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SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1 (BRG1-associated factor 57) (BAF57)

 SMCE1_HUMAN             Reviewed;         411 AA.
Q969G3; B3KMC1; B4DFR4; C0IMW4; C0IMW5; C0IMW7; H7C3F6; O43539;
25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
25-OCT-2004, sequence version 2.
22-NOV-2017, entry version 159.
RecName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1;
AltName: Full=BRG1-associated factor 57;
Short=BAF57;
Name=SMARCE1; Synonyms=BAF57;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM
1).
PubMed=9435219; DOI=10.1073/pnas.95.2.492;
Wang W., Chi T., Xue Y., Zhou S., Kuo A., Crabtree G.R.;
"Architectural DNA binding by a high-mobility-group/kinesin-like
subunit in mammalian SWI/SNF-related complexes.";
Proc. Natl. Acad. Sci. U.S.A. 95:492-498(1998).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 4; 5 AND 6), AND ALTERNATIVE
SPLICING.
Kazantseva A., Kazantseva J., Sadam H., Pruunsild P., Timmusk T.,
Neuman T., Palm K.;
"New players in remodeling neurogenesis: BAF57 neuron-specific
isoforms influence transcription of NRSE-containing genes in a
promoter-specific manner.";
Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
TISSUE=Amygdala, and Hippocampus;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16625196; DOI=10.1038/nature04689;
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
"DNA sequence of human chromosome 17 and analysis of rearrangement in
the human lineage.";
Nature 440:1045-1049(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Testis;
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).
[8]
ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, AND
INTERACTION WITH RCOR1.
PubMed=12192000; DOI=10.1074/jbc.M205691200;
Battaglioli E., Andres M.E., Rose D.W., Chenoweth J.G.,
Rosenfeld M.G., Anderson M.E., Mandel G.;
"REST repression of neuronal genes requires components of the hSWI.SNF
complex.";
J. Biol. Chem. 277:41038-41045(2002).
[9]
CHARACTERIZATION.
PubMed=12110891; DOI=10.1038/nature00876;
Chi T.H., Wan M., Zhao K., Taniuchi I., Chen L., Littman D.R.,
Crabtree G.R.;
"Reciprocal regulation of CD4/CD8 expression by SWI/SNF-like BAF
complexes.";
Nature 418:195-199(2002).
[10]
CHARACTERIZATION.
PubMed=12145209; DOI=10.1093/emboj/cdf412;
Belandia B., Orford R.L., Hurst H.C., Parker M.G.;
"Targeting of SWI/SNF chromatin remodelling complexes to estrogen-
responsive genes.";
EMBO J. 21:4094-4103(2002).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[13]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[15]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-4 AND ARG-40, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Colon carcinoma;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
[16]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-92, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[17]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-92, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[18]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-92 AND LYS-146, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25755297; DOI=10.1074/mcp.O114.044792;
Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
Vertegaal A.C.;
"System-wide analysis of SUMOylation dynamics in response to
replication stress reveals novel small ubiquitin-like modified target
proteins and acceptor lysines relevant for genome stability.";
Mol. Cell. Proteomics 14:1419-1434(2015).
[19]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-3; LYS-92; LYS-131; LYS-146;
LYS-166 AND LYS-277, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[20]
SWI/SNF CHROMATIN REMODELING COMPLEXES.
PubMed=12672490; DOI=10.1016/S0959-437X(03)00022-4;
Martens J.A., Winston F.;
"Recent advances in understanding chromatin remodeling by SWI/SNF
complexes.";
Curr. Opin. Genet. Dev. 13:136-142(2003).
[21]
INTERACTION WITH NR3C1.
PubMed=12917342; DOI=10.1128/MCB.23.17.6210-6220.2003;
Hsiao P.W., Fryer C.J., Trotter K.W., Wang W., Archer T.K.;
"BAF60a mediates critical interactions between nuclear receptors and
the BRG1 chromatin-remodeling complex for transactivation.";
Mol. Cell. Biol. 23:6210-6220(2003).
[22]
INTERACTION WITH ZMIM2.
PubMed=16051670; DOI=10.1210/me.2005-0097;
Huang C.-Y., Beliakoff J., Li X., Lee J., Li X., Sharma M., Lim B.,
Sun Z.;
"hZimp7, a novel PIAS-like protein, enhances androgen receptor-
mediated transcription and interacts with SWI/SNF-like BAF
complexes.";
Mol. Endocrinol. 19:2915-2929(2005).
[23]
IDENTIFICATION IN THE BAF COMPLEX, AND IDENTIFICATION BY MASS
SPECTROMETRY.
PubMed=18765789; DOI=10.1101/gad.471408;
Lange M., Kaynak B., Forster U.B., Toenjes M., Fischer J.J., Grimm C.,
Schlesinger J., Just S., Dunkel I., Krueger T., Mebus S., Lehrach H.,
Lurz R., Gobom J., Rottbauer W., Abdelilah-Seyfried S., Sperling S.;
"Regulation of muscle development by DPF3, a novel histone acetylation
and methylation reader of the BAF chromatin remodeling complex.";
Genes Dev. 22:2370-2384(2008).
[24]
UBIQUITINATION.
PubMed=20829358; DOI=10.1074/jbc.M110.173997;
Keppler B.R., Archer T.K.;
"Ubiquitin-dependent and ubiquitin-independent control of subunit
stoichiometry in the SWI/SNF complex.";
J. Biol. Chem. 285:35665-35674(2010).
[25]
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).
[26]
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).
[27]
INVOLVEMENT IN CSS5, AND VARIANT CSS5 CYS-73.
PubMed=22426308; DOI=10.1038/ng.2219;
Tsurusaki Y., Okamoto N., Ohashi H., Kosho T., Imai Y., Hibi-Ko Y.,
Kaname T., Naritomi K., Kawame H., Wakui K., Fukushima Y., Homma T.,
Kato M., Hiraki Y., Yamagata T., Yano S., Mizuno S., Sakazume S.,
Ishii T., Nagai T., Shiina M., Ogata K., Ohta T., Niikawa N.,
Miyatake S., Okada I., Mizuguchi T., Doi H., Saitsu H., Miyake N.,
Matsumoto N.;
"Mutations affecting components of the SWI/SNF complex cause Coffin-
Siris syndrome.";
Nat. Genet. 44:376-378(2012).
[28]
INVOLVEMENT IN MNGMA.
PubMed=23377182; DOI=10.1038/ng.2552;
Smith M.J., O'Sullivan J., Bhaskar S.S., Hadfield K.D., Poke G.,
Caird J., Sharif S., Eccles D., Fitzpatrick D., Rawluk D.,
du Plessis D., Newman W.G., Evans D.G.;
"Loss-of-function mutations in SMARCE1 cause an inherited disorder of
multiple spinal meningiomas.";
Nat. Genet. 45:295-298(2013).
[29]
VARIANT CSS5 SER-73.
PubMed=23906836; DOI=10.1093/hmg/ddt366;
Wieczorek D., Boegershausen N., Beleggia F., Steiner-Haldenstaett S.,
Pohl E., Li Y., Milz E., Martin M., Thiele H., Altmueller J.,
Alanay Y., Kayserili H., Klein-Hitpass L., Boehringer S.,
Wollstein A., Albrecht B., Boduroglu K., Caliebe A., Chrzanowska K.,
Cogulu O., Cristofoli F., Czeschik J.C., Devriendt K., Dotti M.T.,
Elcioglu N., Gener B., Goecke T.O., Krajewska-Walasek M.,
Guillen-Navarro E., Hayek J., Houge G., Kilic E., Simsek-Kiper P.O.,
Lopez-Gonzalez V., Kuechler A., Lyonnet S., Mari F., Marozza A.,
Mathieu Dramard M., Mikat B., Morin G., Morice-Picard F., Ozkinay F.,
Rauch A., Renieri A., Tinschert S., Utine G.E., Vilain C.,
Vivarelli R., Zweier C., Nuernberg P., Rahmann S., Vermeesch J.,
Luedecke H.J., Zeschnigk M., Wollnik B.;
"A comprehensive molecular study on Coffin-Siris and Nicolaides-
Baraitser syndromes identifies a broad molecular and clinical spectrum
converging on altered chromatin remodeling.";
Hum. Mol. Genet. 22:5121-5135(2013).
