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Database: UniProt
Entry: Q3TKT4
LinkDB: Q3TKT4
Original site: Q3TKT4 
ID   SMCA4_MOUSE             Reviewed;        1613 AA.
AC   Q3TKT4; Q3TUD7; Q6AXG8;
DT   09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   18-SEP-2019, entry version 141.
DE   RecName: Full=Transcription activator BRG1;
DE            EC=3.6.4.-;
DE   AltName: Full=ATP-dependent helicase SMARCA4;
DE   AltName: Full=BRG1-associated factor 190A;
DE            Short=BAF190A;
DE   AltName: Full=Protein brahma homolog 1;
DE   AltName: Full=SNF2-beta;
DE   AltName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4;
GN   Name=Smarca4; Synonyms=Baf190a, Brg1, Snf2b, Snf2l4;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
OC   Muroidea; Muridae; Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J; TISSUE=Placenta;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
RA   Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
RA   Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
RA   Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
RA   Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
RA   Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
RA   di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
RA   Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
RA   Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
RA   Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
RA   Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
RA   Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
RA   Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
RA   Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
RA   Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
RA   Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
RA   Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
RA   Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
RA   Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
RA   Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
RA   Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
RA   Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
RA   Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
RA   Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
RA   Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
RA   Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
RA   Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
RA   Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
RA   Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
RA   Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
RA   Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
RA   Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Brain;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   FUNCTION, FUNCTION OF THE NBAF AND NPBAF COMPLEXES, IDENTIFICATION BY
RP   MASS SPECTROMETRY, IDENTIFICATION IN THE NBAF AND NPBAF COMPLEXES, AND
RP   INTERACTION WITH PHF10.
RX   PubMed=17640523; DOI=10.1016/j.neuron.2007.06.019;
RA   Lessard J., Wu J.I., Ranish J.A., Wan M., Winslow M.M., Staahl B.T.,
RA   Wu H., Aebersold R., Graef I.A., Crabtree G.R.;
RT   "An essential switch in subunit composition of a chromatin remodeling
RT   complex during neural development.";
RL   Neuron 55:201-215(2007).
RN   [5]
RP   INTERACTION WITH MYOG.
RX   PubMed=16424906; DOI=10.1038/sj.emboj.7600943;
RA   Ohkawa Y., Marfella C.G., Imbalzano A.N.;
RT   "Skeletal muscle specification by myogenin and Mef2D via the SWI/SNF
RT   ATPase Brg1.";
RL   EMBO J. 25:490-501(2006).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-610 AND SER-613, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-610; SER-613; SER-695;
RP   SER-699; THR-1390; SER-1536; SER-1541 AND SER-1552, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas,
RC   Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and
RT   expression.";
RL   Cell 143:1174-1189(2010).
RN   [9]
RP   INTERACTION WITH KDM6A; KDM6B AND TBX21.
RX   PubMed=21095589; DOI=10.1016/j.molcel.2010.10.028;
RA   Miller S.A., Mohn S.E., Weinmann A.S.;
RT   "Jmjd3 and UTX play a demethylase-independent role in chromatin
RT   remodeling to regulate T-box family member-dependent gene
RT   expression.";
RL   Mol. Cell 40:594-605(2010).
RN   [10]
RP   INTERACTION WITH HNRNPU, AND SUBCELLULAR LOCATION.
RX   PubMed=22162999; DOI=10.1371/journal.pone.0028049;
RA   Vizlin-Hodzic D., Runnberg R., Ryme J., Simonsson S., Simonsson T.;
RT   "SAF-A forms a complex with BRG1 and both components are required for
RT   RNA polymerase II mediated transcription.";
RL   PLoS ONE 6:E28049-E28049(2011).
RN   [11]
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   [12]
RP   FUNCTION, INTERACTION WITH DLX1, SUBCELLULAR LOCATION, AND RNA-BINDING
RP   REGION.
RX   PubMed=26138476; DOI=10.1242/dev.126318;
RA   Cajigas I., Leib D.E., Cochrane J., Luo H., Swyter K.R., Chen S.,
RA   Clark B.S., Thompson J., Yates J.R. III, Kingston R.E., Kohtz J.D.;
RT   "Evf2 lncRNA/BRG1/DLX1 interactions reveal RNA-dependent inhibition of
RT   chromatin remodeling.";
RL   Development 142:2641-2652(2015).
