ID   ACL6A_MOUSE             Reviewed;         429 AA.
AC   Q9Z2N8; Q8C1W3; Q99M56;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   19-SEP-2002, sequence version 2.
DT   24-JAN-2024, entry version 194.
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=BRG1-associated factor 53A;
DE            Short=BAF53A;
GN   Name=Actl6a; Synonyms=Actl6, Baf53a;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
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 [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryonic brain;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Mammary gland;
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   [4]
RP   FUNCTION, FUNCTION OF THE NBAF AND NPBAF COMPLEXES, IDENTIFICATION BY MASS
RP   SPECTROMETRY, IDENTIFICATION IN THE NPBAF COMPLEX, INTERACTION WITH PHF10,
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=17640523; DOI=10.1016/j.neuron.2007.06.019;
RA   Lessard J., Wu J.I., Ranish J.A., Wan M., Winslow M.M., Staahl B.T., Wu H.,
RA   Aebersold R., Graef I.A., Crabtree G.R.;
RT   "An essential switch in subunit composition of a chromatin remodeling
RT   complex during neural development.";
RL   Neuron 55:201-215(2007).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, Kidney, Lung, Spleen, and Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
RN   [6]
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   [7]
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   [8]
RP   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       (PubMed:17640523). Component of the NuA4 histone acetyltransferase
CC       (HAT) complex which is involved in transcriptional activation of select
CC       genes principally by acetylation of nucleosomal histones H4 and H2A.
CC       This modification may both alter nucleosome - DNA interactions and
CC       promote 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 (By similarity).
CC       {ECO:0000250|UniProtKB:O96019, ECO:0000269|PubMed:17640523,
CC       ECO:0000303|PubMed:22952240, 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       The NuA4 complex interacts with MYC and the adenovirus E1A protein.
CC       Component of a NuA4-related complex which contains EP400, TRRAP/PAF400,
CC       SRCAP, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, actin,
CC       ACTL6A/BAF53A, VPS72 and YEATS4/GAS41. 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. Component of the BAF complex,
CC       which includes at least actin (ACTB), ARID1A/BAF250A, ARID1B/BAF250B,
CC       SMARCA2/BRM, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B,
CC       SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and
CC       one or more SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In
CC       muscle cells, the BAF complex also contains DPF3 (Probable). Component
CC       of the BAF53 complex, at least composed of ACTL6A/BAF53A, RUVBL1/TIP49,
CC       SMARCA2/BRM/BAF190B and TRRAP/PAF400, and which may also include a HAT
CC       activity related to, but distinct from, that of KAT5. Component of
CC       neural progenitors-specific chromatin remodeling complex (npBAF
CC       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       SWI/SNF (GBAF) subcomplex, which includes at least BICRA or BICRAL
CC       (mutually 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 (By similarity). Interacts with
CC       SMARCA4/BRG1/BAF190A (By similarity). Interacts with PHF10/BAF45A
CC       (PubMed:17640523). Component of the chromatin remodeling INO80 complex;
CC       specifically part of a complex module associated with the DBINO domain
CC       of INO80 (By similarity). Interacts with DPF2 (By similarity).
CC       {ECO:0000250|UniProtKB:O96019, ECO:0000269|PubMed:17640523,
CC       ECO:0000269|PubMed:29374058, ECO:0000303|PubMed:22952240,
CC       ECO:0000303|PubMed:26601204}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:O96019}.
CC   -!- TISSUE SPECIFICITY: Widely expressed. Expressed selectively in neural
CC       stem and progenitor cells (at protein level).
CC       {ECO:0000269|PubMed:17640523}.
CC   -!- DEVELOPMENTAL STAGE: Expressed predominantly in 10.5 dpc-11.5 dpc
CC       neural cells. In the developing spinal cord (10.5 dpc-16.5 dpc), is
CC       specifically expressed in proliferating neural progenitors of the
CC       ventricular zone. In the developing forebrain and cerebellar
CC       primordium, expression is restricted to proliferating neuroepithelial
CC       progenitors and cerebellar granule precursors.
CC       {ECO:0000269|PubMed:17640523}.
CC   -!- SIMILARITY: Belongs to the actin family. {ECO:0000305}.
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DR   EMBL; AF041476; AAC94992.1; -; mRNA.
DR   EMBL; AK090154; BAC41116.1; -; mRNA.
DR   EMBL; BC001994; AAH01994.1; -; mRNA.
DR   CCDS; CCDS17298.1; -.
