Q92830 (KAT2A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone acetyltransferase KAT2A
EC=2.3.1.48

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

Gene names

Name:	KAT2A
Synonyms:	GCN5, GCN5L2, HGCN5

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

General annotation (Comments)

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.14
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 deubiquitination 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. Interacts with PML By similarity. Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13 Ref.14
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.

Ontologies

Keywords
Biological process	Host-virus interaction Transcription Transcription regulation
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
Domain	Bromodomain
Molecular function	Transferase
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell proliferation Inferred from electronic annotation. Source: Compara chromatin remodeling Traceable author statement Ref.1. Source: ProtInc histone H3-K14 acetylation Inferred from electronic annotation. Source: Compara histone deubiquitination Inferred from direct assay Ref.13. Source: UniProtKB in utero embryonic development Inferred from electronic annotation. Source: Compara metencephalon development Inferred from electronic annotation. Source: Compara midbrain development Inferred from electronic annotation. Source: Compara multicellular organism growth Inferred from electronic annotation. Source: Compara neural tube closure Inferred from electronic annotation. Source: Compara regulation of apoptotic process Inferred from electronic annotation. Source: Compara regulation of protein stability Inferred from mutant phenotype PubMed 20562830. Source: MGI regulation of transcription from RNA polymerase II promoter Traceable author statement Ref.1. Source: ProtInc somitogenesis Inferred from electronic annotation. Source: Compara telencephalon development Inferred from electronic annotation. Source: Compara transcription from RNA polymerase II promoter Traceable author statement Ref.1. Source: ProtInc virus-host interaction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Ada2/Gcn5/Ada3 transcription activator complex Inferred from direct assay PubMed 18838386. Source: BHF-UCL STAGA complex Inferred from direct assay Ref.6. Source: UniProtKB mitotic spindle Inferred from electronic annotation. Source: Compara transcription factor TFTC complex Inferred from direct assay Ref.7. Source: UniProtKB
Molecular_function	H3 histone acetyltransferase activity Inferred from direct assay PubMed 18838386. Source: BHF-UCL chromatin binding Inferred from electronic annotation. Source: Compara histone acetyltransferase activity (H4-K12 specific) Inferred from electronic annotation. Source: Compara transcription coactivator activity Inferred from direct assay Ref.6. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
WDHD1	O75717	5	EBI-477622,EBI-3951691

Alternative products

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.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 837

837

Histone acetyltransferase KAT2A

PRO_0000211202

Regions

Domain

503 – 656

154

N-acetyltransferase

Domain

745 – 815

71

Bromo

Natural variations

Alternative sequence

1 – 410

410

Missing in isoform 2.

VSP_000556

Experimental info

Sequence conflict

116

1

E → G in AAC39769. Ref.1

Sequence conflict

134

1

M → I in AAC39769. Ref.1

Sequence conflict

269

1

K → E in AAC39769. Ref.1

Secondary structure

1

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837

Helix Strand Turn

Details...

Beta strand

498 – 504

7

Helix

514 – 530

17

Helix

536 – 543

8

Beta strand

549 – 555

7

Beta strand

558 – 568

11

Turn

569 – 572

4

Beta strand

573 – 581

9

Helix

583 – 585

3

Beta strand

587 – 589

3

Helix

590 – 604

15

Beta strand

609 – 614

6

Helix

616 – 618

3

Helix

619 – 624

6

Beta strand

627 – 629

3

Helix

635 – 638

4

Turn

639 – 641

3

Beta strand

649 – 654

6

Helix

730 – 746

17

Helix

748 – 753

6

Turn

759 – 761

3

Helix

765 – 768

4

Helix

775 – 783

9

Helix

790 – 807

18

Helix

813 – 831

19

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 (GCN5-L) [UniParc]. Last modified October 14, 2008. Version 3. Checksum: 728CC8ACF08600EA	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
	Isoform 2 (GCN5-S) [UniParc]. Checksum: A6EAE20DB0B49ADC	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

References

	« 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] [Europe PMC] [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] [Europe PMC] [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. , 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 (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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]	"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] [Europe PMC] [Abstract] Cited for: IDENTIFICATION IN STAGA COMPLEX.
[14]	"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] [Europe PMC] [Abstract] Cited for: FUNCTION, IDENTIFICATION IN ATAC COMPLEX.
[15]	"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] [Europe PMC] [Abstract] Cited for: STRUCTURE BY NMR OF 730-832.
[16]	"Histone recognition and large-scale structural analysis of the human bromodomain family." Filippakopoulos P., Picaud S., Mangos M., Keates T., Lambert J.P., Barsyte-Lovejoy D., Felletar I., Volkmer R., Muller S., Pawson T., Gingras A.C., Arrowsmith C.H., Knapp S. Cell 149:214-231(2012) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) OF 729-837.
+	Additional computationally mapped references.

Cross-references

Sequence databases

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. NM_021078.2.

UniGene

Hs.463045.

3D structure databases

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	[»]

ProteinModelPortal

Q92830.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-28146N.

IntAct

Q92830. 21 interactions.

MINT

MINT-199927.

STRING

9606.ENSP00000225916.

PTM databases

PhosphoSite

Q92830.

Polymorphism databases

DMDM

209572743.

Proteomic databases

PaxDb

Q92830.

PRIDE

Q92830.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000225916; ENSP00000225916; ENSG00000108773.
ENST00000564173; ENSP00000456712; ENSG00000259958.

GeneID

2648.

KEGG

hsa:2648.

UCSC

uc002hyx.2. human.

Organism-specific databases

CTD

2648.

GeneCards

GC17M040265.

HGNC

HGNC:4201. KAT2A.

HPA

HPA048958.

MIM

602301. gene.

neXtProt

NX_Q92830.

PharmGKB

PA162392664.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5076.

HOGENOM

HOG000007151.

InParanoid

Q92830.

KO

K06062.

OMA

GENSPIW.

OrthoDB

EOG4F1X2G.

PhylomeDB

Q92830.

Enzyme and pathway databases

Pathway_Interaction_DB

smad2_3nuclearpathway. Regulation of nuclear SMAD2/3 signaling.

Reactome

REACT_111102. Signal Transduction.
REACT_2155. NICD traffics to nucleus.
REACT_71. Gene Expression.

Gene expression databases

Bgee

Q92830.

CleanEx

HS_KAT2A.

Genevestigator

Q92830.

GermOnline

ENSG00000108773. Homo sapiens.

Family and domain databases

Gene3D

1.20.920.10. 1 hit.
3.40.630.30. 1 hit.

InterPro

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

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]

SUPFAM

SSF55729. Acyl_CoA_acyltransferase. 1 hit.
SSF47370. Bromodomain. 1 hit.

PROSITE

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

ProtoNet

Search...

Other

ChEMBL

CHEMBL5501.

ChiTaRS

KAT2A. human.

EvolutionaryTrace

Q92830.

GenomeRNAi

2648.

NextBio

10450.

SOURCE

Search...

Entry information

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:	May 1, 2013
This is version 146 of the entry and version 3 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.