SMCE1_HUMAN
ID SMCE1_HUMAN Reviewed; 411 AA.
AC Q969G3; B3KMC1; B4DFR4; C0IMW4; C0IMW5; C0IMW7; H7C3F6; O43539;
DT 25-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 2.
DT 03-AUG-2022, entry version 191.
DE RecName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily E member 1;
DE AltName: Full=BRG1-associated factor 57;
DE Short=BAF57;
GN Name=SMARCE1; Synonyms=BAF57;
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 [GENOMIC DNA], AND ALTERNATIVE SPLICING (ISOFORM 1).
RX PubMed=9435219; DOI=10.1073/pnas.95.2.492;
RA Wang W., Chi T., Xue Y., Zhou S., Kuo A., Crabtree G.R.;
RT "Architectural DNA binding by a high-mobility-group/kinesin-like subunit in
RT mammalian SWI/SNF-related complexes.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:492-498(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2; 4; 5 AND 6), AND ALTERNATIVE
RP SPLICING.
RA Kazantseva A., Kazantseva J., Sadam H., Pruunsild P., Timmusk T.,
RA Neuman T., Palm K.;
RT "New players in remodeling neurogenesis: BAF57 neuron-specific isoforms
RT influence transcription of NRSE-containing genes in a promoter-specific
RT manner.";
RL Submitted (DEC-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Amygdala, and Hippocampus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Testis;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP ALTERNATIVE SPLICING (ISOFORMS 1 AND 2), SUBCELLULAR LOCATION, AND
RP INTERACTION WITH RCOR1.
RX PubMed=12192000; DOI=10.1074/jbc.m205691200;
RA Battaglioli E., Andres M.E., Rose D.W., Chenoweth J.G., Rosenfeld M.G.,
RA Anderson M.E., Mandel G.;
RT "REST repression of neuronal genes requires components of the hSWI.SNF
RT complex.";
RL J. Biol. Chem. 277:41038-41045(2002).
RN [9]
RP CHARACTERIZATION.
RX PubMed=12110891; DOI=10.1038/nature00876;
RA Chi T.H., Wan M., Zhao K., Taniuchi I., Chen L., Littman D.R.,
RA Crabtree G.R.;
RT "Reciprocal regulation of CD4/CD8 expression by SWI/SNF-like BAF
RT complexes.";
RL Nature 418:195-199(2002).
RN [10]
RP CHARACTERIZATION.
RX PubMed=12145209; DOI=10.1093/emboj/cdf412;
RA Belandia B., Orford R.L., Hurst H.C., Parker M.G.;
RT "Targeting of SWI/SNF chromatin remodelling complexes to estrogen-
RT responsive genes.";
RL EMBO J. 21:4094-4103(2002).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265, 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 [12]
RP 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 [13]
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [15]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-4 AND ARG-40, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-92, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [17]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-92, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [18]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-92 AND LYS-146, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [19]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-3; LYS-92; LYS-131; LYS-146;
RP LYS-166 AND LYS-277, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [20]
RP SWI/SNF CHROMATIN REMODELING COMPLEXES.
RX PubMed=12672490; DOI=10.1016/s0959-437x(03)00022-4;
RA Martens J.A., Winston F.;
RT "Recent advances in understanding chromatin remodeling by SWI/SNF
RT complexes.";
RL Curr. Opin. Genet. Dev. 13:136-142(2003).
RN [21]
RP INTERACTION WITH NR3C1.
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 [22]
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 [23]
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 [24]
RP UBIQUITINATION.
RX PubMed=20829358; DOI=10.1074/jbc.m110.173997;
RA Keppler B.R., Archer T.K.;
RT "Ubiquitin-dependent and ubiquitin-independent control of subunit
RT stoichiometry in the SWI/SNF complex.";
RL J. Biol. Chem. 285:35665-35674(2010).
RN [25]
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 [26]
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 [27]
RP INVOLVEMENT IN CSS5, AND VARIANT CSS5 CYS-73.
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).
RN [28]
RP INVOLVEMENT IN MNGMA.
RX PubMed=23377182; DOI=10.1038/ng.2552;
RA Smith M.J., O'Sullivan J., Bhaskar S.S., Hadfield K.D., Poke G., Caird J.,
RA Sharif S., Eccles D., Fitzpatrick D., Rawluk D., du Plessis D.,
RA Newman W.G., Evans D.G.;
RT "Loss-of-function mutations in SMARCE1 cause an inherited disorder of
RT multiple spinal meningiomas.";
RL Nat. Genet. 45:295-298(2013).
