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 27-MAR-2024, entry version 223. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 PDB; 7VDV; EM; 3.40 A; N=1-429. DR PDB; 7Y8R; EM; 4.40 A; K=1-429. DR PDBsum; 6LTJ; -. DR PDBsum; 7VDV; -. DR PDBsum; 7Y8R; -. DR AlphaFoldDB; O96019; -. DR EMDB; EMD-0974; -. DR EMDB; EMD-31926; -. DR EMDB; EMD-33684; -. DR SMR; O96019; -. DR BioGRID; 106601; 277. 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; 103. DR MINT; O96019; -. DR STRING; 9606.ENSP00000397552; -. DR GlyGen; O96019; 2 sites, 1 O-linked glycan (2 sites). 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; 9606-ENSP00000397552; -. DR PeptideAtlas; O96019; -. DR ProteomicsDB; 51211; -. [O96019-1] DR ProteomicsDB; 51212; -. [O96019-2] DR Pumba; O96019; -. DR TopDownProteomics; O96019-1; -. [O96019-1] DR Antibodypedia; 33747; 428 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 AGR; HGNC:24124; -. 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; MTEAPWN; -. DR OrthoDB; 5477470at2759; -. 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; 802 hits in 1148 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 primordial germ cell in gonad and 188 other cell types or tissues. DR ExpressionAtlas; O96019; baseline and differential. DR GO; GO:0035060; C:brahma complex; NAS:ComplexPortal. DR GO; GO:0000785; C:chromatin; HDA:UniProtKB. DR GO; GO:0140288; C:GBAF complex; NAS:ComplexPortal. DR GO; GO:0031011; C:Ino80 complex; IDA:UniProtKB. DR GO; GO:0000776; C:kinetochore; NAS: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; NAS: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; NAS: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:0045596; P:negative regulation of cell differentiation; NAS: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; NAS:ComplexPortal. DR GO; GO:0008284; P:positive regulation of cell population proliferation; NAS:ComplexPortal. DR GO; GO:0045739; P:positive regulation of DNA repair; ISO:ComplexPortal. DR GO; GO:0045893; P:positive regulation of DNA-templated transcription; IMP:ComplexPortal. DR GO; GO:2000781; P:positive regulation of double-strand break repair; NAS: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; NAS:ComplexPortal. DR GO; GO:1902459; P:positive regulation of stem cell population maintenance; NAS:ComplexPortal. DR GO; GO:0045582; P:positive regulation of T cell differentiation; NAS:ComplexPortal. DR GO; GO:1904507; P:positive regulation of telomere maintenance in response to DNA damage; ISO:ComplexPortal. DR GO; GO:0042981; P:regulation of apoptotic process; NAS: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:0006282; P:regulation of DNA repair; ISO: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:0006355; P:regulation of DNA-templated transcription; NAS:ComplexPortal. DR GO; GO:2000779; P:regulation of double-strand break repair; NAS:ComplexPortal. DR GO; GO:0045995; P:regulation of embryonic development; ISO:ComplexPortal. DR GO; GO:0070316; P:regulation of G0 to G1 transition; NAS:ComplexPortal. DR GO; GO:2000045; P:regulation of G1/S transition of mitotic cell cycle; NAS:ComplexPortal. DR GO; GO:0030071; P:regulation of mitotic metaphase/anaphase transition; NAS:ComplexPortal. DR GO; GO:2000819; P:regulation of nucleotide-excision repair; NAS:ComplexPortal. DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central. 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; ISO:ComplexPortal. DR CDD; cd00012; NBD_sugar-kinase_HSP70_actin; 1. DR Gene3D; 3.30.420.40; -; 2. DR InterPro; IPR004000; Actin. DR InterPro; IPR004001; Actin_CS. DR InterPro; IPR043129; ATPase_NBD. DR PANTHER; PTHR11937; ACTIN; 1. DR PANTHER; PTHR11937:SF487; ACTIN-LIKE PROTEIN 6A; 1. DR Pfam; PF00022; Actin; 1. DR PRINTS; PR00190; ACTIN. DR SMART; SM00268; ACTIN; 1. DR SUPFAM; SSF53067; Actin-like ATPase domain; 2. DR PROSITE; PS00432; ACTINS_2; 1. DR Genevisible; O96019; HS. 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 uncertain significance; dbSNP:rs1035631360)" FT /evidence="ECO:0000269|PubMed:28649782" FT /id="VAR_079728" FT VARIANT 377 FT /note="R -> W (found in a patient with developmental delay, FT speech and learning difficulties, dysmorphic features and FT abnormal digits; likely pathogenic; 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" FT STRAND 14..18 FT /evidence="ECO:0007829|PDB:7VDV" FT STRAND 20..29 FT /evidence="ECO:0007829|PDB:7VDV" FT STRAND 34..39 FT /evidence="ECO:0007829|PDB:7VDV" FT STRAND 41..43 FT /evidence="ECO:0007829|PDB:7VDV" FT HELIX 73..76 FT /evidence="ECO:0007829|PDB:7VDV" FT STRAND 83..85 FT /evidence="ECO:0007829|PDB:7VDV" FT STRAND 87..89 FT /evidence="ECO:0007829|PDB:7VDV" FT HELIX 96..109 FT /evidence="ECO:0007829|PDB:7VDV" FT HELIX 130..142 FT /evidence="ECO:0007829|PDB:7VDV" FT HELIX 154..161 FT /evidence="ECO:0007829|PDB:7VDV" FT STRAND 165..172 FT /evidence="ECO:0007829|PDB:7VDV" FT STRAND 177..183 FT /evidence="ECO:0007829|PDB:7VDV" FT STRAND 193..196 FT /evidence="ECO:0007829|PDB:7VDV" FT HELIX 199..212 FT /evidence="ECO:0007829|PDB:7VDV" FT HELIX 248..265 FT /evidence="ECO:0007829|PDB:7VDV" FT HELIX 300..302 FT /evidence="ECO:0007829|PDB:7VDV" FT HELIX 304..309 FT /evidence="ECO:0007829|PDB:7VDV" FT HELIX 325..334 FT /evidence="ECO:0007829|PDB:7VDV" FT HELIX 341..346 FT /evidence="ECO:0007829|PDB:7VDV" FT STRAND 347..352 FT /evidence="ECO:0007829|PDB:7VDV" FT HELIX 353..356 FT /evidence="ECO:0007829|PDB:7VDV" FT HELIX 361..370 FT /evidence="ECO:0007829|PDB:7VDV" FT HELIX 387..389 FT /evidence="ECO:0007829|PDB:7VDV" FT HELIX 392..400 FT /evidence="ECO:0007829|PDB:7VDV" FT HELIX 405..408 FT /evidence="ECO:0007829|PDB:7VDV" FT STRAND 409..411 FT /evidence="ECO:0007829|PDB:7VDV" 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 //