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Transcription activator BRG1 (EC 3.6.4.-) (ATP-dependent helicase SMARCA4) (BRG1-associated factor 190A) (BAF190A) (Mitotic growth and transcription activator) (Protein BRG-1) (Protein brahma homolog 1) (SNF2-beta) (SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4)

 SMCA4_HUMAN             Reviewed;        1647 AA.
P51532; B1A8Z4; B1A8Z5; B1A8Z6; B1A8Z7; E9PBR8; O95052; Q9HBD3;
01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
17-OCT-2006, sequence version 2.
10-OCT-2018, entry version 212.
RecName: Full=Transcription activator BRG1;
EC=3.6.4.-;
AltName: Full=ATP-dependent helicase SMARCA4;
AltName: Full=BRG1-associated factor 190A;
Short=BAF190A;
AltName: Full=Mitotic growth and transcription activator;
AltName: Full=Protein BRG-1;
AltName: Full=Protein brahma homolog 1;
AltName: Full=SNF2-beta;
AltName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4;
Name=SMARCA4; Synonyms=BAF190A, BRG1, SNF2B, SNF2L4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=8232556; DOI=10.1038/366170a0;
Khavari P.A., Peterson C.L., Tamkun J.W., Mendel D.B., Crabtree G.R.;
"BRG1 contains a conserved domain of the SWI2/SNF2 family necessary
for normal mitotic growth and transcription.";
Nature 366:170-174(1993).
[2]
SEQUENCE REVISION.
Khavari P.A., Peterson C.L., Tamkun J.W., Mendel D.B., Crabtree G.R.;
Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Fetal brain;
PubMed=8208605; DOI=10.1093/nar/22.10.1815;
Chiba H., Muramatsu M., Nomoto A., Kato H.;
"Two human homologues of Saccharomyces cerevisiae SWI2/SNF2 and
Drosophila brahma are transcriptional coactivators cooperating with
the estrogen receptor and the retinoic acid receptor.";
Nucleic Acids Res. 22:1815-1820(1994).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11085541;
Wong A.K.C., Shanahan F., Chen Y., Lian L., Ha P., Hendricks K.,
Ghaffari S., Iliev D., Penn B., Woodland A.-M., Smith R., Salada G.,
Carillo A., Laity K., Gupte J., Swedlund B., Tavtigian S.V.,
Teng D.H.-F., Lees E.;
"BRG1, a component of the SWI-SNF complex, is mutated in multiple
human tumor cell lines.";
Cancer Res. 60:6171-6177(2000).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5).
TISSUE=Lung;
PubMed=18386774; DOI=10.1002/humu.20730;
Medina P.P., Romero O.A., Kohno T., Montuenga L.M., Pio R., Yokota J.,
Sanchez-Cespedes M.;
"Frequent BRG1/SMARCA4-inactivating mutations in human lung cancer
cell lines.";
Hum. Mutat. 29:617-622(2008).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[8]
INTERACTION WITH NR3C1 AND PGR.
PubMed=9590696; DOI=10.1038/30032;
Fryer C.J., Archer T.K.;
"Chromatin remodelling by the glucocorticoid receptor requires the
BRG1 complex.";
Nature 393:88-91(1998).
[9]
INTERACTION WITH IKZF1.
PubMed=10204490; DOI=10.1016/S1074-7613(00)80034-5;
Kim J., Sif S., Jones B., Jackson A., Koipally J., Heller E.,
Winandy S., Viel A., Sawyer A., Ikeda T., Kingston R.,
Georgopoulos K.;
"Ikaros DNA-binding proteins direct formation of chromatin remodeling
complexes in lymphocytes.";
Immunity 10:345-355(1999).
[10]
IDENTIFICATION IN THE BAF53 COMPLEX WITH BAF53A; RUVBL1 AND TRRAP.
PubMed=11839798; DOI=10.1128/MCB.22.5.1307-1316.2002;
Park J., Wood M.A., Cole M.D.;
"BAF53 forms distinct nuclear complexes and functions as a critical c-
Myc-interacting nuclear cofactor for oncogenic transformation.";
Mol. Cell. Biol. 22:1307-1316(2002).
[11]
INTERACTION WITH NR3C1 AND SMARD1.
PubMed=12917342; DOI=10.1128/MCB.23.17.6210-6220.2003;
Hsiao P.W., Fryer C.J., Trotter K.W., Wang W., Archer T.K.;
"BAF60a mediates critical interactions between nuclear receptors and
the BRG1 chromatin-remodeling complex for transactivation.";
Mol. Cell. Biol. 23:6210-6220(2003).
[12]
INTERACTION WITH TOPBP1.
PubMed=15075294; DOI=10.1101/gad.1180204;
Liu K., Luo Y., Lin F.-T., Lin W.-C.;
"TopBP1 recruits Brg1/Brm to repress E2F1-induced apoptosis, a novel
pRb-independent and E2F1-specific control for cell survival.";
Genes Dev. 18:673-686(2004).
[13]
INTERACTION WITH ZMIM2.
