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

 SMCA4_MOUSE             Reviewed;        1613 AA.
Q3TKT4; Q3TUD7; Q6AXG8;
09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
11-OCT-2005, sequence version 1.
28-MAR-2018, entry version 125.
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=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;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
STRAIN=C57BL/6J; TISSUE=Placenta;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
FUNCTION, FUNCTION OF THE NBAF AND NPBAF COMPLEXES, IDENTIFICATION BY
MASS SPECTROMETRY, IDENTIFICATION IN THE NBAF AND NPBAF COMPLEXES, AND
INTERACTION WITH PHF10.
PubMed=17640523; DOI=10.1016/j.neuron.2007.06.019;
Lessard J., Wu J.I., Ranish J.A., Wan M., Winslow M.M., Staahl B.T.,
Wu H., Aebersold R., Graef I.A., Crabtree G.R.;
"An essential switch in subunit composition of a chromatin remodeling
complex during neural development.";
Neuron 55:201-215(2007).
[5]
INTERACTION WITH MYOG.
PubMed=16424906; DOI=10.1038/sj.emboj.7600943;
Ohkawa Y., Marfella C.G., Imbalzano A.N.;
"Skeletal muscle specification by myogenin and Mef2D via the SWI/SNF
ATPase Brg1.";
EMBO J. 25:490-501(2006).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-610 AND SER-613, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-610; SER-613; SER-695;
SER-699; THR-1390; SER-1536; SER-1541 AND SER-1552, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas,
Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[9]
INTERACTION WITH KDM6A; KDM6B AND TBX21.
PubMed=21095589; DOI=10.1016/j.molcel.2010.10.028;
Miller S.A., Mohn S.E., Weinmann A.S.;
"Jmjd3 and UTX play a demethylase-independent role in chromatin
remodeling to regulate T-box family member-dependent gene
expression.";
Mol. Cell 40:594-605(2010).
[10]
INTERACTION WITH HNRNPU, AND SUBCELLULAR LOCATION.
PubMed=22162999; DOI=10.1371/journal.pone.0028049;
Vizlin-Hodzic D., Runnberg R., Ryme J., Simonsson S., Simonsson T.;
"SAF-A forms a complex with BRG1 and both components are required for
RNA polymerase II mediated transcription.";
PLoS ONE 6:E28049-E28049(2011).
[11]
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).
[12]
FUNCTION, INTERACTION WITH DLX1, SUBCELLULAR LOCATION, AND RNA-BINDING
REGION.
PubMed=26138476; DOI=10.1242/dev.126318;
Cajigas I., Leib D.E., Cochrane J., Luo H., Swyter K.R., Chen S.,
Clark B.S., Thompson J., Yates J.R. III, Kingston R.E., Kohtz J.D.;
"Evf2 lncRNA/BRG1/DLX1 interactions reveal RNA-dependent inhibition of
chromatin remodeling.";
Development 142:2641-2652(2015).
[13]
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).
-!- 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 (By similarity).
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 in
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. Acts as a
corepressor of ZEB1 to regulate E-cadherin transcription and is
required for induction of epithelial-mesenchymal transition (EMT)
by ZEB1 (By similarity). 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
(PubMed:26138476). Binds to RNA in a promiscuous manner
(PubMed:26138476). Binding to RNAs including lncRNA Evf2 leads to
inhibition of SMARCA4 ATPase and chromatin remodeling activities
(PubMed:26138476). {ECO:0000250|UniProtKB:P51532,
ECO:0000269|PubMed:17640523, ECO:0000269|PubMed:26138476}.
-!- 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 (Probable).
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. 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 (PubMed:17640523). 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. 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 (By similarity). 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 (PubMed:17640523).
Interacts with MYOG (PubMed:16424906). Interacts directly with
IKFZ1; the interaction associates IKFZ1 with the BAF complex.
Interacts with ZEB1 (via N-terminus). Interacts with NR3C1, PGR,
SMARD1, TOPBP1 and ZMIM2/ZIMP7. Interacts with (via the
bromodomain) with TERT; the interaction regulates Wnt-mediated
signaling (By similarity). Interacts with KDM6A and KDM6B
(PubMed:21095589). Interacts with TBX21 in a KDM6B-dependent
manner (PubMed:21095589). Interacts with HNRNPU; this interaction
occurs in embryonic stem cells and stimulates global Pol II-
mediated transcription (PubMed:22162999). Interacts with ACTL6A
(By similarity). Interacts with DLX1 (PubMed:26138476).
{ECO:0000250|UniProtKB:P51532, ECO:0000269|PubMed:16424906,
ECO:0000269|PubMed:17640523, ECO:0000269|PubMed:21095589,
ECO:0000269|PubMed:22162999, ECO:0000269|PubMed:26138476,
ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}.
-!- INTERACTION:
A2BH40:Arid1a; NbExp=7; IntAct=EBI-1210244, EBI-371499;
E9Q4N7:Arid1b; NbExp=5; IntAct=EBI-1210244, EBI-6900614;
Q62908:Csrp2 (xeno); NbExp=3; IntAct=EBI-1210244, EBI-918425;
O09106:Hdac1; NbExp=2; IntAct=EBI-1210244, EBI-301912;
P70288:Hdac2; NbExp=4; IntAct=EBI-1210244, EBI-302251;
O88895:Hdac3; NbExp=2; IntAct=EBI-1210244, EBI-302263;
Q99N13:Hdac9; NbExp=3; IntAct=EBI-1210244, EBI-645361;
Q8VEK3:Hnrnpu; NbExp=3; IntAct=EBI-1210244, EBI-529674;
Q01705:Notch1; NbExp=2; IntAct=EBI-1210244, EBI-1392707;
P11103:Parp1; NbExp=2; IntAct=EBI-1210244, EBI-642213;
P06400:RB1 (xeno); NbExp=4; IntAct=EBI-1210244, EBI-491274;
P13405:Rb1; NbExp=3; IntAct=EBI-1210244, EBI-971782;
P97496:Smarcc1; NbExp=7; IntAct=EBI-1210244, EBI-648047;
Q6P9Z1:Smarcd3; NbExp=3; IntAct=EBI-1210244, EBI-7525857;
O70372:Tert; NbExp=2; IntAct=EBI-1210244, EBI-9662790;
Q01320:Top2a; NbExp=3; IntAct=EBI-1210244, EBI-642809;
Q6P1E1:Zmiz1; NbExp=2; IntAct=EBI-1210244, EBI-647033;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00549, ECO:0000269|PubMed:26138476}. Note=Colocalizes
with long non-coding RNA Evf2 in nuclear RNA clouds.
{ECO:0000269|PubMed:26138476}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q3TKT4-1; Sequence=Displayed;
Name=2;
IsoId=Q3TKT4-2; Sequence=VSP_038696;
-!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
{ECO:0000305}.
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EMBL; AK147285; BAE27821.1; -; mRNA.
EMBL; AK160825; BAE36034.1; -; mRNA.
EMBL; AK166837; BAE39059.1; -; mRNA.
EMBL; BC079560; AAH79560.1; -; mRNA.
EMBL; CH466522; EDL25209.1; -; Genomic_DNA.
CCDS; CCDS22909.1; -. [Q3TKT4-2]
CCDS; CCDS57662.1; -. [Q3TKT4-1]
RefSeq; NP_001167549.1; NM_001174078.1.
RefSeq; NP_001167550.1; NM_001174079.1. [Q3TKT4-1]
RefSeq; NP_035547.2; NM_011417.3. [Q3TKT4-2]
RefSeq; XP_006510180.2; XM_006510117.2.
RefSeq; XP_006510182.2; XM_006510119.2. [Q3TKT4-2]
RefSeq; XP_006510183.2; XM_006510120.2. [Q3TKT4-1]
UniGene; Mm.286593; -.
ProteinModelPortal; Q3TKT4; -.
SMR; Q3TKT4; -.
BioGrid; 203336; 76.
CORUM; Q3TKT4; -.
DIP; DIP-40650N; -.
DIP; DIP-59249N; -.
IntAct; Q3TKT4; 48.
MINT; Q3TKT4; -.
