SNF5_HUMAN
ID SNF5_HUMAN Reviewed; 385 AA.
AC Q12824; O75784; O95474; Q17S11; Q38GA1; Q76N08; Q9UBH2;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 03-AUG-2022, entry version 215.
DE RecName: Full=SWI/SNF-related matrix-associated actin-dependent regulator of chromatin subfamily B member 1;
DE AltName: Full=BRG1-associated factor 47;
DE Short=BAF47;
DE AltName: Full=Integrase interactor 1 protein;
DE AltName: Full=SNF5 homolog;
DE Short=hSNF5;
GN Name=SMARCB1; Synonyms=BAF47, INI1, SNF5L1;
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 A).
RX PubMed=7801128; DOI=10.1126/science.7801128;
RA Kalpana G.V., Marmon S., Wang W., Crabtree G.R., Goff S.P.;
RT "Binding and stimulation of HIV-1 integrase by a human homolog of yeast
RT transcription factor SNF5.";
RL Science 266:2002-2006(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INVOLVEMENT IN RTPS1.
RX PubMed=9671307; DOI=10.1038/28212;
RA Versteege I., Sevenet N., Lange J., Rousseau-Merck M.-F., Ambros P.,
RA Handgretinger R., Aurias A., Delattre O.;
RT "Truncating mutations of hSNF5/INI1 in aggressive paediatric cancer.";
RL Nature 394:203-206(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A AND B).
RX PubMed=10208879; DOI=10.1006/bbrc.1999.0563;
RA Bruder C.E., Dumanski J.P., Kedra D.;
RT "The mouse ortholog of the human SMARCB1 gene encodes two splice forms.";
RL Biochem. Biophys. Res. Commun. 257:886-890(1999).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM B).
RA Tozaki H., Yasuda J., Iwakura Y.;
RT "Human Ini1 27bp deletion form.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
RA Beare D.M., Dunham I.;
RT "A genome annotation-driven approach to cloning the human ORFeome.";
RL Genome Biol. 5:R84.1-R84.11(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC TISSUE=Embryo;
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 [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RG NIEHS SNPs program;
RL Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases.
RN [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM B).
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [10]
RP IDENTIFICATION IN BAF COMPLEX.
RX PubMed=8895581; DOI=10.1002/j.1460-2075.1996.tb00921.x;
RA Wang W., Cote J., Xue Y., Zhou S., Khavari P.A., Biggar S.R., Muchardt C.,
RA Kalpana G.V., Goff S.P., Yaniv M., Workman J.L., Crabtree G.R.;
RT "Purification and biochemical heterogeneity of the mammalian SWI-SNF
RT complex.";
RL EMBO J. 15:5370-5382(1996).
RN [11]
RP INTERACTION WITH EPSTEIN-BARR VIRUS EBNA2 (MICROBIAL INFECTION).
RX PubMed=8709224; DOI=10.1128/jvi.70.9.6020-6028.1996;
RA Wu D.Y., Kalpana G.V., Goff S.P., Schubach W.H.;
RT "Epstein-Barr virus nuclear protein 2 (EBNA2) binds to a component of the
RT human SNF-SWI complex, hSNF5/Ini1.";
RL J. Virol. 70:6020-6028(1996).
RN [12]
RP FUNCTION.
RX PubMed=9448295; DOI=10.1073/pnas.95.3.1120;
RA Morozov A., Yung E., Kalpana G.V.;
RT "Structure-function analysis of integrase interactor 1/hSNF5L1 reveals
RT differential properties of two repeat motifs present in the highly
RT conserved region.";
RL Proc. Natl. Acad. Sci. U.S.A. 95:1120-1125(1998).
RN [13]
RP INTERACTION WITH PPP1R15A.
RX PubMed=10490642; DOI=10.1128/mcb.19.10.7050;
RA Adler H.T., Chinery R., Wu D.Y., Kussick S.J., Payne J.M.,
RA Fornace A.J. Jr., Tkachuk D.C.;
RT "Leukemic HRX fusion proteins inhibit GADD34-induced apoptosis and
RT associate with the GADD34 and hSNF5/INI1 proteins.";
RL Mol. Cell. Biol. 19:7050-7060(1999).
RN [14]
RP INTERACTION WITH MYC.
RX PubMed=10319872; DOI=10.1038/8811;
RA Cheng S.-W., Davies K.P., Yung E., Beltran R.J., Yu J., Kalpana G.V.;
RT "c-MYC interacts with INI1/hSNF5 and requires the SWI/SNF complex for
RT transactivation function.";
RL Nat. Genet. 22:102-105(1999).
RN [15]
RP INTERACTION WITH HUMAN PAPILLOMAVIRUS 18 PROTEIN E1 (MICROBIAL INFECTION).
