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Protein

Actin-like protein 6A

Gene

Actl6a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in transcriptional activation and repression of select genes by chromatin remodeling (alteration of DNA-nucleosome topology). Required for maximal ATPase activity of SMARCA4/BRG1/BAF190A and for association of the SMARCA4/BRG1/BAF190A containing remodeling complex BAF with chromatin/nuclear matrix. Component of the NuA4 histone acetyltransferase (HAT) complex which is involved in transcriptional activation of select genes principally by acetylation of nucleosomal histones H4 and H2A. This modification may both alter nucleosome - DNA interactions and promote interaction of the modified histones with other proteins which positively regulate transcription. This complex may be required for the activation of transcriptional programs associated with oncogene and proto-oncogene mediated growth induction, tumor suppressor mediated growth arrest and replicative senescence, apoptosis, and DNA repair. NuA4 may also play a direct role in DNA repair when recruited to sites of DNA damage. Belongs to the neural progenitors-specific chromatin remodeling complex (npBAF complex) and is required for the proliferation of neural progenitors. During neural development a switch from a stem/progenitor to a post-mitotic chromatin remodeling mechanism occurs as neurons exit the cell cycle and become committed to their adult state. The transition from proliferating neural stem/progenitor cells to post-mitotic neurons requires a switch in subunit composition of the npBAF and nBAF complexes. As neural progenitors exit mitosis and differentiate into neurons, npBAF complexes which contain ACTL6A/BAF53A and PHF10/BAF45A, are exchanged for homologous alternative ACTL6B/BAF53B and DPF1/BAF45B or DPF3/BAF45C subunits in neuron-specific complexes (nBAF). The npBAF complex is essential for the self-renewal/proliferative capacity of the multipotent neural stem cells. The nBAF complex along with CREST plays a role regulating the activity of genes essential for dendrite growth. Proposed core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair (By similarity).By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Activator, Chromatin regulator

Keywords - Biological processi

DNA damage, DNA recombination, DNA repair, Growth regulation, Neurogenesis, Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_291621. HATs acetylate histones.
REACT_319868. RMTs methylate histone arginines.

Names & Taxonomyi

Protein namesi
Recommended name:
Actin-like protein 6A
Alternative name(s):
53 kDa BRG1-associated factor A
Actin-related protein Baf53a
BRG1-associated factor 53A
Short name:
BAF53A
Gene namesi
Name:Actl6a
Synonyms:Actl6, Baf53a
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1861453. Actl6a.

Subcellular locationi

GO - Cellular componenti

  • BAF-type complex Source: MGI
  • Ino80 complex Source: MGI
  • npBAF complex Source: UniProtKB
  • NuA4 histone acetyltransferase complex Source: UniProtKB
  • nuclear chromatin Source: MGI
  • nucleus Source: MGI
  • plasma membrane Source: MGI
  • protein complex Source: MGI
  • SWI/SNF complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 429428Actin-like protein 6APRO_0000089134Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei233 – 2331PhosphoserineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ9Z2N8.
PaxDbiQ9Z2N8.
PRIDEiQ9Z2N8.

2D gel databases

REPRODUCTION-2DPAGEQ9Z2N8.

PTM databases

PhosphoSiteiQ9Z2N8.

Expressioni

Tissue specificityi

Widely expressed. Expressed selectively in neural stem and progenitor cells (at protein level).1 Publication

Developmental stagei

Expressed predominantly in E10.5-E11.5 neural cells. In the developing spinal cord (E10.5-E16.5), is specifically expressed in proliferating neural progenitors of the ventricular zone. In the developing forebrain and cerebellar primordium, expression is restricted to proliferating neuroepithelial progenitors and cerebellar granule precursors.1 Publication

Gene expression databases

BgeeiQ9Z2N8.
CleanExiMM_ACTL6A.
ExpressionAtlasiQ9Z2N8. baseline and differential.
GenevisibleiQ9Z2N8. MM.