RN [29]
RP VARIANT CSS5 SER-73.
RX PubMed=23906836; DOI=10.1093/hmg/ddt366;
RA Wieczorek D., Boegershausen N., Beleggia F., Steiner-Haldenstaett S.,
RA Pohl E., Li Y., Milz E., Martin M., Thiele H., Altmueller J., Alanay Y.,
RA Kayserili H., Klein-Hitpass L., Boehringer S., Wollstein A., Albrecht B.,
RA Boduroglu K., Caliebe A., Chrzanowska K., Cogulu O., Cristofoli F.,
RA Czeschik J.C., Devriendt K., Dotti M.T., Elcioglu N., Gener B.,
RA Goecke T.O., Krajewska-Walasek M., Guillen-Navarro E., Hayek J., Houge G.,
RA Kilic E., Simsek-Kiper P.O., Lopez-Gonzalez V., Kuechler A., Lyonnet S.,
RA Mari F., Marozza A., Mathieu Dramard M., Mikat B., Morin G.,
RA Morice-Picard F., Ozkinay F., Rauch A., Renieri A., Tinschert S.,
RA Utine G.E., Vilain C., Vivarelli R., Zweier C., Nuernberg P., Rahmann S.,
RA Vermeesch J., Luedecke H.J., Zeschnigk M., Wollnik B.;
RT "A comprehensive molecular study on Coffin-Siris and Nicolaides-Baraitser
RT syndromes identifies a broad molecular and clinical spectrum converging on
RT altered chromatin remodeling.";
RL Hum. Mol. Genet. 22:5121-5135(2013).
RN [30]
RP VARIANT MNGMA 125-GLU--ALA-132 DELINS GLY-LEU-HIS-ARG-PHE-ILE-VAL-LEU.
RX PubMed=25249420; DOI=10.1007/s00381-014-2558-5;
RA Raffalli-Ebezant H., Rutherford S.A., Stivaros S., Kelsey A., Smith M.,
RA Evans D.G., Kilday J.P.;
RT "Pediatric intracranial clear cell meningioma associated with a germline
RT mutation of SMARCE1: a novel case.";
RL Childs Nerv. Syst. 31:441-447(2015).
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. Belongs to the neural progenitors-specific chromatin remodeling
CC complex (npBAF complex) and the neuron-specific chromatin remodeling
CC complex (nBAF complex). During neural development a switch from a
CC stem/progenitor to a postmitotic chromatin remodeling mechanism occurs
CC as neurons exit the cell cycle and become committed to their adult
CC state. The transition from proliferating neural stem/progenitor cells
CC to postmitotic neurons requires a switch in subunit composition of the
CC npBAF and nBAF complexes. As neural progenitors exit mitosis and
CC differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A
CC and 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 self-
CC renewal/proliferative capacity of the multipotent neural stem cells.
CC The nBAF complex along with CREST plays a role regulating the activity
CC of genes essential for dendrite growth (By similarity). Required for
CC the coactivation of estrogen responsive promoters by SWI/SNF complexes
CC and the SRC/p160 family of histone acetyltransferases (HATs). Also
CC specifically interacts with the CoREST corepressor resulting in
CC repression of neuronal specific gene promoters in non-neuronal cells.
CC {ECO:0000250|UniProtKB:O54941, ECO:0000303|PubMed:12672490,
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 combinations developmentally and tissue
CC specific (PubMed:12672490, PubMed:22952240, PubMed:26601204). Component
CC of the BAF complex, which includes at least actin (ACTB),
CC ARID1A/BAF250A, ARID1B/BAF250B, SMARCA2/BRM/BAF190B,
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 cells, the
CC BAF complex also contains DPF3 (PubMed:18765789). Component of neural
CC progenitors-specific chromatin remodeling complex (npBAF complex)
CC composed of 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 PHF10/BAF45A, ACTL6A/BAF53A and actin. Component of neuron-specific
CC chromatin remodeling complex (nBAF complex) composed of at least,
CC ARID1A/BAF250A or 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. May be a 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 (ACTB) (PubMed:22952240, PubMed:26601204). Interacts with BRDT (By
CC similarity). Also binds to the SRC/p160 family of histone
CC acetyltransferases (HATs) composed of NCOA1, NCOA2, and NCOA3.