STRING; 10090.ENSMUSP00000096547; -.
iPTMnet; Q3TKT4; -.
PhosphoSitePlus; Q3TKT4; -.
MaxQB; Q3TKT4; -.
PaxDb; Q3TKT4; -.
PeptideAtlas; Q3TKT4; -.
PRIDE; Q3TKT4; -.
Ensembl; ENSMUST00000034707; ENSMUSP00000034707; ENSMUSG00000032187. [Q3TKT4-2]
Ensembl; ENSMUST00000174008; ENSMUSP00000133922; ENSMUSG00000032187. [Q3TKT4-1]
GeneID; 20586; -.
KEGG; mmu:20586; -.
UCSC; uc009omd.2; mouse. [Q3TKT4-2]
UCSC; uc009ome.2; mouse. [Q3TKT4-1]
CTD; 6597; -.
MGI; MGI:88192; Smarca4.
eggNOG; KOG0386; Eukaryota.
eggNOG; COG0553; LUCA.
eggNOG; COG5076; LUCA.
GeneTree; ENSGT00550000074659; -.
HOGENOM; HOG000172363; -.
HOVERGEN; HBG056636; -.
InParanoid; Q3TKT4; -.
KO; K11647; -.
PhylomeDB; Q3TKT4; -.
TreeFam; TF300785; -.
Reactome; R-MMU-1266695; Interleukin-7 signaling.
Reactome; R-MMU-201722; Formation of the beta-catenin:TCF transactivating complex.
Reactome; R-MMU-3214858; RMTs methylate histone arginines.
Reactome; R-MMU-3247509; Chromatin modifying enzymes.
Reactome; R-MMU-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
ChiTaRS; Smarca4; mouse.
PRO; PR:Q3TKT4; -.
Proteomes; UP000000589; Chromosome 9.
Bgee; ENSMUSG00000032187; -.
ExpressionAtlas; Q3TKT4; baseline and differential.
Genevisible; Q3TKT4; MM.
GO; GO:0000792; C:heterochromatin; IDA:MGI.
GO; GO:0071565; C:nBAF complex; IDA:UniProtKB.
GO; GO:0071564; C:npBAF complex; IDA:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
GO; GO:0005719; C:nuclear euchromatin; IDA:MGI.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005726; C:perichromatin fibrils; IDA:MGI.
GO; GO:0016514; C:SWI/SNF complex; IDA:MGI.
GO; GO:0050681; F:androgen receptor binding; ISO:MGI.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0016887; F:ATPase activity; IMP:MGI.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0070182; F:DNA polymerase binding; IPI:BHF-UCL.
GO; GO:0008094; F:DNA-dependent ATPase activity; ISO:MGI.
GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
GO; GO:0070577; F:lysine-acetylated histone binding; ISO:MGI.
GO; GO:0002039; F:p53 binding; ISO:MGI.
GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
GO; GO:0001164; F:RNA polymerase I CORE element sequence-specific DNA binding; ISO:MGI.
GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:MGI.
GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:MGI.
GO; GO:0001105; F:RNA polymerase II transcription coactivator activity; ISO:MGI.
GO; GO:0030957; F:Tat protein binding; ISO:MGI.
GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:MGI.
GO; GO:0035904; P:aorta development; IMP:MGI.
GO; GO:0035887; P:aortic smooth muscle cell differentiation; IMP:MGI.
GO; GO:0043044; P:ATP-dependent chromatin remodeling; IEA:InterPro.
GO; GO:0001832; P:blastocyst growth; IMP:MGI.
GO; GO:0001835; P:blastocyst hatching; IMP:MGI.
GO; GO:0001568; P:blood vessel development; IMP:MGI.
GO; GO:0000902; P:cell morphogenesis; IMP:MGI.
GO; GO:0006338; P:chromatin remodeling; IMP:MGI.
GO; GO:0060976; P:coronary vasculature development; IMP:MGI.
GO; GO:0060318; P:definitive erythrocyte differentiation; IMP:MGI.
GO; GO:0010424; P:DNA methylation on cytosine within a CG sequence; IMP:MGI.