PubMed=16051670; DOI=10.1210/me.2005-0097;
Huang C.-Y., Beliakoff J., Li X., Lee J., Li X., Sharma M., Lim B.,
Sun Z.;
"hZimp7, a novel PIAS-like protein, enhances androgen receptor-
mediated transcription and interacts with SWI/SNF-like BAF
complexes.";
Mol. Endocrinol. 19:2915-2929(2005).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-11 AND SER-1452, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16964243; DOI=10.1038/nbt1240;
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein
phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic kidney;
PubMed=17525332; DOI=10.1126/science.1140321;
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
"ATM and ATR substrate analysis reveals extensive protein networks
responsive to DNA damage.";
Science 316:1160-1166(2007).
[17]
IDENTIFICATION IN THE BAF COMPLEX, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=18765789; DOI=10.1101/gad.471408;
Lange M., Kaynak B., Forster U.B., Toenjes M., Fischer J.J., Grimm C.,
Schlesinger J., Just S., Dunkel I., Krueger T., Mebus S., Lehrach H.,
Lurz R., Gobom J., Rottbauer W., Abdelilah-Seyfried S., Sperling S.;
"Regulation of muscle development by DPF3, a novel histone acetylation
and methylation reader of the BAF chromatin remodeling complex.";
Genes Dev. 22:2370-2384(2008).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-613; SER-1382; SER-1452;
SER-1570; SER-1575 AND SER-1586, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[20]
INTERACTION WITH TERT, AND FUNCTION.
PubMed=19571879; DOI=10.1038/nature08137;
Park J.I., Venteicher A.S., Hong J.Y., Choi J., Jun S., Shkreli M.,
Chang W., Meng Z., Cheung P., Ji H., McLaughlin M., Veenstra T.D.,
Nusse R., McCrea P.D., Artandi S.E.;
"Telomerase modulates Wnt signalling by association with target gene
chromatin.";
Nature 460:66-72(2009).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-353; THR-609; SER-610;
SER-613; SER-695; SER-1570; SER-1575 AND SER-1627, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[22]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-188, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[23]
INVOLVEMENT IN RTPS2.
PubMed=20137775; DOI=10.1016/j.ajhg.2010.01.013;
Schneppenheim R., Fruhwald M.C., Gesk S., Hasselblatt M., Jeibmann A.,
Kordes U., Kreuz M., Leuschner I., Martin Subero J.I., Obser T.,
Oyen F., Vater I., Siebert R.;
"Germline nonsense mutation and somatic inactivation of SMARCA4/BRG1
in a family with rhabdoid tumor predisposition syndrome.";
Am. J. Hum. Genet. 86:279-284(2010).
[24]
FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ZEB1, AND TISSUE
SPECIFICITY.
PubMed=20418909; DOI=10.1038/onc.2010.102;
Sanchez-Tillo E., Lazaro A., Torrent R., Cuatrecasas M., Vaquero E.C.,
Castells A., Engel P., Postigo A.;
"ZEB1 represses E-cadherin and induces an EMT by recruiting the
SWI/SNF chromatin-remodeling protein BRG1.";
Oncogene 29:3490-3500(2010).
[25]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-695; SER-699; SER-1570
AND SER-1575, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[26]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-613; SER-695; SER-699;
SER-1382; SER-1627 AND SER-1631, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-695; SER-699 AND
SER-1452, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-613 AND SER-1631, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[30]
INTERACTION WITH ACTL6A.
PubMed=28649782; DOI=10.1002/humu.23282;
Marom R., Jain M., Burrage L.C., Song I.W., Graham B.H., Brown C.W.,
Stevens S.J.C., Stegmann A.P.A., Gunter A.T., Kaplan J.D.,
Gavrilova R.H., Shinawi M., Rosenfeld J.A., Bae Y., Tran A.A.,
Chen Y., Lu J.T., Gibbs R.A., Eng C., Yang Y., Rousseau J.,
de Vries B.B.A., Campeau P.M., Lee B.;
"Heterozygous variants in ACTL6A, encoding a component of the BAF
complex, are associated with intellectual disability.";
Hum. Mutat. 38:1365-1371(2017).
[31]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1365, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[32]
REVIEW ON SWI/SNF CHROMATIN REMODELING COMPLEXES.
PubMed=22952240; DOI=10.1074/jbc.R111.309302;
Euskirchen G., Auerbach R.K., Snyder M.;
"SWI/SNF chromatin-remodeling factors: multiscale analyses and diverse
functions.";
J. Biol. Chem. 287:30897-30905(2012).
[33]
REVIEW ON SWI/SNF CHROMATIN REMODELING COMPLEXES.
PubMed=26601204; DOI=10.1126/sciadv.1500447;
Kadoch C., Crabtree G.R.;
"Mammalian SWI/SNF chromatin remodeling complexes and cancer:
Mechanistic insights gained from human genomics.";
Sci. Adv. 1:E1500447-E1500447(2015).
[34]
FUNCTION, AND IDENTIFICATION IN THE GBAF COMPLEX.
PubMed=29374058; DOI=10.1074/jbc.RA117.001065;
Alpsoy A., Dykhuizen E.C.;
"Glioma tumor suppressor candidate region gene 1 (GLTSCR1) and its
paralog GLTSCR1-like form SWI/SNF chromatin remodeling subcomplexes.";
J. Biol. Chem. 293:3892-3903(2018).
[35]
STRUCTURE BY NMR OF 1452-1570 IN COMPLEX WITH ACETYLATED HISTONES, AND
MUTAGENESIS OF VAL-1484; PHE-1539 AND ASN-1540.
