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Q9Z2N8 (ACL6A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 119. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Actl6a
Synonyms:Actl6, Baf53a
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length429 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Also involved in vitamin D-coupled transcription regulation via its association with the WINAC complex, a chromatin-remodeling complex recruited by vitamin D receptor (VDR), which is required for the ligand-bound VDR-mediated transrepression of the CYP27B1 gene By similarity. 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. Ref.4

Subunit structure

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 the WINAC complex, at least composed of SMARCA2, SMARCA4, SMARCB1, SMARCC1, SMARCC2, SMARCD1, SMARCE1, ACTL6A, BAZ1B/WSTF, ARID1A, SUPT16H, CHAF1A and TOP2B By similarity. 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. Ref.4

Subcellular location

Nucleus By similarity.

Tissue specificity

Widely expressed. Expressed selectively in neural stem and progenitor cells (at protein level). Ref.4

Developmental stage

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. Ref.4

Sequence similarities

Belongs to the actin family.

Ontologies

Keywords
   Biological processDNA damage
DNA recombination
DNA repair
Growth regulation
Neurogenesis
Transcription
Transcription regulation
   Cellular componentNucleus
   Molecular functionActivator
Chromatin regulator
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA recombination

Inferred from electronic annotation. Source: UniProtKB-KW

DNA repair

Inferred from electronic annotation. Source: UniProtKB-KW

chromatin remodeling

Inferred from direct assay Ref.1. Source: MGI

histone H2A acetylation

Inferred from sequence or structural similarity. Source: UniProtKB

histone H4 acetylation

Inferred from sequence or structural similarity. Source: UniProtKB

nervous system development

Inferred from mutant phenotype Ref.4. Source: UniProtKB

neural retina development

Inferred from electronic annotation. Source: Ensembl

regulation of growth

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentIno80 complex

Inferred from electronic annotation. Source: Ensembl

NuA4 histone acetyltransferase complex

Inferred from sequence or structural similarity. Source: UniProtKB

SWI/SNF complex

Inferred from electronic annotation. Source: Ensembl

npBAF complex

Inferred from direct assay Ref.4. Source: UniProtKB

nucleus

Inferred from direct assay PubMed 12437990. Source: MGI

plasma membrane

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionchromatin binding

Inferred from direct assay Ref.1. Source: MGI

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 429428Actin-like protein 6A
PRO_0000089134

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue2331Phosphoserine By similarity

Experimental info

Sequence conflict381P → H in BAC41116. Ref.2
Sequence conflict1531K → Q in BAC41116. Ref.2
Sequence conflict3221M → I in AAC94992. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9Z2N8 [UniParc].

Last modified September 19, 2002. Version 2.
Checksum: F3FF706C69808B13

FASTA42947,448
        10         20         30         40         50         60 
MSGGVYGGDE VGALVFDIGS YTVRAGYAGE DCPKVDFPTA IGVVLERDDG STMMEIDGDK 

        70         80         90        100        110        120 
GKQGGPTYYI DTNALRVPRE NMEAISPLKN GMVEDWDSFQ AILDHTYKMH VKSEASLHPV 

       130        140        150        160        170        180 
LMSEAPWNTR AKREKLTELM FEHYSIPAFF LCKTAVLTAF ANGRSTGLIL DSGATHTTAI 

       190        200        210        220        230        240 
PVHDGYVLQQ GIVKSPLAGD FITMQCRELF QEMNIELIPP YMIASKEAVR EGSPANWKRK 

       250        260        270        280        290        300 
EKLPQVTRSW HNYMCNCVIQ DFQASVLQVS DSTYDEQVAA QMPTVHYEFP NGYNCDFGAE 

       310        320        330        340        350        360 
RLKIPEGLFD PSNVKGLSGN TMLGVSHVVT TSVGMCDIDI RPGLYGSVIV AGGNTLIQSF 

       370        380        390        400        410        420 
TDRLNRELSQ KTPPSMRLKL IANNTTVERR FSSWIGGSIL ASLGTFQQMW ISKQEYEEGG 


KQCVERKCP 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF041476 mRNA. Translation: AAC94992.1.
AK090154 mRNA. Translation: BAC41116.1.
BC001994 mRNA. Translation: AAH01994.1.
RefSeqNP_062647.2. NM_019673.2.
UniGeneMm.41077.

3D structure databases

ProteinModelPortalQ9Z2N8.
SMRQ9Z2N8. Positions 8-428.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid207995. 9 interactions.
IntActQ9Z2N8. 9 interactions.
MINTMINT-4086691.
STRING10090.ENSMUSP00000029214.

PTM databases

PhosphoSiteQ9Z2N8.

2D gel databases

REPRODUCTION-2DPAGEQ9Z2N8.

Proteomic databases

PaxDbQ9Z2N8.
PRIDEQ9Z2N8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000029214; ENSMUSP00000029214; ENSMUSG00000027671.
GeneID56456.
KEGGmmu:56456.
UCSCuc012coo.1. mouse.

Organism-specific databases

CTD86.
MGIMGI:1861453. Actl6a.

Phylogenomic databases

eggNOGCOG5277.
GeneTreeENSGT00660000095557.
HOGENOMHOG000233340.
HOVERGENHBG003771.
InParanoidQ9Z2N8.
KOK11340.
OMAGYHQDFG.
OrthoDBEOG7JT6W3.
PhylomeDBQ9Z2N8.
TreeFamTF312863.

Gene expression databases

ArrayExpressQ9Z2N8.
BgeeQ9Z2N8.
CleanExMM_ACTL6A.
GenevestigatorQ9Z2N8.

Family and domain databases

InterProIPR004000. Actin-related.
IPR004001. Actin_CS.
[Graphical view]
PANTHERPTHR11937. PTHR11937. 1 hit.
PfamPF00022. Actin. 1 hit.
[Graphical view]
PRINTSPR00190. ACTIN.
SMARTSM00268. ACTIN. 1 hit.
[Graphical view]
PROSITEPS00432. ACTINS_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio312690.
PROQ9Z2N8.
SOURCESearch...

Entry information

Entry nameACL6A_MOUSE
AccessionPrimary (citable) accession number: Q9Z2N8
Secondary accession number(s): Q8C1W3, Q99M56
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: September 19, 2002
Last modified: April 16, 2014
This is version 119 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot