ACL6A_HUMAN
ID ACL6A_HUMAN Reviewed; 429 AA.
AC O96019; B3KMN1; D3DNR9; Q8TAE5; Q9BVS8; Q9H0W6;
DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 214.
DE RecName: Full=Actin-like protein 6A;
DE AltName: Full=53 kDa BRG1-associated factor A;
DE AltName: Full=Actin-related protein Baf53a;
DE AltName: Full=ArpNbeta;
DE AltName: Full=BRG1-associated factor 53A;
DE Short=BAF53A;
DE AltName: Full=INO80 complex subunit K;
GN Name=ACTL6A; Synonyms=BAF53, BAF53A, INO80K;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, AND
RP IDENTIFICATION IN BAF COMPLEX.
RX PubMed=9845365; DOI=10.1016/s0092-8674(00)81633-5;
RA Zhao K., Wang W., Rando O.J., Xue Y., Swiderek K., Kuo A., Crabtree G.R.;
RT "Rapid and phosphoinositol-dependent binding of the SWI/SNF-like BAF
RT complex to chromatin after T lymphocyte receptor signaling.";
RL Cell 95:625-636(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10380635; DOI=10.1271/bbb.63.917;
RA Harata M., Mochizuki R., Mizuno S.;
RT "Two isoforms of a human actin-related protein show nuclear localization
RT and mutually selective expression between brain and other tissues.";
RL Biosci. Biotechnol. Biochem. 63:917-923(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Harata M., Ohfuchi E.;
RT "Characterization of an alternative splicing product of hArpNbeta/BAF53.";
RL Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Placenta, Skin, 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 PROTEIN SEQUENCE OF 2-24; 63-76; 113-130; 195-207 AND 380-389, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V.;
RL Submitted (JAN-2010) to UniProtKB.
RN [9]
RP PROTEIN SEQUENCE OF 35-60; 63-76; 113-130; 154-164; 195-207; 304-315 AND
RP 380-389, IDENTIFICATION IN NUA4 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=12963728; DOI=10.1074/jbc.c300389200;
RA Cai Y., Jin J., Tomomori-Sato C., Sato S., Sorokina I., Parmely T.J.,
RA Conaway R.C., Conaway J.W.;
RT "Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-
RT containing histone acetyltransferase complex.";
RL J. Biol. Chem. 278:42733-42736(2003).
RN [10]
RP IDENTIFICATION IN NUA4 COMPLEX, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=10966108; DOI=10.1016/s0092-8674(00)00051-9;
RA Ikura T., Ogryzko V.V., Grigoriev M., Groisman R., Wang J., Horikoshi M.,
RA Scully R., Qin J., Nakatani Y.;
RT "Involvement of the TIP60 histone acetylase complex in DNA repair and
RT apoptosis.";
RL Cell 102:463-473(2000).
RN [11]
RP IDENTIFICATION IN NUA4-LIKE COMPLEX.
RX PubMed=11509179; DOI=10.1016/s0092-8674(01)00450-0;
RA Fuchs M., Gerber J., Drapkin R., Sif S., Ikura T., Ogryzko V., Lane W.S.,
RA Nakatani Y., Livingston D.M.;
RT "The p400 complex is an essential E1A transformation target.";
RL Cell 106:297-307(2001).
RN [12]
RP IDENTIFICATION IN THE BAF53 COMPLEX WITH RUVBL1; SMARCA2 AND TRRAP.
RX PubMed=11839798; DOI=10.1128/mcb.22.5.1307-1316.2002;
RA Park J., Wood M.A., Cole M.D.;
RT "BAF53 forms distinct nuclear complexes and functions as a critical c-Myc-
RT interacting nuclear cofactor for oncogenic transformation.";
RL Mol. Cell. Biol. 22:1307-1316(2002).
RN [13]
RP REVIEW ON NUA4 COMPLEX.
RX PubMed=15196461; DOI=10.1016/j.gde.2004.02.009;
RA Doyon Y., Cote J.;
RT "The highly conserved and multifunctional NuA4 HAT complex.";
RL Curr. Opin. Genet. Dev. 14:147-154(2004).
RN [14]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN NUA4
RP COMPLEX, AND IDENTIFICATION IN A NUA4-RELATED SRCAP-CONTAINING COMPLEX.
RX PubMed=14966270; DOI=10.1128/mcb.24.5.1884-1896.2004;
RA Doyon Y., Selleck W., Lane W.S., Tan S., Cote J.;
RT "Structural and functional conservation of the NuA4 histone
RT acetyltransferase complex from yeast to humans.";
RL Mol. Cell. Biol. 24:1884-1896(2004).