CC Interacts with RCOR1/CoREST, NR3C1 and ZMIM2/ZIMP7 (PubMed:12192000,
CC PubMed:12917342, PubMed:16051670). {ECO:0000250|UniProtKB:O54941,
CC ECO:0000250|UniProtKB:Q56A18, ECO:0000269|PubMed:12192000,
CC ECO:0000269|PubMed:12917342, ECO:0000269|PubMed:16051670,
CC ECO:0000269|PubMed:18765789, ECO:0000303|PubMed:12672490,
CC ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}.
CC -!- INTERACTION:
CC Q969G3; Q9Y2J4: AMOTL2; NbExp=3; IntAct=EBI-455078, EBI-746752;
CC Q969G3; Q9Y2J4-4: AMOTL2; NbExp=3; IntAct=EBI-455078, EBI-10187270;
CC Q969G3; Q68CP9: ARID2; NbExp=5; IntAct=EBI-455078, EBI-637818;
CC Q969G3; Q9HCU9: BRMS1; NbExp=3; IntAct=EBI-455078, EBI-714781;
CC Q969G3; Q96JN2-2: CCDC136; NbExp=3; IntAct=EBI-455078, EBI-10171416;
CC Q969G3; P0C7W6: CCDC172; NbExp=4; IntAct=EBI-455078, EBI-2548868;
CC Q969G3; G5E9W6: CCDC183; NbExp=3; IntAct=EBI-455078, EBI-17212717;
CC Q969G3; Q8TD31-3: CCHCR1; NbExp=3; IntAct=EBI-455078, EBI-10175300;
CC Q969G3; Q01850: CDR2; NbExp=6; IntAct=EBI-455078, EBI-1181367;
CC Q969G3; Q96L14: CEP170P1; NbExp=3; IntAct=EBI-455078, EBI-743488;
CC Q969G3; Q96MT8: CEP63; NbExp=4; IntAct=EBI-455078, EBI-741977;
CC Q969G3; Q96MT8-3: CEP63; NbExp=3; IntAct=EBI-455078, EBI-11522539;
CC Q969G3; Q8NHQ1: CEP70; NbExp=6; IntAct=EBI-455078, EBI-739624;
CC Q969G3; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-455078, EBI-3867333;
CC Q969G3; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-455078, EBI-11988027;
CC Q969G3; Q12929: EPS8; NbExp=3; IntAct=EBI-455078, EBI-375576;
CC Q969G3; Q96A65-2: EXOC4; NbExp=3; IntAct=EBI-455078, EBI-17869840;
CC Q969G3; Q9UPT5: EXOC7; NbExp=5; IntAct=EBI-455078, EBI-720048;
CC Q969G3; Q9NTX9: FAM217B; NbExp=3; IntAct=EBI-455078, EBI-19153639;
CC Q969G3; A1L4K1: FSD2; NbExp=3; IntAct=EBI-455078, EBI-5661036;
CC Q969G3; Q08379: GOLGA2; NbExp=6; IntAct=EBI-455078, EBI-618309;
CC Q969G3; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-455078, EBI-5916454;
CC Q969G3; Q4V328: GRIPAP1; NbExp=3; IntAct=EBI-455078, EBI-717919;
CC Q969G3; Q96LB3-2: IFT74; NbExp=3; IntAct=EBI-455078, EBI-12066130;
CC Q969G3; Q13099: IFT88; NbExp=3; IntAct=EBI-455078, EBI-347427;
CC Q969G3; Q8WYH8: ING5; NbExp=3; IntAct=EBI-455078, EBI-488533;
CC Q969G3; Q96AA8: JAKMIP2; NbExp=3; IntAct=EBI-455078, EBI-752007;
CC Q969G3; Q9BVG8: KIFC3; NbExp=4; IntAct=EBI-455078, EBI-2125614;
CC Q969G3; P02533: KRT14; NbExp=3; IntAct=EBI-455078, EBI-702178;
CC Q969G3; P19012: KRT15; NbExp=3; IntAct=EBI-455078, EBI-739566;
CC Q969G3; P08779: KRT16; NbExp=3; IntAct=EBI-455078, EBI-356410;
CC Q969G3; P08727: KRT19; NbExp=3; IntAct=EBI-455078, EBI-742756;
CC Q969G3; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-455078, EBI-3044087;
CC Q969G3; Q15323: KRT31; NbExp=6; IntAct=EBI-455078, EBI-948001;
CC Q969G3; O76011: KRT34; NbExp=3; IntAct=EBI-455078, EBI-1047093;
CC Q969G3; Q92764: KRT35; NbExp=3; IntAct=EBI-455078, EBI-1058674;