GO; GO:0035116; P:embryonic hindlimb morphogenesis; IMP:MGI.
GO; GO:0048562; P:embryonic organ morphogenesis; IMP:MGI.
GO; GO:0048730; P:epidermis morphogenesis; IMP:MGI.
GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
GO; GO:0030900; P:forebrain development; IMP:MGI.
GO; GO:0007403; P:glial cell fate determination; IMP:MGI.
GO; GO:0007507; P:heart development; IMP:MGI.
GO; GO:0060347; P:heart trabecula formation; IGI:MGI.
GO; GO:0030902; P:hindbrain development; IMP:MGI.
GO; GO:0043966; P:histone H3 acetylation; IMP:MGI.
GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
GO; GO:0030216; P:keratinocyte differentiation; IMP:MGI.
GO; GO:0070307; P:lens fiber cell development; IMP:MGI.
GO; GO:0001889; P:liver development; IMP:MGI.
GO; GO:0006346; P:methylation-dependent chromatin silencing; IDA:MGI.
GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; ISO:MGI.
GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0007399; P:nervous system development; IMP:UniProtKB.
GO; GO:0022008; P:neurogenesis; IDA:MGI.
GO; GO:0006334; P:nucleosome assembly; TAS:MGI.
GO; GO:0006337; P:nucleosome disassembly; ISO:MGI.
GO; GO:0003151; P:outflow tract morphogenesis; IMP:MGI.
GO; GO:0061626; P:pharyngeal arch artery morphogenesis; IMP:MGI.
GO; GO:0043923; P:positive regulation by host of viral transcription; ISO:MGI.
GO; GO:0045597; P:positive regulation of cell differentiation; IMP:MGI.
GO; GO:0008284; P:positive regulation of cell proliferation; IMP:MGI.
GO; GO:0043388; P:positive regulation of DNA binding; IGI:MGI.
GO; GO:0051091; P:positive regulation of DNA binding transcription factor activity; ISO:MGI.
GO; GO:1902661; P:positive regulation of glucose mediated signaling pathway; ISO:MGI.
GO; GO:1902895; P:positive regulation of pri-miRNA transcription by RNA polymerase II; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
GO; GO:1901838; P:positive regulation of transcription of nucleolar large rRNA by RNA polymerase I; ISO:MGI.
GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IMP:BHF-UCL.
GO; GO:0030334; P:regulation of cell migration; IMP:MGI.
GO; GO:0019827; P:stem cell population maintenance; IMP:MGI.
GO; GO:0001570; P:vasculogenesis; IMP:MGI.
GO; GO:0003281; P:ventricular septum development; IMP:MGI.
CDD; cd00079; HELICc; 1.
Gene3D; 1.20.920.10; -; 1.
Gene3D; 2.20.28.130; -; 1.
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; 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;
Acetylation; Activator; Alternative splicing; ATP-binding;
Bromodomain; Chromatin regulator; Complete proteome; Helicase;
Hydrolase; Isopeptide bond; Neurogenesis; Nucleotide-binding; Nucleus;
Phosphoprotein; Reference proteome; Repressor; RNA-binding;
Transcription; Transcription regulation; Ubl conjugation.
CHAIN 1 1613 Transcription activator BRG1.
/FTId=PRO_0000391343.
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 1443 1513 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:0000269|PubMed:26138476}.
REGION 837 916 Sufficient for interaction with DLX1.
{ECO:0000269|PubMed:26138476}.
REGION 1247 1413 Sufficient for interaction with DLX1.
{ECO:0000269|PubMed:26138476}.
MOTIF 881 884 DEGH box. {ECO:0000250}.
COMPBIAS 4 344 Pro-rich.
COMPBIAS 663 672 Poly-Glu.
COMPBIAS 1252 1370 Glu-rich.
COMPBIAS 1531 1555 Glu-rich.
SITE 1505 1506 Required for binding to 'Lys-15'-
acetylated histone 3. {ECO:0000250}.
MOD_RES 11 11 Phosphothreonine.
{ECO:0000250|UniProtKB:P51532}.
MOD_RES 188 188 N6-acetyllysine.
{ECO:0000250|UniProtKB:P51532}.
MOD_RES 353 353 Phosphothreonine.
{ECO:0000250|UniProtKB:P51532}.
MOD_RES 609 609 Phosphothreonine.
{ECO:0000250|UniProtKB:P51532}.
MOD_RES 610 610 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 613 613 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 695 695 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 699 699 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1027 1027 N6-acetyllysine.
{ECO:0000250|UniProtKB:P51531}.
MOD_RES 1029 1029 N6-acetyllysine.
{ECO:0000250|UniProtKB:P51531}.
MOD_RES 1349 1349 Phosphoserine.
{ECO:0000250|UniProtKB:P51532}.
MOD_RES 1390 1390 Phosphothreonine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1419 1419 Phosphoserine.
{ECO:0000250|UniProtKB:P51532}.
MOD_RES 1536 1536 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1541 1541 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1552 1552 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1593 1593 Phosphoserine.
{ECO:0000250|UniProtKB:P51532}.
MOD_RES 1597 1597 Phosphoserine.
{ECO:0000250|UniProtKB:P51532}.
CROSSLNK 1332 1332 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:P51532}.
VAR_SEQ 1441 1441 D -> DS (in isoform 2).
{ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:16141072}.
/FTId=VSP_038696.
CONFLICT 1355 1355 W -> WLKT (in Ref. 1; BAE36034).
{ECO:0000305}.
SEQUENCE 1613 AA; 181427 MW; C23804ED858F98FE CRC64;
MSTPDPPLGG TPRPGPSPGP GPSPGAMLGP SPGPSPGSAH SMMGPSPGPP SAGHPMPTQG
PGGYPQDNMH QMHKPMESMH EKGMPDDPRY NQMKGMGMRS GAHTGMAPPP SPMDQHSQGY
PSPLGGSEHA SSPVPASGPS SGPQMSSGPG GAPLDGSDPQ ALGQQNRGPT PFNQNQLHQL
RAQIMAYKML ARGQPLPDHL QMAVQGKRPM PGMQQQMPTL PPPSVSATGP GPGPGPGPGP
GPGPAPPNYS RPHGMGGPNM PPPGPSGVPP GMPGQPPGGP PKPWPEGPMA NAAAPTSTPQ
KLIPPQPTGR PSPAPPAVPP AASPVMPPQT QSPGQPAQPA PLVPLHQKQS RITPIQKPRG
LDPVEILQER EYRLQARIAH RIQELENLPG SLAGDLRTKA TIELKALRLL NFQRQLRQEV
VVCMRRDTAL ETALNAKAYK RSKRQSLREA RITEKLEKQQ KIEQERKRRQ KHQEYLNSIL
QHAKDFREYH RSVTGKLQKL TKAVATYHAN TEREQKKENE RIEKERMRRL MAEDEEGYRK
LIDQKKDKRL AYLLQQTDEY VANLTELVRQ HKAAQVAKEK KKKKKKKKAE NAEGQTPAIG
PDGEPLDETS QMSDLPVKVI HVESGKILTG TDAPKAGQLE AWLEMNPGYE VAPRSDSEES
GSEEEEEEEE EEQPQPAQPP 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 LEHEEQDEEE
DEVPDDETVN QMIARHEEEF DLFMRMDLDR RREEARNPKR KPRLMEEDEL PSWIIKDDAE
VERLTCEEEE EKMFGRGSRH RKEVDYSDSL TEKQWLKAIE EGTLEEIEEE VRQKKSSRKR
KRDSEAGSST PTTSTRSRDK DEESKKQKKR GRPPAEKLSP NPPNLTKKMK KIVDAVIKYK
DSSGRQLSEV FIQLPSRKEL PEYYELIRKP VDFKKIKERI RNHKYRSLND LEKDVMLLCQ
NAQTFNLEGS LIYEDSIVLQ SVFTSVRQKI EKEDDSEGEE SEEEEEGEEE GSESESRSVK
VKIKLGRKEK AQDRLKGGRR RPSRGSRAKP VVSDDDSEEE QEEDRSGSGS EED


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