[30]
VARIANT MNGMA 125-GLU--ALA-132 DELINS GLY-LEU-HIS-ARG-PHE-ILE-VAL-LEU.
PubMed=25249420; DOI=10.1007/s00381-014-2558-5;
Raffalli-Ebezant H., Rutherford S.A., Stivaros S., Kelsey A.,
Smith M., Evans D.G., Kilday J.P.;
"Pediatric intracranial clear cell meningioma associated with a
germline mutation of SMARCE1: a novel case.";
Childs Nerv. Syst. 31:441-447(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. Belongs to the neural progenitors-
specific chromatin remodeling complex (npBAF complex) and the
neuron-specific chromatin remodeling complex (nBAF complex).
During neural development a switch from a stem/progenitor to a
postmitotic chromatin remodeling mechanism occurs as neurons exit
the cell cycle and become committed to their adult state. The
transition from proliferating neural stem/progenitor cells to
postmitotic neurons requires a switch in subunit composition of
the npBAF and nBAF complexes. As neural progenitors exit mitosis
and differentiate into neurons, npBAF complexes which contain
ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous
alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits
in neuron-specific complexes (nBAF). The npBAF complex is
essential for the self-renewal/proliferative capacity of the
multipotent neural stem cells. The nBAF complex along with CREST
plays a role regulating the activity of genes essential for
dendrite growth (By similarity). Required for the coactivation of
estrogen responsive promoters by SWI/SNF complexes and the
SRC/p160 family of histone acetyltransferases (HATs). Also
specifically interacts with the CoREST corepressor resulting in
repression of neuronal specific gene promoters in non-neuronal
cells. {ECO:0000250|UniProtKB:O54941, ECO:0000303|PubMed:12672490,
ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}.
-!- SUBUNIT: Component of the multiprotein chromatin-remodeling
complexes SWI/SNF: SWI/SNF-A (BAF), SWI/SNF-B (PBAF) and related
complexes. The canonical complex contains a catalytic subunit
(either SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B), and at least
SMARCE1, ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and
SMARCB1/SNF5/BAF47. Other subunits specific to each of the
complexes may also be present permitting several possible
combinations developmentally and tissue specific (PubMed:12672490,
PubMed:22952240, PubMed:26601204). Component of the BAF complex,
which includes at least actin (ACTB), ARID1A/BAF250A,
ARID1B/BAF250B, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A,
ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155,
SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more SMARCD1/BAF60A,
SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the BAF
complex also contains DPF3 (PubMed:18765789). Component of neural
progenitors-specific chromatin remodeling complex (npBAF complex)
composed of at least, ARID1A/BAF250A or ARID1B/BAF250B,
SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B,
SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155,
SMARCE1/BAF57, SMARCC2/BAF170, PHF10/BAF45A, ACTL6A/BAF53A and
actin. Component of neuron-specific chromatin remodeling complex
(nBAF complex) composed of at least, ARID1A/BAF250A or
ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C,
SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47,
SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, DPF1/BAF45B,
DPF3/BAF45C, ACTL6B/BAF53B and actin. May be a 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 (ACTB) (PubMed:22952240,
PubMed:26601204). Interacts with BRDT (By similarity). Also binds
to the SRC/p160 family of histone acetyltransferases (HATs)
composed of NCOA1, NCOA2, and NCOA3. Interacts with RCOR1/CoREST,
NR3C1 and ZMIM2/ZIMP7 (PubMed:12192000, PubMed:12917342,
PubMed:16051670). {ECO:0000250|UniProtKB:O54941,
ECO:0000250|UniProtKB:Q56A18, ECO:0000269|PubMed:12192000,
ECO:0000269|PubMed:12917342, ECO:0000269|PubMed:16051670,
ECO:0000269|PubMed:18765789, ECO:0000303|PubMed:12672490,
ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}.