RN [15]
RP IDENTIFICATION IN THE INO80 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16230350; DOI=10.1074/jbc.m509128200;
RA Jin J., Cai Y., Yao T., Gottschalk A.J., Florens L., Swanson S.K.,
RA Gutierrez J.L., Coleman M.K., Workman J.L., Mushegian A., Washburn M.P.,
RA Conaway R.C., Conaway J.W.;
RT "A mammalian chromatin remodeling complex with similarities to the yeast
RT INO80 complex.";
RL J. Biol. Chem. 280:41207-41212(2005).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [17]
RP SUBCELLULAR LOCATION, AND ASSOCIATION WITH THE INO80 COMPLEX.
RX PubMed=18026119; DOI=10.1038/nsmb1332;
RA Wu S., Shi Y., Mulligan P., Gay F., Landry J., Liu H., Lu J., Qi H.H.,
RA Wang W., Nickoloff J.A., Wu C., Shi Y.;
RT "A YY1-INO80 complex regulates genomic stability through homologous
RT recombination-based repair.";
RL Nat. Struct. Mol. Biol. 14:1165-1172(2007).
RN [18]
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 [19]
RP IDENTIFICATION IN THE INO80 COMPLEX, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=18922472; DOI=10.1016/j.molcel.2008.08.027;
RA Yao T., Song L., Jin J., Cai Y., Takahashi H., Swanson S.K., Washburn M.P.,
RA Florens L., Conaway R.C., Cohen R.E., Conaway J.W.;
RT "Distinct modes of regulation of the Uch37 deubiquitinating enzyme in the
RT proteasome and in the Ino80 chromatin-remodeling complex.";
RL Mol. Cell 31:909-917(2008).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233, AND IDENTIFICATION BY
RP 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 [21]
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 [22]
RP IDENTIFICATION IN THE INO80 COMPLEX.
RX PubMed=21303910; DOI=10.1074/jbc.m111.222505;
RA Chen L., Cai Y., Jin J., Florens L., Swanson S.K., Washburn M.P.,
RA Conaway J.W., Conaway R.C.;
RT "Subunit organization of the human INO80 chromatin remodeling complex: An
RT evolutionarily conserved core complex catalyzes ATP-dependent nucleosome
RT remodeling.";
RL J. Biol. Chem. 286:11283-11289(2011).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-86 AND SER-233, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [25]
RP INTERACTION WITH SMARCA4, POSSIBLE INVOLVEMENT IN SYNDROMIC INTELLECTUAL
RP DISABILITY, AND VARIANTS GLN-227 AND TRP-377.
RX PubMed=28649782; DOI=10.1002/humu.23282;
RA Marom R., Jain M., Burrage L.C., Song I.W., Graham B.H., Brown C.W.,
RA Stevens S.J.C., Stegmann A.P.A., Gunter A.T., Kaplan J.D., Gavrilova R.H.,
RA Shinawi M., Rosenfeld J.A., Bae Y., Tran A.A., Chen Y., Lu J.T.,
RA Gibbs R.A., Eng C., Yang Y., Rousseau J., de Vries B.B.A., Campeau P.M.,
RA Lee B.;
RT "Heterozygous variants in ACTL6A, encoding a component of the BAF complex,
RT are associated with intellectual disability.";
RL Hum. Mutat. 38:1365-1371(2017).
RN [26]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-62, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [27]
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 [28]
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 [29]
RP INTERACTION WITH DPF2.
RX PubMed=28533407; DOI=10.1073/pnas.1700328114;
RA Huber F.M., Greenblatt S.M., Davenport A.M., Martinez C., Xu Y., Vu L.P.,
RA Nimer S.D., Hoelz A.;
RT "Histone-binding of DPF2 mediates its repressive role in myeloid
RT differentiation.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:6016-6021(2017).
RN [30]
RP FUNCTION, AND IDENTIFICATION IN THE GBAF COMPLEX.
RX PubMed=29374058; DOI=10.1074/jbc.ra117.001065;
RA Alpsoy A., Dykhuizen E.C.;
RT "Glioma tumor suppressor candidate region gene 1 (GLTSCR1) and its paralog
RT GLTSCR1-like form SWI/SNF chromatin remodeling subcomplexes.";
RL J. Biol. Chem. 293:3892-3903(2018).