DR   RefSeq; NP_062647.2; NM_019673.2.
DR   AlphaFoldDB; Q9Z2N8; -.
DR   SMR; Q9Z2N8; -.
DR   BioGRID; 207995; 27.
DR   ComplexPortal; CPX-1232; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant.
DR   ComplexPortal; CPX-1233; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant.
DR   ComplexPortal; CPX-1234; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant.
DR   ComplexPortal; CPX-1235; SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant.
DR   ComplexPortal; CPX-1240; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA2 variant.
DR   ComplexPortal; CPX-1241; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1A-SMARCA4 variant.
DR   ComplexPortal; CPX-1242; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA2 variant.
DR   ComplexPortal; CPX-1243; Muscle cell-specific SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A-ARID1B-SMARCA4 variant.
DR   ComplexPortal; CPX-1248; Polybromo-associated SWI/SNF ATP-dependent chromatin remodeling complex, ACTL6A variant.
DR   ComplexPortal; CPX-1251; Embryonic stem cell-specific SWI/SNF ATP-dependent chromatin remodeling complex.
DR   ComplexPortal; CPX-1252; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA2 variant.
DR   ComplexPortal; CPX-1253; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1A-SMARCA4 variant.
DR   ComplexPortal; CPX-1254; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA2 variant.
DR   ComplexPortal; CPX-1255; Neural progenitor-specific SWI/SNF ATP-dependent chromatin remodeling complex, ARID1B-SMARCA4 variant.
DR   ComplexPortal; CPX-4202; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA2 variant.
DR   ComplexPortal; CPX-4204; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA2 variant.
DR   ComplexPortal; CPX-4221; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRA-SMARCA4 variant.
DR   ComplexPortal; CPX-4222; GBAF (SWI/SNF) ATP-dependent chromatin remodeling complex, ACTL6A-BICRAL-SMARCA4 variant.
DR   ComplexPortal; CPX-878; INO80 chromatin remodeling complex.
DR   ComplexPortal; CPX-976; SRCAP chromatin remodeling complex.
DR   ComplexPortal; CPX-990; NuA4 histone acetyltransferase complex.
DR   CORUM; Q9Z2N8; -.
DR   IntAct; Q9Z2N8; 12.
DR   MINT; Q9Z2N8; -.
DR   STRING; 10090.ENSMUSP00000029214; -.
DR   iPTMnet; Q9Z2N8; -.
DR   PhosphoSitePlus; Q9Z2N8; -.
DR   SwissPalm; Q9Z2N8; -.
DR   REPRODUCTION-2DPAGE; Q9Z2N8; -.
DR   EPD; Q9Z2N8; -.
DR   jPOST; Q9Z2N8; -.
DR   MaxQB; Q9Z2N8; -.
DR   PaxDb; 10090-ENSMUSP00000029214; -.
DR   ProteomicsDB; 285978; -.
DR   Pumba; Q9Z2N8; -.
DR   Antibodypedia; 33747; 428 antibodies from 39 providers.
DR   DNASU; 56456; -.
DR   Ensembl; ENSMUST00000029214.14; ENSMUSP00000029214.8; ENSMUSG00000027671.15.
DR   GeneID; 56456; -.
DR   KEGG; mmu:56456; -.
DR   UCSC; uc012coo.1; mouse.
DR   AGR; MGI:1861453; -.
DR   CTD; 86; -.
DR   MGI; MGI:1861453; Actl6a.
DR   VEuPathDB; HostDB:ENSMUSG00000027671; -.
DR   eggNOG; KOG0679; Eukaryota.
DR   GeneTree; ENSGT00940000156305; -.
DR   HOGENOM; CLU_027965_6_0_1; -.
DR   InParanoid; Q9Z2N8; -.
DR   OMA; MTEAPWN; -.
DR   OrthoDB; 5477470at2759; -.
DR   PhylomeDB; Q9Z2N8; -.
DR   TreeFam; TF312863; -.
DR   Reactome; R-MMU-3214858; RMTs methylate histone arginines.
DR   Reactome; R-MMU-5689603; UCH proteinases.
DR   Reactome; R-MMU-5696394; DNA Damage Recognition in GG-NER.
DR   Reactome; R-MMU-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR   BioGRID-ORCS; 56456; 36 hits in 117 CRISPR screens.
DR   ChiTaRS; Actl6a; mouse.
DR   PRO; PR:Q9Z2N8; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q9Z2N8; Protein.
