Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O96019 (ACL6A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·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
ArpNbeta
BRG1-associated factor 53A
Short name=BAF53A
INO80 complex subunit K
Gene names
Name:ACTL6A
Synonyms:BAF53, BAF53A, INO80K
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

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. 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 By similarity. 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. Putative core component of the chromatin remodeling INO80 complex which is involved in transcriptional regulation, DNA replication and probably DNA repair. Ref.13 Ref.15

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 and the adenovirus E1A protein. 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. 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 similarity. Ref.1 Ref.9 Ref.10 Ref.11 Ref.12 Ref.13 Ref.15 Ref.16 Ref.19 Ref.20 Ref.23

Subcellular location

Nucleus Ref.18.

Sequence similarities

Belongs to the actin family.

Ontologies

Keywords
   Biological processDNA damage
DNA recombination
DNA repair
Growth regulation
Neurogenesis
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   Molecular functionActivator
Chromatin regulator
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
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 organization

Traceable author statement. Source: Reactome

chromatin remodeling

Inferred from direct assay PubMed 11726552. Source: BHF-UCL

histone H2A acetylation

Inferred from direct assay Ref.15. Source: UniProtKB

histone H4 acetylation

Inferred from direct assay Ref.15. Source: UniProtKB

nervous system development

Inferred from electronic annotation. Source: UniProtKB-KW

neural retina development

Inferred from expression pattern PubMed 18816825. Source: BHF-UCL

regulation of growth

Inferred from electronic annotation. Source: UniProtKB-KW

regulation of transcription from RNA polymerase II promoter

Non-traceable author statement PubMed 8804307. Source: BHF-UCL

signal transduction

Traceable author statement Ref.1. Source: ProtInc

transcription, DNA-templated

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentIno80 complex

Inferred from direct assay Ref.18Ref.23. Source: UniProtKB

NuA4 histone acetyltransferase complex

Inferred from direct assay Ref.10Ref.15. Source: UniProtKB

SWI/SNF complex

Inferred from direct assay PubMed 11078522. Source: UniProtKB

npBAF complex

Inferred from sequence or structural similarity. Source: UniProtKB

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay Ref.18. Source: UniProtKB

plasma membrane

Inferred from direct assay. Source: LIFEdb

   Molecular_functionchromatin binding

Traceable author statement Ref.1. Source: ProtInc

transcription coactivator activity

Non-traceable author statement PubMed 8804307. Source: BHF-UCL

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

YY1P254905EBI-355018,EBI-765538

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O96019-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: O96019-2)

Also known as: HArpNbeta-s;

The sequence of this isoform differs from the canonical sequence as follows:
     1-42: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.8
Chain2 – 429428Actin-like protein 6A
PRO_0000089133

Amino acid modifications

Modified residue21N-acetylserine Ref.8 Ref.24
Modified residue2331Phosphoserine Ref.17 Ref.21

Natural variations

Alternative sequence1 – 4242Missing in isoform 2.
VSP_000150

Experimental info

Sequence conflict921M → T in CAB66543. Ref.4
Sequence conflict2101F → L in CAB66543. Ref.4
Sequence conflict2541M → T in CAB66543. Ref.4
Sequence conflict3201N → K in CAB66543. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: ECD92D29BD1854E0

FASTA42947,461
        10         20         30         40         50         60 
MSGGVYGGDE VGALVFDIGS YTVRAGYAGE DCPKVDFPTA IGMVVERDDG STLMEIDGDK 

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

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

       190        200        210        220        230        240 
PVHDGYVLQQ GIVKSPLAGD FITMQCRELF QEMNIELVPP 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

Isoform 2 (HArpNbeta-s) [UniParc].