Interactioni

Subunit structurei

Component of numerous complexes with chromatin remodeling and histone acetyltransferase activity. Component of the NuA4 histone acetyltransferase complex which contains the catalytic subunit KAT5/TIP60 and the subunits EP400, TRRAP/PAF400, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, ING3, actin, ACTL6A/BAF53A, MORF4L1/MRG15, MORF4L2/MRGX, MRGBP, YEATS4/GAS41, VPS72/YL1 and MEAF6. The NuA4 complex interacts with MYC. Component of a NuA4-related complex which contains EP400, TRRAP/PAF400, SRCAP, BRD8/SMAP, EPC1, DMAP1/DNMAP1, RUVBL1/TIP49, RUVBL2, actin, ACTL6A/BAF53A, VPS72 and YEATS4/GAS41. Component of the BAF complex, which includes at least actin (ACTB), ARID1A, ARID1B/BAF250, SMARCA2, SMARCA4/BRG1/BAF190A, ACTL6A/BAF53, ACTL6B/BAF53B, SMARCE1/BAF57, SMARCC1/BAF155, SMARCC2/BAF170, SMARCB1/SNF5/INI1, and one or more of SMARCD1/BAF60A, SMARCD2/BAF60B, or SMARCD3/BAF60C. In muscle cells, the BAF complex also contains DPF3. Component of the BAF53 complex, at least composed of ACTL6A/BAF53A, RUVBL1/TIP49, SMARCA2/BRM/BAF190B, and TRRAP/PAF400, and which may also include a HAT activity related to, but distinct from, that of KAT5. ACTL6A interacts with SMARCA4/BRG1/BAF190A. Component of the chromatin-remodeling INO80 complex; specifically part of a complex module associated with the DBINO domain of INO80. Component of neural progenitors-specific chromatin remodeling complex (npBAF complex) composed of at least, ARID1A/BAF250A or ARID1B/BAF250B, SMARCD1/BAF60A, SMARCD3/BAF60C, SMARCA2/BRM/BAF190B, SMARCA4/BRG1/BAF190A, SMARCB1/BAF47, SMARCC1/BAF155, SMARCE1/BAF57, SMARCC2/BAF170, PHF10/BAF45A, ACTL6A/BAF53A and actin. Interacts with PHF10/BAF45A.By similarity1 Publication

Protein-protein interaction databases

BioGridi207995. 9 interactions.
IntActiQ9Z2N8. 10 interactions.
MINTiMINT-4086691.
STRINGi10090.ENSMUSP00000029214.

Structurei

3D structure databases

ProteinModelPortaliQ9Z2N8.
SMRiQ9Z2N8. Positions 8-428.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the actin family.Curated

Phylogenomic databases

eggNOGiCOG5277.
GeneTreeiENSGT00660000095557.
HOGENOMiHOG000233340.
HOVERGENiHBG003771.
InParanoidiQ9Z2N8.
KOiK11340.
OMAiLMSEASW.
OrthoDBiEOG7JT6W3.
PhylomeDBiQ9Z2N8.
TreeFamiTF312863.

Family and domain databases

InterProiIPR029912. ACL6A.
IPR004000. Actin.
IPR004001. Actin_CS.
[Graphical view]
PANTHERiPTHR11937. PTHR11937. 1 hit.
PTHR11937:SF191. PTHR11937:SF191. 1 hit.
PfamiPF00022. Actin. 1 hit.
[Graphical view]
PRINTSiPR00190. ACTIN.
SMARTiSM00268. ACTIN. 1 hit.
[Graphical view]
PROSITEiPS00432. ACTINS_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9Z2N8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSGGVYGGDE VGALVFDIGS YTVRAGYAGE DCPKVDFPTA IGVVLERDDG
60 70 80 90 100
STMMEIDGDK GKQGGPTYYI DTNALRVPRE NMEAISPLKN GMVEDWDSFQ
110 120 130 140 150
AILDHTYKMH VKSEASLHPV LMSEAPWNTR AKREKLTELM FEHYSIPAFF
160 170 180 190 200
LCKTAVLTAF ANGRSTGLIL DSGATHTTAI PVHDGYVLQQ GIVKSPLAGD
210 220 230 240 250
FITMQCRELF QEMNIELIPP YMIASKEAVR EGSPANWKRK EKLPQVTRSW
260 270 280 290 300
HNYMCNCVIQ DFQASVLQVS DSTYDEQVAA QMPTVHYEFP NGYNCDFGAE
310 320 330 340 350
RLKIPEGLFD PSNVKGLSGN TMLGVSHVVT TSVGMCDIDI RPGLYGSVIV
360 370 380 390 400
AGGNTLIQSF TDRLNRELSQ KTPPSMRLKL IANNTTVERR FSSWIGGSIL
410 420
ASLGTFQQMW ISKQEYEEGG KQCVERKCP
Length:429
Mass (Da):47,448
Last modified:September 19, 2002 - v2
Checksum:iF3FF706C69808B13
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti38 – 381P → H in BAC41116 (PubMed:16141072).Curated
Sequence conflicti153 – 1531K → Q in BAC41116 (PubMed:16141072).Curated
Sequence conflicti322 – 3221M → I in AAC94992 (PubMed:9845365).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF041476 mRNA. Translation: AAC94992.1.
AK090154 mRNA. Translation: BAC41116.1.
BC001994 mRNA. Translation: AAH01994.1.
CCDSiCCDS17298.1.
RefSeqiNP_062647.2. NM_019673.2.
UniGeneiMm.41077.

