SMCA4_HUMAN
ID SMCA4_HUMAN Reviewed; 1647 AA.
AC P51532; B1A8Z4; B1A8Z5; B1A8Z6; B1A8Z7; E9PBR8; O95052; Q9HBD3;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 2.
DT 03-AUG-2022, entry version 237.
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=Mitotic growth and transcription activator;
DE AltName: Full=Protein BRG-1;
DE AltName: Full=Protein brahma homolog 1;
DE AltName: Full=SNF2-beta;
DE AltName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily A member 4;
GN Name=SMARCA4; Synonyms=BAF190A, BRG1, SNF2B, SNF2L4;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=8232556; DOI=10.1038/366170a0;
RA Khavari P.A., Peterson C.L., Tamkun J.W., Mendel D.B., Crabtree G.R.;
RT "BRG1 contains a conserved domain of the SWI2/SNF2 family necessary for
RT normal mitotic growth and transcription.";
RL Nature 366:170-174(1993).
RN [2]
RP SEQUENCE REVISION.
RA Khavari P.A., Peterson C.L., Tamkun J.W., Mendel D.B., Crabtree G.R.;
RL Submitted (JUN-1995) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Fetal brain;
RX PubMed=8208605; DOI=10.1093/nar/22.10.1815;
RA Chiba H., Muramatsu M., Nomoto A., Kato H.;
RT "Two human homologues of Saccharomyces cerevisiae SWI2/SNF2 and Drosophila
RT brahma are transcriptional coactivators cooperating with the estrogen
RT receptor and the retinoic acid receptor.";
RL Nucleic Acids Res. 22:1815-1820(1994).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11085541;
RA Wong A.K.C., Shanahan F., Chen Y., Lian L., Ha P., Hendricks K.,
RA Ghaffari S., Iliev D., Penn B., Woodland A.-M., Smith R., Salada G.,
RA Carillo A., Laity K., Gupte J., Swedlund B., Tavtigian S.V., Teng D.H.-F.,
RA Lees E.;
RT "BRG1, a component of the SWI-SNF complex, is mutated in multiple human
RT tumor cell lines.";
RL Cancer Res. 60:6171-6177(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 3; 4 AND 5).
RC TISSUE=Lung;
RX PubMed=18386774; DOI=10.1002/humu.20730;
RA Medina P.P., Romero O.A., Kohno T., Montuenga L.M., Pio R., Yokota J.,
RA Sanchez-Cespedes M.;
RT "Frequent BRG1/SMARCA4-inactivating mutations in human lung cancer cell
RT lines.";
RL Hum. Mutat. 29:617-622(2008).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP INTERACTION WITH NR3C1 AND PGR.
RX PubMed=9590696; DOI=10.1038/30032;
RA Fryer C.J., Archer T.K.;
RT "Chromatin remodelling by the glucocorticoid receptor requires the BRG1
RT complex.";
RL Nature 393:88-91(1998).
RN [9]
RP INTERACTION WITH IKZF1.
RX PubMed=10204490; DOI=10.1016/s1074-7613(00)80034-5;
RA Kim J., Sif S., Jones B., Jackson A., Koipally J., Heller E., Winandy S.,
RA Viel A., Sawyer A., Ikeda T., Kingston R., Georgopoulos K.;
RT "Ikaros DNA-binding proteins direct formation of chromatin remodeling
RT complexes in lymphocytes.";
RL Immunity 10:345-355(1999).
RN [10]
RP IDENTIFICATION IN THE BAF53 COMPLEX WITH BAF53A; RUVBL1 AND TRRAP.
RX PubMed=11839798; DOI=10.1128/mcb.22.5.1307-1316.2002;
RA Park J., Wood M.A., Cole M.D.;
RT "BAF53 forms distinct nuclear complexes and functions as a critical c-Myc-
RT interacting nuclear cofactor for oncogenic transformation.";
RL Mol. Cell. Biol. 22:1307-1316(2002).
RN [11]
RP INTERACTION WITH NR3C1 AND SMARD1.
RX PubMed=12917342; DOI=10.1128/mcb.23.17.6210-6220.2003;
RA Hsiao P.W., Fryer C.J., Trotter K.W., Wang W., Archer T.K.;
RT "BAF60a mediates critical interactions between nuclear receptors and the
RT BRG1 chromatin-remodeling complex for transactivation.";
RL Mol. Cell. Biol. 23:6210-6220(2003).
RN [12]
RP INTERACTION WITH TOPBP1.
RX PubMed=15075294; DOI=10.1101/gad.1180204;
RA Liu K., Luo Y., Lin F.-T., Lin W.-C.;
RT "TopBP1 recruits Brg1/Brm to repress E2F1-induced apoptosis, a novel pRb-
RT independent and E2F1-specific control for cell survival.";
RL Genes Dev. 18:673-686(2004).
RN [13]
RP INTERACTION WITH ZMIM2.
RX PubMed=16051670; DOI=10.1210/me.2005-0097;
RA Huang C.-Y., Beliakoff J., Li X., Lee J., Li X., Sharma M., Lim B., Sun Z.;
RT "hZimp7, a novel PIAS-like protein, enhances androgen receptor-mediated
RT transcription and interacts with SWI/SNF-like BAF complexes.";
RL Mol. Endocrinol. 19:2915-2929(2005).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-11 AND SER-1452, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [16]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [17]
RP IDENTIFICATION IN THE BAF COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18765789; DOI=10.1101/gad.471408;
RA Lange M., Kaynak B., Forster U.B., Toenjes M., Fischer J.J., Grimm C.,
RA Schlesinger J., Just S., Dunkel I., Krueger T., Mebus S., Lehrach H.,
RA Lurz R., Gobom J., Rottbauer W., Abdelilah-Seyfried S., Sperling S.;
RT "Regulation of muscle development by DPF3, a novel histone acetylation and
RT methylation reader of the BAF chromatin remodeling complex.";
RL Genes Dev. 22:2370-2384(2008).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-613; SER-1382; SER-1452;
RP SER-1570; SER-1575 AND SER-1586, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [20]
RP INTERACTION WITH TERT, AND FUNCTION.