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. Required for maximal ATPase activity of SMARCA4/BRG1/BAF190A
CC and for association of the SMARCA4/BRG1/BAF190A containing remodeling
CC complex BAF with chromatin/nuclear matrix. Belongs to the neural
CC progenitors-specific chromatin remodeling complex (npBAF complex) and
CC is required for the proliferation of neural progenitors. During neural
CC development a switch from a stem/progenitor to a postmitotic chromatin
CC remodeling mechanism occurs as neurons exit the cell cycle and become
CC committed to their adult state. The transition from proliferating
CC neural stem/progenitor cells to postmitotic neurons requires a switch
CC in subunit composition of the npBAF and nBAF complexes. As neural
CC progenitors exit mitosis and differentiate into neurons, npBAF
CC complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged
CC for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C
CC subunits in neuron-specific complexes (nBAF). The npBAF complex is
CC 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). Component of the NuA4 histone acetyltransferase (HAT)
CC complex which is involved in transcriptional activation of select genes
CC principally by acetylation of nucleosomal histones H4 and H2A. This
CC modification may both alter nucleosome - DNA interactions and promote
CC interaction of the modified histones with other proteins which
CC positively regulate transcription. This complex may be required for the
CC activation of transcriptional programs associated with oncogene and
CC proto-oncogene mediated growth induction, tumor suppressor mediated
CC growth arrest and replicative senescence, apoptosis, and DNA repair.
CC NuA4 may also play a direct role in DNA repair when recruited to sites
CC of DNA damage. Putative core component of the chromatin remodeling
CC INO80 complex which is involved in transcriptional regulation, DNA
CC replication and probably DNA repair. {ECO:0000250|UniProtKB:Q9Z2N8,
CC ECO:0000269|PubMed:14966270, ECO:0000269|PubMed:29374058,
CC ECO:0000303|PubMed:15196461, ECO:0000303|PubMed:22952240,
CC ECO:0000303|PubMed:26601204}.
CC -!- SUBUNIT: Component of numerous complexes with chromatin remodeling and
CC histone acetyltransferase activity. Component of the NuA4 histone
CC acetyltransferase complex which contains the catalytic subunit
CC KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1,
CC DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A,
CC MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6
CC (PubMed:12963728, PubMed:10966108, PubMed:15196461, PubMed:14966270).
CC The NuA4 complex interacts with MYC and the adenovirus E1A protein
CC (PubMed:11509179). Component of a NuA4-related complex which contains
CC EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP, EPC1, DMAP1/DNMAP1,
CC RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A, VPS72 and YEATS4/GAS41
CC (PubMed:11509179, PubMed:14966270). Component of the multiprotein
CC chromatin-remodeling complexes SWI/SNF: SWI/SNF-A (BAF), SWI/SNF-B
CC (PBAF) and related complexes. The canonical complex contains a
CC catalytic subunit (either SMARCA4/BRG1/BAF190A or SMARCA2/BRM/BAF190B)
CC and at least SMARCE1, ACTL6A/BAF53, SMARCC1/BAF155, SMARCC2/BAF170, and
CC SMARCB1/SNF5/BAF47. Other subunits specific to each of the complexes
CC may also be present permitting several possible combinations
CC developmentally and tissue specific (Probable). Component of the BAF
CC complex, which includes at least actin (ACTB), ARID1A/BAF250A,
CC ARID1B/BAF250B, SMARCA2/BRM, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53,
CC ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170,
CC SMARCB1/SNF5/INI1, and one or more SMARCD1/BAF60A, SMARCD2/BAF60B, or
CC SMARCD3/BAF60C (PubMed:9845365, PubMed:18765789). In muscle cells, the
CC BAF complex also contains DPF3. Component of the BAF53 complex, at
CC least composed of ACTL6A/BAF53A, RUVBL1/TIP49, SMARCA2/BRM/BAF190B and
CC TRRAP/PAF400, and which may also include a HAT activity related to, but
CC distinct from, that of KAT5 (PubMed:11839798). 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 SWI/SNF (GBAF)
CC subcomplex, which includes at least BICRA or BICRAL (mutually
CC exclusive), BRD9, SS18, SMARCA2/BRM, SMARCA4/BRG1/BAF190A,
CC ACTL6A/BAF53, SMARCC1/BAF155, and SMARCD1/BAF60A (PubMed:29374058). May
CC be a 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). Interacts with
CC SMARCA4/BRG1/BAF190A (PubMed:28649782). Interacts with PHF10/BAF45A (By
CC similarity). Component of the chromatin remodeling INO80 complex;
CC specifically part of a complex module associated with the DBINO domain
CC of INO80 (PubMed:16230350, PubMed:18026119, PubMed:18922472,
CC PubMed:21303910). Interacts with DPF2 (PubMed:28533407).
CC {ECO:0000250|UniProtKB:Q9Z2N8, ECO:0000269|PubMed:10966108,
CC ECO:0000269|PubMed:11509179, ECO:0000269|PubMed:11839798,
CC ECO:0000269|PubMed:12963728, ECO:0000269|PubMed:14966270,
CC ECO:0000269|PubMed:16230350, ECO:0000269|PubMed:18026119,
CC ECO:0000269|PubMed:18765789, ECO:0000269|PubMed:18922472,
CC ECO:0000269|PubMed:21303910, ECO:0000269|PubMed:28533407,
CC ECO:0000269|PubMed:28649782, ECO:0000269|PubMed:29374058,
CC ECO:0000269|PubMed:9845365, ECO:0000303|PubMed:15196461,
CC ECO:0000303|PubMed:22952240, ECO:0000303|PubMed:26601204}.
CC -!- INTERACTION:
CC O96019; P25490: YY1; NbExp=7; IntAct=EBI-355018, EBI-765538;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18026119}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O96019-1; Sequence=Displayed;
CC Name=2; Synonyms=HArpNbeta-s;
CC IsoId=O96019-2; Sequence=VSP_000150;
CC -!- DISEASE: Note=ACTL6A mutations have been found in patients with
CC intellectual disability of variable severity, developmental delay,
CC dysmorphic features and digit abnormalities. Additional features may
CC include genitourinary and cardiac defects. The disease phenotype
CC resembles Coffin-Siris syndrome and brachymorphism-onychodysplasia-
CC dysphalangism syndrome. {ECO:0000269|PubMed:28649782}.
CC -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR EMBL; AF041474; AAC94991.1; -; mRNA.
DR EMBL; AB015907; BAA74577.1; -; mRNA.
DR EMBL; AB060168; BAB87844.1; -; mRNA.
DR EMBL; AB061315; BAB87848.1; -; mRNA.
DR EMBL; AL136608; CAB66543.1; -; mRNA.
DR EMBL; AK021756; BAG51043.1; -; mRNA.
DR EMBL; CH471052; EAW78401.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78397.1; -; Genomic_DNA.
DR EMBL; CH471052; EAW78399.1; -; Genomic_DNA.
DR EMBL; BC000949; AAH00949.1; -; mRNA.
DR EMBL; BC001391; AAH01391.1; -; mRNA.
DR EMBL; BC036371; AAH36371.1; -; mRNA.
DR CCDS; CCDS3231.1; -. [O96019-1]
DR CCDS; CCDS43174.1; -. [O96019-2]
DR RefSeq; NP_004292.1; NM_004301.4. [O96019-1]
DR RefSeq; NP_817126.1; NM_177989.3. [O96019-2]
DR RefSeq; NP_829888.1; NM_178042.3. [O96019-2]
DR PDB; 6LTJ; EM; 3.70 A; J=12-417.
DR PDBsum; 6LTJ; -.
DR AlphaFoldDB; O96019; -.
DR SMR; O96019; -.
DR BioGRID; 106601; 213.
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-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-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-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-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-4084; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA2 variant.
DR ComplexPortal; CPX-4203; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA2 variant.
DR ComplexPortal; CPX-4206; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA4 variant.
DR ComplexPortal; CPX-4207; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA4 variant.
DR ComplexPortal; CPX-846; INO80 chromatin remodeling complex.
DR ComplexPortal; CPX-974; SRCAP chromatin remodeling complex.
DR ComplexPortal; CPX-978; NuA4 histone acetyltransferase complex.
DR CORUM; O96019; -.
DR DIP; DIP-27565N; -.
DR IntAct; O96019; 101.
DR MINT; O96019; -.
DR STRING; 9606.ENSP00000397552; -.
DR GlyGen; O96019; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O96019; -.
DR MetOSite; O96019; -.
DR PhosphoSitePlus; O96019; -.
DR SwissPalm; O96019; -.
DR BioMuta; ACTL6A; -.
DR EPD; O96019; -.
DR jPOST; O96019; -.
DR MassIVE; O96019; -.
DR MaxQB; O96019; -.
DR PaxDb; O96019; -.
DR PeptideAtlas; O96019; -.
DR PRIDE; O96019; -.