PubMed=17274598; DOI=10.1021/bi0611208;
Shen W., Xu C., Huang W., Zhang J., Carlson J.E., Tu X., Wu J.,
Shi Y.;
"Solution structure of human Brg1 bromodomain and its specific binding
to acetylated histone tails.";
Biochemistry 46:2100-2110(2007).
[36]
X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1448-1575 IN COMPLEX WITH
ACETYLATED HISTONE 3.
PubMed=17582821; DOI=10.1002/cbic.200600562;
Singh M., Popowicz G.M., Krajewski M., Holak T.A.;
"Structural ramification for acetyl-lysine recognition by the
bromodomain of human BRG1 protein, a central ATPase of the SWI/SNF
remodeling complex.";
ChemBioChem 8:1308-1316(2007).
[37]
VARIANTS CSS4 LYS-546 DEL; MET-859; CYS-885; PHE-921; THR-1011 AND
GLY-1157.
PubMed=22426308; DOI=10.1038/ng.2219;
Tsurusaki Y., Okamoto N., Ohashi H., Kosho T., Imai Y., Hibi-Ko Y.,
Kaname T., Naritomi K., Kawame H., Wakui K., Fukushima Y., Homma T.,
Kato M., Hiraki Y., Yamagata T., Yano S., Mizuno S., Sakazume S.,
Ishii T., Nagai T., Shiina M., Ogata K., Ohta T., Niikawa N.,
Miyatake S., Okada I., Mizuguchi T., Doi H., Saitsu H., Miyake N.,
Matsumoto N.;
"Mutations affecting components of the SWI/SNF complex cause Coffin-
Siris syndrome.";
Nat. Genet. 44:376-378(2012).
-!- FUNCTION: Involved in transcriptional activation and repression of
select genes by chromatin remodeling (alteration of DNA-nucleosome
topology). Component of SWI/SNF chromatin remodeling complexes
that carry out key enzymatic activities, changing chromatin
structure by altering DNA-histone contacts within a nucleosome in
an ATP-dependent manner. Component of the CREST-BRG1 complex, a
multiprotein complex that regulates promoter activation by
orchestrating the calcium-dependent release of a repressor complex
and the recruitment of an activator complex. In resting neurons,
transcription of the c-FOS promoter is inhibited by SMARCA4-
dependent recruitment of a phospho-RB1-HDAC repressor complex.
Upon calcium influx, RB1 is dephosphorylated by calcineurin, which
leads to release of the repressor complex. At the same time, there
is increased recruitment of CREBBP to the promoter by a CREST-
dependent mechanism, which leads to transcriptional activation.
The CREST-BRG1 complex also binds to the NR2B promoter, and
activity-dependent induction of NR2B expression involves the
release of HDAC1 and recruitment of CREBBP. Belongs to the neural
progenitors-specific chromatin remodeling complex (npBAF complex)
and the neuron-specific chromatin remodeling complex (nBAF
complex). During neural development, a switch from a
stem/progenitor to a postmitotic chromatin remodeling mechanism
occurs as neurons exit the cell cycle and become committed to
their adult state. The transition from proliferating neural
stem/progenitor cells to postmitotic neurons requires a switch in
subunit composition of the npBAF and nBAF complexes. As neural
progenitors exit mitosis and differentiate into neurons, npBAF
complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are
exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B
or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The
npBAF complex is essential for the self-renewal/proliferative
capacity of the multipotent neural stem cells. The nBAF complex
along with CREST plays a role regulating the activity of genes
essential for dendrite growth. SMARCA4/BAF190A may promote neural
stem cell self-renewal/proliferation by enhancing Notch-dependent
proliferative signals, while concurrently making the neural stem
cell insensitive to SHH-dependent differentiating cues (By
similarity). Acts as a corepressor of ZEB1 to regulate E-cadherin
transcription and is required for induction of epithelial-
mesenchymal transition (EMT) by ZEB1. Binds via DLX1 to enhancers
located in the intergenic region between DLX5 and DLX6 and this
binding is stabilized by the long non-coding RNA (lncRNA) Evf2 (By
similarity). Binds to RNA in a promiscuous manner (By similarity).
Binding to RNAs including lncRNA Evf2 leads to inhibition of
SMARCA4 ATPase and chromatin remodeling activities (By
similarity). {ECO:0000250|UniProtKB:Q3TKT4,
ECO:0000269|PubMed:19571879, ECO:0000269|PubMed:20418909,
ECO:0000269|PubMed:29374058, ECO:0000303|PubMed:22952240,
ECO:0000303|PubMed:26601204}.
-!- SUBUNIT: Component of the multiprotein chromatin-remodeling
complexes SWI/SNF: SWI/SNF-A (BAF), SWI/SNF-B (PBAF) and related
complexes. The canonical complex contains a catalytic subunit
(either SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B) and at least
SMARCE1, ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and
SMARCB1/SNF5/BAF47. Other subunits specific to each of the
complexes may also be present permitting several possible
developmental- and tissue-specific combinations (PubMed:22952240,
PubMed:26601204). Component of the BAF complex, which includes at
least actin (ACTB), ARID1A/BAF250A, ARID1B/BAF250B, SMARCA2/BRM,
SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57,
SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more
SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle
cells, the BAF complex also contains DPF3 (PubMed:18765789).