RX PubMed=10365963; DOI=10.1038/20966;
RA Lee D., Sohn H., Kalpana G.V., Choe J.;
RT "Interaction of E1 and hSNF5 proteins stimulates replication of human
RT papillomavirus DNA.";
RL Nature 399:487-491(1999).
RN [16]
RP FUNCTION.
RX PubMed=10078207; DOI=10.1016/s1097-2765(00)80315-9;
RA Phelan M.L., Sif S., Narlikar G.J., Kingston R.E.;
RT "Reconstitution of a core chromatin remodeling complex from SWI/SNF
RT subunits.";
RL Mol. Cell 3:247-253(1999).
RN [17]
RP INVOLVEMENT IN RTPS1.
RX PubMed=9892189;
RA Biegel J.A., Zhou J.-Y., Rorke L.B., Stenstrom C., Wainwright L.M.,
RA Fogelgren B.;
RT "Germ-line and acquired mutations of INI1 in atypical teratoid and rhabdoid
RT tumors.";
RL Cancer Res. 59:74-79(1999).
RN [18]
RP INTERACTION WITH PPP1R15A.
RX PubMed=12016208; DOI=10.1074/jbc.m200955200;
RA Wu D.Y., Tkachuck D.C., Roberson R.S., Schubach W.H.;
RT "The human SNF5/INI1 protein facilitates the function of the growth arrest
RT and DNA damage-inducible protein (GADD34) and modulates GADD34-bound
RT protein phosphatase-1 activity.";
RL J. Biol. Chem. 277:27706-27715(2002).
RN [19]
RP FUNCTION IN CELL CYCLE.
RX PubMed=12226744; DOI=10.1038/sj.onc.1205841;
RA Versteege I., Medjkane S., Rouillard D., Delattre O.;
RT "A key role of the hSNF5/INI1 tumour suppressor in the control of the G1-S
RT transition of the cell cycle.";
RL Oncogene 21:6403-6412(2002).
RN [20]
RP FUNCTION IN CELL CYCLE.
RX PubMed=14604992; DOI=10.1074/jbc.m309333200;
RA Oruetxebarria I., Venturini F., Kekarainen T., Houweling A.,
RA Zuijderduijn L.M.P., Mohd-Sarip A., Vries R.G.J., Hoeben R.C.,
RA Verrijzer C.P.;
RT "P16INK4a is required for hSNF5 chromatin remodeler-induced cellular
RT senescence in malignant rhabdoid tumor cells.";
RL J. Biol. Chem. 279:3807-3816(2004).
RN [21]
RP FUNCTION IN ACTIVATION OF COLONY STIMULATING FACTOR 1 PROMOTER.
RX PubMed=16267391;
RA Pan X., Song Z., Zhai L., Li X., Zeng X.;
RT "Chromatin-remodeling factor INI1/hSNF5/BAF47 is involved in activation of
RT the colony stimulating factor 1 promoter.";
RL Mol. Cells 20:183-188(2005).
RN [22]
RP DISEASE.
RX PubMed=15899790; DOI=10.1158/0008-5472.can-04-3050;
RA Modena P., Lualdi E., Facchinetti F., Galli L., Teixeira M.R., Pilotti S.,
RA Sozzi G.;
RT "SMARCB1/INI1 tumor suppressor gene is frequently inactivated in
RT epithelioid sarcomas.";
RL Cancer Res. 65:4012-4019(2005).
RN [23]
RP INTERACTION WITH YWHAZ.
RX PubMed=16959763; DOI=10.1074/mcp.m600147-mcp200;
RA Angrand P.O., Segura I., Voelkel P., Ghidelli S., Terry R., Brajenovic M.,
RA Vintersten K., Klein R., Superti-Furga G., Drewes G., Kuster B.,
RA Bouwmeester T., Acker-Palmer A.;
RT "Transgenic mouse proteomics identifies new 14-3-3-associated proteins
RT involved in cytoskeletal rearrangements and cell signaling.";
RL Mol. Cell. Proteomics 5:2211-2227(2006).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-129, AND IDENTIFICATION BY
RP 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 [25]
RP INTERACTION WITH CEBPB.
RX PubMed=20111005; DOI=10.1038/emboj.2010.3;
RA Kowenz-Leutz E., Pless O., Dittmar G., Knoblich M., Leutz A.;
RT "Crosstalk between C/EBPbeta phosphorylation, arginine methylation, and
RT SWI/SNF/Mediator implies an indexing transcription factor code.";
RL EMBO J. 29:1105-1115(2010).
RN [26]
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 [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 SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-106; LYS-108; LYS-124 AND
RP LYS-161, AND IDENTIFICATION BY MASS 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 [29]
RP FUNCTION OF BAF COMPLEX IN CHROMATIN REMODELING.
RX PubMed=16314535; DOI=10.1128/mcb.25.24.11156-11170.2005;
RA Ulyanova N.P., Schnitzler G.R.;
RT "Human SWI/SNF generates abundant, structurally altered dinucleosomes on
RT polynucleosomal templates.";
RL Mol. Cell. Biol. 25:11156-11170(2005).
RN [30]
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 [31]
RP INVOLVEMENT IN SWNTS1.
RX PubMed=17357086; DOI=10.1086/513207;
RA Hulsebos T.J.M., Plomp A.S., Wolterman R.A., Robanus-Maandag E.C., Baas F.,
RA Wesseling P.;
RT "Germline mutation of INI1/SMARCB1 in familial schwannomatosis.";
RL Am. J. Hum. Genet. 80:805-810(2007).
RN [32]
RP INVOLVEMENT IN SWNTS1.
RX PubMed=18072270; DOI=10.1002/humu.20679;
RA Sestini R., Bacci C., Provenzano A., Genuardi M., Papi L.;
RT "Evidence of a four-hit mechanism involving SMARCB1 and NF2 in
RT schwannomatosis-associated schwannomas.";
RL Hum. Mutat. 29:227-231(2008).
RN [33]
RP INTERACTION WITH PIH1D1.
RX PubMed=22368283; DOI=10.1093/jmcb/mjs003;
RA Zhai N., Zhao Z.L., Cheng M.B., Di Y.W., Yan H.X., Cao C.Y., Dai H.,
RA Zhang Y., Shen Y.F.;
RT "Human PIH1 associates with histone H4 to mediate the glucose-dependent
RT enhancement of pre-rRNA synthesis.";
RL J. Mol. Cell Biol. 4:231-241(2012).
RN [34]
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 [35]
RP INTERACTION WITH ERCC6.
RX PubMed=24874740; DOI=10.1038/cddis.2014.228;
RA Ciaffardini F., Nicolai S., Caputo M., Canu G., Paccosi E., Costantino M.,
RA Frontini M., Balajee A.S., Proietti-De-Santis L.;
RT "The cockayne syndrome B protein is essential for neuronal differentiation
RT and neuritogenesis.";
RL Cell Death Dis. 5:E1268-E1268(2014).
RN [36]
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 [37]
RP INVOLVEMENT IN CSS3, AND VARIANTS CSS3 CYS-366 AND GLN-374.
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 [38]
RP STRUCTURE BY NMR OF 2-113, DOMAIN, AND DNA-BINDING.
RX PubMed=26073604; DOI=10.1016/j.str.2015.04.021;
RA Allen M.D., Freund S.M., Zinzalla G., Bycroft M.;
RT "The SWI/SNF subunit INI1 contains an N-terminal winged helix DNA binding
RT domain that is a target for mutations in schwannomatosis.";
RL Structure 23:1344-1349(2015).
RN [39]
RP VARIANT CSS3 HIS-37.
RX PubMed=22726846; DOI=10.1016/j.ajhg.2012.05.003;
RA Kleefstra T., Kramer J.M., Neveling K., Willemsen M.H., Koemans T.S.,
RA Vissers L.E., Wissink-Lindhout W., Fenckova M., van den Akker W.M.,
RA Kasri N.N., Nillesen W.M., Prescott T., Clark R.D., Devriendt K.,
RA van Reeuwijk J., de Brouwer A.P., Gilissen C., Zhou H., Brunner H.G.,
RA Veltman J.A., Schenck A., van Bokhoven H.;
RT "Disruption of an EHMT1-associated chromatin-modification module causes
RT intellectual disability.";
RL Am. J. Hum. Genet. 91:73-82(2012).
RN [40]
RP VARIANTS CSS3 LYS-364 DEL AND HIS-377.
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: Core component of the BAF (hSWI/SNF) complex. This ATP-
CC dependent chromatin-remodeling complex plays important roles in cell
CC proliferation and differentiation, in cellular antiviral activities and
CC inhibition of tumor formation. The BAF complex is able to create a
CC stable, altered form of chromatin that constrains fewer negative
CC supercoils than normal. This change in supercoiling would be due to the
CC conversion of up to one-half of the nucleosomes on polynucleosomal
CC arrays into asymmetric structures, termed altosomes, each composed of 2
CC histones octamers. Stimulates in vitro the remodeling activity of
CC SMARCA4/BRG1/BAF190A. Involved in activation of CSF1 promoter. Belongs
CC to the 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 (By similarity). Plays a key role in cell-cycle control and causes cell
CC cycle arrest in G0/G1. {ECO:0000250|UniProtKB:Q9Z0H3,
CC ECO:0000269|PubMed:10078207, ECO:0000269|PubMed:12226744,
CC ECO:0000269|PubMed:14604992, ECO:0000269|PubMed:16267391,
CC ECO:0000269|PubMed:16314535, ECO:0000269|PubMed:9448295}.
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 (Probable). Component of the BAF complex, which includes at
CC least actin (ACTB), ARID1A/BAF250A, ARID1B/BAF250B, SMARCA2/BRM,
CC SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57
CC SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more
CC SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the
CC BAF complex also contains DPF3 (PubMed:8895581, PubMed:18765789).