-!- INTERACTION:
Q9Y2J4-4:AMOTL2; NbExp=3; IntAct=EBI-455078, EBI-10187270;
Q68CP9:ARID2; NbExp=4; IntAct=EBI-455078, EBI-637818;
Q9HCU9:BRMS1; NbExp=3; IntAct=EBI-455078, EBI-714781;
Q96JN2-2:CCDC136; NbExp=3; IntAct=EBI-455078, EBI-10171416;
P0C7W6:CCDC172; NbExp=3; IntAct=EBI-455078, EBI-2548868;
Q8TD31-3:CCHCR1; NbExp=4; IntAct=EBI-455078, EBI-10175300;
Q01850:CDR2; NbExp=5; IntAct=EBI-455078, EBI-1181367;
Q96L14:CEP170P1; NbExp=5; IntAct=EBI-455078, EBI-743488;
Q96MT8:CEP63; NbExp=4; IntAct=EBI-455078, EBI-741977;
Q8NHQ1:CEP70; NbExp=7; IntAct=EBI-455078, EBI-739624;
Q12929:EPS8; NbExp=3; IntAct=EBI-455078, EBI-375576;
Q9UPT5:EXOC7; NbExp=5; IntAct=EBI-455078, EBI-720048;
Q08379:GOLGA2; NbExp=5; IntAct=EBI-455078, EBI-618309;
Q8WYH8:ING5; NbExp=3; IntAct=EBI-455078, EBI-488533;
Q96AA8:JAKMIP2; NbExp=3; IntAct=EBI-455078, EBI-752007;
Q9BVG8:KIFC3; NbExp=4; IntAct=EBI-455078, EBI-2125614;
P19012:KRT15; NbExp=3; IntAct=EBI-455078, EBI-739566;
Q15323:KRT31; NbExp=5; IntAct=EBI-455078, EBI-948001;
Q6A162:KRT40; NbExp=5; IntAct=EBI-455078, EBI-10171697;
P60411:KRTAP10-9; NbExp=3; IntAct=EBI-455078, EBI-10172052;
Q9NPJ6:MED4; NbExp=3; IntAct=EBI-455078, EBI-394607;
P50222:MEOX2; NbExp=7; IntAct=EBI-455078, EBI-748397;
Q8TD10:MIPOL1; NbExp=5; IntAct=EBI-455078, EBI-2548751;
Q96HT8:MRFAP1L1; NbExp=3; IntAct=EBI-455078, EBI-748896;
Q5JR59:MTUS2; NbExp=3; IntAct=EBI-455078, EBI-742948;
Q7Z3S9:NOTCH2NL; NbExp=3; IntAct=EBI-455078, EBI-945833;
P37198:NUP62; NbExp=3; IntAct=EBI-455078, EBI-347978;
Q15311:RALBP1; NbExp=5; IntAct=EBI-455078, EBI-749285;
Q9UKL0:RCOR1; NbExp=4; IntAct=EBI-455096, EBI-926563;
Q6NUQ1:RINT1; NbExp=3; IntAct=EBI-455078, EBI-726876;
Q96R06:SPAG5; NbExp=3; IntAct=EBI-455078, EBI-413317;
O75558:STX11; NbExp=3; IntAct=EBI-455078, EBI-714135;
Q8N0S2:SYCE1; NbExp=3; IntAct=EBI-455078, EBI-6872807;
Q9UBB9:TFIP11; NbExp=5; IntAct=EBI-455078, EBI-1105213;
Q9BYV2:TRIM54; NbExp=5; IntAct=EBI-455078, EBI-2130429;
Q15642:TRIP10; NbExp=3; IntAct=EBI-455078, EBI-739936;
Q15642-2:TRIP10; NbExp=4; IntAct=EBI-455078, EBI-6550597;
P40222:TXLNA; NbExp=3; IntAct=EBI-455078, EBI-359793;
Q8N6Y0:USHBP1; NbExp=3; IntAct=EBI-455078, EBI-739895;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00267, ECO:0000269|PubMed:12192000}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=6;
Name=1; Synonyms=BAF57;
IsoId=Q969G3-1; Sequence=Displayed;
Name=2; Synonyms=BAF57v;
IsoId=Q969G3-2; Sequence=VSP_011801, VSP_011802;
Name=3;
IsoId=Q969G3-3; Sequence=VSP_047604;
Name=4;
IsoId=Q969G3-4; Sequence=VSP_047825;
Name=5;
IsoId=Q969G3-5; Sequence=VSP_047825, VSP_047826;
Name=6;
IsoId=Q969G3-6; Sequence=VSP_047604, VSP_047826;
-!- DOMAIN: The HMG domain is essential for CD4 silencing and CD8
activation; mutation of this domain blocks thymus development.