Component of neural progenitors-specific chromatin remodeling
complex (npBAF complex) composed of at least, ARID1A/BAF250A or
ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C,
SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47,
SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, PHF10/BAF45A,
ACTL6A/BAF53A and actin. Component of neuron-specific chromatin
remodeling complex (nBAF complex) composed of at least,
ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C,
SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47,
SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B,
DPF3/BAF45C, ACTL6B/BAF53B and actin. Component of the SWI/SNF-B
(PBAF) chromatin remodeling complex, at least composed of
SMARCA4/BRG1, SMARCB1/BAF47/SNF5, ACTL6A/BAF53A or ACTL6B/BAF53B,
SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B, perhaps
SMARCD3/BAF60C, SMARCC1/BAF155, SMARCC2/BAF170, PBRM1/BAF180,
ARID2/BAF200 and actin (PubMed:26601204). Component of SWI/SNF
(GBAF) subcomplex, which includes at least BICRA or BICRAL
(mutually exclusive), BRD9, SS18, SMARCA2/BRM,
SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, SMARCC1/BAF155, and
SMARCD1/BAF60A (PubMed:29374058). Component of the BAF53 complex,
at least composed of BAF53A, RUVBL1, SMARCA4/BRG1/BAF190A, and
TRRAP, which preferentially acetylates histone H4 (and H2A) within
nucleosomes (PubMed:11839798). Component of the CREST-BRG1
complex, at least composed of SMARCA4/BRG1/BAF190A, SS18L1/CREST,
HDAC1, RB1 and SP1 (By similarity). Interacts with PHF10/BAF45A
(By similarity). Interacts with MYOG (By similarity). Interacts
directly with IKFZ1; the interaction associates IKFZ1 with the BAF
complex (PubMed:10204490). Interacts with ZEB1 (via N-terminus)
(PubMed:20418909). Interacts with NR3C1, PGR, SMARD1, TOPBP1 and
ZMIM2/ZIMP7 (PubMed:9590696, PubMed:12917342, PubMed:15075294,
PubMed:16051670). Interacts with (via the bromodomain) with TERT;
the interaction regulates Wnt-mediated signaling
(PubMed:19571879). Interacts with TBX21 in a KDM6B-dependent
manner (By similarity). Interacts with KDM6A and KDM6B (By
similarity). Interacts with HNRNPU; this interaction occurs in
embryonic stem cells and stimulates global Pol II-mediated
transcription (By similarity). Interacts with ACTL6A
(PubMed:28649782). Interacts with DLX1 (By similarity).
{ECO:0000250|UniProtKB:Q3TKT4, ECO:0000269|PubMed:10204490,
ECO:0000269|PubMed:11839798, ECO:0000269|PubMed:12917342,
ECO:0000269|PubMed:15075294, ECO:0000269|PubMed:16051670,
ECO:0000269|PubMed:17274598, ECO:0000269|PubMed:17582821,
ECO:0000269|PubMed:18765789, ECO:0000269|PubMed:19571879,
ECO:0000269|PubMed:20418909, ECO:0000269|PubMed:28649782,
ECO:0000269|PubMed:29374058, ECO:0000269|PubMed:9590696,
ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}.
-!- INTERACTION:
O14497:ARID1A; NbExp=22; IntAct=EBI-302489, EBI-637887;
Q8NFD5:ARID1B; NbExp=3; IntAct=EBI-302489, EBI-679921;
Q68CP9:ARID2; NbExp=9; IntAct=EBI-302489, EBI-637818;
P16104:H2AFX; NbExp=9; IntAct=EBI-302489, EBI-494830;
O60341:KDM1A; NbExp=3; IntAct=EBI-302489, EBI-710124;
Q9Y466:NR2E1; NbExp=4; IntAct=EBI-302489, EBI-11792373;
P06536:Nr3c1 (xeno); NbExp=3; IntAct=EBI-302489, EBI-1187143;
Q86U86:PBRM1; NbExp=6; IntAct=EBI-302489, EBI-637807;
Q06330:RBPJ; NbExp=2; IntAct=EBI-302489, EBI-632552;
Q13127:REST; NbExp=2; IntAct=EBI-302489, EBI-926706;
Q12824:SMARCB1; NbExp=22; IntAct=EBI-302489, EBI-358419;
Q92922:SMARCC1; NbExp=26; IntAct=EBI-302489, EBI-355653;
Q96GM5:SMARCD1; NbExp=7; IntAct=EBI-302489, EBI-358489;
A4PIV7:SYT-SSX1; NbExp=14; IntAct=EBI-302489, EBI-6901002;
O14746:TERT; NbExp=8; IntAct=EBI-302489, EBI-1772203;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00549, ECO:0000269|PubMed:20418909}. Note=Colocalizes
with long non-coding RNA Evf2 in nuclear RNA clouds.