CC Component of neural progenitors-specific chromatin remodeling complex
CC (npBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B,
CC SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B,
CC SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, 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 (By similarity).
CC Component of the SWI/SNF-B (PBAF) chromatin remodeling complex, at
CC least composed of SMARCA4/BRG1, SMARCB1/BAF47/SNF5, ACTL6A/BAF53A or
CC ACTL6B/BAF53B, SMARCE1/BAF57, SMARCD1/BAF60A, SMARCD2/BAF60B, perhaps
CC SMARCD3/BAF60C, SMARCC1/BAF155, SMARCC2/BAF170, PBRM1/BAF180,
CC ARID2/BAF200 and actin (PubMed:26601204). Binds to double-stranded DNA.
CC Interacts with CEBPB (when not methylated) (PubMed:20111005). Interacts
CC with PIH1D1 (PubMed:22368283). Interacts with MYK and MAEL
CC (PubMed:10319872). Interacts with PPP1R15A (PubMed:10490642,
CC PubMed:12016208). Interacts with DPF2 (PubMed:20460684). Interacts with
CC YWHAZ (PubMed:16959763). Interacts with ERCC6 (PubMed:24874740).
CC Interacts with FOS, FOSB isoform 1 and 2, FOSL1 and FOSL2 (By
CC similarity). {ECO:0000250|UniProtKB:Q9Z0H3,
CC ECO:0000269|PubMed:10319872, ECO:0000269|PubMed:10490642,
CC ECO:0000269|PubMed:12016208, ECO:0000269|PubMed:16959763,
CC ECO:0000269|PubMed:18765789, ECO:0000269|PubMed:20111005,
CC ECO:0000269|PubMed:20460684, ECO:0000269|PubMed:22368283,
CC ECO:0000269|PubMed:24874740, ECO:0000269|PubMed:8895581,
CC ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}.
CC -!- SUBUNIT: (Microbial infection) Binds tightly to the human
CC immunodeficiency virus-type 1 (HIV-1) integrase in vitro and stimulates
CC its DNA-joining activity. Interacts with human papillomavirus 18 E1
CC protein to stimulate its viral replication (PubMed:10365963). Interacts
CC with Epstein-Barr virus protein EBNA-2 (PubMed:8709224).
CC {ECO:0000269|PubMed:10365963, ECO:0000269|PubMed:8709224}.
CC -!- INTERACTION:
CC Q12824; Q68CP9: ARID2; NbExp=11; IntAct=EBI-358419, EBI-637818;
CC Q12824; P27797: CALR; NbExp=5; IntAct=EBI-358419, EBI-1049597;
CC Q12824; G5E9A7: DMWD; NbExp=3; IntAct=EBI-358419, EBI-10976677;
CC Q12824; P50570-2: DNM2; NbExp=3; IntAct=EBI-358419, EBI-10968534;
CC Q12824; P22607: FGFR3; NbExp=3; IntAct=EBI-358419, EBI-348399;
CC Q12824; P14136: GFAP; NbExp=4; IntAct=EBI-358419, EBI-744302;
CC Q12824; Q53GS7: GLE1; NbExp=3; IntAct=EBI-358419, EBI-1955541;
CC Q12824; P06396: GSN; NbExp=3; IntAct=EBI-358419, EBI-351506;
CC Q12824; Q6FI13: H2AC19; NbExp=5; IntAct=EBI-358419, EBI-353620;
CC Q12824; O60814: H2BC12; NbExp=5; IntAct=EBI-358419, EBI-4409738;
CC Q12824; P68431: H3C12; NbExp=5; IntAct=EBI-358419, EBI-79722;
CC Q12824; P62805: H4C9; NbExp=2; IntAct=EBI-358419, EBI-302023;
CC Q12824; P01112: HRAS; NbExp=3; IntAct=EBI-358419, EBI-350145;
CC Q12824; P42858: HTT; NbExp=9; IntAct=EBI-358419, EBI-466029;
CC Q12824; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-358419, EBI-1055254;
CC Q12824; P51608: MECP2; NbExp=3; IntAct=EBI-358419, EBI-1189067;
CC Q12824; P19404: NDUFV2; NbExp=3; IntAct=EBI-358419, EBI-713665;
CC Q12824; P16284: PECAM1; NbExp=3; IntAct=EBI-358419, EBI-716404;
CC Q12824; P51532: SMARCA4; NbExp=34; IntAct=EBI-358419, EBI-302489;
CC Q12824; Q12824: SMARCB1; NbExp=5; IntAct=EBI-358419, EBI-358419;
CC Q12824; Q16637: SMN2; NbExp=3; IntAct=EBI-358419, EBI-395421;
CC Q12824; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-358419, EBI-5235340;
