Histone acetyltransferase KAT2A - Homo sapiens (Human)

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

Alternative products

Sequence annotation (Features)

Sequences

References

Cross-references

Entry information

Relevant documents

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

Alternative products

Sequence annotation (Features)

Sequences

References

Cross-references

Entry information

Relevant documents

Molecule processing

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Amino acid modifications

Natural variations

Experimental info

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Sequence databases

3D structure databases

Protein-protein interaction databases

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Entry

#Exp.

IntAct

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Molecule processing

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Amino acid modifications

Natural variations

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Sequence databases

3D structure databases

Protein-protein interaction databases

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Reviewed, UniProtKB/Swiss-Prot Q92830 (KAT2A_HUMAN)

Last modified February 9, 2010. Version 115. History...

Clusters with 100%, 90%, 50% identity |

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Protein names

Recommended name:
    Histone acetyltransferase KAT2A
    EC=2.3.1.48
Alternative name(s):
    Lysine acetyltransferase 2A
    Histone acetyltransferase GCN5
      Short name=HsGCN5
    General control of amino acid synthesis protein 5-like 2
    STAF97

Gene names

Name:	KAT2A
Synonyms:	GCN5, GCN5L2, HGCN5

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Sequence length	837 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level.

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Function	Functions as a histone acetyltransferase (HAT) to promote transcriptional activation. Acetylation of histones gives a specific tag for epigenetic transcription activation. Has significant histone acetyltransferase activity with core histones, but not with nucleosome core particles. In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat's transactivating activity and may help inducing chromatin remodeling of proviral genes. Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4. Ref.15
Catalytic activity	Acetyl-CoA + [histone] = CoA + acetyl-[histone].
Subunit structure	Interacts with EP300, CREBBP and ADA2. Component of the TFTC-HAT complex, at least composed of TAF5L, TAF6L, TAF3, TADA3L, SUPT3H/SPT3, TAF2/TAFII150, TAF4/TAFII135, TAF5/TAFII100, KAT2A/GCN5L2, TAF10 and TRRAP. Interacts with TRRAP. Component of the STAGA transcription coactivator-HAT complex, at least composed of SUPT3H, KAT2A, SUPT7L, TAF5L, TAF6L, TADA3L, TAD1L, TAF10, TAF12, TRRAP and TAF9. The STAGA core complex is associated with a subcomplex required for histone deubiquitinylation composed of ATXN7L3, ENY2 and USP22. Interacts with and acetylates HIV-1 Tat. Component of the ADA2A-containing complex (ATAC), composed of CSRP2BP, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1. In the complex, it probably interacts directly with CSRP2BP, MBIP and WDR5. Ref.8 Ref.9 Ref.10 Ref.11
Subcellular location	Nucleus Ref.6.
Tissue specificity	Expressed in all tissues tested, with most abundant expression in ovary.
Sequence similarities	Belongs to the GCN5 family. Contains 1 bromo domain. Contains 1 N-acetyltransferase domain.

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Keywords
Biological process	Host-virus interaction Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Bromodomain
Molecular function	Transferase
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome
Gene Ontology (GO)
Biological process	chromatin remodeling Ref.1 Traceable author statement. Source: ProtInc histone H3 acetylation Ref.6 Ref.7 Inferred from direct assay. Source: UniProtKB histone deubiquitination Ref.14 Inferred from direct assay. Source: UniProtKB interspecies interaction between organisms Inferred from electronic annotation. Source: UniProtKB-KW regulation of transcription from RNA polymerase II promoter Ref.1 Traceable author statement. Source: ProtInc transcription from RNA polymerase II promoter Ref.1 Traceable author statement. Source: ProtInc
Cellular component	STAGA complex Ref.6 Inferred from direct assay. Source: UniProtKB transcription factor TFTC complex Ref.7 Inferred from direct assay. Source: UniProtKB
Molecular function	histone acetyltransferase activity Ref.6 Ref.7 Inferred from direct assay. Source: UniProtKB histone deacetylase binding Inferred from physical interaction. Source: UniProtKB transcription coactivator activity Ref.6 Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

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With	Entry	#Exp.	IntAct	Notes
SIRT2	Q8IXJ6	1	EBI-477636,EBI-477232
SIRT2	Q8IXJ6	1	EBI-477641,EBI-477232

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Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Chain

1 – 837

837

Histone acetyltransferase KAT2A

PRO_0000211202

Domain

503 – 656

154

N-acetyltransferase

Domain

745 – 815

Bromo

Modified residue

734

Phosphotyrosine Ref.12 Ref.13

Alternative sequence

1 – 410

410

Missing in isoform 2.