DR ProteomicsDB; 51211; -. [O96019-1]
DR ProteomicsDB; 51212; -. [O96019-2]
DR TopDownProteomics; O96019-1; -. [O96019-1]
DR Antibodypedia; 33747; 388 antibodies from 39 providers.
DR DNASU; 86; -.
DR Ensembl; ENST00000392662.5; ENSP00000376430.1; ENSG00000136518.17. [O96019-2]
DR Ensembl; ENST00000429709.7; ENSP00000397552.2; ENSG00000136518.17. [O96019-1]
DR Ensembl; ENST00000450518.6; ENSP00000394014.2; ENSG00000136518.17. [O96019-2]
DR GeneID; 86; -.
DR KEGG; hsa:86; -.
DR MANE-Select; ENST00000429709.7; ENSP00000397552.2; NM_004301.5; NP_004292.1.
DR UCSC; uc003fjw.4; human. [O96019-1]
DR CTD; 86; -.
DR DisGeNET; 86; -.
DR GeneCards; ACTL6A; -.
DR HGNC; HGNC:24124; ACTL6A.
DR HPA; ENSG00000136518; Low tissue specificity.
DR MalaCards; ACTL6A; -.
DR MIM; 604958; gene.
DR neXtProt; NX_O96019; -.
DR OpenTargets; ENSG00000136518; -.
DR Orphanet; 528084; Non-specific syndromic intellectual disability.
DR PharmGKB; PA134914203; -.
DR VEuPathDB; HostDB:ENSG00000136518; -.
DR eggNOG; KOG0679; Eukaryota.
DR GeneTree; ENSGT00940000156305; -.
DR HOGENOM; CLU_027965_6_0_1; -.
DR InParanoid; O96019; -.
DR OMA; GIVEKRC; -.
DR OrthoDB; 649708at2759; -.
DR PhylomeDB; O96019; -.
DR TreeFam; TF312863; -.
DR PathwayCommons; O96019; -.
DR Reactome; R-HSA-3214847; HATs acetylate histones.
DR Reactome; R-HSA-3214858; RMTs methylate histone arginines.
DR Reactome; R-HSA-5689603; UCH proteinases.
DR Reactome; R-HSA-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-HSA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR SignaLink; O96019; -.
DR SIGNOR; O96019; -.
DR BioGRID-ORCS; 86; 768 hits in 1066 CRISPR screens.
DR ChiTaRS; ACTL6A; human.
DR GeneWiki; ACTL6A; -.
DR GenomeRNAi; 86; -.
DR Pharos; O96019; Tbio.
DR PRO; PR:O96019; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; O96019; protein.
DR Bgee; ENSG00000136518; Expressed in calcaneal tendon and 186 other tissues.
DR ExpressionAtlas; O96019; baseline and differential.
DR Genevisible; O96019; HS.
DR GO; GO:0035060; C:brahma complex; IC:ComplexPortal.
DR GO; GO:0000785; C:chromatin; HDA:UniProtKB.
DR GO; GO:0140288; C:GBAF complex; IC:ComplexPortal.
DR GO; GO:0031011; C:Ino80 complex; IDA:UniProtKB.
DR GO; GO:0000776; C:kinetochore; IC:ComplexPortal.
DR GO; GO:0071564; C:npBAF complex; IDA:BHF-UCL.
DR GO; GO:0035267; C:NuA4 histone acetyltransferase complex; IDA:UniProtKB.
DR GO; GO:0016363; C:nuclear matrix; IC:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000786; C:nucleosome; IDA:ComplexPortal.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; 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; IBA:GO_Central.
DR GO; GO:0003713; F:transcription coactivator activity; NAS:BHF-UCL.
DR GO; GO:0001825; P:blastocyst formation; IEA:Ensembl.
DR GO; GO:0006338; P:chromatin remodeling; IDA:BHF-UCL.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0016573; P:histone acetylation; IC:ComplexPortal.
DR GO; GO:0043486; P:histone exchange; IC:ComplexPortal.
DR GO; GO:0043968; P:histone H2A acetylation; IDA:UniProtKB.
DR GO; GO:0043967; P:histone H4 acetylation; IDA:UniProtKB.
DR GO; GO:0045596; P:negative regulation of cell differentiation; IC:ComplexPortal.
DR GO; GO:0007399; P:nervous system development; IBA:GO_Central.
DR GO; GO:0003407; P:neural retina development; IEP:BHF-UCL.
DR GO; GO:0045597; P:positive regulation of cell differentiation; IC:ComplexPortal.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; IC:ComplexPortal.