CC Q969G3; O76014: KRT37; NbExp=3; IntAct=EBI-455078, EBI-1045716;
CC Q969G3; Q6A163: KRT39; NbExp=3; IntAct=EBI-455078, EBI-11958242;
CC Q969G3; Q6A162: KRT40; NbExp=6; IntAct=EBI-455078, EBI-10171697;
CC Q969G3; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-455078, EBI-11959885;
CC Q969G3; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-455078, EBI-10171774;
CC Q969G3; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-455078, EBI-10172052;
CC Q969G3; Q9NPJ6: MED4; NbExp=3; IntAct=EBI-455078, EBI-394607;
CC Q969G3; P50222: MEOX2; NbExp=3; IntAct=EBI-455078, EBI-748397;
CC Q969G3; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-455078, EBI-16439278;
CC Q969G3; Q8TD10: MIPOL1; NbExp=6; IntAct=EBI-455078, EBI-2548751;
CC Q969G3; Q96HT8: MRFAP1L1; NbExp=3; IntAct=EBI-455078, EBI-748896;
CC Q969G3; Q5JR59: MTUS2; NbExp=3; IntAct=EBI-455078, EBI-742948;
CC Q969G3; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-455078, EBI-11522433;
CC Q969G3; Q7Z3S9: NOTCH2NLA; NbExp=3; IntAct=EBI-455078, EBI-945833;
CC Q969G3; P37198: NUP62; NbExp=3; IntAct=EBI-455078, EBI-347978;
CC Q969G3; O43482: OIP5; NbExp=3; IntAct=EBI-455078, EBI-536879;
CC Q969G3; P62333: PSMC6; NbExp=3; IntAct=EBI-455078, EBI-357669;
CC Q969G3; Q15311: RALBP1; NbExp=6; IntAct=EBI-455078, EBI-749285;
CC Q969G3; Q6NUQ1: RINT1; NbExp=3; IntAct=EBI-455078, EBI-726876;
CC Q969G3; Q96R06: SPAG5; NbExp=3; IntAct=EBI-455078, EBI-413317;
CC Q969G3; O75558: STX11; NbExp=3; IntAct=EBI-455078, EBI-714135;
CC Q969G3; Q8N0S2: SYCE1; NbExp=3; IntAct=EBI-455078, EBI-6872807;
CC Q969G3; Q9BXU0: TEX12; NbExp=3; IntAct=EBI-455078, EBI-12090309;
CC Q969G3; Q9UBB9: TFIP11; NbExp=7; IntAct=EBI-455078, EBI-1105213;
CC Q969G3; Q9BYV2: TRIM54; NbExp=6; IntAct=EBI-455078, EBI-2130429;
CC Q969G3; Q15642: TRIP10; NbExp=3; IntAct=EBI-455078, EBI-739936;
CC Q969G3; Q15642-2: TRIP10; NbExp=6; IntAct=EBI-455078, EBI-6550597;
CC Q969G3; P40222: TXLNA; NbExp=3; IntAct=EBI-455078, EBI-359793;
CC Q969G3; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-455078, EBI-739895;
CC Q969G3; Q8N1B4: VPS52; NbExp=3; IntAct=EBI-455078, EBI-2799833;
CC Q969G3-1; Q9UKL0: RCOR1; NbExp=2; IntAct=EBI-455091, EBI-926563;
CC Q969G3-2; Q9UKL0: RCOR1; NbExp=4; IntAct=EBI-455096, EBI-926563;
CC Q969G3-2; P51532: SMARCA4; NbExp=2; IntAct=EBI-455096, EBI-302489;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00267,
CC ECO:0000269|PubMed:12192000}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=BAF57;
CC IsoId=Q969G3-1; Sequence=Displayed;
CC Name=2; Synonyms=BAF57v;
CC IsoId=Q969G3-2; Sequence=VSP_011801, VSP_011802;
CC Name=3;
CC IsoId=Q969G3-3; Sequence=VSP_047604;
CC Name=4;
CC IsoId=Q969G3-4; Sequence=VSP_047825;
CC Name=5;
CC IsoId=Q969G3-5; Sequence=VSP_047825, VSP_047826;
CC Name=6;
CC IsoId=Q969G3-6; Sequence=VSP_047604, VSP_047826;
CC -!- DOMAIN: The HMG domain is essential for CD4 silencing and CD8
CC activation; mutation of this domain blocks thymus development.