RX PubMed=19571879; DOI=10.1038/nature08137;
RA Park J.I., Venteicher A.S., Hong J.Y., Choi J., Jun S., Shkreli M.,
RA Chang W., Meng Z., Cheung P., Ji H., McLaughlin M., Veenstra T.D.,
RA Nusse R., McCrea P.D., Artandi S.E.;
RT "Telomerase modulates Wnt signalling by association with target gene
RT chromatin.";
RL Nature 460:66-72(2009).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-353; THR-609; SER-610;
RP SER-613; SER-695; SER-1570; SER-1575 AND SER-1627, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-188, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [23]
RP INVOLVEMENT IN RTPS2.
RX PubMed=20137775; DOI=10.1016/j.ajhg.2010.01.013;
RA Schneppenheim R., Fruhwald M.C., Gesk S., Hasselblatt M., Jeibmann A.,
RA Kordes U., Kreuz M., Leuschner I., Martin Subero J.I., Obser T., Oyen F.,
RA Vater I., Siebert R.;
RT "Germline nonsense mutation and somatic inactivation of SMARCA4/BRG1 in a
RT family with rhabdoid tumor predisposition syndrome.";
RL Am. J. Hum. Genet. 86:279-284(2010).
RN [24]
RP INTERACTION WITH DEPF2.
RX PubMed=20460684; DOI=10.1074/jbc.m109.087783;
RA Tando T., Ishizaka A., Watanabe H., Ito T., Iida S., Haraguchi T.,
RA Mizutani T., Izumi T., Isobe T., Akiyama T., Inoue J., Iba H.;
RT "Requiem protein links RelB/p52 and the Brm-type SWI/SNF complex in a
RT noncanonical NF-kappaB pathway.";
RL J. Biol. Chem. 285:21951-21960(2010).
RN [25]
RP FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH ZEB1, AND TISSUE
RP SPECIFICITY.
RX PubMed=20418909; DOI=10.1038/onc.2010.102;
RA Sanchez-Tillo E., Lazaro A., Torrent R., Cuatrecasas M., Vaquero E.C.,
RA Castells A., Engel P., Postigo A.;
RT "ZEB1 represses E-cadherin and induces an EMT by recruiting the SWI/SNF
RT chromatin-remodeling protein BRG1.";
RL Oncogene 29:3490-3500(2010).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-695; SER-699; SER-1570 AND
RP SER-1575, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [27]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-613; SER-695; SER-699;
RP SER-1382; SER-1627 AND SER-1631, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [29]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-695; SER-699 AND SER-1452,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-613 AND SER-1631, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [31]
RP INTERACTION WITH ACTL6A.
RX PubMed=28649782; DOI=10.1002/humu.23282;
RA Marom R., Jain M., Burrage L.C., Song I.W., Graham B.H., Brown C.W.,
RA Stevens S.J.C., Stegmann A.P.A., Gunter A.T., Kaplan J.D., Gavrilova R.H.,
RA Shinawi M., Rosenfeld J.A., Bae Y., Tran A.A., Chen Y., Lu J.T.,
RA Gibbs R.A., Eng C., Yang Y., Rousseau J., de Vries B.B.A., Campeau P.M.,
RA Lee B.;
RT "Heterozygous variants in ACTL6A, encoding a component of the BAF complex,
RT are associated with intellectual disability.";
RL Hum. Mutat. 38:1365-1371(2017).
RN [32]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-1365, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [33]
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 [34]
RP REVIEW ON SWI/SNF CHROMATIN REMODELING COMPLEXES.
RX PubMed=26601204; DOI=10.1126/sciadv.1500447;
RA Kadoch C., Crabtree G.R.;
RT "Mammalian SWI/SNF chromatin remodeling complexes and cancer: Mechanistic
RT insights gained from human genomics.";
RL Sci. Adv. 1:E1500447-E1500447(2015).
RN [35]
RP FUNCTION, AND IDENTIFICATION IN THE GBAF COMPLEX.
RX PubMed=29374058; DOI=10.1074/jbc.ra117.001065;
RA Alpsoy A., Dykhuizen E.C.;
RT "Glioma tumor suppressor candidate region gene 1 (GLTSCR1) and its paralog
RT GLTSCR1-like form SWI/SNF chromatin remodeling subcomplexes.";
RL J. Biol. Chem. 293:3892-3903(2018).
RN [36]
RP INTERACTION WITH HDGFL2 AND DPF3.
RX PubMed=32459350; DOI=10.1093/nar/gkaa441;
RA Zhu X., Lan B., Yi X., He C., Dang L., Zhou X., Lu Y., Sun Y., Liu Z.,
RA Bai X., Zhang K., Li B., Li M.J., Chen Y., Zhang L.;
RT "HRP2-DPF3a-BAF complex coordinates histone modification and chromatin
RT remodeling to regulate myogenic gene transcription.";
RL Nucleic Acids Res. 48:6563-6582(2020).
RN [37]
RP STRUCTURE BY NMR OF 1452-1570 IN COMPLEX WITH ACETYLATED HISTONES, AND
RP MUTAGENESIS OF VAL-1484; PHE-1539 AND ASN-1540.
RX PubMed=17274598; DOI=10.1021/bi0611208;
RA Shen W., Xu C., Huang W., Zhang J., Carlson J.E., Tu X., Wu J., Shi Y.;
RT "Solution structure of human Brg1 bromodomain and its specific binding to
RT acetylated histone tails.";
RL Biochemistry 46:2100-2110(2007).
RN [38]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 1448-1575 IN COMPLEX WITH
RP ACETYLATED HISTONE 3.
RX PubMed=17582821; DOI=10.1002/cbic.200600562;
RA Singh M., Popowicz G.M., Krajewski M., Holak T.A.;
RT "Structural ramification for acetyl-lysine recognition by the bromodomain
RT of human BRG1 protein, a central ATPase of the SWI/SNF remodeling
RT complex.";
RL ChemBioChem 8:1308-1316(2007).
RN [39]
RP VARIANTS CSS4 LYS-546 DEL; MET-859; CYS-885; PHE-921; THR-1011 AND
RP GLY-1157.
RX PubMed=22426308; DOI=10.1038/ng.2219;
RA Tsurusaki Y., Okamoto N., Ohashi H., Kosho T., Imai Y., Hibi-Ko Y.,
RA Kaname T., Naritomi K., Kawame H., Wakui K., Fukushima Y., Homma T.,
RA Kato M., Hiraki Y., Yamagata T., Yano S., Mizuno S., Sakazume S., Ishii T.,
RA Nagai T., Shiina M., Ogata K., Ohta T., Niikawa N., Miyatake S., Okada I.,
RA Mizuguchi T., Doi H., Saitsu H., Miyake N., Matsumoto N.;
RT "Mutations affecting components of the SWI/SNF complex cause Coffin-Siris
RT syndrome.";
RL Nat. Genet. 44:376-378(2012).
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 that
CC carry out key enzymatic activities, changing chromatin structure by
CC altering DNA-histone contacts within a nucleosome in an ATP-dependent
CC manner. Component of the CREST-BRG1 complex, a multiprotein complex
CC that regulates promoter activation by orchestrating the calcium-
CC dependent release of a repressor complex and the recruitment of an
CC activator complex. In resting neurons, transcription of the c-FOS
CC promoter is inhibited by SMARCA4-dependent recruitment of a phospho-
CC RB1-HDAC repressor complex. Upon calcium influx, RB1 is
CC dephosphorylated by calcineurin, which leads to release of the
CC repressor complex. At the same time, there is increased recruitment of
CC CREBBP to the promoter by a CREST-dependent mechanism, which leads to
CC transcriptional activation. The CREST-BRG1 complex also binds to the
CC NR2B promoter, and activity-dependent induction of NR2B expression
CC involves the release of HDAC1 and recruitment of CREBBP. Belongs to the
CC neural progenitors-specific chromatin remodeling complex (npBAF
CC complex) and the neuron-specific chromatin remodeling complex (nBAF
CC complex). During neural development, a switch from a stem/progenitor to
CC a postmitotic chromatin remodeling mechanism occurs as neurons exit the
CC cell cycle and become committed to their adult state. The transition
CC from 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 into
CC neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A,
CC are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B
CC or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF
CC complex is essential for the self-renewal/proliferative capacity of the
CC multipotent neural stem cells. The nBAF complex along with CREST plays
CC a role regulating the activity of genes essential for dendrite growth.
CC SMARCA4/BAF190A may promote neural stem cell self-renewal/proliferation
CC by enhancing Notch-dependent proliferative signals, while concurrently
CC making the neural stem cell insensitive to SHH-dependent
CC differentiating cues (By similarity). Acts as a corepressor of ZEB1 to
CC regulate E-cadherin transcription and is required for induction of
CC epithelial-mesenchymal transition (EMT) by ZEB1. Binds via DLX1 to
CC enhancers located in the intergenic region between DLX5 and DLX6 and
CC this binding is stabilized by the long non-coding RNA (lncRNA) Evf2 (By
CC similarity). Binds to RNA in a promiscuous manner (By similarity).
CC Binding to RNAs including lncRNA Evf2 leads to inhibition of SMARCA4
CC ATPase and chromatin remodeling activities (By similarity).
CC {ECO:0000250|UniProtKB:Q3TKT4, ECO:0000269|PubMed:19571879,
CC ECO:0000269|PubMed:20418909, ECO:0000269|PubMed:29374058,
CC ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}.
CC -!- SUBUNIT: Component of the multiprotein chromatin-remodeling complexes
CC SWI/SNF: SWI/SNF-A (BAF), SWI/SNF-B (PBAF) and related complexes. The
CC canonical complex contains a catalytic subunit (either
CC SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B) and at least SMARCE1,
CC ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and SMARCB1/SNF5/BAF47.
CC Other subunits specific to each of the complexes may also be present
CC permitting several possible developmental- and tissue-specific
CC combinations (PubMed:22952240, PubMed:26601204). Component of the BAF
CC complex, which includes at least actin (ACTB), ARID1A/BAF250A,
CC ARID1B/BAF250B, SMARCA2/BRM, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53,
CC ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170,
CC SMARCB1/SNF5/INI1, and one or more SMARCD1/BAF60A, SMARCD2/BAF60B, or
CC SMARCD3/BAF60C. In muscle cells, the BAF complex also contains DPF3
CC (PubMed:18765789). Component of neural progenitors-specific chromatin
CC remodeling complex (npBAF complex) composed of at least, ARID1A/BAF250A
CC or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B,
CC SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57,
CC SMARCC2/BAF170, PHF10/BAF45A, ACTL6A/BAF53A and actin. Component of
CC neuron-specific chromatin remodeling complex (nBAF complex) composed of
CC at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A,
CC SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A,
CC SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170,
CC DPF1/BAF45B, DPF3/BAF45C, ACTL6B/BAF53B and actin. Component of the
CC SWI/SNF-B (PBAF) chromatin remodeling complex, at least composed of
CC SMARCA4/BRG1, SMARCB1/BAF47/SNF5, ACTL6A/BAF53A or ACTL6B/BAF53B,
CC SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B, perhaps SMARCD3/BAF60C,
CC SMARCC1/BAF155, SMARCC2/BAF170, PBRM1/BAF180, ARID2/BAF200 and actin
CC (PubMed:26601204). Component of SWI/SNF (GBAF) subcomplex, which
CC includes at least BICRA or BICRAL (mutually exclusive), BRD9, SS18,
CC SMARCA2/BRM, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, SMARCC1/BAF155, and
CC SMARCD1/BAF60A (PubMed:29374058). Component of the BAF53 complex, at
CC least composed of BAF53A, RUVBL1, SMARCA4/BRG1/BAF190A, and TRRAP,
CC which preferentially acetylates histone H4 (and H2A) within nucleosomes
CC (PubMed:11839798). Component of the CREST-BRG1 complex, at least
CC composed of SMARCA4/BRG1/BAF190A, SS18L1/CREST, HDAC1, RB1 and SP1 (By
CC similarity). Interacts with PHF10/BAF45A (By similarity). Interacts
CC with MYOG (By similarity). Interacts directly with IKFZ1; the
CC interaction associates IKFZ1 with the BAF complex (PubMed:10204490).