VSP_000556

Sequence conflict

116

E → G in AAC39769. Ref.1

Sequence conflict

134

M → I in AAC39769. Ref.1

Sequence conflict

269

K → E in AAC39769. Ref.1

837

Helix Strand Turn

Details...

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Sequence		Length	Mass (Da)
Isoform 1 (GCN5-L) [UniParc]. Last modified October 14, 2008. Version 3. Checksum: 728CC8ACF08600EA Show »	FASTA	837	93,926
10 20 30 40 50 60 MAEPSQAPTP APAAQPRPLQ SPAPAPTPTP APSPASAPIP TPTPAPAPAP AAAPAGSTGT 70 80 90 100 110 120 GGPGVGSGGA GSGGDPARPG LSQQQRASQR KAQVRGLPRA KKLEKLGVFS ACKANETCKC 130 140 150 160 170 180 NGWKNPKPPT APRMDLQQPA ANLSELCRSC EHPLADHVSH LENVSEDEIN RLLGMVVDVE 190 200 210 220 230 240 NLFMSVHKEE DTDTKQVYFY LFKLLRKCIL QMTRPVVEGS LGSPPFEKPN IEQGVLNFVQ 250 260 270 280 290 300 YKFSHLAPRE RQTMFELSKM FLLCLNYWKL ETPAQFRQRS QAEDVATYKV NYTRWLCYCH 310 320 330 340 350 360 VPQSCDSLPR YETTHVFGRS LLRSIFTVTR RQLLEKFRVE KDKLVPEKRT LILTHFPKFL 370 380 390 400 410 420 SMLEEEIYGA NSPIWESGFT MPPSEGTQLV PRPASVSAAV VPSTPIFSPS MGGGSNSSLS 430 440 450 460 470 480 LDSAGAEPMP GEKRTLPENL TLEDAKRLRV MGDIPMELVN EVMLTITDPA AMLGPETSLL 490 500 510 520 530 540 SANAARDETA RLEERRGIIE FHVIGNSLTP KANRRVLLWL VGLQNVFSHQ LPRMPKEYIA 550 560 570 580 590 600 RLVFDPKHKT LALIKDGRVI GGICFRMFPT QGFTEIVFCA VTSNEQVKGY GTHLMNHLKE 610 620 630 640 650 660 YHIKHNILYF LTYADEYAIG YFKKQGFSKD IKVPKSRYLG YIKDYEGATL MECELNPRIP 670 680 690 700 710 720 YTELSHIIKK QKEIIKKLIE RKQAQIRKVY PGLSCFKEGV RQIPVESVPG IRETGWKPLG 730 740 750 760 770 780 KEKGKELKDP DQLYTTLKNL LAQIKSHPSA WPFMEPVKKS EAPDYYEVIR FPIDLKTMTE 790 800 810 820 830 RLRSRYYVTR KLFVADLQRV IANCREYNPP DSEYCRCASA LEKFFYFKLK EGGLIDK « Hide
Isoform 2 (GCN5-S). Checksum: A6EAE20DB0B49ADC Show »	FASTA	427	48,921
10 20 30 40 50 60 MGGGSNSSLS LDSAGAEPMP GEKRTLPENL TLEDAKRLRV MGDIPMELVN EVMLTITDPA 70 80 90 100 110 120 AMLGPETSLL SANAARDETA RLEERRGIIE FHVIGNSLTP KANRRVLLWL VGLQNVFSHQ 130 140 150 160 170 180 LPRMPKEYIA RLVFDPKHKT LALIKDGRVI GGICFRMFPT QGFTEIVFCA VTSNEQVKGY 190 200 210 220 230 240 GTHLMNHLKE YHIKHNILYF LTYADEYAIG YFKKQGFSKD IKVPKSRYLG YIKDYEGATL 250 260 270 280 290 300 MECELNPRIP YTELSHIIKK QKEIIKKLIE RKQAQIRKVY PGLSCFKEGV RQIPVESVPG 310 320 330 340 350 360 IRETGWKPLG KEKGKELKDP DQLYTTLKNL LAQIKSHPSA WPFMEPVKKS EAPDYYEVIR 370 380 390 400 410 420 FPIDLKTMTE RLRSRYYVTR KLFVADLQRV IANCREYNPP DSEYCRCASA LEKFFYFKLK EGGLIDK « Hide