RN   [13]
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:
RT   Mechanistic insights gained from human genomics.";
RL   Sci. Adv. 1:E1500447-E1500447(2015).
RN   [14]
RP   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
RT   paralog GLTSCR1-like form SWI/SNF chromatin remodeling subcomplexes.";
RL   J. Biol. Chem. 293:3892-3903(2018).
CC   -!- FUNCTION: Involved in transcriptional activation and repression of
CC       select genes by chromatin remodeling (alteration of DNA-nucleosome
CC       topology). Component of SWI/SNF chromatin remodeling complexes
CC       that carry out key enzymatic activities, changing chromatin
CC       structure by altering DNA-histone contacts within a nucleosome in
CC       an ATP-dependent manner. Component of the CREST-BRG1 complex, a
CC       multiprotein complex that regulates promoter activation by
CC       orchestrating the calcium-dependent release of a repressor complex
CC       and the recruitment of an activator complex. In resting neurons,
CC       transcription of the c-FOS promoter is inhibited by SMARCA4-
CC       dependent recruitment of a phospho-RB1-HDAC repressor complex.
CC       Upon calcium influx, RB1 is dephosphorylated by calcineurin, which
CC       leads to release of the repressor complex. At the same time, there
CC       is increased recruitment of CREBBP to the promoter by a CREST-
CC       dependent mechanism, which leads to transcriptional activation.
CC       The CREST-BRG1 complex also binds to the NR2B promoter, and
CC       activity-dependent induction of NR2B expression involves the
CC       release of HDAC1 and recruitment of CREBBP (By similarity).
CC       Belongs to the neural progenitors-specific chromatin remodeling
CC       complex (npBAF complex) and the neuron-specific chromatin
CC       remodeling complex (nBAF complex). During neural development, a
CC       switch from a stem/progenitor to a postmitotic chromatin
CC       remodeling mechanism occurs as neurons exit the cell cycle and
CC       become committed to their adult state. The transition from
CC       proliferating neural stem/progenitor cells to postmitotic neurons
CC       requires a switch in subunit composition of the npBAF and nBAF
CC       complexes. As neural progenitors exit mitosis and differentiate
CC       into neurons, npBAF complexes which contain ACTL6A/BAF53A and
CC       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
CC       self-renewal/proliferative capacity of the multipotent neural stem
CC       cells. The nBAF complex along with CREST plays a role in
CC       regulating the activity of genes essential for dendrite growth.
CC       SMARCA4/BAF190A may promote neural stem cell self-
CC       renewal/proliferation by enhancing Notch-dependent proliferative
CC       signals, while concurrently making the neural stem cell
CC       insensitive to SHH-dependent differentiating cues. Acts as a
CC       corepressor of ZEB1 to regulate E-cadherin transcription and is
CC       required for induction of epithelial-mesenchymal transition (EMT)
CC       by ZEB1 (By similarity). Binds via DLX1 to enhancers located in
CC       the intergenic region between DLX5 and DLX6 and this binding is
CC       stabilized by the long non-coding RNA (lncRNA) Evf2
CC       (PubMed:26138476). Binds to RNA in a promiscuous manner
CC       (PubMed:26138476). Binding to RNAs including lncRNA Evf2 leads to
CC       inhibition of SMARCA4 ATPase and chromatin remodeling activities
CC       (PubMed:26138476). {ECO:0000250|UniProtKB:P51532,
CC       ECO:0000269|PubMed:17640523, ECO:0000269|PubMed:26138476}.
CC   -!- SUBUNIT: Component of the multiprotein chromatin-remodeling
CC       complexes SWI/SNF: SWI/SNF-A (BAF), SWI/SNF-B (PBAF) and related
CC       complexes. The canonical complex contains a catalytic subunit
CC       (either SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B) and at least
CC       SMARCE1, ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and
CC       SMARCB1/SNF5/BAF47. Other subunits specific to each of the
CC       complexes may also be present permitting several possible
CC       developmental- and tissue-specific combinations (Probable).