CC Interacts with ZEB1 (via N-terminus) (PubMed:20418909). Interacts with
CC NR3C1, PGR, SMARD1, TOPBP1 and ZMIM2/ZIMP7 (PubMed:9590696,
CC PubMed:12917342, PubMed:15075294, PubMed:16051670). Interacts with (via
CC the bromodomain) with TERT; the interaction regulates Wnt-mediated
CC signaling (PubMed:19571879). Interacts with TBX21 in a KDM6B-dependent
CC manner (By similarity). Interacts with KDM6A and KDM6B (By similarity).
CC Interacts with HNRNPU; this interaction occurs in embryonic stem cells
CC and stimulates global Pol II-mediated transcription (By similarity).
CC Interacts with ACTL6A (PubMed:28649782). Interacts with DLX1 (By
CC similarity). Interacts with DPF2 (PubMed:20460684). Interacts with
CC DPF3a (isoform 2 of DPF3/BAF45C) and with HDGFL2 in a DPF3a-dependent
CC manner (PubMed:32459350). {ECO:0000250|UniProtKB:Q3TKT4,
CC ECO:0000269|PubMed:10204490, ECO:0000269|PubMed:11839798,
CC ECO:0000269|PubMed:12917342, ECO:0000269|PubMed:15075294,
CC ECO:0000269|PubMed:16051670, ECO:0000269|PubMed:17274598,
CC ECO:0000269|PubMed:17582821, ECO:0000269|PubMed:18765789,
CC ECO:0000269|PubMed:19571879, ECO:0000269|PubMed:20418909,
CC ECO:0000269|PubMed:20460684, ECO:0000269|PubMed:28649782,
CC ECO:0000269|PubMed:29374058, ECO:0000269|PubMed:32459350,
CC ECO:0000269|PubMed:9590696, ECO:0000303|PubMed:22952240,
CC ECO:0000303|PubMed:26601204}.
CC -!- INTERACTION:
CC P51532; O14497: ARID1A; NbExp=23; IntAct=EBI-302489, EBI-637887;
CC P51532; Q8NFD5: ARID1B; NbExp=3; IntAct=EBI-302489, EBI-679921;
CC P51532; Q68CP9: ARID2; NbExp=9; IntAct=EBI-302489, EBI-637818;
CC P51532; P16104: H2AX; NbExp=9; IntAct=EBI-302489, EBI-494830;
CC P51532; Q86U86: PBRM1; NbExp=6; IntAct=EBI-302489, EBI-637807;
CC P51532; Q06330: RBPJ; NbExp=2; IntAct=EBI-302489, EBI-632552;
CC P51532; Q13127: REST; NbExp=2; IntAct=EBI-302489, EBI-926706;
CC P51532; Q12824: SMARCB1; NbExp=34; IntAct=EBI-302489, EBI-358419;
CC P51532; Q92922: SMARCC1; NbExp=28; IntAct=EBI-302489, EBI-355653;
CC P51532; Q96GM5: SMARCD1; NbExp=7; IntAct=EBI-302489, EBI-358489;
CC P51532; Q969G3-2: SMARCE1; NbExp=2; IntAct=EBI-302489, EBI-455096;
CC P51532; A4PIV7: SYT-SSX1; NbExp=14; IntAct=EBI-302489, EBI-6901002;
CC P51532; O14746: TERT; NbExp=8; IntAct=EBI-302489, EBI-1772203;
CC P51532; P06536: Nr3c1; Xeno; NbExp=3; IntAct=EBI-302489, EBI-1187143;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00549,
CC ECO:0000269|PubMed:20418909}. Note=Colocalizes with long non-coding RNA
CC Evf2 in nuclear RNA clouds. {ECO:0000250|UniProtKB:Q3TKT4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=P51532-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P51532-2; Sequence=VSP_043137;
CC Name=3;
CC IsoId=P51532-3; Sequence=VSP_043137, VSP_043677, VSP_043678;
CC Name=4;
CC IsoId=P51532-4; Sequence=VSP_043137, VSP_043677;
CC Name=5;
CC IsoId=P51532-5; Sequence=VSP_043137, VSP_043678;
CC -!- TISSUE SPECIFICITY: Colocalizes with ZEB1 in E-cadherin-negative cells
CC from established lines, and stroma of normal colon as well as in de-
CC differentiated epithelial cells at the invasion front of colorectal
CC carcinomas (at protein level). {ECO:0000269|PubMed:20418909}.
CC -!- DISEASE: Rhabdoid tumor predisposition syndrome 2 (RTPS2) [MIM:613325]:
CC A familial cancer syndrome predisposing to renal or extrarenal
CC malignant rhabdoid tumors and to a variety of tumors of the central
CC nervous system, including choroid plexus carcinoma, medulloblastoma,
CC and central primitive neuroectodermal tumors. Rhabdoid tumors are the
CC most aggressive and lethal malignancies occurring in early childhood.
CC {ECO:0000269|PubMed:20137775}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- DISEASE: Coffin-Siris syndrome 4 (CSS4) [MIM:614609]: A form of Coffin-
CC Siris syndrome, a congenital multiple malformation syndrome with broad
CC phenotypic and genetic variability. Cardinal features are intellectual
CC disability, coarse facial features, hypertrichosis, and hypoplastic or
CC absent fifth digit nails or phalanges. Additional features include
CC malformations of the cardiac, gastrointestinal, genitourinary, and/or
CC central nervous systems. Sucking/feeding difficulties, poor growth,
CC ophthalmologic abnormalities, hearing impairment, and spinal anomalies
CC are common findings. Both autosomal dominant and autosomal recessive
CC inheritance patterns have been reported. {ECO:0000269|PubMed:22426308}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/SMARCA4ID42333ch19p13.html";
CC -!- WEB RESOURCE: Name=Mendelian genes SWI/SNF related, matrix associated,
CC actin dependent regulator of chromatin, subfamily a, member 4
CC (SMARCA4); Note=Leiden Open Variation Database (LOVD);
CC URL="https://databases.lovd.nl/shared/genes/SMARCA4";
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DR EMBL; U29175; AAB40977.1; -; mRNA.