CC -!- PTM: Ubiquitinated by TRIP12, leading to its degradation by the
CC proteasome. Ubiquitination is prevented upon interaction between TRIP12
CC and SMARCC1. {ECO:0000269|PubMed:20829358}.
CC -!- DISEASE: Meningioma (MNGMA) [MIM:607174]: A common neoplasm of the
CC central nervous system derived from arachnoidal cells. The majority of
CC meningiomas are well differentiated vascular tumors which grow slowly
CC and have a low potential to be invasive, although malignant subtypes
CC occur. Most cases are sporadic. Familial occurrence of meningioma is
CC rare. {ECO:0000269|PubMed:23377182, ECO:0000269|PubMed:25249420}.
CC Note=Disease susceptibility is associated with variants affecting the
CC gene represented in this entry.
CC -!- DISEASE: Coffin-Siris syndrome 5 (CSS5) [MIM:616938]: 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 ECO:0000269|PubMed:23906836}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
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DR EMBL; AF035262; AAC04509.1; -; Genomic_DNA.
DR EMBL; EU327017; ACA81391.1; -; mRNA.
DR EMBL; EU327018; ACA81392.1; -; mRNA.
DR EMBL; EU327019; ACA81393.1; -; mRNA.
DR EMBL; EU327020; ACA81394.1; -; mRNA.
DR EMBL; BT007176; AAP35840.1; -; mRNA.
DR EMBL; AK001532; BAG50933.1; -; mRNA.
DR EMBL; AK095047; BAG52975.1; -; mRNA.
DR EMBL; AK294218; BAG57525.1; -; mRNA.
DR EMBL; AC004585; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC073508; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471152; EAW60670.1; -; Genomic_DNA.
DR EMBL; BC007082; AAH07082.1; -; mRNA.
DR EMBL; BC011017; AAH11017.1; -; mRNA.
DR EMBL; BC063700; AAH63700.1; -; mRNA.
DR CCDS; CCDS11370.1; -. [Q969G3-1]
DR RefSeq; NP_003070.3; NM_003079.4. [Q969G3-1]
DR PDB; 6LTH; EM; 3.00 A; Q=1-411.
DR PDB; 6LTJ; EM; 3.70 A; Q=1-411.
DR PDB; 7CYU; X-ray; 2.55 A; A=66-134.
DR PDBsum; 6LTH; -.
DR PDBsum; 6LTJ; -.
DR PDBsum; 7CYU; -.
DR AlphaFoldDB; Q969G3; -.
DR SMR; Q969G3; -.
DR BioGRID; 112489; 212.
DR ComplexPortal; CPX-1164; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1194; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant.
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-1201; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1202; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1203; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1204; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1205; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1206; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1207; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1209; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1210; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 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-1213; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 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-1217; Neuron-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 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-1220; Brain-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 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-1223; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1224; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant.
DR ComplexPortal; CPX-1225; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA2 variant.
DR ComplexPortal; CPX-1226; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1A-SMARCA4 variant.
DR ComplexPortal; CPX-1227; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA2 variant.
DR ComplexPortal; CPX-1228; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6B-ARID1B-SMARCA4 variant.
DR CORUM; Q969G3; -.
DR DIP; DIP-27614N; -.
DR DIP; DIP-33041N; -.
DR IntAct; Q969G3; 139.
DR MINT; Q969G3; -.
DR STRING; 9606.ENSP00000323967; -.
DR DrugBank; DB12695; Phenethyl Isothiocyanate.
DR iPTMnet; Q969G3; -.
DR PhosphoSitePlus; Q969G3; -.
DR BioMuta; SMARCE1; -.
DR DMDM; 61247587; -.
DR EPD; Q969G3; -.
DR jPOST; Q969G3; -.
DR MassIVE; Q969G3; -.