CC Q12824; O14656-2: TOR1A; NbExp=3; IntAct=EBI-358419, EBI-25847109;
CC Q12824; P08670: VIM; NbExp=4; IntAct=EBI-358419, EBI-353844;
CC Q12824; Q9Y649; NbExp=3; IntAct=EBI-358419, EBI-25900580;
CC Q12824; PRO_0000042447 [P04585]: gag-pol; Xeno; NbExp=3; IntAct=EBI-358419, EBI-9872653;
CC Q12824; Q8K1P7: Smarca4; Xeno; NbExp=2; IntAct=EBI-358419, EBI-689301;
CC Q12824; P04326: tat; Xeno; NbExp=3; IntAct=EBI-358419, EBI-7333987;
CC Q12824-1; P06789: E1; Xeno; NbExp=5; IntAct=EBI-7015645, EBI-7015660;
CC Q12824-2; P50570-2: DNM2; NbExp=3; IntAct=EBI-358436, EBI-10968534;
CC Q12824-2; Q86YD7: FAM90A1; NbExp=3; IntAct=EBI-358436, EBI-6658203;
CC Q12824-2; Q8IZU0: FAM9B; NbExp=3; IntAct=EBI-358436, EBI-10175124;
CC Q12824-2; O14964: HGS; NbExp=3; IntAct=EBI-358436, EBI-740220;
CC Q12824-2; O75031: HSF2BP; NbExp=3; IntAct=EBI-358436, EBI-7116203;
CC Q12824-2; Q14005-2: IL16; NbExp=3; IntAct=EBI-358436, EBI-17178971;
CC Q12824-2; Q14696: MESD; NbExp=3; IntAct=EBI-358436, EBI-6165891;
CC Q12824-2; Q96EL3: MRPL53; NbExp=3; IntAct=EBI-358436, EBI-2513715;
CC Q12824-2; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-358436, EBI-79165;
CC Q12824-2; O43741: PRKAB2; NbExp=3; IntAct=EBI-358436, EBI-1053424;
CC Q12824-2; P20618: PSMB1; NbExp=3; IntAct=EBI-358436, EBI-372273;
CC Q12824-2; Q9BVN2: RUSC1; NbExp=3; IntAct=EBI-358436, EBI-6257312;
CC Q12824-2; Q8TAQ2-2: SMARCC2; NbExp=4; IntAct=EBI-358436, EBI-11990400;
CC Q12824-2; Q96GM5: SMARCD1; NbExp=3; IntAct=EBI-358436, EBI-358489;
CC Q12824-2; Q08117-2: TLE5; NbExp=3; IntAct=EBI-358436, EBI-11741437;
CC Q12824-2; Q9UPQ4-2: TRIM35; NbExp=3; IntAct=EBI-358436, EBI-17716262;
CC Q12824-2; P0C7X2: ZNF688; NbExp=3; IntAct=EBI-358436, EBI-4395732;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=A; Synonyms=INI1A;
CC IsoId=Q12824-1; Sequence=Displayed;
CC Name=B; Synonyms=INI1B;
CC IsoId=Q12824-2; Sequence=VSP_004399;
CC -!- DOMAIN: The N-terminal DNA-binding region is structurally similar to
CC winged helix domains. {ECO:0000305|PubMed:26073604}.
CC -!- DISEASE: Rhabdoid tumor predisposition syndrome 1 (RTPS1) [MIM:609322]:
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:9671307, ECO:0000269|PubMed:9892189}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- DISEASE: Schwannomatosis 1 (SWNTS1) [MIM:162091]: A cancer syndrome in
CC which patients develop multiple non-vestibular schwannomas, benign
CC neoplasms that arise from Schwann cells of the cranial, peripheral, and
CC autonomic nerves. {ECO:0000269|PubMed:17357086,
CC ECO:0000269|PubMed:18072270}. Note=Disease susceptibility is associated
CC with variants affecting the gene represented in this entry.
CC -!- DISEASE: Coffin-Siris syndrome 3 (CSS3) [MIM:614608]: 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:22726846, ECO:0000269|PubMed:23906836}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- SIMILARITY: Belongs to the SNF5 family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/SMARCB1ID169.html";
CC -!- WEB RESOURCE: Name=NIEHS-SNPs;
CC URL="http://egp.gs.washington.edu/data/smarcb1/";
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DR EMBL; U04847; AAA81905.1; -; mRNA.
DR EMBL; Y17118; CAA76639.1; ALT_SEQ; Genomic_DNA.
DR EMBL; Y17119; CAA76639.1; JOINED; Genomic_DNA.
DR EMBL; Y17120; CAA76639.1; JOINED; Genomic_DNA.
DR EMBL; Y17121; CAA76639.1; JOINED; Genomic_DNA.
DR EMBL; Y17122; CAA76639.1; JOINED; Genomic_DNA.
DR EMBL; Y17123; CAA76639.1; JOINED; Genomic_DNA.