Checksum: 5FF2B5B41C15C03A
Show »

FASTA38743,236

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] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE, IDENTIFICATION IN BAF COMPLEX.
[2]"Two isoforms of a human actin-related protein show nuclear localization and mutually selective expression between brain and other tissues."
Harata M., Mochizuki R., Mizuno S.
Biosci. Biotechnol. Biochem. 63:917-923(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"Characterization of an alternative splicing product of hArpNbeta/BAF53."
Harata M., Ohfuchi E.
Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
[4]"Towards a catalog of human genes and proteins: sequencing and analysis of 500 novel complete protein coding human cDNAs."
Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., Ottenwaelder B., Obermaier B. expand/collapse author list , Tampe J., Heubner D., Wambutt R., Korn B., Klein M., Poustka A.
Genome Res. 11:422-435(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[5]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Embryo.
[6]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]"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] (ISOFORM 1).
Tissue: Placenta, Skin and Testis.
[8]Bienvenut W.V.
Submitted (JAN-2010) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-24; 63-76; 113-130; 195-207 AND 380-389, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Ovarian carcinoma.
[9]"Identification of new subunits of the multiprotein mammalian TRRAP/TIP60-containing histone acetyltransferase complex."
Cai Y., Jin J., Tomomori-Sato C., Sato S., Sorokina I., Parmely T.J., Conaway R.C., Conaway J.W.
J. Biol. Chem. 278:42733-42736(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 35-60; 63-76; 113-130; 154-164; 195-207; 304-315 AND 380-389, IDENTIFICATION IN NUA4 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[10]"Involvement of the TIP60 histone acetylase complex in DNA repair and apoptosis."
Ikura T., Ogryzko V.V., Grigoriev M., Groisman R., Wang J., Horikoshi M., Scully R., Qin J., Nakatani Y.
Cell 102:463-473(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN NUA4 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[11]"The p400 complex is an essential E1A transformation target."
Fuchs M., Gerber J., Drapkin R., Sif S., Ikura T., Ogryzko V., Lane W.S., Nakatani Y., Livingston D.M.
Cell 106:297-307(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN NUA4-LIKE COMPLEX.
[12]"BAF53 forms distinct nuclear complexes and functions as a critical c-Myc-interacting nuclear cofactor for oncogenic transformation."
Park J., Wood M.A., Cole M.D.
Mol. Cell. Biol. 22:1307-1316(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE BAF53 COMPLEX WITH RUVBL1; SMARCA2 AND TRRAP.
[13]"The chromatin-remodeling complex WINAC targets a nuclear receptor to promoters and is impaired in Williams syndrome."
Kitagawa H., Fujiki R., Yoshimura K., Mezaki Y., Uematsu Y., Matsui D., Ogawa S., Unno K., Okubo M., Tokita A., Nakagawa T., Ito T., Ishimi Y., Nagasawa H., Matsumoto T., Yanagisawa J., Kato S.
Cell 113:905-917(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN THE WINAC COMPLEX, FUNCTION.
[14]"The highly conserved and multifunctional NuA4 HAT complex."
Doyon Y., Cote J.
Curr. Opin. Genet. Dev. 14:147-154(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW ON NUA4 COMPLEX.
[15]"Structural and functional conservation of the NuA4 histone acetyltransferase complex from yeast to humans."
Doyon Y., Selleck W., Lane W.S., Tan S., Cote J.
Mol. Cell. Biol. 24:1884-1896(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, IDENTIFICATION IN NUA4 COMPLEX, IDENTIFICATION IN A NUA4-RELATED SRCAP-CONTAINING COMPLEX.
[16]"A mammalian chromatin remodeling complex with similarities to the yeast INO80 complex."
Jin J., Cai Y., Yao T., Gottschalk A.J., Florens L., Swanson S.K., Gutierrez J.L., Coleman M.K., Workman J.L., Mushegian A., Washburn M.P., Conaway R.C., Conaway J.W.
J. Biol. Chem. 280:41207-41212(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE INO80 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[17]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"A YY1-INO80 complex regulates genomic stability through homologous recombination-based repair."
Wu S., Shi Y., Mulligan P., Gay F., Landry J., Liu H., Lu J., Qi H.H., Wang W., Nickoloff J.A., Wu C., Shi Y.
Nat. Struct. Mol. Biol. 14:1165-1172(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, ASSOCIATION WITH THE INO80 COMPLEX.
[19]"Regulation of muscle development by DPF3, a novel histone acetylation and methylation reader of the BAF chromatin remodeling complex."
Lange M., Kaynak B., Forster U.B., Toenjes M., Fischer J.J., Grimm C., Schlesinger J., Just S., Dunkel I., Krueger T., Mebus S., Lehrach H., Lurz R., Gobom J., Rottbauer W., Abdelilah-Seyfried S., Sperling S.
Genes Dev. 22:2370-2384(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE BAF COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[20]"Distinct modes of regulation of the Uch37 deubiquitinating enzyme in the proteasome and in the Ino80 chromatin-remodeling complex."
Yao T., Song L., Jin J., Cai Y., Takahashi H., Swanson S.K., Washburn M.P., Florens L., Conaway R.C., Cohen R.E., Conaway J.W.
Mol. Cell 31:909-917(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE INO80 COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY.
[21]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-233, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"Subunit organization of the human INO80 chromatin remodeling complex: An evolutionarily conserved core complex catalyzes ATP-dependent nucleosome remodeling."
Chen L., Cai Y., Jin J., Florens L., Swanson S.K., Washburn M.P., Conaway J.W., Conaway R.C.
J. Biol. Chem. 286:11283-11289(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE INO80 COMPLEX.
[24]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF041474 mRNA. Translation: AAC94991.1.
AB015907 mRNA. Translation: BAA74577.1.
AB060168 mRNA. Translation: BAB87844.1.
AB061315 mRNA. Translation: BAB87848.1.
AL136608 mRNA. Translation: CAB66543.1.
AK021756 mRNA. Translation: BAG51043.1.
CH471052 Genomic DNA. Translation: EAW78401.1.
CH471052 Genomic DNA. Translation: EAW78397.1.
CH471052 Genomic DNA. Translation: EAW78399.1.
BC000949 mRNA. Translation: AAH00949.1.
BC001391 mRNA. Translation: AAH01391.1.
BC036371 mRNA. Translation: AAH36371.1.
RefSeqNP_004292.1. NM_004301.3.
NP_817126.1. NM_177989.2.
NP_829888.1. NM_178042.2.
UniGeneHs.435326.

