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Q92830 (KAT2A_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 159. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length837 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 acetyltransferase family. GCN5 subfamily.

Contains 1 bromo domain.

Contains 1 N-acetyltransferase domain.

Ontologies

Keywords
   Biological processHost-virus interaction
Transcription
Transcription regulation
   Cellular componentNucleus
   Coding sequence diversityAlternative splicing
   DomainBromodomain
   Molecular functionAcyltransferase
Transferase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell proliferation

Inferred from electronic annotation. Source: Ensembl

chromatin organization

Traceable author statement. Source: Reactome

chromatin remodeling

Traceable author statement Ref.1. Source: ProtInc

histone H3 acetylation

Inferred from direct assay Ref.7Ref.6. Source: UniProtKB

histone H3-K14 acetylation

Inferred from electronic annotation. Source: Ensembl

histone deubiquitination

Inferred from direct assay Ref.13. Source: UniProtKB

in utero embryonic development

Inferred from electronic annotation. Source: Ensembl

metencephalon development

Inferred from electronic annotation. Source: Ensembl

midbrain development

Inferred from electronic annotation. Source: Ensembl

multicellular organism growth

Inferred from electronic annotation. Source: Ensembl

neural tube closure

Inferred from electronic annotation. Source: Ensembl

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: Ensembl

telencephalon development

Inferred from electronic annotation. Source: Ensembl

transcription from RNA polymerase II promoter

Traceable author statement Ref.1. Source: ProtInc

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentAda2/Gcn5/Ada3 transcription activator complex

Inferred from direct assay PubMed 18838386. Source: BHF-UCL

STAGA complex

Inferred from direct assay Ref.6. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 22664934. Source: UniProt

mitotic spindle

Inferred from electronic annotation. Source: Ensembl

nucleoplasm

Traceable author statement. Source: Reactome

transcription factor TFTC complex

Inferred from direct assay Ref.7. Source: UniProtKB

   Molecular_functionH3 histone acetyltransferase activity

Inferred from direct assay PubMed 18838386. Source: BHF-UCL

chromatin binding

Inferred from electronic annotation. Source: Ensembl

histone acetyltransferase activity

Inferred from direct assay Ref.7. Source: UniProtKB

histone acetyltransferase activity (H4-K12 specific)

Inferred from electronic annotation. Source: Ensembl

histone deacetylase binding

Inferred from physical interaction PubMed 12887892. Source: UniProtKB

protein binding

Inferred from physical interaction PubMed 17664281. Source: UniProtKB

transcription coactivator activity

Inferred from direct assay Ref.6. Source: UniProtKB

Complete GO annotation...

Binary interactions

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.15
Chain2 – 837836Histone acetyltransferase KAT2A
PRO_0000211202

Regions

Domain503 – 656154N-acetyltransferase
Domain745 – 81571Bromo

Amino acid modifications

Modified residue21N-acetylalanine Ref.15

Natural variations

Alternative sequence1 – 410410Missing in isoform 2.
VSP_000556

Experimental info

Sequence conflict1161E → G in AAC39769. Ref.1
Sequence conflict1341M → I in AAC39769. Ref.1
Sequence conflict2691K → E in AAC39769. Ref.1

Secondary structure

............................................ 837
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 (GCN5-L) [UniParc].

Last modified October 14, 2008. Version 3.
Checksum: 728CC8ACF08600EA

FASTA83793,926
        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) [UniParc].

Checksum: A6EAE20DB0B49ADC
Show »

FASTA42748,921

References

« Hide '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. 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 (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: SUBCELLULAR LOCATION, IDENTIFICATION IN THE STAGA COMPLEX WITH SUPT3H; KIAA0764; TAF5L; TAF6L; TRRAP; TADA3L; TAF10; TAF12 AND TAF9, IDENTIFICATION BY MASS SPECTROMETRY.
[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]"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 ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[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] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 730-832.
[17]"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.
CCDSCCDS11417.1. [Q92830-1]
PIRS71789.
RefSeqNP_066564.2. NM_021078.2. [Q92830-1]
UniGeneHs.463045.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1F68NMR-A730-832[»]
1Z4RX-ray1.74A497-662[»]
3D7CX-ray2.06A/B729-837[»]
ProteinModelPortalQ92830.
SMRQ92830. Positions 497-658, 730-835.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid108918. 103 interactions.
DIPDIP-28146N.
IntActQ92830. 36 interactions.
MINTMINT-199927.
STRING9606.ENSP00000225916.

Chemistry

ChEMBLCHEMBL5501.

PTM databases

PhosphoSiteQ92830.

Polymorphism databases

DMDM209572743.

Proteomic databases

MaxQBQ92830.
PaxDbQ92830.
PRIDEQ92830.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000225916; ENSP00000225916; ENSG00000108773. [Q92830-1]
ENST00000564173; ENSP00000456712; ENSG00000259958. [Q92830-1]
GeneID2648.
KEGGhsa:2648.
UCSCuc002hyx.2. human. [Q92830-1]

Organism-specific databases

CTD2648.
GeneCardsGC17M040265.
HGNCHGNC:4201. KAT2A.
HPAHPA048958.
MIM602301. gene.
neXtProtNX_Q92830.
PharmGKBPA162392664.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5076.
HOGENOMHOG000007151.
InParanoidQ92830.
KOK06062.
OMANSPIWES.
PhylomeDBQ92830.
TreeFamTF105399.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_116125. Disease.
REACT_172623. Chromatin organization.
REACT_1788. Transcription.
REACT_2155. NICD traffics to nucleus.
REACT_71. Gene Expression.
SignaLinkQ92830.

Gene expression databases

ArrayExpressQ92830.
BgeeQ92830.
CleanExHS_KAT2A.
GenevestigatorQ92830.

Family and domain databases

Gene3D1.20.920.10. 1 hit.
3.40.630.30. 1 hit.
InterProIPR016181. Acyl_CoA_acyltransferase.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR000182. GNAT_dom.
IPR016376. Hist_acetylase_PCAF.
IPR009464. PCAF_N.
[Graphical view]
PfamPF00583. Acetyltransf_1. 1 hit.
PF00439. Bromodomain. 1 hit.
PF06466. PCAF_N. 1 hit.
[Graphical view]
PIRSFPIRSF003048. Histone_acetylase_PCAF. 1 hit.
PRINTSPR00503. BROMODOMAIN.
SMARTSM00297. BROMO. 1 hit.
[Graphical view]
SUPFAMSSF47370. SSF47370. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEPS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSKAT2A. human.
EvolutionaryTraceQ92830.
GeneWikiGCN5L2.
GenomeRNAi2648.
NextBio10450.
PROQ92830.
SOURCESearch...

Entry information

Entry nameKAT2A_HUMAN
AccessionPrimary (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: July 9, 2014
This is version 159 of the entry and version 3 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 17

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