DR MaxQB; Q969G3; -.
DR PaxDb; Q969G3; -.
DR PeptideAtlas; Q969G3; -.
DR PRIDE; Q969G3; -.
DR ProteomicsDB; 4071; -.
DR ProteomicsDB; 45313; -.
DR ProteomicsDB; 7575; -.
DR ProteomicsDB; 75754; -. [Q969G3-1]
DR ProteomicsDB; 75755; -. [Q969G3-2]
DR ABCD; Q969G3; 1 sequenced antibody.
DR Antibodypedia; 1299; 404 antibodies from 43 providers.
DR DNASU; 6605; -.
DR Ensembl; ENST00000264640.9; ENSP00000466608.2; ENSG00000073584.20. [Q969G3-2]
DR Ensembl; ENST00000348513.12; ENSP00000323967.6; ENSG00000073584.20. [Q969G3-1]
DR Ensembl; ENST00000377808.9; ENSP00000367039.4; ENSG00000073584.20. [Q969G3-5]
DR Ensembl; ENST00000400122.8; ENSP00000411607.2; ENSG00000073584.20. [Q969G3-6]
DR Ensembl; ENST00000447024.6; ENSP00000392958.2; ENSG00000073584.20. [Q969G3-2]
DR Ensembl; ENST00000578044.6; ENSP00000464511.1; ENSG00000073584.20. [Q969G3-3]
DR Ensembl; ENST00000643318.1; ENSP00000494771.1; ENSG00000073584.20. [Q969G3-3]
DR Ensembl; ENST00000643683.1; ENSP00000496094.1; ENSG00000073584.20. [Q969G3-1]
DR Ensembl; ENST00000644701.1; ENSP00000496097.1; ENSG00000073584.20. [Q969G3-2]
DR Ensembl; ENST00000647508.1; ENSP00000496445.1; ENSG00000073584.20. [Q969G3-4]
DR GeneID; 6605; -.
DR KEGG; hsa:6605; -.
DR MANE-Select; ENST00000348513.12; ENSP00000323967.6; NM_003079.5; NP_003070.3.
DR UCSC; uc002hux.4; human. [Q969G3-1]
DR CTD; 6605; -.
DR DisGeNET; 6605; -.
DR GeneCards; SMARCE1; -.
DR GeneReviews; SMARCE1; -.
DR HGNC; HGNC:11109; SMARCE1.
DR HPA; ENSG00000073584; Low tissue specificity.
DR MalaCards; SMARCE1; -.
DR MIM; 603111; gene.
DR MIM; 607174; phenotype.
DR MIM; 616938; phenotype.
DR neXtProt; NX_Q969G3; -.
DR OpenTargets; ENSG00000073584; -.
DR Orphanet; 1465; Coffin-Siris syndrome.
DR Orphanet; 263662; Familial multiple meningioma.
DR Orphanet; 2495; Meningioma.
DR PharmGKB; PA35959; -.
DR VEuPathDB; HostDB:ENSG00000073584; -.
DR eggNOG; KOG4715; Eukaryota.
DR GeneTree; ENSGT00390000003628; -.
DR InParanoid; Q969G3; -.
DR OMA; QEYDIER; -.
DR PhylomeDB; Q969G3; -.
DR TreeFam; TF321146; -.
DR PathwayCommons; Q969G3; -.
DR Reactome; R-HSA-3214858; RMTs methylate histone arginines.
DR Reactome; R-HSA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR SignaLink; Q969G3; -.
DR SIGNOR; Q969G3; -.
DR BioGRID-ORCS; 6605; 528 hits in 1113 CRISPR screens.
DR ChiTaRS; SMARCE1; human.
DR GeneWiki; SMARCE1; -.
DR GenomeRNAi; 6605; -.
DR Pharos; Q969G3; Tbio.
DR PRO; PR:Q969G3; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q969G3; protein.
DR Bgee; ENSG00000073584; Expressed in calcaneal tendon and 123 other tissues.
DR ExpressionAtlas; Q969G3; baseline and differential.
DR Genevisible; Q969G3; HS.
DR GO; GO:0140092; C:bBAF complex; IC:ComplexPortal.
DR GO; GO:0035060; C:brahma complex; IC:ComplexPortal.
DR GO; GO:0000785; C:chromatin; HDA:UniProtKB.
DR GO; GO:0000776; C:kinetochore; IC:ComplexPortal.