-!- PTM: Ubiquitinated by TRIP12, leading to its degradation by the
proteasome. Ubiquitination is prevented upon interaction between
TRIP12 and SMARCC1. {ECO:0000269|PubMed:20829358}.
-!- DISEASE: Meningioma (MNGMA) [MIM:607174]: A common neoplasm of the
central nervous system derived from arachnoidal cells. The
majority of meningiomas are well differentiated vascular tumors
which grow slowly and have a low potential to be invasive,
although malignant subtypes occur. Most cases are sporadic.
Familial occurrence of meningioma is rare.
{ECO:0000269|PubMed:23377182, ECO:0000269|PubMed:25249420}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- DISEASE: Coffin-Siris syndrome 5 (CSS5) [MIM:616938]: A form of
Coffin-Siris syndrome, a congenital multiple malformation syndrome
with broad phenotypic and genetic variability. Cardinal features
are intellectual disability, coarse facial features,
hypertrichosis, and hypoplastic or absent fifth digit nails or
phalanges. Additional features include malformations of the
cardiac, gastrointestinal, genitourinary, and/or central nervous
systems. Sucking/feeding difficulties, poor growth, ophthalmologic
abnormalities, hearing impairment, and spinal anomalies are common
findings. Both autosomal dominant and autosomal recessive
inheritance patterns have been reported.
{ECO:0000269|PubMed:22426308, ECO:0000269|PubMed:23906836}.
Note=The disease is caused by mutations affecting the gene
represented in this entry.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF035262; AAC04509.1; -; Genomic_DNA.
EMBL; EU327017; ACA81391.1; -; mRNA.
EMBL; EU327018; ACA81392.1; -; mRNA.
EMBL; EU327019; ACA81393.1; -; mRNA.
EMBL; EU327020; ACA81394.1; -; mRNA.
EMBL; BT007176; AAP35840.1; -; mRNA.
EMBL; AK001532; BAG50933.1; -; mRNA.
EMBL; AK095047; BAG52975.1; -; mRNA.
EMBL; AK294218; BAG57525.1; -; mRNA.
EMBL; AC004585; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC073508; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471152; EAW60670.1; -; Genomic_DNA.
EMBL; BC007082; AAH07082.1; -; mRNA.
EMBL; BC011017; AAH11017.1; -; mRNA.
EMBL; BC063700; AAH63700.1; -; mRNA.
CCDS; CCDS11370.1; -. [Q969G3-1]
RefSeq; NP_003070.3; NM_003079.4. [Q969G3-1]
UniGene; Hs.743978; -.
ProteinModelPortal; Q969G3; -.
SMR; Q969G3; -.
BioGrid; 112489; 126.
CORUM; Q969G3; -.
DIP; DIP-27614N; -.
DIP; DIP-33041N; -.
IntAct; Q969G3; 95.
MINT; MINT-1137973; -.
STRING; 9606.ENSP00000323967; -.
iPTMnet; Q969G3; -.
PhosphoSitePlus; Q969G3; -.
BioMuta; SMARCE1; -.
DMDM; 61247587; -.
EPD; Q969G3; -.
MaxQB; Q969G3; -.
PaxDb; Q969G3; -.
PeptideAtlas; Q969G3; -.
PRIDE; Q969G3; -.
DNASU; 6605; -.