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	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Identification of human proteins functionally conserved with the yeast putative adaptors ADA2 and GCN5." Candau R., Moore P.A., Wang L., Barlev N., Ying C.Y., Rosen C.A., Berger S.L. Mol. Cell. Biol. 16:593-602(1996) [PubMed: 8552087] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), CHARACTERIZATION. Tissue: Testis.
[2]	"Cloning of Drosophila GCN5: conserved features among metazoan GCN5 family members." Smith E.R., Belote J.M., Schlitz R.L., Yang X.-J., Moore P.A., Berger S.L., Nakatani Y., Allis C.D. Nucleic Acids Res. 26:2948-2954(1998) [PubMed: 9611240] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], ALTERNATIVE SPLICING. Tissue: Liver.
[3]	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. Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Eye, Skin and Testis.
[5]	"A p300/CBP-associated factor that competes with the adenoviral oncoprotein E1A." Yang X.-J., Ogryzko V.V., Nishikawa J., Howard B.H., Nakatani Y. Nature 382:319-324(1996) [PubMed: 8684459] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 362-837 (ISOFORM 1). Tissue: Brain.
[6]	"Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo." Martinez E., Palhan V.B., Tjernberg A., Lymar E.S., Gamper A.M., Kundu T.K., Chait B.T., Roeder R.G. Mol. Cell. Biol. 21:6782-6795(2001) [PubMed: 11564863] [Abstract] Cited for: MASS SPECTROMETRY, SUBCELLULAR LOCATION, IDENTIFICATION IN THE STAGA COMPLEX WITH SUPT3H; KIAA0764; TAF5L; TAF6L; TRRAP; TADA3L; TAF10; TAF12 AND TAF9.
[7]	"Identification of TATA-binding protein-free TAFII-containing complex subunits suggests a role in nucleosome acetylation and signal transduction." Brand M., Yamamoto K., Staub A., Tora L. J. Biol. Chem. 274:18285-18289(1999) [PubMed: 10373431] [Abstract] Cited for: IDENTIFICATION IN THE TFTC-HAT COMPLEX WITH TAF5L; TAF6L; TADA3L; SUPT3H; TAF2; TAF4; TAF5; TRRAP AND TAF10.
[8]	"The essential cofactor TRRAP recruits the histone acetyltransferase hGCN5 to c-Myc." McMahon S.B., Wood M.A., Cole M.D. Mol. Cell. Biol. 20:556-562(2000) [PubMed: 10611234] [Abstract] Cited for: INTERACTION WITH TRRAP.
[9]	"The histone acetyltransferase, hGCN5, interacts with and acetylates the HIV transactivator, Tat." Col E., Caron C., Seigneurin-Berny D., Gracia J., Favier A., Khochbin S. J. Biol. Chem. 276:28179-28184(2001) [PubMed: 11384967] [Abstract] Cited for: INTERACTION WITH HIV-1 TAT.
[10]	"The TFIID components human TAFII140 and Drosophila BIP2 (TAFII155) are novel metazoan homologues of yeast TAFII47 containing a histone fold and a PHD finger." Gangloff Y.G., Pointud J.-C., Thuault S., Carre L., Romier C., Muratoglu S., Brand M., Tora L., Couderc J.-L., Davidson I. Mol. Cell. Biol. 21:5109-5121(2001) [PubMed: 11438666] [Abstract] Cited for: INTERACTION WITH TAF3.
[11]	"The transforming acidic coiled coil proteins interact with nuclear histone acetyltransferases." Gangisetty O., Lauffart B., Sondarva G.V., Chelsea D.M., Still I.H. Oncogene 23:2559-2563(2004) [PubMed: 14767476] [Abstract] Cited for: INTERACTION WITH TACC1; TACC2 AND TACC3.
[12]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-734, MASS SPECTROMETRY.
[13]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-734, MASS SPECTROMETRY.
[14]	"A TFTC/STAGA module mediates histone H2A and H2B deubiquitination, coactivates nuclear receptors, and counteracts heterochromatin silencing." Zhao Y., Lang G., Ito S., Bonnet J., Metzger E., Sawatsubashi S., Suzuki E., Le Guezennec X., Stunnenberg H.G., Krasnov A., Georgieva S.G., Schuele R., Takeyama K., Kato S., Tora L., Devys D. Mol. Cell 29:92-101(2008) [PubMed: 18206972] [Abstract] Cited for: IDENTIFICATION IN STAGA COMPLEX.
[15]	"The double-histone-acetyltransferase complex ATAC is essential for mammalian development." Guelman S., Kozuka K., Mao Y., Pham V., Solloway M.J., Wang J., Wu J., Lill J.R., Zha J. Mol. Cell. Biol. 29:1176-1188(2009) [PubMed: 19103755] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN ATAC COMPLEX.
[16]	"Solution structure and acetyl-lysine binding activity of the GCN5 bromodomain." Hudson B.P., Martinez-Yamout M.A., Dyson H.J., Wright P.E. J. Mol. Biol. 304:355-370(2000) [PubMed: 11090279] [Abstract] Cited for: STRUCTURE BY NMR OF 730-832.
+	Additional computationally mapped references.

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EMBL
GenBank
DDBJ

AF029777 mRNA. Translation: AAC39769.1.
CH471152 Genomic DNA. Translation: EAW60803.1.
BC032743 mRNA. Translation: AAH32743.1.
BC039907 mRNA. Translation: AAH39907.1.
BC105977 mRNA. Translation: AAI05978.1.
U57316 Genomic DNA. Translation: AAC50641.1.

IPI

IPI00221199.
IPI00306871.

PIR

S71789.

RefSeq

NP_066564.2.

UniGene

Hs.463045

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1F68	NMR	-	A	731-832	[»]
1Z4R	X-ray	1.74	A	497-662	[»]
3D7C	X-ray	2.06	A/B	729-837	[»]

ModBase

Search...

DIP

DIP-28146N.

IntAct

Q92830. 21 interactions.

STRING

Q92830.

PhosphoSite

Q92830.

PRIDE

Q92830.

Ensembl

ENST00000225916; ENSP00000225916; ENSG00000108773; Homo sapiens. [Genome view]

GeneID

2648.

KEGG

hsa:2648.

UCSC

uc002hyx.2. human.

CTD

2648.

GeneCards

GC17M037519.

H-InvDB

HIX0013834.

HGNC

HGNC:4201. KAT2A.

MIM

602301. gene.

PharmGKB

PA28618.

GenAtlas

Search...

eggNOG

prNOG11279.

HOVERGEN

Q92830.

InParanoid

Q92830.

OMA

KTHPSAW.

OrthoDB

EOG9642Z3.

PhylomeDB

Q92830.

BRENDA

2.3.1.48. 247.

Pathway_Interaction_DB

smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.

Reactome

REACT_71. Gene Expression.

ArrayExpress

Q92830.

Bgee

Q92830.

CleanEx

HS_KAT2A.

Genevestigator

Q92830.

GermOnline

ENSG00000108773. Homo sapiens.

InterPro

IPR016181. Acyl_CoA_acyltransferase.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR000182. GCN5-rel_AcTrfase.
IPR016376. Hist_acetylase_PCAF.
IPR009464. PCAF_N.
[Graphical view]

Gene3D

G3DSA:3.40.630.30. Acyl_CoA_acyltransferase. 1 hit.
G3DSA:1.20.920.10. Bromodomain. 1 hit.

Pfam

PF00583. Acetyltransf_1. 1 hit.
PF00439. Bromodomain. 1 hit.
PF06466. PCAF_N. 1 hit.
[Graphical view]

PIRSF

PIRSF003048. Histone_acetylase_PCAF. 1 hit.

PRINTS

PR00503. BROMODOMAIN.

SMART

SM00297. BROMO. 1 hit.
[Graphical view]

PROSITE

PS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS51186. GNAT. 1 hit.
[Graphical view]

ProtoNet

Search...

SOURCE

Search...

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Entry name

KAT2A_HUMAN

Accession

Primary (citable) accession number: Q92830
Secondary accession number(s): Q8N1A2, Q9UCW1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 27, 2001
Last sequence update:	October 14, 2008
Last modified:	February 9, 2010
This is version 115 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.

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Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

MIM cross-references

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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q92830-1)

Also known as: GCN5-L;

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: Q92830-2)

Also known as: GCN5-S;

The sequence of this isoform differs from the canonical sequence as follows:
1-410: Missing.