DR EMBL; D26156; BAA05143.1; -; mRNA.
DR EMBL; AF254822; AAG24789.1; -; Genomic_DNA.
DR EMBL; EU430756; ACA09750.1; -; mRNA.
DR EMBL; EU430757; ACA09751.1; -; mRNA.
DR EMBL; EU430758; ACA09752.1; -; mRNA.
DR EMBL; EU430759; ACA09753.1; -; mRNA.
DR EMBL; AC006127; AAC97986.1; -; Genomic_DNA.
DR EMBL; AC006127; AAC97987.1; -; Genomic_DNA.
DR EMBL; AC011442; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC011485; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471106; EAW84167.1; -; Genomic_DNA.
DR CCDS; CCDS12253.1; -. [P51532-1]
DR CCDS; CCDS45972.1; -. [P51532-4]
DR CCDS; CCDS45973.1; -. [P51532-3]
DR CCDS; CCDS54217.1; -. [P51532-2]
DR CCDS; CCDS54218.1; -. [P51532-5]
DR PIR; S45252; S45252.
DR RefSeq; NP_001122316.1; NM_001128844.1. [P51532-1]
DR RefSeq; NP_001122317.1; NM_001128845.1. [P51532-4]
DR RefSeq; NP_001122318.1; NM_001128846.1. [P51532-3]
DR RefSeq; NP_001122319.1; NM_001128847.1. [P51532-2]
DR RefSeq; NP_001122320.1; NM_001128848.1. [P51532-5]
DR RefSeq; NP_003063.2; NM_003072.3. [P51532-1]
DR RefSeq; XP_016882654.1; XM_017027165.1.
DR RefSeq; XP_016882655.1; XM_017027166.1.
DR RefSeq; XP_016882656.1; XM_017027167.1.
DR RefSeq; XP_016882657.1; XM_017027168.1.
DR PDB; 2GRC; X-ray; 1.50 A; A=1448-1575.
DR PDB; 2H60; NMR; -; A=1452-1570.
DR PDB; 3UVD; X-ray; 1.85 A; A=1448-1569.
DR PDB; 5DKD; X-ray; 2.00 A; A/B=1451-1569.
DR PDB; 5EA1; X-ray; 2.00 A; A/B/C=1451-1580.
DR PDB; 6BGH; NMR; -; B=1591-1602.
DR PDB; 6HR2; X-ray; 1.76 A; A/E=1449-1568.
DR PDB; 6LTH; EM; 3.00 A; I=1-1647.
DR PDB; 6LTJ; EM; 3.70 A; I=1-1647.
DR PDB; 6SY2; NMR; -; A=610-658.
DR PDB; 6ZS2; X-ray; 1.57 A; A/B=1451-1569.
DR PDBsum; 2GRC; -.
DR PDBsum; 2H60; -.
DR PDBsum; 3UVD; -.
DR PDBsum; 5DKD; -.
DR PDBsum; 5EA1; -.
DR PDBsum; 6BGH; -.
DR PDBsum; 6HR2; -.
DR PDBsum; 6LTH; -.
DR PDBsum; 6LTJ; -.
DR PDBsum; 6SY2; -.
DR PDBsum; 6ZS2; -.
DR AlphaFoldDB; P51532; -.
DR SMR; P51532; -.
DR BioGRID; 112481; 329.
DR ComplexPortal; CPX-1195; Embryonic stem cell-specific SWI/SNF ATP-dependent chromatin remodeling complex.
DR ComplexPortal; CPX-1196; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B variant.
DR ComplexPortal; CPX-1199; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A variant.
DR ComplexPortal; CPX-1204; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1206; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1209; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1211; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1212; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1215; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1216; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1218; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1219; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1221; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1222; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1224; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1226; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1228; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-4206; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA4 variant.
DR ComplexPortal; CPX-4207; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA4 variant.
DR ComplexPortal; CPX-4225; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRA-SMARCA4 variant.
DR ComplexPortal; CPX-4226; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6B-BICRAL-SMARCA4 variant.
DR CORUM; P51532; -.
DR DIP; DIP-24249N; -.
DR IntAct; P51532; 125.
DR MINT; P51532; -.
DR STRING; 9606.ENSP00000395654; -.
DR BindingDB; P51532; -.
DR ChEMBL; CHEMBL3085620; -.
DR GuidetoPHARMACOLOGY; 2740; -.
DR CarbonylDB; P51532; -.
DR GlyGen; P51532; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P51532; -.
DR MetOSite; P51532; -.
DR PhosphoSitePlus; P51532; -.
DR SwissPalm; P51532; -.
DR BioMuta; SMARCA4; -.
DR DMDM; 116242792; -.
DR CPTAC; CPTAC-1367; -.
DR EPD; P51532; -.
DR jPOST; P51532; -.
DR MassIVE; P51532; -.
DR MaxQB; P51532; -.
DR PaxDb; P51532; -.
DR PeptideAtlas; P51532; -.
DR PRIDE; P51532; -.
DR ProteomicsDB; 56327; -. [P51532-1]
DR ProteomicsDB; 56328; -. [P51532-2]
DR ProteomicsDB; 56329; -. [P51532-3]
DR ProteomicsDB; 56330; -. [P51532-4]
DR ProteomicsDB; 56331; -. [P51532-5]
DR ABCD; P51532; 4 sequenced antibodies.
DR Antibodypedia; 3778; 546 antibodies from 45 providers.
DR DNASU; 6597; -.
DR Ensembl; ENST00000344626.10; ENSP00000343896.4; ENSG00000127616.20. [P51532-1]
DR Ensembl; ENST00000429416.8; ENSP00000395654.1; ENSG00000127616.20. [P51532-1]
DR Ensembl; ENST00000444061.8; ENSP00000392837.2; ENSG00000127616.20. [P51532-5]
DR Ensembl; ENST00000541122.6; ENSP00000445036.2; ENSG00000127616.20. [P51532-4]
DR Ensembl; ENST00000589677.5; ENSP00000464778.1; ENSG00000127616.20. [P51532-3]
DR Ensembl; ENST00000590574.6; ENSP00000466963.1; ENSG00000127616.20. [P51532-2]
DR Ensembl; ENST00000643296.1; ENSP00000496635.1; ENSG00000127616.20. [P51532-4]
DR Ensembl; ENST00000644737.1; ENSP00000495548.1; ENSG00000127616.20. [P51532-4]
DR Ensembl; ENST00000645460.1; ENSP00000494463.1; ENSG00000127616.20. [P51532-5]
DR Ensembl; ENST00000646484.1; ENSP00000495536.1; ENSG00000127616.20. [P51532-2]
DR Ensembl; ENST00000646510.1; ENSP00000494772.1; ENSG00000127616.20. [P51532-2]
DR Ensembl; ENST00000647230.1; ENSP00000494676.1; ENSG00000127616.20. [P51532-2]
DR GeneID; 6597; -.
DR KEGG; hsa:6597; -.
DR MANE-Select; ENST00000344626.10; ENSP00000343896.4; NM_003072.5; NP_003063.2.
DR UCSC; uc002mqf.5; human. [P51532-1]
DR CTD; 6597; -.
DR DisGeNET; 6597; -.
DR GeneCards; SMARCA4; -.
DR GeneReviews; SMARCA4; -.
DR HGNC; HGNC:11100; SMARCA4.
DR HPA; ENSG00000127616; Low tissue specificity.
DR MalaCards; SMARCA4; -.
DR MIM; 603254; gene.
DR MIM; 613325; phenotype.
DR MIM; 614609; phenotype.
DR neXtProt; NX_P51532; -.
DR OpenTargets; ENSG00000127616; -.
DR Orphanet; 1465; Coffin-Siris syndrome.
DR Orphanet; 231108; Familial rhabdoid tumor.
DR Orphanet; 370396; Small cell carcinoma of the ovary.
DR Orphanet; 466962; SMARCA4-deficient sarcoma of thorax.
DR PharmGKB; PA35950; -.
DR VEuPathDB; HostDB:ENSG00000127616; -.
DR eggNOG; KOG0386; Eukaryota.
DR GeneTree; ENSGT00940000156887; -.
DR HOGENOM; CLU_000315_15_0_1; -.
DR InParanoid; P51532; -.
DR OMA; THNKLAV; -.
DR OrthoDB; 651627at2759; -.
DR PhylomeDB; P51532; -.
DR PathwayCommons; P51532; -.
DR Reactome; R-HSA-1266695; Interleukin-7 signaling.
DR Reactome; R-HSA-201722; Formation of the beta-catenin:TCF transactivating complex.
DR Reactome; R-HSA-3214858; RMTs methylate histone arginines.
DR Reactome; R-HSA-3247509; Chromatin modifying enzymes.
DR Reactome; R-HSA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR Reactome; R-HSA-9619665; EGR2 and SOX10-mediated initiation of Schwann cell myelination.
DR SignaLink; P51532; -.
DR SIGNOR; P51532; -.
DR BioGRID-ORCS; 6597; 203 hits in 1113 CRISPR screens.
DR ChiTaRS; SMARCA4; human.
DR EvolutionaryTrace; P51532; -.
DR GeneWiki; SMARCA4; -.
DR GenomeRNAi; 6597; -.
DR Pharos; P51532; Tchem.
DR PRO; PR:P51532; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; P51532; protein.
DR Bgee; ENSG00000127616; Expressed in ganglionic eminence and 198 other tissues.
DR ExpressionAtlas; P51532; baseline and differential.
DR Genevisible; P51532; HS.
DR GO; GO:0140092; C:bBAF complex; IC:ComplexPortal.
DR GO; GO:0000785; C:chromatin; IDA:BHF-UCL.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0140288; C:GBAF complex; IC:ComplexPortal.
DR GO; GO:0000776; C:kinetochore; IC:ComplexPortal.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0071565; C:nBAF complex; ISS:UniProtKB.
DR GO; GO:0071564; C:npBAF complex; IDA:BHF-UCL.
DR GO; GO:0016363; C:nuclear matrix; IC:ComplexPortal.
DR GO; GO:0005730; C:nucleolus; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; HDA:UniProtKB.
DR GO; GO:0016586; C:RSC-type complex; IC:ComplexPortal.
DR GO; GO:0016514; C:SWI/SNF complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IGI:BHF-UCL.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR GO; GO:0070182; F:DNA polymerase binding; IPI:BHF-UCL.
DR GO; GO:0004386; F:helicase activity; TAS:ProtInc.
DR GO; GO:0070577; F:lysine-acetylated histone binding; IDA:BHF-UCL.
DR GO; GO:0050681; F:nuclear androgen receptor binding; IPI:BHF-UCL.
DR GO; GO:0002039; F:p53 binding; IPI:BHF-UCL.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030957; F:Tat protein binding; IPI:BHF-UCL.
DR GO; GO:0003713; F:transcription coactivator activity; IDA:BHF-UCL.
DR GO; GO:0001221; F:transcription coregulator binding; IPI:UniProtKB.
DR GO; GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
DR GO; GO:0006338; P:chromatin remodeling; IDA:BHF-UCL.
DR GO; GO:0060766; P:negative regulation of androgen receptor signaling pathway; IMP:BHF-UCL.
DR GO; GO:0045596; P:negative regulation of cell differentiation; IC:ComplexPortal.
DR GO; GO:0030308; P:negative regulation of cell growth; IMP:BHF-UCL.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; TAS:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:BHF-UCL.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0003407; P:neural retina development; IEP:BHF-UCL.
DR GO; GO:0006337; P:nucleosome disassembly; IDA:BHF-UCL.
DR GO; GO:0043923; P:positive regulation by host of viral transcription; IMP:BHF-UCL.
DR GO; GO:0045597; P:positive regulation of cell differentiation; IC:ComplexPortal.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IC:ComplexPortal.
DR GO; GO:0051091; P:positive regulation of DNA-binding transcription factor activity; IDA:BHF-UCL.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; IC:ComplexPortal.
DR GO; GO:1902661; P:positive regulation of glucose mediated signaling pathway; IDA:UniProtKB.
DR GO; GO:1902895; P:positive regulation of miRNA transcription; IMP:BHF-UCL.
