O96019 (ACL6A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	429 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 process	DNA damage DNA recombination DNA repair Growth regulation Neurogenesis Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Molecular function	Activator Chromatin regulator
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	DNA recombination Inferred from electronic annotation. Source: UniProtKB-KW DNA repair Inferred from electronic annotation. Source: UniProtKB-KW 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-dependent Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Ino80 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 plasma membrane Inferred from direct assay. Source: LIFEdb
Molecular_function	ATP binding Inferred from electronic annotation. Source: InterPro chromatin 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
YY1	P25490	5	EBI-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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.8
	Chain	2 – 429	428	Actin-like protein 6A		PRO_0000089133
Amino acid modifications
	Modified residue	2	1	N-acetylserine Ref.8
	Modified residue	233	1	Phosphoserine Ref.17 Ref.21
Natural variations
	Alternative sequence	1 – 42	42	Missing in isoform 2.		VSP_000150
Experimental info
	Sequence conflict	92	1	M → T in CAB66543. Ref.4
	Sequence conflict	210	1	F → L in CAB66543. Ref.4
	Sequence conflict	254	1	M → T in CAB66543. Ref.4
	Sequence conflict	320	1	N → K in CAB66543. Ref.4

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 1, 1999. Version 1. Checksum: ECD92D29BD1854E0	FASTA	429	47,461
	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
	Isoform 2 (HArpNbeta-s) [UniParc]. Checksum: 5FF2B5B41C15C03A	FASTA	387	43,236
	10 20 30 40 50 60 MVVERDDGST LMEIDGDKGK QGGPTYYIDT NALRVPRENM EAISPLKNGM VEDWDSFQAI 70 80 90 100 110 120 LDHTYKMHVK SEASLHPVLM SEAPWNTRAK REKLTELMFE HYNIPAFFLC KTAVLTAFAN 130 140 150 160 170 180 GRSTGLILDS GATHTTAIPV HDGYVLQQGI VKSPLAGDFI TMQCRELFQE MNIELVPPYM 190 200 210 220 230 240 IASKEAVREG SPANWKRKEK LPQVTRSWHN YMCNCVIQDF QASVLQVSDS TYDEQVAAQM 250 260 270 280 290 300 PTVHYEFPNG YNCDFGAERL KIPEGLFDPS NVKGLSGNTM LGVSHVVTTS VGMCDIDIRP 310 320 330 340 350 360 GLYGSVIVAG GNTLIQSFTD RLNRELSQKT PPSMRLKLIA NNTTVERRFS SWIGGSILAS 370 380 LGTFQQMWIS KQEYEEGGKQ CVERKCP

References

	« Hide 'large scale' referencesShow '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. , 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. , 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. , 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, 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, 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, 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, MASS SPECTROMETRY. 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, 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, MASS SPECTROMETRY. 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.
+	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.
IPI	IPI00003627. IPI00216622.
RefSeq	NP_004292.1. NM_004301.3. NP_817126.1. NM_177989.2. NP_829888.1. NM_178042.2.
UniGene	Hs.435326.
3D structure databases
ProteinModelPortal	O96019.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-27565N.
IntAct	O96019. 48 interactions.
MINT	MINT-1136373.
STRING	9606.ENSP00000397552.
PTM databases
PhosphoSite	O96019.
Proteomic databases
PaxDb	O96019.
PeptideAtlas	O96019.
PRIDE	O96019.
Protocols and materials databases
DNASU	86.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000392662; ENSP00000376430; ENSG00000136518. ENST00000429709; ENSP00000397552; ENSG00000136518. ENST00000450518; ENSP00000394014; ENSG00000136518.
GeneID	86.
KEGG	hsa:86.
UCSC	uc003fjw.3. human.
Organism-specific databases
CTD	86.
GeneCards	GC03P179280.
HGNC	HGNC:24124. ACTL6A.
HPA	CAB012188.
MIM	604958. gene.
neXtProt	NX_O96019.
PharmGKB	PA134914203.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5277.
HOGENOM	HOG000233340.
HOVERGEN	HBG003771.
InParanoid	O96019.
KO	K11340.
OMA	DFGSERF.
OrthoDB	EOG4XKV6Z.
PhylomeDB	O96019.
Gene expression databases
ArrayExpress	O96019.
Bgee	O96019.
CleanEx	HS_ACTL6A.
Genevestigator	O96019.
GermOnline	ENSG00000136518. Homo sapiens.
Family and domain databases
InterPro	IPR004000. Actin-related. IPR004001. Actin_CS. [Graphical view]
PANTHER	PTHR11937. PTHR11937. 1 hit.
Pfam	PF00022. Actin. 1 hit. [Graphical view]
PRINTS	PR00190. ACTIN.
SMART	SM00268. ACTIN. 1 hit. [Graphical view]
PROSITE	PS00406. ACTINS_1. False negative. PS00432. ACTINS_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	ACTL6A. human.
GenomeRNAi	86.
NextBio	315.
PMAP-CutDB	O96019.
SOURCE	Search...

Entry information

Entry name

ACL6A_HUMAN

Accession

Primary (citable) accession number: O96019
Secondary accession number(s): B3KMN1 , D3DNR9, Q8TAE5, Q9BVS8, Q9H0W6

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 19, 2002
Last sequence update:	May 1, 1999
Last modified:	May 1, 2013
This is version 134 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.