Genome annotation databases

EnsembliENSMUST00000029214; ENSMUSP00000029214; ENSMUSG00000027671.
GeneIDi56456.
KEGGimmu:56456.
UCSCiuc012coo.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF041476 mRNA. Translation: AAC94992.1.
AK090154 mRNA. Translation: BAC41116.1.
BC001994 mRNA. Translation: AAH01994.1.
CCDSiCCDS17298.1.
RefSeqiNP_062647.2. NM_019673.2.
UniGeneiMm.41077.

3D structure databases

ProteinModelPortaliQ9Z2N8.
SMRiQ9Z2N8. Positions 8-428.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi207995. 9 interactions.
IntActiQ9Z2N8. 10 interactions.
MINTiMINT-4086691.
STRINGi10090.ENSMUSP00000029214.

PTM databases

PhosphoSiteiQ9Z2N8.

2D gel databases

REPRODUCTION-2DPAGEQ9Z2N8.

Proteomic databases

MaxQBiQ9Z2N8.
PaxDbiQ9Z2N8.
PRIDEiQ9Z2N8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029214; ENSMUSP00000029214; ENSMUSG00000027671.
GeneIDi56456.
KEGGimmu:56456.
UCSCiuc012coo.1. mouse.

Organism-specific databases

CTDi86.
MGIiMGI:1861453. Actl6a.

Phylogenomic databases

eggNOGiCOG5277.
GeneTreeiENSGT00660000095557.
HOGENOMiHOG000233340.
HOVERGENiHBG003771.
InParanoidiQ9Z2N8.
KOiK11340.
OMAiLMSEASW.
OrthoDBiEOG7JT6W3.
PhylomeDBiQ9Z2N8.
TreeFamiTF312863.

Enzyme and pathway databases

ReactomeiREACT_291621. HATs acetylate histones.
REACT_319868. RMTs methylate histone arginines.

Miscellaneous databases

NextBioi312690.
PROiQ9Z2N8.
SOURCEiSearch...

Gene expression databases

BgeeiQ9Z2N8.
CleanExiMM_ACTL6A.
ExpressionAtlasiQ9Z2N8. baseline and differential.
GenevisibleiQ9Z2N8. MM.

Family and domain databases

InterProiIPR029912. ACL6A.
IPR004000. Actin.
IPR004001. Actin_CS.
[Graphical view]
PANTHERiPTHR11937. PTHR11937. 1 hit.
PTHR11937:SF191. PTHR11937:SF191. 1 hit.
PfamiPF00022. Actin. 1 hit.
[Graphical view]
PRINTSiPR00190. ACTIN.
SMARTiSM00268. ACTIN. 1 hit.
[Graphical view]
PROSITEiPS00432. ACTINS_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Rapid and phosphoinositol-dependent binding of the SWI/SNF-like BAF complex to chromatin after T lymphocyte receptor signaling."
    Zhao K., Wang W., Rando O.J., Xue Y., Swiderek K., Kuo A., Crabtree G.R.
    Cell 95:625-636(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Embryonic brain.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Mammary gland.
  4. "An essential switch in subunit composition of a chromatin remodeling complex during neural development."
    Lessard J., Wu J.I., Ranish J.A., Wan M., Winslow M.M., Staahl B.T., Wu H., Aebersold R., Graef I.A., Crabtree G.R.
    Neuron 55:201-215(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, FUNCTION OF THE NBAF AND NPBAF COMPLEXES, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE NPBAF COMPLEX, INTERACTION WITH PHF10, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiACL6A_MOUSE
AccessioniPrimary (citable) accession number: Q9Z2N8
Secondary accession number(s): Q8C1W3, Q99M56
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: September 19, 2002
Last modified: July 22, 2015
This is version 132 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.