DR GO; GO:0045663; P:positive regulation of myoblast differentiation; IC:ComplexPortal.
DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; IC:ComplexPortal.
DR GO; GO:0045582; P:positive regulation of T cell differentiation; IC:ComplexPortal.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:1901838; P:positive regulation of transcription of nucleolar large rRNA by RNA polymerase I; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:BHF-UCL.
DR GO; GO:0030177; P:positive regulation of Wnt signaling pathway; IMP:BHF-UCL.
DR GO; GO:0070316; P:regulation of G0 to G1 transition; IC:ComplexPortal.
DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; IC:ComplexPortal.
DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; IC:ComplexPortal.
DR GO; GO:2000819; P:regulation of nucleotide-excision repair; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; NAS:BHF-UCL.
DR GO; GO:0001188; P:RNA polymerase I preinitiation complex assembly; IEA:GOC.
DR Gene3D; 1.20.920.10; -; 1.
DR Gene3D; 3.40.5.120; -; 1.
DR Gene3D; 3.40.50.10810; -; 1.
DR Gene3D; 3.40.50.300; -; 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-rel_dom; 1.
DR PRINTS; PR00503; BROMODOMAIN.
DR SMART; SM00592; BRK; 1.
DR SMART; SM00297; BROMO; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00573; HSA; 1.
DR SMART; SM00951; QLQ; 1.
DR SMART; SM01314; SnAC; 1.
DR SUPFAM; SSF160481; 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 3D-structure; Acetylation; Activator; Alternative splicing; ATP-binding;
KW Bromodomain; Chromatin regulator; Disease variant; Helicase; Hydrolase;
KW Intellectual disability; Isopeptide bond; Neurogenesis; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repressor; RNA-binding;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..1647
FT /note="Transcription activator BRG1"
FT /id="PRO_0000074353"
FT DOMAIN 171..206
FT /note="QLQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01001"
FT DOMAIN 460..532
FT /note="HSA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00549"
FT DOMAIN 766..931
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 1084..1246
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 1477..1547
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 1..282
FT /note="Necessary for interaction with SS18L1/CREST"
FT /evidence="ECO:0000250"
FT REGION 1..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 198..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 462..728
FT /note="RNA-binding region which is sufficient for binding
FT to lncRNA Evf2"
FT /evidence="ECO:0000250|UniProtKB:Q3TKT4"
FT REGION 577..610
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 647..699
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 837..916
FT /note="Sufficient for interaction with DLX1"
FT /evidence="ECO:0000250|UniProtKB:Q3TKT4"
FT REGION 1247..1446
FT /note="Sufficient for interaction with DLX1"
FT /evidence="ECO:0000250|UniProtKB:Q3TKT4"
FT REGION 1254..1299
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1400..1460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1564..1647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 881..884
FT /note="DEGH box"
FT COMPBIAS 1..31
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..177
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..288
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..340
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 659..674
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 685..699
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1400..1419
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1428..1448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1569..1586
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1587..1613
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1629..1647
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 779..786
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT SITE 1539..1540
FT /note="Required for binding to 'Lys-15'-acetylated histone
FT 3"
FT MOD_RES 11
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT MOD_RES 188
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 353
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 609
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 610
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 613
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 626
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q6DIC0"
FT MOD_RES 695
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 699
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1382
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 1423
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q3TKT4"
FT MOD_RES 1452
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163"
FT MOD_RES 1570
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 1575
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231"
FT MOD_RES 1586
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 1627
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 1631
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT CROSSLNK 1365
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1259..1291
FT /note="Missing (in isoform 2, isoform 3, isoform 4 and
FT isoform 5)"
FT /evidence="ECO:0000303|PubMed:18386774"
FT /id="VSP_043137"
FT VAR_SEQ 1388
FT /note="W -> WLKT (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:18386774"
FT /id="VSP_043677"
FT VAR_SEQ 1475
FT /note="Missing (in isoform 3 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:18386774"
FT /id="VSP_043678"
FT VARIANT 546
FT /note="Missing (in CSS4)"
FT /evidence="ECO:0000269|PubMed:22426308"
FT /id="VAR_068209"
FT VARIANT 561
FT /note="V -> E (in dbSNP:rs1804579)"
FT /id="VAR_028215"
FT VARIANT 859
FT /note="T -> M (in CSS4; dbSNP:rs281875226)"
FT /evidence="ECO:0000269|PubMed:22426308"
FT /id="VAR_068210"
FT VARIANT 885
FT /note="R -> C (in CSS4; dbSNP:rs281875227)"
FT /evidence="ECO:0000269|PubMed:22426308"
FT /id="VAR_068211"
FT VARIANT 921
FT /note="L -> F (in CSS4; dbSNP:rs281875228)"
FT /evidence="ECO:0000269|PubMed:22426308"
FT /id="VAR_068212"
FT VARIANT 1011
FT /note="M -> T (in CSS4; dbSNP:rs281875229)"
FT /evidence="ECO:0000269|PubMed:22426308"
FT /id="VAR_068213"
FT VARIANT 1036
FT /note="M -> I (in dbSNP:rs1801514)"
FT /id="VAR_028216"
FT VARIANT 1157
FT /note="R -> G (in CSS4; dbSNP:rs281875230)"
FT /evidence="ECO:0000269|PubMed:22426308"
FT /id="VAR_068214"
FT MUTAGEN 1484
FT /note="V->A: No effect on binding to 'Lys-15'-acetylated
FT histone H3."
FT /evidence="ECO:0000269|PubMed:17274598"
FT MUTAGEN 1539
FT /note="F->A: Abolishes binding to 'Lys-15'-acetylated
FT histone H3."
FT /evidence="ECO:0000269|PubMed:17274598"
FT MUTAGEN 1540
FT /note="N->A: Abolishes binding to 'Lys-15'-acetylated
FT histone H3."
FT /evidence="ECO:0000269|PubMed:17274598"
FT CONFLICT 569
FT /note="R -> P (in Ref. 1; AAB40977 and 3; BAA05143)"
FT /evidence="ECO:0000305"
FT HELIX 363..386
FT /evidence="ECO:0007829|PDB:6LTH"
FT HELIX 397..408
FT /evidence="ECO:0007829|PDB:6LTH"
FT HELIX 410..427
FT /evidence="ECO:0007829|PDB:6LTH"
FT HELIX 431..433
FT /evidence="ECO:0007829|PDB:6LTH"
FT STRAND 434..437
FT /evidence="ECO:0007829|PDB:6LTH"
FT HELIX 447..474
FT /evidence="ECO:0007829|PDB:6LTH"
FT TURN 612..614
FT /evidence="ECO:0007829|PDB:6SY2"
FT STRAND 619..621
FT /evidence="ECO:0007829|PDB:6SY2"
FT TURN 622..624
FT /evidence="ECO:0007829|PDB:6SY2"
FT TURN 630..632
FT /evidence="ECO:0007829|PDB:6SY2"
FT TURN 636..638
FT /evidence="ECO:0007829|PDB:6SY2"
FT HELIX 639..645
FT /evidence="ECO:0007829|PDB:6SY2"
FT STRAND 649..651
FT /evidence="ECO:0007829|PDB:6SY2"
FT HELIX 1456..1471
FT /evidence="ECO:0007829|PDB:2GRC"
FT TURN 1475..1477
FT /evidence="ECO:0007829|PDB:2GRC"
FT HELIX 1481..1485
FT /evidence="ECO:0007829|PDB:2GRC"
FT TURN 1491..1493
FT /evidence="ECO:0007829|PDB:2GRC"
FT HELIX 1495..1500
FT /evidence="ECO:0007829|PDB:2GRC"
FT HELIX 1507..1515
FT /evidence="ECO:0007829|PDB:2GRC"
FT HELIX 1522..1539
FT /evidence="ECO:0007829|PDB:2GRC"
FT STRAND 1542..1544
FT /evidence="ECO:0007829|PDB:2H60"
FT HELIX 1545..1567
FT /evidence="ECO:0007829|PDB:2GRC"
FT HELIX 1571..1577
FT /evidence="ECO:0007829|PDB:5EA1"
SQ SEQUENCE 1647 AA; 184646 MW; ABDA5EDBF10D7D28 CRC64;
MSTPDPPLGG TPRPGPSPGP GPSPGAMLGP SPGPSPGSAH SMMGPSPGPP SAGHPIPTQG
PGGYPQDNMH QMHKPMESMH EKGMSDDPRY NQMKGMGMRS GGHAGMGPPP SPMDQHSQGY
PSPLGGSEHA SSPVPASGPS SGPQMSSGPG GAPLDGADPQ ALGQQNRGPT PFNQNQLHQL
RAQIMAYKML ARGQPLPDHL QMAVQGKRPM PGMQQQMPTL PPPSVSATGP GPGPGPGPGP
GPGPAPPNYS RPHGMGGPNM PPPGPSGVPP GMPGQPPGGP PKPWPEGPMA NAAAPTSTPQ
KLIPPQPTGR PSPAPPAVPP AASPVMPPQT QSPGQPAQPA PMVPLHQKQS RITPIQKPRG
LDPVEILQER EYRLQARIAH RIQELENLPG SLAGDLRTKA TIELKALRLL NFQRQLRQEV
VVCMRRDTAL ETALNAKAYK RSKRQSLREA RITEKLEKQQ KIEQERKRRQ KHQEYLNSIL
QHAKDFKEYH RSVTGKIQKL TKAVATYHAN TEREQKKENE RIEKERMRRL MAEDEEGYRK
LIDQKKDKRL AYLLQQTDEY VANLTELVRQ HKAAQVAKEK KKKKKKKKAE NAEGQTPAIG
PDGEPLDETS QMSDLPVKVI HVESGKILTG TDAPKAGQLE AWLEMNPGYE VAPRSDSEES
GSEEEEEEEE EEQPQAAQPP TLPVEEKKKI PDPDSDDVSE VDARHIIENA KQDVDDEYGV
SQALARGLQS YYAVAHAVTE RVDKQSALMV NGVLKQYQIK GLEWLVSLYN NNLNGILADE
MGLGKTIQTI ALITYLMEHK RINGPFLIIV PLSTLSNWAY EFDKWAPSVV KVSYKGSPAA
RRAFVPQLRS GKFNVLLTTY EYIIKDKHIL AKIRWKYMIV DEGHRMKNHH CKLTQVLNTH
YVAPRRLLLT GTPLQNKLPE LWALLNFLLP TIFKSCSTFE QWFNAPFAMT GEKVDLNEEE
TILIIRRLHK VLRPFLLRRL KKEVEAQLPE KVEYVIKCDM SALQRVLYRH MQAKGVLLTD
GSEKDKKGKG GTKTLMNTIM QLRKICNHPY MFQHIEESFS EHLGFTGGIV QGLDLYRASG
KFELLDRILP KLRATNHKVL LFCQMTSLMT IMEDYFAYRG FKYLRLDGTT KAEDRGMLLK
TFNEPGSEYF IFLLSTRAGG LGLNLQSADT VIIFDSDWNP HQDLQAQDRA HRIGQQNEVR
VLRLCTVNSV EEKILAAAKY KLNVDQKVIQ AGMFDQKSSS HERRAFLQAI LEHEEQDESR
HCSTGSGSAS FAHTAPPPAG VNPDLEEPPL KEEDEVPDDE TVNQMIARHE EEFDLFMRMD
LDRRREEARN PKRKPRLMEE DELPSWIIKD DAEVERLTCE EEEEKMFGRG SRHRKEVDYS
DSLTEKQWLK AIEEGTLEEI EEEVRQKKSS RKRKRDSDAG SSTPTTSTRS RDKDDESKKQ
KKRGRPPAEK LSPNPPNLTK KMKKIVDAVI KYKDSSSGRQ LSEVFIQLPS RKELPEYYEL
IRKPVDFKKI KERIRNHKYR SLNDLEKDVM LLCQNAQTFN LEGSLIYEDS IVLQSVFTSV
RQKIEKEDDS EGEESEEEEE GEEEGSESES RSVKVKIKLG RKEKAQDRLK GGRRRPSRGS
RAKPVVSDDD SEEEQEEDRS GSGSEED