DR GO; GO:0071565; C:nBAF complex; ISS:UniProtKB.
DR GO; GO:0071564; C:npBAF complex; ISS:UniProtKB.
DR GO; GO:0000228; C:nuclear chromosome; TAS:ProtInc.
DR GO; GO:0016363; C:nuclear matrix; IC:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:LIFEdb.
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:0003682; F:chromatin binding; TAS:ProtInc.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008080; F:N-acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0016922; F:nuclear receptor binding; IPI:BHF-UCL.
DR GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:Ensembl.
DR GO; GO:0003713; F:transcription coactivator activity; TAS:ProtInc.
DR GO; GO:0006338; P:chromatin remodeling; IDA:BHF-UCL.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:UniProtKB.
DR GO; GO:0022008; P:neurogenesis; IEA:Ensembl.
DR GO; GO:0006337; P:nucleosome disassembly; IDA:BHF-UCL.
DR GO; GO:0045597; P:positive regulation of cell differentiation; IC:ComplexPortal.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; IC:ComplexPortal.
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: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; TAS:ProtInc.
DR Gene3D; 1.10.30.10; -; 1.
DR InterPro; IPR030089; BAF57.
DR InterPro; IPR009071; HMG_box_dom.
DR InterPro; IPR036910; HMG_box_dom_sf.
DR PANTHER; PTHR46232; PTHR46232; 1.
DR Pfam; PF00505; HMG_box; 1.
DR SMART; SM00398; HMG; 1.
DR SUPFAM; SSF47095; SSF47095; 1.
DR PROSITE; PS50118; HMG_BOX_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromatin regulator; Coiled coil;
KW Disease variant; DNA-binding; Intellectual disability; Isopeptide bond;
KW Methylation; Neurogenesis; Nucleus; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..411
FT /note="SWI/SNF-related matrix-associated actin-dependent
FT regulator of chromatin subfamily E member 1"
FT /id="PRO_0000048577"
FT DNA_BIND 66..134
FT /note="HMG box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00267"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..175
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 220..319
FT /evidence="ECO:0000255"
FT COMPBIAS 1..18
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 42..56
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..311
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 324..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..398
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 4
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 40
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 3
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 92
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 92
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 131
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 146
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 166
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 277
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..70
FT /note="Missing (in isoform 3 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT /id="VSP_047604"
FT VAR_SEQ 17..51
FT /note="Missing (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_047825"
FT VAR_SEQ 344..411
FT /note="ETHLEETTESQQNGEEGTSTPEDKESGQEGVDSMAEEGTSDSNTGSESNSAT
FT VEEPPTDPIPEDEKKE -> KNCQLCPRKTLTSRYTDFPD (in isoform 5 and
FT isoform 6)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_047826"
FT VAR_SEQ 344..363
FT /note="ETHLEETTESQQNGEEGTST -> KNCQLCPRKTLTSRYTDFPD (in
FT isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_011801"
FT VAR_SEQ 364..411
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_011802"
FT VARIANT 73
FT /note="Y -> C (in CSS5; dbSNP:rs387906857)"
FT /evidence="ECO:0000269|PubMed:22426308"
FT /id="VAR_068215"
FT VARIANT 73
FT /note="Y -> S (in CSS5; dbSNP:rs387906857)"
FT /evidence="ECO:0000269|PubMed:23906836"
FT /id="VAR_076932"
FT VARIANT 125..132
FT /note="EYNESMKA -> GLHRFIVL (in MNGMA; found in a case of
FT childhood clear cell meningioma; associated with disease
FT susceptibility)"
FT /evidence="ECO:0000269|PubMed:25249420"
FT /id="VAR_071873"
FT CONFLICT 46
FT /note="G -> S (in Ref. 3; AAP35840 and 7; AAH07082/
FT AAH11017)"
FT /evidence="ECO:0000305"
FT HELIX 72..87
FT /evidence="ECO:0007829|PDB:7CYU"
FT HELIX 93..105
FT /evidence="ECO:0007829|PDB:7CYU"
FT HELIX 109..127
FT /evidence="ECO:0007829|PDB:7CYU"
FT HELIX 187..206
FT /evidence="ECO:0007829|PDB:6LTH"
FT HELIX 221..275
FT /evidence="ECO:0007829|PDB:6LTH"
SQ 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