3D structure databases

ProteinModelPortalO96019.
SMRO96019. Positions 8-428.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106601. 64 interactions.
DIPDIP-27565N.
IntActO96019. 52 interactions.
MINTMINT-1136373.
STRING9606.ENSP00000397552.

PTM databases

PhosphoSiteO96019.

Proteomic databases

PaxDbO96019.
PeptideAtlasO96019.
PRIDEO96019.

Protocols and materials databases

DNASU86.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000392662; ENSP00000376430; ENSG00000136518. [O96019-2]
ENST00000429709; ENSP00000397552; ENSG00000136518. [O96019-1]
ENST00000450518; ENSP00000394014; ENSG00000136518. [O96019-2]
GeneID86.
KEGGhsa:86.
UCSCuc003fjw.3. human. [O96019-1]

Organism-specific databases

CTD86.
GeneCardsGC03P179280.
HGNCHGNC:24124. ACTL6A.
HPACAB012188.
MIM604958. gene.
neXtProtNX_O96019.
PharmGKBPA134914203.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5277.
HOGENOMHOG000233340.
HOVERGENHBG003771.
InParanoidO96019.
KOK11340.
OMAGYHQDFG.
OrthoDBEOG7JT6W3.
PhylomeDBO96019.
TreeFamTF312863.

Enzyme and pathway databases

ReactomeREACT_172623. Chromatin organization.
REACT_197818. Chromatin organization.
SignaLinkO96019.

Gene expression databases

ArrayExpressO96019.
BgeeO96019.
CleanExHS_ACTL6A.
GenevestigatorO96019.

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

ChiTaRSACTL6A. human.
GeneWikiACTL6A.
GenomeRNAi86.
NextBio315.
PMAP-CutDBO96019.
PROO96019.
SOURCESearch...

Entry information

Entry nameACL6A_HUMAN
AccessionPrimary (citable) accession number: O96019
Secondary accession number(s): B3KMN1 expand/collapse secondary AC list , D3DNR9, Q8TAE5, Q9BVS8, Q9H0W6
Entry history
Integrated into UniProtKB/Swiss-Prot: September 19, 2002
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 143 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM