FT /note="RNA-binding region which is sufficient for binding FT to lncRNA Evf2" FT /evidence="ECO:0000250|UniProtKB:Q3TKT4" FT REGION 577..610 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 647..699 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 837..916 FT /note="Sufficient for interaction with DLX1" FT /evidence="ECO:0000250|UniProtKB:Q3TKT4" FT REGION 1247..1446 FT /note="Sufficient for interaction with DLX1" FT /evidence="ECO:0000250|UniProtKB:Q3TKT4" FT REGION 1254..1299 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1400..1460 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1564..1647 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 881..884 FT /note="DEGH box" FT MOTIF 1596..1599 FT /note="KIKL" FT /evidence="ECO:0000269|PubMed:29567837" FT COMPBIAS 1..23 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 24..45 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 74..89 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 130..147 FT /note="Low complexity" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 162..177 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 231..249 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 259..286 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 302..327 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 579..588 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 658..673 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1262..1271 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1284..1299 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1429..1438 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1567..1587 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1600..1610 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1611..1621 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1627..1637 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT BINDING 779..786 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541" FT SITE 1539..1540 FT /note="Required for binding to 'Lys-15'-acetylated histone FT 3" FT MOD_RES 11 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:17081983" FT MOD_RES 188 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 353 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 609 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 610 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 613 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:24275569" FT MOD_RES 626 FT /note="N6-acetyllysine" FT /evidence="ECO:0000250|UniProtKB:Q6DIC0" FT MOD_RES 695 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 699 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 1382 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692" FT MOD_RES 1423 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q3TKT4" FT MOD_RES 1452 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163" FT MOD_RES 1570 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231" FT MOD_RES 1575 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231" FT MOD_RES 1586 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 1627 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:21406692" FT MOD_RES 1631 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:24275569" FT CROSSLNK 1365 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in SUMO2)" FT /evidence="ECO:0007744|PubMed:28112733" FT VAR_SEQ 1259..1291 FT /note="Missing (in isoform 2, isoform 3, isoform 4 and FT isoform 5)" FT /evidence="ECO:0000303|PubMed:18386774" FT /id="VSP_043137" FT VAR_SEQ 1388 FT /note="W -> WLKT (in isoform 3 and isoform 4)" FT /evidence="ECO:0000303|PubMed:18386774" FT /id="VSP_043677" FT VAR_SEQ 1475 FT /note="Missing (in isoform 3 and isoform 5)" FT /evidence="ECO:0000303|PubMed:18386774" FT /id="VSP_043678" FT VARIANT 546 FT /note="Missing (in CSS4)" FT /evidence="ECO:0000269|PubMed:22426308" FT /id="VAR_068209" FT VARIANT 561 FT /note="V -> E (in dbSNP:rs1804579)" FT /id="VAR_028215" FT VARIANT 859 FT /note="T -> M (in CSS4; dbSNP:rs281875226)" FT /evidence="ECO:0000269|PubMed:22426308" FT /id="VAR_068210" FT VARIANT 885 FT /note="R -> C (in CSS4; dbSNP:rs281875227)" FT /evidence="ECO:0000269|PubMed:22426308" FT /id="VAR_068211" FT VARIANT 921 FT /note="L -> F (in CSS4; dbSNP:rs281875228)" FT /evidence="ECO:0000269|PubMed:22426308" FT /id="VAR_068212" FT VARIANT 1011 FT /note="M -> T (in CSS4; dbSNP:rs281875229)" FT /evidence="ECO:0000269|PubMed:22426308" FT /id="VAR_068213" FT VARIANT 1036 FT /note="M -> I (in dbSNP:rs1801514)" FT /id="VAR_028216" FT VARIANT 1157 FT /note="R -> G (in CSS4; dbSNP:rs281875230)" FT /evidence="ECO:0000269|PubMed:22426308" FT /id="VAR_068214" FT VARIANT 1578 FT /note="E -> K (in OTSC12; likely pathogenic; CRISP-Cas9 FT transgenic mice carrying this variant exhibit marked FT hearing impairment, with a highly irregular structure of FT the incus bone in the auditory bullae, causing disruption FT in the ossicular chain)" FT /evidence="ECO:0000269|PubMed:37399313" FT /id="VAR_089541" FT MUTAGEN 1484 FT /note="V->A: No effect on binding to 'Lys-15'-acetylated FT histone H3." FT /evidence="ECO:0000269|PubMed:17274598" FT MUTAGEN 1539 FT /note="F->A: Abolishes binding to 'Lys-15'-acetylated FT histone H3." FT /evidence="ECO:0000269|PubMed:17274598" FT MUTAGEN 1540 FT /note="N->A: Abolishes binding to 'Lys-15'-acetylated FT histone H3." FT /evidence="ECO:0000269|PubMed:17274598" FT CONFLICT 569 FT /note="R -> P (in Ref. 1; AAB40977 and 3; BAA05143)" FT /evidence="ECO:0000305" FT HELIX 174..191 FT /evidence="ECO:0007829|PDB:7VRB" FT HELIX 194..197 FT /evidence="ECO:0007829|PDB:7VRB" FT HELIX 198..203 FT /evidence="ECO:0007829|PDB:7VRB" FT HELIX 363..386 FT /evidence="ECO:0007829|PDB:6LTH" FT TURN 392..394 FT /evidence="ECO:0007829|PDB:7VDV" FT HELIX 397..408 FT /evidence="ECO:0007829|PDB:6LTH" FT HELIX 410..427 FT /evidence="ECO:0007829|PDB:6LTH" FT HELIX 431..433 FT /evidence="ECO:0007829|PDB:6LTH" FT STRAND 434..437 FT /evidence="ECO:0007829|PDB:6LTH" FT HELIX 447..474 FT /evidence="ECO:0007829|PDB:6LTH" FT HELIX 543..557 FT /evidence="ECO:0007829|PDB:7VDT" FT TURN 612..614 FT /evidence="ECO:0007829|PDB:6SY2" FT STRAND 619..621 FT /evidence="ECO:0007829|PDB:6SY2" FT TURN 622..624 FT /evidence="ECO:0007829|PDB:6SY2" FT TURN 630..632 FT /evidence="ECO:0007829|PDB:6SY2" FT TURN 636..638 FT /evidence="ECO:0007829|PDB:6SY2" FT HELIX 639..645 FT /evidence="ECO:0007829|PDB:6SY2" FT STRAND 649..651 FT /evidence="ECO:0007829|PDB:6SY2" FT HELIX 732..735 FT /evidence="ECO:0007829|PDB:7VDT" FT TURN 741..744 FT /evidence="ECO:0007829|PDB:7VDV" FT HELIX 756..770 FT /evidence="ECO:0007829|PDB:7VDT" FT HELIX 785..798 FT /evidence="ECO:0007829|PDB:7VDT" FT STRAND 807..810 FT /evidence="ECO:0007829|PDB:7VDT" FT HELIX 812..814 FT /evidence="ECO:0007829|PDB:7VDT" FT HELIX 815..825 FT /evidence="ECO:0007829|PDB:7VDT" FT STRAND 831..833 FT /evidence="ECO:0007829|PDB:7VDT" FT HELIX 838..843 FT /evidence="ECO:0007829|PDB:7VDT" FT HELIX 845..850 FT /evidence="ECO:0007829|PDB:7VDT" FT STRAND 854..859 FT /evidence="ECO:0007829|PDB:7VDT" FT HELIX 860..865 FT /evidence="ECO:0007829|PDB:7VDT" FT HELIX 867..870 FT /evidence="ECO:0007829|PDB:7VDT" FT STRAND 878..882 FT /evidence="ECO:0007829|PDB:7VDT" FT HELIX 883..887 FT /evidence="ECO:0007829|PDB:7VDT" FT HELIX 892..900 FT /evidence="ECO:0007829|PDB:7VDT" FT STRAND 904..909 FT /evidence="ECO:0007829|PDB:7VDT" FT STRAND 911..913 FT /evidence="ECO:0007829|PDB:7VDV" FT HELIX 919..928 FT /evidence="ECO:0007829|PDB:7VDT" FT TURN 930..933 FT /evidence="ECO:0007829|PDB:7VDT" FT STRAND 942..945 FT /evidence="ECO:0007829|PDB:7VDV" FT STRAND 956..960 FT /evidence="ECO:0007829|PDB:7VDT" FT HELIX 963..971 FT /evidence="ECO:0007829|PDB:7VDT" FT HELIX 973..975 FT /evidence="ECO:0007829|PDB:7VDV" FT HELIX 981..984 FT /evidence="ECO:0007829|PDB:7VDT" FT STRAND 992..996 FT /evidence="ECO:0007829|PDB:7VDT" FT HELIX 999..1001 FT /evidence="ECO:0007829|PDB:7VDT" FT HELIX 1002..1013 FT /evidence="ECO:0007829|PDB:7VDT" FT STRAND 1016..1018 FT /evidence="ECO:0007829|PDB:7VDV" FT STRAND 1032..1034 FT /evidence="ECO:0007829|PDB:7VDV" FT HELIX 1038..1047 FT /evidence="ECO:0007829|PDB:7VDT" FT HELIX 1049..1052 FT /evidence="ECO:0007829|PDB:7VDT" FT HELIX 1055..1062 FT /evidence="ECO:0007829|PDB:7VDT" FT STRAND 1067..1069 FT /evidence="ECO:0007829|PDB:7VDT" FT HELIX 1073..1078 FT /evidence="ECO:0007829|PDB:7VDT" FT HELIX 1080..1094 FT /evidence="ECO:0007829|PDB:7VDT" FT STRAND 1099..1104 FT /evidence="ECO:0007829|PDB:7VDT" FT HELIX 1106..1118 FT /evidence="ECO:0007829|PDB:7VDT" FT STRAND 1123..1126 FT /evidence="ECO:0007829|PDB:7VDT" FT STRAND 1128..1130 FT /evidence="ECO:0007829|PDB:7VDV" FT HELIX 1132..1143 FT /evidence="ECO:0007829|PDB:7VDT" FT STRAND 1151..1155 FT /evidence="ECO:0007829|PDB:7VDT" FT HELIX 1156..1159 FT /evidence="ECO:0007829|PDB:7VDT" FT STRAND 1160..1162 FT /evidence="ECO:0007829|PDB:7VDT" FT STRAND 1170..1175 FT /evidence="ECO:0007829|PDB:7VDT" FT HELIX 1180..1187 FT /evidence="ECO:0007829|PDB:7VDT" FT TURN 1188..1190 FT /evidence="ECO:0007829|PDB:7VDT" FT STRAND 1200..1204 FT /evidence="ECO:0007829|PDB:7VDT" FT HELIX 1210..1225 FT /evidence="ECO:0007829|PDB:7VDT" FT HELIX 1226..1230 FT /evidence="ECO:0007829|PDB:7VDT" FT STRAND 1235..1237 FT /evidence="ECO:0007829|PDB:7VDT" FT HELIX 1242..1252 FT /evidence="ECO:0007829|PDB:7VDT" FT TURN 1253..1256 FT /evidence="ECO:0007829|PDB:7VDT" FT HELIX 1301..1306 FT /evidence="ECO:0007829|PDB:7VDT" FT HELIX 1310..1327 FT /evidence="ECO:0007829|PDB:7VDT" FT TURN 1337..1343 FT /evidence="ECO:0007829|PDB:7VDT" FT HELIX 1344..1348 FT /evidence="ECO:0007829|PDB:7VDT" FT STRAND 1368..1370 FT /evidence="ECO:0007829|PDB:7VDT" FT HELIX 1449..1455 FT /evidence="ECO:0007829|PDB:7TAB" FT HELIX 1456..1471 FT /evidence="ECO:0007829|PDB:7TAB" FT TURN 1475..1477 FT /evidence="ECO:0007829|PDB:7TAB" FT HELIX 1481..1485 FT /evidence="ECO:0007829|PDB:7TAB" FT HELIX 1488..1490 FT /evidence="ECO:0007829|PDB:7TAB" FT TURN 1491..1493 FT /evidence="ECO:0007829|PDB:7TAB" FT HELIX 1495..1500 FT /evidence="ECO:0007829|PDB:7TAB" FT HELIX 1507..1515 FT /evidence="ECO:0007829|PDB:7TAB" FT HELIX 1522..1539 FT /evidence="ECO:0007829|PDB:7TAB" FT STRAND 1542..1544 FT /evidence="ECO:0007829|PDB:2H60" FT HELIX 1545..1568 FT /evidence="ECO:0007829|PDB:7TAB" FT HELIX 1571..1577 FT /evidence="ECO:0007829|PDB:5EA1" SQ SEQUENCE 1647 AA; 184646 MW; ABDA5EDBF10D7D28 CRC64; MSTPDPPLGG TPRPGPSPGP GPSPGAMLGP SPGPSPGSAH SMMGPSPGPP SAGHPIPTQG PGGYPQDNMH QMHKPMESMH EKGMSDDPRY NQMKGMGMRS GGHAGMGPPP SPMDQHSQGY PSPLGGSEHA SSPVPASGPS SGPQMSSGPG GAPLDGADPQ ALGQQNRGPT PFNQNQLHQL RAQIMAYKML ARGQPLPDHL QMAVQGKRPM PGMQQQMPTL PPPSVSATGP GPGPGPGPGP GPGPAPPNYS RPHGMGGPNM PPPGPSGVPP GMPGQPPGGP PKPWPEGPMA NAAAPTSTPQ KLIPPQPTGR PSPAPPAVPP AASPVMPPQT QSPGQPAQPA PMVPLHQKQS RITPIQKPRG LDPVEILQER EYRLQARIAH RIQELENLPG SLAGDLRTKA TIELKALRLL NFQRQLRQEV VVCMRRDTAL ETALNAKAYK RSKRQSLREA RITEKLEKQQ KIEQERKRRQ KHQEYLNSIL QHAKDFKEYH RSVTGKIQKL TKAVATYHAN TEREQKKENE RIEKERMRRL MAEDEEGYRK LIDQKKDKRL AYLLQQTDEY VANLTELVRQ HKAAQVAKEK KKKKKKKKAE NAEGQTPAIG PDGEPLDETS QMSDLPVKVI HVESGKILTG TDAPKAGQLE AWLEMNPGYE VAPRSDSEES GSEEEEEEEE EEQPQAAQPP TLPVEEKKKI PDPDSDDVSE VDARHIIENA KQDVDDEYGV SQALARGLQS YYAVAHAVTE RVDKQSALMV NGVLKQYQIK GLEWLVSLYN NNLNGILADE MGLGKTIQTI ALITYLMEHK RINGPFLIIV PLSTLSNWAY EFDKWAPSVV KVSYKGSPAA RRAFVPQLRS GKFNVLLTTY EYIIKDKHIL AKIRWKYMIV DEGHRMKNHH CKLTQVLNTH YVAPRRLLLT GTPLQNKLPE LWALLNFLLP TIFKSCSTFE QWFNAPFAMT GEKVDLNEEE TILIIRRLHK VLRPFLLRRL KKEVEAQLPE KVEYVIKCDM SALQRVLYRH MQAKGVLLTD GSEKDKKGKG GTKTLMNTIM QLRKICNHPY MFQHIEESFS EHLGFTGGIV QGLDLYRASG KFELLDRILP KLRATNHKVL LFCQMTSLMT IMEDYFAYRG FKYLRLDGTT KAEDRGMLLK TFNEPGSEYF IFLLSTRAGG LGLNLQSADT VIIFDSDWNP HQDLQAQDRA HRIGQQNEVR VLRLCTVNSV EEKILAAAKY KLNVDQKVIQ AGMFDQKSSS HERRAFLQAI LEHEEQDESR HCSTGSGSAS FAHTAPPPAG VNPDLEEPPL KEEDEVPDDE TVNQMIARHE EEFDLFMRMD LDRRREEARN PKRKPRLMEE DELPSWIIKD DAEVERLTCE EEEEKMFGRG SRHRKEVDYS DSLTEKQWLK AIEEGTLEEI EEEVRQKKSS RKRKRDSDAG SSTPTTSTRS RDKDDESKKQ KKRGRPPAEK LSPNPPNLTK KMKKIVDAVI KYKDSSSGRQ LSEVFIQLPS RKELPEYYEL IRKPVDFKKI KERIRNHKYR SLNDLEKDVM LLCQNAQTFN LEGSLIYEDS IVLQSVFTSV RQKIEKEDDS EGEESEEEEE GEEEGSESES RSVKVKIKLG RKEKAQDRLK GGRRRPSRGS RAKPVVSDDD SEEEQEEDRS GSGSEED //