CC       Component of the BAF complex, which includes at least actin
CC       (ACTB), ARID1A/BAF250A, ARID1B/BAF250B, SMARCA2/BRM,
CC       SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57,
CC       SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more
CC       SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle
CC       cells, the BAF complex also contains DPF3. Component of neural
CC       progenitors-specific chromatin remodeling complex (npBAF complex)
CC       composed of at least, ARID1A/BAF250A or ARID1B/BAF250B,
CC       SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B,
CC       SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155,
CC       SMARCE1/BAF57, SMARCC2/BAF170, PHF10/BAF45A, ACTL6A/BAF53A and
CC       actin. Component of neuron-specific chromatin remodeling complex
CC       (nBAF complex) composed of at least, ARID1A/BAF250A or
CC       ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C,
CC       SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47,
CC       SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B,
CC       DPF3/BAF45C, ACTL6B/BAF53B and actin (PubMed:17640523). Component
CC       of the SWI/SNF-B (PBAF) chromatin remodeling complex, at least
CC       composed of SMARCA4/BRG1, SMARCB1/BAF47/SNF5, ACTL6A/BAF53A or
CC       ACTL6B/BAF53B, SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B,
CC       perhaps SMARCD3/BAF60C, SMARCC1/BAF155, SMARCC2/BAF170,
CC       PBRM1/BAF180, ARID2/BAF200 and actin. Component of SWI/SNF (GBAF)
CC       subcomplex, which includes at least BICRA or BICRAL (mutually
CC       exclusive), BRD9, SS18, SMARCA2/BRM, SMARCA4/BRG1/BAF190A,
CC       ACTL6A/BAF53, SMARCC1/BAF155, and SMARCD1/BAF60A
CC       (PubMed:29374058). Component of the BAF53 complex, at least
CC       composed of BAF53A, RUVBL1, SMARCA4/BRG1/BAF190A, and TRRAP, which
CC       preferentially acetylates histone H4 (and H2A) within nucleosomes
CC       (By similarity). Component of the CREST-BRG1 complex, at least
CC       composed of SMARCA4/BRG1/BAF190A, SS18L1/CREST, HDAC1, RB1 and SP1
CC       (By similarity). Interacts with PHF10/BAF45A (PubMed:17640523).
CC       Interacts with MYOG (PubMed:16424906). Interacts directly with
CC       IKFZ1; the interaction associates IKFZ1 with the BAF complex.
CC       Interacts with ZEB1 (via N-terminus). Interacts with NR3C1, PGR,
CC       SMARD1, TOPBP1 and ZMIM2/ZIMP7. Interacts with (via the
CC       bromodomain) with TERT; the interaction regulates Wnt-mediated
CC       signaling (By similarity). Interacts with KDM6A and KDM6B
CC       (PubMed:21095589). Interacts with TBX21 in a KDM6B-dependent
CC       manner (PubMed:21095589). Interacts with HNRNPU; this interaction
CC       occurs in embryonic stem cells and stimulates global Pol II-
CC       mediated transcription (PubMed:22162999). Interacts with ACTL6A
CC       (By similarity). Interacts with DLX1 (PubMed:26138476). Interacts
CC       with DPF2 (By similarity). {ECO:0000250|UniProtKB:P51532,
CC       ECO:0000269|PubMed:16424906, ECO:0000269|PubMed:17640523,
CC       ECO:0000269|PubMed:21095589, ECO:0000269|PubMed:22162999,
CC       ECO:0000269|PubMed:26138476, ECO:0000269|PubMed:29374058,
CC       ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}.