Ensembl; ENST00000348513; ENSP00000323967; ENSG00000073584. [Q969G3-1]
Ensembl; ENST00000377808; ENSP00000367039; ENSG00000073584. [Q969G3-5]
Ensembl; ENST00000400122; ENSP00000411607; ENSG00000073584. [Q969G3-6]
Ensembl; ENST00000578044; ENSP00000464511; ENSG00000073584. [Q969G3-3]
Ensembl; ENST00000580419; ENSP00000462475; ENSG00000073584. [Q969G3-4]
GeneID; 6605; -.
KEGG; hsa:6605; -.
UCSC; uc002hux.4; human. [Q969G3-1]
CTD; 6605; -.
DisGeNET; 6605; -.
EuPathDB; HostDB:ENSG00000073584.18; -.
GeneCards; SMARCE1; -.
GeneReviews; SMARCE1; -.
HGNC; HGNC:11109; SMARCE1.
HPA; CAB037318; -.
HPA; HPA003916; -.
MalaCards; SMARCE1; -.
MIM; 603111; gene.
MIM; 607174; phenotype.
MIM; 616938; phenotype.
neXtProt; NX_Q969G3; -.
OpenTargets; ENSG00000073584; -.
Orphanet; 1465; Coffin-Siris syndrome.
Orphanet; 263662; Familial multiple meningioma.
PharmGKB; PA35959; -.
eggNOG; KOG4715; Eukaryota.
eggNOG; ENOG410Y9B3; LUCA.
GeneTree; ENSGT00390000003628; -.
HOGENOM; HOG000230965; -.
HOVERGEN; HBG054558; -.
InParanoid; Q969G3; -.
KO; K11651; -.
OMA; CCMKVEV; -.
OrthoDB; EOG091G0ER1; -.
PhylomeDB; Q969G3; -.
TreeFam; TF321146; -.
Reactome; R-HSA-3214858; RMTs methylate histone arginines.
Reactome; R-HSA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
SIGNOR; Q969G3; -.
GeneWiki; SMARCE1; -.
GenomeRNAi; 6605; -.
PRO; PR:Q969G3; -.
Proteomes; UP000005640; Chromosome 17.
Bgee; ENSG00000073584; -.
CleanEx; HS_SMARCE1; -.
ExpressionAtlas; Q969G3; baseline and differential.
Genevisible; Q969G3; HS.
GO; GO:0071565; C:nBAF complex; ISS:UniProtKB.
GO; GO:0071564; C:npBAF complex; ISS:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; IDA:UniProtKB.
GO; GO:0000228; C:nuclear chromosome; TAS:ProtInc.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:LIFEdb.
GO; GO:0043234; C:protein complex; IDA:UniProtKB.
GO; GO:0016514; C:SWI/SNF complex; IDA:UniProtKB.
GO; GO:0017053; C:transcriptional repressor complex; IPI:UniProtKB.
GO; GO:0003682; F:chromatin binding; TAS:ProtInc.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0016922; F:ligand-dependent nuclear receptor binding; IPI:BHF-UCL.
GO; GO:0008080; F:N-acetyltransferase activity; IDA:UniProtKB.
GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; IEA:Ensembl.
GO; GO:0003713; F:transcription coactivator activity; TAS:ProtInc.
GO; GO:0043044; P:ATP-dependent chromatin remodeling; IDA:UniProtKB.
GO; GO:0006338; P:chromatin remodeling; IDA:BHF-UCL.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
GO; GO:0022008; P:neurogenesis; IEA:Ensembl.
GO; GO:0006337; P:nucleosome disassembly; IDA:BHF-UCL.
GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
Gene3D; 1.10.30.10; -; 1.
InterPro; IPR030089; BAF57.
InterPro; IPR009071; HMG_box_dom.
InterPro; IPR036910; HMG_box_dom_sf.
PANTHER; PTHR13711:SF206; PTHR13711:SF206; 1.
Pfam; PF00505; HMG_box; 1.
SMART; SM00398; HMG; 1.
SUPFAM; SSF47095; SSF47095; 1.
PROSITE; PS50118; HMG_BOX_2; 1.
1: Evidence at protein level;
Alternative splicing; Chromatin regulator; Coiled coil;
Complete proteome; Disease mutation; DNA-binding; Isopeptide bond;
Mental retardation; Methylation; Neurogenesis; Nucleus;
Phosphoprotein; Reference proteome; Ubl conjugation.
CHAIN 1 411 SWI/SNF-related matrix-associated actin-
dependent regulator of chromatin
subfamily E member 1.
/FTId=PRO_0000048577.
DNA_BIND 66 134 HMG box. {ECO:0000255|PROSITE-
ProRule:PRU00267}.
COILED 220 319 {ECO:0000255}.
COMPBIAS 5 65 Pro-rich.
COMPBIAS 320 411 Glu-rich.
MOD_RES 4 4 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 40 40 Omega-N-methylarginine.
{ECO:0000244|PubMed:24129315}.
MOD_RES 265 265 Phosphoserine.
{ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:23186163}.
CROSSLNK 3 3 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 92 92 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 92 92 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25114211,
ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 131 131 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 146 146 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25755297,
ECO:0000244|PubMed:28112733}.
CROSSLNK 166 166 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
CROSSLNK 277 277 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 70 Missing (in isoform 3 and isoform 6).
{ECO:0000303|PubMed:14702039,
ECO:0000303|Ref.2}.
/FTId=VSP_047604.
VAR_SEQ 17 51 Missing (in isoform 4 and isoform 5).
{ECO:0000303|Ref.2}.
/FTId=VSP_047825.
VAR_SEQ 344 411 ETHLEETTESQQNGEEGTSTPEDKESGQEGVDSMAEEGTSD
SNTGSESNSATVEEPPTDPIPEDEKKE -> KNCQLCPRKT
LTSRYTDFPD (in isoform 5 and isoform 6).
{ECO:0000303|Ref.2}.
/FTId=VSP_047826.
VAR_SEQ 344 363 ETHLEETTESQQNGEEGTST -> KNCQLCPRKTLTSRYTD
FPD (in isoform 2). {ECO:0000303|Ref.2}.
/FTId=VSP_011801.
VAR_SEQ 364 411 Missing (in isoform 2).
{ECO:0000303|Ref.2}.
/FTId=VSP_011802.
VARIANT 73 73 Y -> C (in CSS5; dbSNP:rs387906857).
{ECO:0000269|PubMed:22426308}.
/FTId=VAR_068215.
VARIANT 73 73 Y -> S (in CSS5).
{ECO:0000269|PubMed:23906836}.
/FTId=VAR_076932.
VARIANT 125 132 EYNESMKA -> GLHRFIVL (in MNGMA; found in
a case of childhood clear cell
meningioma; associated with disease
susceptibility).
{ECO:0000269|PubMed:25249420}.
/FTId=VAR_071873.
CONFLICT 46 46 G -> S (in Ref. 3; AAP35840 and 7;
AAH07082/AAH11017). {ECO:0000305}.
SEQUENCE 411 AA; 46649 MW; 6F1C1B7917BAD506 CRC64;
MSKRPSYAPP PTPAPATQMP STPGFVGYNP YSHLAYNNYR LGGNPGTNSR VTASSGITIP
KPPKPPDKPL MPYMRYSRKV WDQVKASNPD LKLWEIGKII GGMWRDLTDE EKQEYLNEYE
AEKIEYNESM KAYHNSPAYL AYINAKSRAE AALEEESRQR QSRMEKGEPY MSIQPAEDPD
DYDDGFSMKH TATARFQRNH RLISEILSES VVPDVRSVVT TARMQVLKRQ VQSLMVHQRK
LEAELLQIEE RHQEKKRKFL ESTDSFNNEL KRLCGLKVEV DMEKIAAEIA QAEEQARKRQ
EEREKEAAEQ AERSQSSIVP EEEQAANKGE EKKDDENIPM ETEETHLEET TESQQNGEEG
TSTPEDKESG QEGVDSMAEE GTSDSNTGSE SNSATVEEPP TDPIPEDEKK E


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