DR EMBL; Y17124; CAA76639.1; JOINED; Genomic_DNA.
DR EMBL; Y17125; CAA76639.1; JOINED; Genomic_DNA.
DR EMBL; Y17126; CAA76639.1; JOINED; Genomic_DNA.
DR EMBL; AJ011738; CAA09759.1; -; mRNA.
DR EMBL; AJ011737; CAA09758.1; -; mRNA.
DR EMBL; AB017523; BAC77068.1; -; mRNA.
DR EMBL; CR456581; CAG30467.1; -; mRNA.
DR EMBL; AK021419; BAG51033.1; -; mRNA.
DR EMBL; DQ230988; ABB02184.1; -; Genomic_DNA.
DR EMBL; CH471095; EAW59606.1; -; Genomic_DNA.
DR EMBL; BC117114; AAI17115.1; -; mRNA.
DR EMBL; BC143667; AAI43668.1; -; mRNA.
DR CCDS; CCDS13817.1; -. [Q12824-1]
DR CCDS; CCDS46671.1; -. [Q12824-2]
DR PIR; S54705; S54705.
DR RefSeq; NP_001007469.1; NM_001007468.2. [Q12824-2]
DR RefSeq; NP_003064.2; NM_003073.4. [Q12824-1]
DR PDB; 5AJ1; NMR; -; A=2-113.
DR PDB; 5GJK; X-ray; 2.05 A; B=183-249.
DR PDB; 5L7A; X-ray; 2.10 A; A/B/C/D=184-252.
DR PDB; 5L7B; NMR; -; A=184-258.
DR PDB; 6AX5; NMR; -; A=183-265.
DR PDB; 6KAG; X-ray; 2.60 A; A=169-385.
DR PDB; 6KZ7; X-ray; 2.28 A; B/D=171-252.
DR PDB; 6LTH; EM; 3.00 A; M=1-385.
DR PDB; 6LTJ; EM; 3.70 A; M=1-113, M=172-385.
DR PDB; 6LZP; NMR; -; A=171-258.
DR PDB; 6UCH; NMR; -; A=351-385.
DR PDBsum; 5AJ1; -.
DR PDBsum; 5GJK; -.
DR PDBsum; 5L7A; -.
DR PDBsum; 5L7B; -.
DR PDBsum; 6AX5; -.
DR PDBsum; 6KAG; -.
DR PDBsum; 6KZ7; -.
DR PDBsum; 6LTH; -.
DR PDBsum; 6LTJ; -.
DR PDBsum; 6LZP; -.
DR PDBsum; 6UCH; -.
DR AlphaFoldDB; Q12824; -.
DR BMRB; Q12824; -.
DR SMR; Q12824; -.
DR BioGRID; 112482; 267.
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; Q12824; -.
DR DIP; DIP-27550N; -.
DR IntAct; Q12824; 291.
DR MINT; Q12824; -.
DR STRING; 9606.ENSP00000263121; -.
DR GlyGen; Q12824; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q12824; -.
DR PhosphoSitePlus; Q12824; -.
DR BioMuta; SMARCB1; -.
DR DMDM; 51338799; -.
DR EPD; Q12824; -.
DR jPOST; Q12824; -.
DR MassIVE; Q12824; -.
DR MaxQB; Q12824; -.
DR PaxDb; Q12824; -.
DR PeptideAtlas; Q12824; -.
DR PRIDE; Q12824; -.
DR ProteomicsDB; 58970; -. [Q12824-1]
DR ProteomicsDB; 58971; -. [Q12824-2]
DR Antibodypedia; 3973; 546 antibodies from 44 providers.
DR DNASU; 6598; -.
DR Ensembl; ENST00000407422.8; ENSP00000383984.3; ENSG00000099956.20. [Q12824-2]
DR Ensembl; ENST00000618915.3; ENSP00000479330.1; ENSG00000275837.3. [Q12824-1]
DR Ensembl; ENST00000631333.2; ENSP00000486870.1; ENSG00000275837.3. [Q12824-2]
DR Ensembl; ENST00000644036.2; ENSP00000494049.2; ENSG00000099956.20. [Q12824-1]
DR GeneID; 6598; -.
DR KEGG; hsa:6598; -.
DR MANE-Select; ENST00000644036.2; ENSP00000494049.2; NM_003073.5; NP_003064.2.
DR UCSC; uc002zyb.4; human. [Q12824-1]
DR CTD; 6598; -.
DR DisGeNET; 6598; -.
DR GeneCards; SMARCB1; -.
DR GeneReviews; SMARCB1; -.
DR HGNC; HGNC:11103; SMARCB1.
DR HPA; ENSG00000099956; Low tissue specificity.
DR MalaCards; SMARCB1; -.
DR MIM; 162091; phenotype.
DR MIM; 601607; gene.
DR MIM; 609322; phenotype.