CC   -!- INTERACTION:
CC       A2BH40:Arid1a; NbExp=7; IntAct=EBI-1210244, EBI-371499;
CC       E9Q4N7:Arid1b; NbExp=5; IntAct=EBI-1210244, EBI-6900614;
CC       Q62908:Csrp2 (xeno); NbExp=3; IntAct=EBI-1210244, EBI-918425;
CC       O09106:Hdac1; NbExp=2; IntAct=EBI-1210244, EBI-301912;
CC       P70288:Hdac2; NbExp=4; IntAct=EBI-1210244, EBI-302251;
CC       O88895:Hdac3; NbExp=2; IntAct=EBI-1210244, EBI-302263;
CC       Q99N13:Hdac9; NbExp=3; IntAct=EBI-1210244, EBI-645361;
CC       Q8VEK3:Hnrnpu; NbExp=3; IntAct=EBI-1210244, EBI-529674;
CC       Q01705:Notch1; NbExp=2; IntAct=EBI-1210244, EBI-1392707;
CC       P11103:Parp1; NbExp=2; IntAct=EBI-1210244, EBI-642213;
CC       P06400:RB1 (xeno); NbExp=4; IntAct=EBI-1210244, EBI-491274;
CC       P13405:Rb1; NbExp=3; IntAct=EBI-1210244, EBI-971782;
CC       P97496:Smarcc1; NbExp=7; IntAct=EBI-1210244, EBI-648047;
CC       Q6P9Z1:Smarcd3; NbExp=3; IntAct=EBI-1210244, EBI-7525857;
CC       O70372:Tert; NbExp=2; IntAct=EBI-1210244, EBI-9662790;
CC       Q01320:Top2a; NbExp=3; IntAct=EBI-1210244, EBI-642809;
CC       Q6P1E1:Zmiz1; NbExp=2; IntAct=EBI-1210244, EBI-647033;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
CC       ProRule:PRU00549, ECO:0000269|PubMed:26138476}. Note=Colocalizes
CC       with long non-coding RNA Evf2 in nuclear RNA clouds.
CC       {ECO:0000269|PubMed:26138476}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3TKT4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3TKT4-2; Sequence=VSP_038696;
CC   -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family.
CC       {ECO:0000305}.
DR   EMBL; AK147285; BAE27821.1; -; mRNA.
DR   EMBL; AK160825; BAE36034.1; -; mRNA.
DR   EMBL; AK166837; BAE39059.1; -; mRNA.
DR   EMBL; BC079560; AAH79560.1; -; mRNA.
DR   EMBL; CH466522; EDL25209.1; -; Genomic_DNA.
DR   CCDS; CCDS22909.1; -. [Q3TKT4-2]
DR   CCDS; CCDS57662.1; -. [Q3TKT4-1]
DR   RefSeq; NP_001167549.1; NM_001174078.1.
DR   RefSeq; NP_001167550.1; NM_001174079.1. [Q3TKT4-1]
DR   RefSeq; NP_035547.2; NM_011417.3. [Q3TKT4-2]
DR   RefSeq; XP_006510180.2; XM_006510117.2.
DR   RefSeq; XP_006510182.2; XM_006510119.2. [Q3TKT4-2]
DR   RefSeq; XP_006510183.2; XM_006510120.2. [Q3TKT4-1]
DR   SMR; Q3TKT4; -.
DR   BioGrid; 203336; 76.
DR   ComplexPortal; CPX-1233; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant.
DR   ComplexPortal; CPX-1235; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant.
DR   ComplexPortal; CPX-1237; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant.
DR   ComplexPortal; CPX-1239; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant.
DR   ComplexPortal; CPX-1241; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant.
DR   ComplexPortal; CPX-1243; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant.
DR   ComplexPortal; CPX-1245; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant.
DR   ComplexPortal; CPX-1247; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant.
DR   ComplexPortal; CPX-1248; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A variant.
DR   ComplexPortal; CPX-1250; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B variant.
DR   ComplexPortal; CPX-1251; Embryonic stem cell-specific SWI/SNF ATP-dependent chromatin remodeling complex.
DR   ComplexPortal; CPX-1253; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
DR   ComplexPortal; CPX-1255; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
DR   ComplexPortal; CPX-1257; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
DR   ComplexPortal; CPX-1259; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
DR   ComplexPortal; CPX-1262; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
DR   ComplexPortal; CPX-1264; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
DR   ComplexPortal; CPX-4221; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA4 variant.
DR   ComplexPortal; CPX-4222; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA4 variant.
DR   ComplexPortal; CPX-4229; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRA-SMARCA4 variant.
DR   ComplexPortal; CPX-4230; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRAL-SMARCA4 variant.
DR   CORUM; Q3TKT4; -.
DR   DIP; DIP-40650N; -.
DR   DIP; DIP-59249N; -.
DR   IntAct; Q3TKT4; 48.
DR   MINT; Q3TKT4; -.
DR   STRING; 10090.ENSMUSP00000034707; -.
DR   iPTMnet; Q3TKT4; -.
DR   PhosphoSitePlus; Q3TKT4; -.
DR   SwissPalm; Q3TKT4; -.
DR   jPOST; Q3TKT4; -.
DR   MaxQB; Q3TKT4; -.
DR   PaxDb; Q3TKT4; -.
DR   PeptideAtlas; Q3TKT4; -.
DR   PRIDE; Q3TKT4; -.
DR   Ensembl; ENSMUST00000034707; ENSMUSP00000034707; ENSMUSG00000032187. [Q3TKT4-2]
DR   Ensembl; ENSMUST00000174008; ENSMUSP00000133922; ENSMUSG00000032187. [Q3TKT4-1]
DR   GeneID; 20586; -.
DR   KEGG; mmu:20586; -.
DR   UCSC; uc009omd.2; mouse. [Q3TKT4-2]
DR   UCSC; uc009ome.2; mouse. [Q3TKT4-1]
DR   CTD; 6597; -.
DR   MGI; MGI:88192; Smarca4.
DR   eggNOG; KOG0386; Eukaryota.
DR   eggNOG; COG0553; LUCA.
DR   eggNOG; COG5076; LUCA.
DR   GeneTree; ENSGT00940000156887; -.
DR   HOGENOM; HOG000172363; -.
DR   InParanoid; Q3TKT4; -.
DR   KO; K11647; -.
DR   OMA; TALNIKF; -.
DR   OrthoDB; 685477at2759; -.
DR   PhylomeDB; Q3TKT4; -.
DR   TreeFam; TF300785; -.
DR   Reactome; R-MMU-1266695; Interleukin-7 signaling.
DR   Reactome; R-MMU-201722; Formation of the beta-catenin:TCF transactivating complex.
DR   Reactome; R-MMU-3214858; RMTs methylate histone arginines.
DR   Reactome; R-MMU-3247509; Chromatin modifying enzymes.
DR   Reactome; R-MMU-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR   ChiTaRS; Smarca4; mouse.
DR   PRO; PR:Q3TKT4; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   Bgee; ENSMUSG00000032187; Expressed in 367 organ(s), highest expression level in bone marrow.
DR   ExpressionAtlas; Q3TKT4; baseline and differential.
DR   Genevisible; Q3TKT4; MM.
DR   GO; GO:0000792; C:heterochromatin; IDA:MGI.
DR   GO; GO:0071565; C:nBAF complex; IDA:UniProtKB.
DR   GO; GO:0071564; C:npBAF complex; IDA:UniProtKB.
DR   GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
DR   GO; GO:0005719; C:nuclear euchromatin; IDA:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0005726; C:perichromatin fibrils; IDA:MGI.
DR   GO; GO:0016514; C:SWI/SNF complex; IDA:UniProtKB.
DR   GO; GO:0050681; F:androgen receptor binding; ISO:MGI.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATPase activity; IMP:MGI.
DR   GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0070182; F:DNA polymerase binding; IPI:BHF-UCL.
DR   GO; GO:0008094; F:DNA-dependent ATPase activity; ISO:MGI.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR   GO; GO:0070577; F:lysine-acetylated histone binding; ISO:MGI.
DR   GO; GO:0002039; F:p53 binding; ISO:MGI.
DR   GO; GO:0047485; F:protein N-terminus binding; ISO:MGI.
DR   GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0001164; F:RNA polymerase I CORE element sequence-specific DNA binding; ISO:MGI.
DR   GO; GO:0000978; F:RNA polymerase II proximal promoter sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0000977; F:RNA polymerase II regulatory region sequence-specific DNA binding; IDA:MGI.
DR   GO; GO:0030957; F:Tat protein binding; ISO:MGI.
DR   GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
DR   GO; GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
DR   GO; GO:0008134; F:transcription factor binding; IPI:MGI.
DR   GO; GO:0035904; P:aorta development; IMP:MGI.
DR   GO; GO:0035887; P:aortic smooth muscle cell differentiation; IMP:MGI.
DR   GO; GO:0043044; P:ATP-dependent chromatin remodeling; ISO:MGI.
DR   GO; GO:0001832; P:blastocyst growth; IMP:MGI.
DR   GO; GO:0001835; P:blastocyst hatching; IMP:MGI.
DR   GO; GO:0001568; P:blood vessel development; IMP:MGI.
DR   GO; GO:0000902; P:cell morphogenesis; IMP:MGI.
DR   GO; GO:0006338; P:chromatin remodeling; IMP:MGI.
DR   GO; GO:0060976; P:coronary vasculature development; IMP:MGI.
DR   GO; GO:0060318; P:definitive erythrocyte differentiation; IMP:MGI.
DR   GO; GO:0010424; P:DNA methylation on cytosine within a CG sequence; IMP:MGI.
DR   GO; GO:0035116; P:embryonic hindlimb morphogenesis; IMP:MGI.
DR   GO; GO:0048562; P:embryonic organ morphogenesis; IMP:MGI.
DR   GO; GO:0048730; P:epidermis morphogenesis; IMP:MGI.
DR   GO; GO:0030198; P:extracellular matrix organization; IMP:MGI.
DR   GO; GO:0030900; P:forebrain development; IMP:MGI.
DR   GO; GO:0007403; P:glial cell fate determination; IMP:MGI.
DR   GO; GO:0007507; P:heart development; IMP:MGI.
DR   GO; GO:0060347; P:heart trabecula formation; IGI:MGI.
DR   GO; GO:0030902; P:hindbrain development; IMP:MGI.
DR   GO; GO:0043966; P:histone H3 acetylation; IMP:MGI.
DR   GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR   GO; GO:0030216; P:keratinocyte differentiation; IMP:MGI.
DR   GO; GO:0070307; P:lens fiber cell development; IMP:MGI.
DR   GO; GO:0001889; P:liver development; IMP:MGI.
DR   GO; GO:0006346; P:methylation-dependent chromatin silencing; IDA:MGI.
DR   GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; ISO:MGI.
DR   GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR   GO; GO:0030308; P:negative regulation of cell growth; ISO:MGI.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR   GO; GO:0045892; P:negative regulation of transcription, DNA-templated; ISO:MGI.
DR   GO; GO:0007399; P:nervous system development; IMP:UniProtKB.
DR   GO; GO:0022008; P:neurogenesis; IDA:MGI.
DR   GO; GO:0006334; P:nucleosome assembly; TAS:MGI.
DR   GO; GO:0006337; P:nucleosome disassembly; ISO:MGI.
DR   GO; GO:0003151; P:outflow tract morphogenesis; IMP:MGI.
DR   GO; GO:0061626; P:pharyngeal arch artery morphogenesis; IMP:MGI.
DR   GO; GO:0043923; P:positive regulation by host of viral transcription; ISO:MGI.
DR   GO; GO:0045597; P:positive regulation of cell differentiation; IMP:MGI.
DR   GO; GO:0008284; P:positive regulation of cell population proliferation; IMP:MGI.
DR   GO; GO:0043388; P:positive regulation of DNA binding; IGI:MGI.
DR   GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; ISO:MGI.
DR   GO; GO:1902661; P:positive regulation of glucose mediated signaling pathway; ISO:MGI.
DR   GO; GO:1902895; P:positive regulation of pri-miRNA transcription by RNA polymerase II; ISO:MGI.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:1901838; P:positive regulation of transcription of nucleolar large rRNA by RNA polymerase I; ISO:MGI.
DR   GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISO:MGI.
DR   GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IMP:BHF-UCL.
DR   GO; GO:0030334; P:regulation of cell migration; IMP:MGI.
DR   GO; GO:0019827; P:stem cell population maintenance; IMP:MGI.
DR   GO; GO:0001570; P:vasculogenesis; IMP:MGI.
DR   GO; GO:0003281; P:ventricular septum development; IMP:MGI.
DR   Gene3D; 1.20.920.10; -; 1.
DR   Gene3D; 2.20.28.130; -; 1.
DR   Gene3D; 3.40.50.10810; -; 1.