{ECO:0000250|UniProtKB:Q3TKT4}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=5;
Name=1;
IsoId=P51532-1; Sequence=Displayed;
Name=2;
IsoId=P51532-2; Sequence=VSP_043137;
Note=No experimental confirmation available.;
Name=3;
IsoId=P51532-3; Sequence=VSP_043137, VSP_043677, VSP_043678;
Name=4;
IsoId=P51532-4; Sequence=VSP_043137, VSP_043677;
Name=5;
IsoId=P51532-5; Sequence=VSP_043137, VSP_043678;
-!- TISSUE SPECIFICITY: Colocalizes with ZEB1 in E-cadherin-negative
cells from established lines, and stroma of normal colon as well
as in de-differentiated epithelial cells at the invasion front of
colorectal carcinomas (at protein level).
{ECO:0000269|PubMed:20418909}.
-!- DISEASE: Rhabdoid tumor predisposition syndrome 2 (RTPS2)
[MIM:613325]: A familial cancer syndrome predisposing to renal or
extrarenal malignant rhabdoid tumors and to a variety of tumors of
the central nervous system, including choroid plexus carcinoma,
medulloblastoma, and central primitive neuroectodermal tumors.
Rhabdoid tumors are the most aggressive and lethal malignancies
occurring in early childhood. {ECO:0000269|PubMed:20137775}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-!- DISEASE: Coffin-Siris syndrome 4 (CSS4) [MIM:614609]: A form of
Coffin-Siris syndrome, a congenital multiple malformation syndrome
with broad phenotypic and genetic variability. Cardinal features
are intellectual disability, coarse facial features,
hypertrichosis, and hypoplastic or absent fifth digit nails or
phalanges. Additional features include malformations of the
cardiac, gastrointestinal, genitourinary, and/or central nervous
systems. Sucking/feeding difficulties, poor growth, ophthalmologic
abnormalities, hearing impairment, and spinal anomalies are common
findings. Both autosomal dominant and autosomal recessive
inheritance patterns have been reported.
{ECO:0000269|PubMed:22426308}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
{ECO:0000305}.
-!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology
and Haematology;
URL="http://atlasgeneticsoncology.org/Genes/SMARCA4ID42333ch19p13.html";
-!- WEB RESOURCE: Name=Mendelian genes SWI/SNF related, matrix
associated, actin dependent regulator of chromatin, subfamily a,
member 4 (SMARCA4); Note=Leiden Open Variation Database (LOVD);
URL="http://www.lovd.nl/SMARCA4";
-----------------------------------------------------------------------
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EMBL; U29175; AAB40977.1; -; mRNA.
EMBL; D26156; BAA05143.1; -; mRNA.
EMBL; AF254822; AAG24789.1; -; Genomic_DNA.
EMBL; EU430756; ACA09750.1; -; mRNA.
EMBL; EU430757; ACA09751.1; -; mRNA.
EMBL; EU430758; ACA09752.1; -; mRNA.
EMBL; EU430759; ACA09753.1; -; mRNA.
EMBL; AC006127; AAC97986.1; -; Genomic_DNA.
EMBL; AC006127; AAC97987.1; -; Genomic_DNA.
EMBL; AC011442; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC011485; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471106; EAW84167.1; -; Genomic_DNA.
CCDS; CCDS12253.1; -. [P51532-1]
CCDS; CCDS45972.1; -. [P51532-4]
CCDS; CCDS45973.1; -. [P51532-3]
CCDS; CCDS54217.1; -. [P51532-2]
CCDS; CCDS54218.1; -. [P51532-5]
PIR; S45252; S45252.
RefSeq; NP_001122316.1; NM_001128844.1. [P51532-1]
RefSeq; NP_001122317.1; NM_001128845.1. [P51532-4]
RefSeq; NP_001122318.1; NM_001128846.1. [P51532-3]
RefSeq; NP_001122319.1; NM_001128847.1. [P51532-2]
RefSeq; NP_001122320.1; NM_001128848.1. [P51532-5]
RefSeq; NP_003063.2; NM_003072.3. [P51532-1]
RefSeq; XP_016882654.1; XM_017027165.1.
RefSeq; XP_016882655.1; XM_017027166.1.
RefSeq; XP_016882656.1; XM_017027167.1.
RefSeq; XP_016882657.1; XM_017027168.1.
UniGene; Hs.327527; -.
PDB; 2GRC; X-ray; 1.50 A; A=1448-1575.
PDB; 2H60; NMR; -; A=1452-1570.
PDB; 3UVD; X-ray; 1.85 A; A=1448-1569.
PDB; 5DKD; X-ray; 2.00 A; A/B=1451-1569.
PDB; 5EA1; X-ray; 2.00 A; A/B/C=1451-1580.
PDB; 6BGH; NMR; -; B=1591-1602.
PDBsum; 2GRC; -.
PDBsum; 2H60; -.
PDBsum; 3UVD; -.
PDBsum; 5DKD; -.
PDBsum; 5EA1; -.
PDBsum; 6BGH; -.
ProteinModelPortal; P51532; -.
SMR; P51532; -.
BioGrid; 112481; 222.
ComplexPortal; CPX-1195; Embryonic stem cell-specific SWI/SNF ATP-dependent chromatin remodeling complex.