DR MIM; 614608; phenotype.
DR neXtProt; NX_Q12824; -.
DR OpenTargets; ENSG00000099956; -.
DR Orphanet; 99966; Atypical teratoid rhabdoid tumor.
DR Orphanet; 1465; Coffin-Siris syndrome.
DR Orphanet; 263662; Familial multiple meningioma.
DR Orphanet; 231108; Familial rhabdoid tumor.
DR Orphanet; 2495; Meningioma.
DR Orphanet; 93921; Schwannomatosis.
DR PharmGKB; PA35953; -.
DR VEuPathDB; HostDB:ENSG00000099956; -.
DR eggNOG; KOG1649; Eukaryota.
DR GeneTree; ENSGT00440000038585; -.
DR InParanoid; Q12824; -.
DR OrthoDB; 790205at2759; -.
DR PhylomeDB; Q12824; -.
DR TreeFam; TF105993; -.
DR PathwayCommons; Q12824; -.
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; Q12824; -.
DR SIGNOR; Q12824; -.
DR BioGRID-ORCS; 6598; 613 hits in 1106 CRISPR screens.
DR ChiTaRS; SMARCB1; human.
DR GeneWiki; SMARCB1; -.
DR GenomeRNAi; 6598; -.
DR Pharos; Q12824; Tbio.
DR PRO; PR:Q12824; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; Q12824; protein.
DR Bgee; ENSG00000099956; Expressed in ganglionic eminence and 141 other tissues.
DR ExpressionAtlas; Q12824; baseline and differential.
DR Genevisible; Q12824; HS.
DR GO; GO:0140092; C:bBAF complex; IC:ComplexPortal.
DR GO; GO:0035060; C:brahma complex; IBA:GO_Central.
DR GO; GO:0000785; C:chromatin; HDA:UniProtKB.
DR GO; GO:0001650; C:fibrillar center; IDA:HPA.
DR GO; GO:0043073; C:germ cell nucleus; IEA:Ensembl.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
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; IEA:InterPro.
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:0001741; C:XY body; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0002039; F:p53 binding; IPI:BHF-UCL.
DR GO; GO:0030957; F:Tat protein binding; IPI:BHF-UCL.
DR GO; GO:0003713; F:transcription coactivator activity; IMP:BHF-UCL.
DR GO; GO:0003712; F:transcription coregulator activity; IBA:GO_Central.
DR GO; GO:0001835; P:blastocyst hatching; IEA:Ensembl.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0006338; P:chromatin remodeling; IDA:BHF-UCL.
DR GO; GO:0015074; P:DNA integration; TAS:ProtInc.
DR GO; GO:0070365; P:hepatocyte differentiation; IEA:Ensembl.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IEA:Ensembl.
DR GO; GO:1900110; P:negative regulation of histone H3-K9 dimethylation; IMP:UniProtKB.
DR GO; GO:1900113; P:negative regulation of histone H3-K9 trimethylation; IMP:UniProtKB.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
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: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:2000617; P:positive regulation of histone H3-K9 acetylation; IMP:UniProtKB.
DR GO; GO:0090240; P:positive regulation of histone H4 acetylation; IMP:UniProtKB.
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: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; IBA:GO_Central.
DR GO; GO:0001188; P:RNA polymerase I preinitiation complex assembly; IEA:GOC.
DR GO; GO:0039692; P:single stranded viral RNA replication via double stranded DNA intermediate; IDA:MGI.
DR InterPro; IPR017393; Sfh1/SNF5.
DR InterPro; IPR006939; SNF5.
DR Pfam; PF04855; SNF5; 1.
DR PIRSF; PIRSF038126; SWI_SNF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Cell cycle;
KW Chromatin regulator; Disease variant; DNA-binding; Host-virus interaction;
KW Hypotrichosis; Intellectual disability; Isopeptide bond; Neurogenesis;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription;
KW Transcription regulation; Tumor suppressor; Ubl conjugation.