DR   InterPro; IPR030100; BRG1.
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.
DR   InterPro; IPR014012; HSA_dom.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR029295; SnAC.
DR   InterPro; IPR038718; SNF2-like_sf.
DR   InterPro; IPR000330; SNF2_N.
DR   PANTHER; PTHR10799:SF76; PTHR10799:SF76; 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_N; 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; SSF160481; 1.
DR   SUPFAM; SSF47370; SSF47370; 1.
DR   SUPFAM; SSF52540; SSF52540; 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.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; Alternative splicing; ATP-binding;
KW   Bromodomain; Chromatin regulator; Complete proteome; Helicase;
KW   Hydrolase; Isopeptide bond; Neurogenesis; Nucleotide-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Repressor; RNA-binding;
KW   Transcription; Transcription regulation; Ubl conjugation.
FT   CHAIN         1   1613       Transcription activator BRG1.
FT                                /FTId=PRO_0000391343.
FT   DOMAIN      171    206       QLQ. {ECO:0000255|PROSITE-
FT                                ProRule:PRU01001}.
FT   DOMAIN      460    532       HSA. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00549}.
FT   DOMAIN      766    931       Helicase ATP-binding.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00541}.
FT   DOMAIN     1084   1246       Helicase C-terminal.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00542}.
FT   DOMAIN     1443   1513       Bromo. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00035}.
FT   NP_BIND     779    786       ATP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00541}.
FT   REGION        1    282       Necessary for interaction with
FT                                SS18L1/CREST. {ECO:0000250}.
FT   REGION      462    728       RNA-binding region which is sufficient
FT                                for binding to lncRNA Evf2.
FT                                {ECO:0000269|PubMed:26138476}.
FT   REGION      837    916       Sufficient for interaction with DLX1.
FT                                {ECO:0000269|PubMed:26138476}.
FT   REGION     1247   1413       Sufficient for interaction with DLX1.
FT                                {ECO:0000269|PubMed:26138476}.
FT   MOTIF       881    884       DEGH box. {ECO:0000250}.
FT   COMPBIAS      4    344       Pro-rich.
FT   COMPBIAS    663    672       Poly-Glu.
FT   COMPBIAS   1252   1370       Glu-rich.
FT   COMPBIAS   1531   1555       Glu-rich.
FT   SITE       1505   1506       Required for binding to 'Lys-15'-
FT                                acetylated histone 3. {ECO:0000250}.
FT   MOD_RES      11     11       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P51532}.
FT   MOD_RES     188    188       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:P51532}.
FT   MOD_RES     353    353       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P51532}.
FT   MOD_RES     609    609       Phosphothreonine.
FT                                {ECO:0000250|UniProtKB:P51532}.
FT   MOD_RES     610    610       Phosphoserine.
FT                                {ECO:0000244|PubMed:17242355,
FT                                ECO:0000244|PubMed:21183079}.
FT   MOD_RES     613    613       Phosphoserine.
FT                                {ECO:0000244|PubMed:17242355,
FT                                ECO:0000244|PubMed:21183079}.
FT   MOD_RES     626    626       N6-acetyllysine.
FT                                {ECO:0000250|UniProtKB:Q6DIC0}.
FT   MOD_RES     695    695       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES     699    699       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1349   1349       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P51532}.
FT   MOD_RES    1390   1390       Phosphothreonine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1419   1419       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P51532}.
FT   MOD_RES    1536   1536       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1541   1541       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1552   1552       Phosphoserine.
FT                                {ECO:0000244|PubMed:21183079}.
FT   MOD_RES    1593   1593       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P51532}.
FT   MOD_RES    1597   1597       Phosphoserine.
FT                                {ECO:0000250|UniProtKB:P51532}.
FT   CROSSLNK   1332   1332       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000250|UniProtKB:P51532}.
FT   VAR_SEQ    1441   1441       D -> DS (in isoform 2).
FT                                {ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|PubMed:16141072}.
FT                                /FTId=VSP_038696.
FT   CONFLICT   1355   1355       W -> WLKT (in Ref. 1; BAE36034).
FT                                {ECO:0000305}.
SQ   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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