DR GO; GO:2000781; P:positive regulation of double-strand break repair; IC:ComplexPortal.
DR GO; GO:1905168; P:positive regulation of double-strand break repair via homologous recombination; IDA: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:1904507; P:positive regulation of telomere maintenance in response to DNA damage; IEA:Ensembl.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IMP:ComplexPortal.
DR GO; GO:0042981; P:regulation of apoptotic process; IC:ComplexPortal.
DR GO; GO:0051726; P:regulation of cell cycle; IMP:ComplexPortal.
DR GO; GO:0033044; P:regulation of chromosome organization; IMP:ComplexPortal.
DR GO; GO:0006275; P:regulation of DNA replication; IMP:ComplexPortal.
DR GO; GO:0060382; P:regulation of DNA strand elongation; IMP:ComplexPortal.
DR GO; GO:2000779; P:regulation of double-strand break repair; IC:ComplexPortal.
DR GO; GO:0045995; P:regulation of embryonic development; IEA:Ensembl.
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:0040008; P:regulation of growth; IEA:UniProtKB-KW.
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:0006355; P:regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR GO; GO:0021510; P:spinal cord development; IEA:Ensembl.
DR GO; GO:0000723; P:telomere maintenance; IEA:Ensembl.
DR InterPro; IPR004000; Actin.
DR InterPro; IPR004001; Actin_CS.
DR InterPro; IPR043129; ATPase_NBD.
DR PANTHER; PTHR11937; PTHR11937; 1.
DR Pfam; PF00022; Actin; 1.
DR PRINTS; PR00190; ACTIN.
DR SMART; SM00268; ACTIN; 1.
DR SUPFAM; SSF53067; SSF53067; 2.
DR PROSITE; PS00432; ACTINS_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing;
KW Chromatin regulator; Direct protein sequencing; Disease variant;
KW DNA damage; DNA recombination; DNA repair; Growth regulation;
KW Intellectual disability; Isopeptide bond; Neurogenesis; Nucleus;
KW Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:22814378"
FT CHAIN 2..429
FT /note="Actin-like protein 6A"
FT /id="PRO_0000089133"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.8, ECO:0007744|PubMed:22814378"
FT MOD_RES 86
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT CROSSLNK 62
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..42
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_000150"
FT VARIANT 227
FT /note="E -> Q (found in a patient with developmental delay,
FT speech difficulties, attention deficit hyperactivity
FT disorder, behavioral problems and dysmorphic features;
FT unknown pathological significance; dbSNP:rs1035631360)"
FT /evidence="ECO:0000269|PubMed:28649782"
FT /id="VAR_079728"
FT VARIANT 377
FT /note="R -> W (probable disease-associated variant found in
FT a patient with developmental delay, speech and learning
FT difficulties, dysmorphic features and abnormal digits;
FT dbSNP:rs868064163)"
FT /evidence="ECO:0000269|PubMed:28649782"
FT /id="VAR_079729"
FT CONFLICT 92
FT /note="M -> T (in Ref. 4; CAB66543)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="F -> L (in Ref. 4; CAB66543)"
FT /evidence="ECO:0000305"
FT CONFLICT 254
FT /note="M -> T (in Ref. 4; CAB66543)"
FT /evidence="ECO:0000305"
FT CONFLICT 320
FT /note="N -> K (in Ref. 4; CAB66543)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 429 AA; 47461 MW; ECD92D29BD1854E0 CRC64;
MSGGVYGGDE VGALVFDIGS YTVRAGYAGE DCPKVDFPTA IGMVVERDDG STLMEIDGDK
GKQGGPTYYI DTNALRVPRE NMEAISPLKN GMVEDWDSFQ AILDHTYKMH VKSEASLHPV
LMSEAPWNTR AKREKLTELM FEHYNIPAFF LCKTAVLTAF ANGRSTGLIL DSGATHTTAI
PVHDGYVLQQ GIVKSPLAGD FITMQCRELF QEMNIELVPP YMIASKEAVR EGSPANWKRK
EKLPQVTRSW HNYMCNCVIQ DFQASVLQVS DSTYDEQVAA QMPTVHYEFP NGYNCDFGAE
RLKIPEGLFD PSNVKGLSGN TMLGVSHVVT TSVGMCDIDI RPGLYGSVIV AGGNTLIQSF
TDRLNRELSQ KTPPSMRLKL IANNTTVERR FSSWIGGSIL ASLGTFQQMW ISKQEYEEGG
KQCVERKCP