FT CHAIN 1..385
FT /note="SWI/SNF-related matrix-associated actin-dependent
FT regulator of chromatin subfamily B member 1"
FT /id="PRO_0000205948"
FT REPEAT 186..245
FT /note="1"
FT REPEAT 259..319
FT /note="2"
FT REGION 1..113
FT /note="DNA-binding"
FT /evidence="ECO:0000269|PubMed:26073604"
FT REGION 183..243
FT /note="HIV-1 integrase-binding"
FT REGION 186..319
FT /note="2 X approximate tandem repeats"
FT REGION 186..245
FT /note="MYC-binding"
FT /evidence="ECO:0000269|PubMed:10208879"
FT REGION 304..318
FT /note="Interaction with PPP1R15A"
FT /evidence="ECO:0000269|PubMed:12016208"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17525332"
FT CROSSLNK 106
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 108
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 124
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 161
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 69..77
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:10208879,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT ECO:0000303|Ref.4"
FT /id="VSP_004399"
FT VARIANT 37
FT /note="R -> H (in CSS3; patient with original diagnosis of
FT Kleefstra syndrome; unknown pathological significance;
FT dbSNP:rs398122368)"
FT /evidence="ECO:0000269|PubMed:22726846"
FT /id="VAR_080263"
FT VARIANT 364
FT /note="Missing (in CSS3)"
FT /evidence="ECO:0000269|PubMed:22426308"
FT /id="VAR_068178"
FT VARIANT 366
FT /note="R -> C (in CSS3; dbSNP:rs886039520)"
FT /evidence="ECO:0000269|PubMed:23906836"
FT /id="VAR_076934"
FT VARIANT 374
FT /note="R -> Q (in CSS3; dbSNP:rs1057517825)"
FT /evidence="ECO:0000269|PubMed:23906836"
FT /id="VAR_076935"
FT VARIANT 377
FT /note="R -> H (in CSS3; dbSNP:rs387906812)"
FT /evidence="ECO:0000269|PubMed:22426308"
FT /id="VAR_068179"
FT CONFLICT 136
FT /note="P -> S (in Ref. 1 and 2; CAA76639)"
FT /evidence="ECO:0000305"
FT CONFLICT 378
FT /note="L -> E (in Ref. 2; CAA76639)"
FT /evidence="ECO:0000305"
FT CONFLICT 382
FT /note="A -> G (in Ref. 1 and 2; CAA76639)"
FT /evidence="ECO:0000305"
FT STRAND 16..18
FT /evidence="ECO:0007829|PDB:5AJ1"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:6LTH"
FT HELIX 29..35
FT /evidence="ECO:0007829|PDB:6LTH"
FT HELIX 42..46
FT /evidence="ECO:0007829|PDB:6LTH"
FT STRAND 52..54
FT /evidence="ECO:0007829|PDB:6LTH"
FT HELIX 57..65
FT /evidence="ECO:0007829|PDB:6LTH"
FT STRAND 72..74
FT /evidence="ECO:0007829|PDB:5AJ1"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:6LTH"
FT STRAND 89..92
FT /evidence="ECO:0007829|PDB:6LTH"
FT HELIX 93..97
FT /evidence="ECO:0007829|PDB:6LTH"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:6LTH"
FT HELIX 105..108
FT /evidence="ECO:0007829|PDB:5AJ1"
FT HELIX 172..180
FT /evidence="ECO:0007829|PDB:6KZ7"
FT STRAND 186..195
FT /evidence="ECO:0007829|PDB:5GJK"
FT STRAND 198..207
FT /evidence="ECO:0007829|PDB:5GJK"
FT STRAND 211..213
FT /evidence="ECO:0007829|PDB:6AX5"
FT HELIX 215..226
FT /evidence="ECO:0007829|PDB:5GJK"
FT HELIX 230..247
FT /evidence="ECO:0007829|PDB:5GJK"
FT HELIX 248..250
FT /evidence="ECO:0007829|PDB:6KZ7"
FT STRAND 259..261
FT /evidence="ECO:0007829|PDB:6AX5"
FT STRAND 263..270
FT /evidence="ECO:0007829|PDB:6KAG"
FT STRAND 273..280
FT /evidence="ECO:0007829|PDB:6KAG"
FT HELIX 290..301
FT /evidence="ECO:0007829|PDB:6KAG"
FT HELIX 307..322
FT /evidence="ECO:0007829|PDB:6KAG"
FT STRAND 337..340
FT /evidence="ECO:0007829|PDB:6LTH"
FT TURN 343..349
FT /evidence="ECO:0007829|PDB:6KAG"
FT STRAND 352..355
FT /evidence="ECO:0007829|PDB:6KAG"
FT HELIX 358..377
FT /evidence="ECO:0007829|PDB:6UCH"
SQ SEQUENCE 385 AA; 44141 MW; B7BCA26875BD943D CRC64;
MMMMALSKTF GQKPVKFQLE DDGEFYMIGS EVGNYLRMFR GSLYKRYPSL WRRLATVEER
KKIVASSHGK KTKPNTKDHG YTTLATSVTL LKASEVEEIL DGNDEKYKAV SISTEPPTYL
REQKAKRNSQ WVPTLPNSSH HLDAVPCSTT INRNRMGRDK KRTFPLCFDD HDPAVIHENA
SQPEVLVPIR LDMEIDGQKL RDAFTWNMNE KLMTPEMFSE ILCDDLDLNP LTFVPAIASA
IRQQIESYPT DSILEDQSDQ RVIIKLNIHV GNISLVDQFE WDMSEKENSP EKFALKLCSE
LGLGGEFVTT IAYSIRGQLS WHQKTYAFSE NPLPTVEIAI RNTGDADQWC PLLETLTDAE
MEKKIRDQDR NTRRMRRLAN TAPAW