ComplexPortal; CPX-1196; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B variant.
ComplexPortal; CPX-1199; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A variant.
ComplexPortal; CPX-1204; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant.
ComplexPortal; CPX-1206; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant.
ComplexPortal; CPX-1209; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant.
ComplexPortal; CPX-1211; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant.
ComplexPortal; CPX-1212; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
ComplexPortal; CPX-1215; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
ComplexPortal; CPX-1216; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
ComplexPortal; CPX-1218; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
ComplexPortal; CPX-1219; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
ComplexPortal; CPX-1221; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
ComplexPortal; CPX-1222; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant.
ComplexPortal; CPX-1224; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant.
ComplexPortal; CPX-1226; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant.
ComplexPortal; CPX-1228; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant.
CORUM; P51532; -.
DIP; DIP-24249N; -.
IntAct; P51532; 91.
MINT; P51532; -.
STRING; 9606.ENSP00000350720; -.
BindingDB; P51532; -.
ChEMBL; CHEMBL3085620; -.
GuidetoPHARMACOLOGY; 2740; -.
CarbonylDB; P51532; -.
iPTMnet; P51532; -.
PhosphoSitePlus; P51532; -.
SwissPalm; P51532; -.
BioMuta; SMARCA4; -.
DMDM; 116242792; -.
EPD; P51532; -.
MaxQB; P51532; -.
PaxDb; P51532; -.
PeptideAtlas; P51532; -.
PRIDE; P51532; -.
ProteomicsDB; 56327; -.
ProteomicsDB; 56328; -. [P51532-2]
ProteomicsDB; 56329; -. [P51532-3]
ProteomicsDB; 56330; -. [P51532-4]
ProteomicsDB; 56331; -. [P51532-5]
Ensembl; ENST00000344626; ENSP00000343896; ENSG00000127616. [P51532-1]
Ensembl; ENST00000429416; ENSP00000395654; ENSG00000127616. [P51532-1]
Ensembl; ENST00000444061; ENSP00000392837; ENSG00000127616. [P51532-5]
Ensembl; ENST00000541122; ENSP00000445036; ENSG00000127616. [P51532-4]
Ensembl; ENST00000589677; ENSP00000464778; ENSG00000127616. [P51532-3]
Ensembl; ENST00000590574; ENSP00000466963; ENSG00000127616. [P51532-2]
Ensembl; ENST00000643296; ENSP00000496635; ENSG00000127616. [P51532-4]
Ensembl; ENST00000644737; ENSP00000495548; ENSG00000127616. [P51532-4]
Ensembl; ENST00000645460; ENSP00000494463; ENSG00000127616. [P51532-5]
Ensembl; ENST00000646484; ENSP00000495536; ENSG00000127616. [P51532-2]
Ensembl; ENST00000646510; ENSP00000494772; ENSG00000127616. [P51532-2]
Ensembl; ENST00000647230; ENSP00000494676; ENSG00000127616. [P51532-2]
GeneID; 6597; -.
KEGG; hsa:6597; -.
UCSC; uc002mqf.5; human. [P51532-1]
CTD; 6597; -.
DisGeNET; 6597; -.
EuPathDB; HostDB:ENSG00000127616.17; -.
GeneCards; SMARCA4; -.
GeneReviews; SMARCA4; -.
HGNC; HGNC:11100; SMARCA4.
HPA; CAB004208; -.
MalaCards; SMARCA4; -.
MIM; 603254; gene.
MIM; 613325; phenotype.
MIM; 614609; phenotype.
neXtProt; NX_P51532; -.
OpenTargets; ENSG00000127616; -.
Orphanet; 1465; Coffin-Siris syndrome.
Orphanet; 231108; Familial rhabdoid tumor.
Orphanet; 370396; Small cell carcinoma of the ovary.
PharmGKB; PA35950; -.
eggNOG; KOG0386; Eukaryota.
eggNOG; COG0553; LUCA.
eggNOG; COG5076; LUCA.
GeneTree; ENSGT00550000074659; -.
HOGENOM; HOG000172363; -.
HOVERGEN; HBG056636; -.
InParanoid; P51532; -.
KO; K11647; -.
PhylomeDB; P51532; -.
BRENDA; 3.6.4.11; 2681.
Reactome; R-HSA-1266695; Interleukin-7 signaling.
Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
Reactome; R-HSA-3214858; RMTs methylate histone arginines.
Reactome; R-HSA-3247509; Chromatin modifying enzymes.
Reactome; R-HSA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
SignaLink; P51532; -.
SIGNOR; P51532; -.
ChiTaRS; SMARCA4; human.
EvolutionaryTrace; P51532; -.
GeneWiki; SMARCA4; -.
GenomeRNAi; 6597; -.
PRO; PR:P51532; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000127616; Expressed in 229 organ(s), highest expression level in tendon of biceps brachii.
CleanEx; HS_SMARCA4; -.
ExpressionAtlas; P51532; baseline and differential.
Genevisible; P51532; HS.
GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
GO; GO:0016020; C:membrane; HDA:UniProtKB.
GO; GO:0071565; C:nBAF complex; ISS:UniProtKB.
GO; GO:0071564; C:npBAF complex; IDA:BHF-UCL.
GO; GO:0000790; C:nuclear chromatin; IDA:BHF-UCL.
GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0032991; C:protein-containing complex; HDA:UniProtKB.
GO; GO:0016514; C:SWI/SNF complex; IDA:UniProtKB.
GO; GO:0050681; F:androgen receptor binding; IPI:BHF-UCL.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0070182; F:DNA polymerase binding; IPI:BHF-UCL.
GO; GO:0008094; F:DNA-dependent ATPase activity; IGI:BHF-UCL.
GO; GO:0004386; F:helicase activity; TAS:ProtInc.
GO; GO:0070577; F:lysine-acetylated histone binding; IDA:BHF-UCL.
GO; GO:0002039; F:p53 binding; IPI:BHF-UCL.
GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
GO; GO:0001164; F:RNA polymerase I CORE element sequence-specific DNA binding; IDA:UniProtKB.
GO; GO:0030957; F:Tat protein binding; IPI:BHF-UCL.
GO; GO:0003713; F:transcription coactivator activity; IDA:BHF-UCL.
GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0043044; P:ATP-dependent chromatin remodeling; HDA:UniProtKB.
GO; GO:1904837; P:beta-catenin-TCF complex assembly; TAS:Reactome.
GO; GO:0006325; P:chromatin organization; TAS:Reactome.
GO; GO:0006338; P:chromatin remodeling; IDA:BHF-UCL.
GO; GO:0038111; P:interleukin-7-mediated signaling pathway; TAS:Reactome.
GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; IMP:BHF-UCL.
GO; GO:0030308; P:negative regulation of cell growth; IMP:BHF-UCL.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; TAS:BHF-UCL.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:BHF-UCL.
GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
GO; GO:0003407; P:neural retina development; IEP:BHF-UCL.
GO; GO:0006337; P:nucleosome disassembly; IDA:BHF-UCL.
GO; GO:0043923; P:positive regulation by host of viral transcription; IMP:BHF-UCL.
GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
GO; GO:1902661; P:positive regulation of glucose mediated signaling pathway; IDA:UniProtKB.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription by RNA polymerase II; IMP:BHF-UCL.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
GO; GO:1901838; P:positive regulation of transcription of nucleolar large rRNA by RNA polymerase I; IMP:UniProtKB.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:BHF-UCL.
GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IMP:BHF-UCL.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; NAS:BHF-UCL.
CDD; cd00079; HELICc; 1.
Gene3D; 1.20.920.10; -; 1.
Gene3D; 2.20.28.130; -; 1.
Gene3D; 3.40.50.10810; -; 2.
InterPro; IPR030100; BRG1.
InterPro; IPR006576; BRK_domain.
InterPro; IPR037259; BRK_sf.
InterPro; IPR001487; Bromodomain.
InterPro; IPR036427; Bromodomain-like_sf.
InterPro; IPR018359; Bromodomain_CS.
InterPro; IPR014978; Gln-Leu-Gln_QLQ.
InterPro; IPR014001; Helicase_ATP-bd.
InterPro; IPR001650; Helicase_C.
InterPro; IPR014012; HSA_dom.
InterPro; IPR027417; P-loop_NTPase.
InterPro; IPR029295; SnAC.
InterPro; IPR038718; SNF2-like_sf.
InterPro; IPR000330; SNF2_N.
PANTHER; PTHR10799:SF76; PTHR10799:SF76; 1.
Pfam; PF07533; BRK; 1.
Pfam; PF00439; Bromodomain; 1.
Pfam; PF00271; Helicase_C; 1.
Pfam; PF07529; HSA; 1.
Pfam; PF08880; QLQ; 1.
Pfam; PF14619; SnAC; 1.
Pfam; PF00176; SNF2_N; 1.
PRINTS; PR00503; BROMODOMAIN.
SMART; SM00592; BRK; 1.
SMART; SM00297; BROMO; 1.
SMART; SM00487; DEXDc; 1.
SMART; SM00490; HELICc; 1.
SMART; SM00573; HSA; 1.
SMART; SM00951; QLQ; 1.
SMART; SM01314; SnAC; 1.
SUPFAM; SSF160481; SSF160481; 1.
SUPFAM; SSF47370; SSF47370; 1.
SUPFAM; SSF52540; SSF52540; 2.
PROSITE; PS00633; BROMODOMAIN_1; 1.
PROSITE; PS50014; BROMODOMAIN_2; 1.
PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
PROSITE; PS51194; HELICASE_CTER; 1.
PROSITE; PS51204; HSA; 1.
PROSITE; PS51666; QLQ; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Activator; Alternative splicing;
ATP-binding; Bromodomain; Chromatin regulator; Complete proteome;
Disease mutation; Helicase; Hydrolase; Isopeptide bond;
Mental retardation; Neurogenesis; Nucleotide-binding; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repressor;
RNA-binding; Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 1647 Transcription activator BRG1.
/FTId=PRO_0000074353.
DOMAIN 171 206 QLQ. {ECO:0000255|PROSITE-
ProRule:PRU01001}.
DOMAIN 460 532 HSA. {ECO:0000255|PROSITE-
ProRule:PRU00549}.
DOMAIN 766 931 Helicase ATP-binding.
{ECO:0000255|PROSITE-ProRule:PRU00541}.
DOMAIN 1084 1246 Helicase C-terminal.
{ECO:0000255|PROSITE-ProRule:PRU00542}.
DOMAIN 1477 1547 Bromo. {ECO:0000255|PROSITE-
ProRule:PRU00035}.
NP_BIND 779 786 ATP. {ECO:0000255|PROSITE-
ProRule:PRU00541}.
REGION 1 282 Necessary for interaction with
SS18L1/CREST. {ECO:0000250}.
REGION 462 728 RNA-binding region which is sufficient
for binding to lncRNA Evf2.
{ECO:0000250|UniProtKB:Q3TKT4}.
REGION 837 916 Sufficient for interaction with DLX1.
{ECO:0000250|UniProtKB:Q3TKT4}.
REGION 1247 1446 Sufficient for interaction with DLX1.
{ECO:0000250|UniProtKB:Q3TKT4}.
MOTIF 881 884 DEGH box.
COMPBIAS 578 588 Poly-Lys.
COMPBIAS 663 672 Poly-Glu.
COMPBIAS 1360 1364 Poly-Glu.
COMPBIAS 1571 1584 Poly-Glu.
SITE 1539 1540 Required for binding to 'Lys-15'-
acetylated histone 3.
MOD_RES 11 11 Phosphothreonine.
{ECO:0000244|PubMed:17081983}.
MOD_RES 188 188 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 353 353 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 609 609 Phosphothreonine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 610 610 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 613 613 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
MOD_RES 626 626 N6-acetyllysine.
{ECO:0000250|UniProtKB:Q6DIC0}.
MOD_RES 695 695 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 699 699 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 1382 1382 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692}.
MOD_RES 1423 1423 Phosphothreonine.
{ECO:0000250|UniProtKB:Q3TKT4}.
MOD_RES 1452 1452 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1570 1570 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231}.
MOD_RES 1575 1575 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231}.
MOD_RES 1586 1586 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1627 1627 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:21406692}.
MOD_RES 1631 1631 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:24275569}.
CROSSLNK 1365 1365 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1259 1291 Missing (in isoform 2, isoform 3, isoform
4 and isoform 5).
{ECO:0000303|PubMed:18386774}.
/FTId=VSP_043137.
VAR_SEQ 1388 1388 W -> WLKT (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:18386774}.
/FTId=VSP_043677.
VAR_SEQ 1475 1475 Missing (in isoform 3 and isoform 5).
{ECO:0000303|PubMed:18386774}.
/FTId=VSP_043678.
VARIANT 546 546 Missing (in CSS4).
{ECO:0000269|PubMed:22426308}.
/FTId=VAR_068209.
VARIANT 561 561 V -> E (in dbSNP:rs1804579).
/FTId=VAR_028215.
VARIANT 859 859 T -> M (in CSS4; dbSNP:rs281875226).
{ECO:0000269|PubMed:22426308}.
/FTId=VAR_068210.
VARIANT 885 885 R -> C (in CSS4; dbSNP:rs281875227).
{ECO:0000269|PubMed:22426308}.
/FTId=VAR_068211.
VARIANT 921 921 L -> F (in CSS4; dbSNP:rs281875228).
{ECO:0000269|PubMed:22426308}.
/FTId=VAR_068212.
VARIANT 1011 1011 M -> T (in CSS4; dbSNP:rs281875229).
{ECO:0000269|PubMed:22426308}.
/FTId=VAR_068213.
VARIANT 1036 1036 M -> I (in dbSNP:rs1801514).
/FTId=VAR_028216.
VARIANT 1157 1157 R -> G (in CSS4; dbSNP:rs281875230).
{ECO:0000269|PubMed:22426308}.
/FTId=VAR_068214.
MUTAGEN 1484 1484 V->A: No effect on binding to 'Lys-15'-
acetylated histone H3.
{ECO:0000269|PubMed:17274598}.
MUTAGEN 1539 1539 F->A: Abolishes binding to 'Lys-15'-
acetylated histone H3.
{ECO:0000269|PubMed:17274598}.
MUTAGEN 1540 1540 N->A: Abolishes binding to 'Lys-15'-
acetylated histone H3.
{ECO:0000269|PubMed:17274598}.
CONFLICT 569 569 R -> P (in Ref. 1; AAB40977 and 3;
BAA05143). {ECO:0000305}.
HELIX 1456 1471 {ECO:0000244|PDB:2GRC}.
TURN 1475 1477 {ECO:0000244|PDB:2GRC}.
HELIX 1481 1485 {ECO:0000244|PDB:2GRC}.
TURN 1491 1493 {ECO:0000244|PDB:2GRC}.
HELIX 1495 1500 {ECO:0000244|PDB:2GRC}.
HELIX 1507 1515 {ECO:0000244|PDB:2GRC}.
HELIX 1522 1539 {ECO:0000244|PDB:2GRC}.
STRAND 1542 1544 {ECO:0000244|PDB:2H60}.
HELIX 1545 1567 {ECO:0000244|PDB:2GRC}.
HELIX 1571 1577 {ECO:0000244|PDB:5EA1}.
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


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