DR   Bgee; ENSMUSG00000027671; Expressed in urogenital fold and 289 other cell types or tissues.
DR   ExpressionAtlas; Q9Z2N8; baseline and differential.
DR   GO; GO:0035060; C:brahma complex; NAS:ComplexPortal.
DR   GO; GO:0000785; C:chromatin; NAS:ComplexPortal.
DR   GO; GO:0140288; C:GBAF complex; NAS:ComplexPortal.
DR   GO; GO:0031011; C:Ino80 complex; ISO:MGI.
DR   GO; GO:0000776; C:kinetochore; NAS:ComplexPortal.
DR   GO; GO:0071564; C:npBAF complex; IDA:UniProtKB.
DR   GO; GO:0035267; C:NuA4 histone acetyltransferase complex; ISS:UniProtKB.
DR   GO; GO:0016363; C:nuclear matrix; NAS:ComplexPortal.
DR   GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR   GO; GO:0000786; C:nucleosome; ISO:MGI.
DR   GO; GO:0005634; C:nucleus; IDA:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
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; IDA:MGI.
DR   GO; GO:0001825; P:blastocyst formation; IMP:MGI.
DR   GO; GO:0006338; P:chromatin remodeling; IDA:MGI.
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; IMP:UniProtKB.
DR   GO; GO:0003407; P:neural retina development; IEA:Ensembl.
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; IDA:ComplexPortal.
DR   GO; GO:0045893; P:positive regulation of DNA-templated transcription; ISO:MGI.
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; ISO:MGI.
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; IMP:ComplexPortal.
DR   GO; GO:0042981; P:regulation of apoptotic process; NAS:ComplexPortal.
DR   GO; GO:0051726; P:regulation of cell cycle; ISO:MGI.
DR   GO; GO:0033044; P:regulation of chromosome organization; ISO:MGI.
DR   GO; GO:0006282; P:regulation of DNA repair; IDA:ComplexPortal.
DR   GO; GO:0006275; P:regulation of DNA replication; ISO:MGI.
DR   GO; GO:0060382; P:regulation of DNA strand elongation; ISO:MGI.
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; IMP: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:0021510; P:spinal cord development; IEA:Ensembl.
DR   GO; GO:0000723; P:telomere maintenance; IMP: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; Q9Z2N8; MM.
PE   1: Evidence at protein level;
KW   Acetylation; Activator; Chromatin regulator; DNA damage; DNA recombination;
KW   DNA repair; Growth regulation; Isopeptide bond; Neurogenesis; Nucleus;
KW   Phosphoprotein; Reference proteome; Transcription;
KW   Transcription regulation; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250|UniProtKB:O96019"
FT   CHAIN           2..429
FT                   /note="Actin-like protein 6A"
FT                   /id="PRO_0000089134"
FT   MOD_RES         2
FT                   /note="N-acetylserine"
FT                   /evidence="ECO:0000250|UniProtKB:O96019"
FT   MOD_RES         86
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O96019"
FT   MOD_RES         233
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:O96019"
FT   CROSSLNK        62
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:O96019"
FT   CONFLICT        38
FT                   /note="P -> H (in Ref. 2; BAC41116)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        153
FT                   /note="K -> Q (in Ref. 2; BAC41116)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        322
FT                   /note="M -> I (in Ref. 1; AAC94992)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   429 AA;  47448 MW;  F3FF706C69808B13 CRC64;
     MSGGVYGGDE VGALVFDIGS YTVRAGYAGE DCPKVDFPTA IGVVLERDDG STMMEIDGDK
     GKQGGPTYYI DTNALRVPRE NMEAISPLKN GMVEDWDSFQ AILDHTYKMH VKSEASLHPV
     LMSEAPWNTR AKREKLTELM FEHYSIPAFF LCKTAVLTAF ANGRSTGLIL DSGATHTTAI
     PVHDGYVLQQ GIVKSPLAGD FITMQCRELF QEMNIELIPP YMIASKEAVR EGSPANWKRK
     EKLPQVTRSW HNYMCNCVIQ DFQASVLQVS DSTYDEQVAA QMPTVHYEFP NGYNCDFGAE
     RLKIPEGLFD PSNVKGLSGN TMLGVSHVVT TSVGMCDIDI RPGLYGSVIV AGGNTLIQSF
     TDRLNRELSQ KTPPSMRLKL IANNTTVERR FSSWIGGSIL ASLGTFQQMW ISKQEYEEGG
     KQCVERKCP
//