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Q9JHD2 (KAT2A_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·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=MmGCN5
Lysine acetyltransferase 2A
Gene names
Name:Kat2a
Synonyms:Gcn5l2
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length830 AA.
Sequence statusComplete.
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 By similarity. Component of the ATAC complex, a complex with histone acetyltransferase activity on histones H3 and H4 By similarity.

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, 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 By similarity. Component of the ADA2A-containing complex (ATAC), composed of CSRP2BP, KAT2A, TADA2L, TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1 By similarity. In the complex, it probably interacts directly with CSRP2BP, MBIP and WDR5 By similarity. Interacts with PML. Ref.5

Subcellular location

Nucleus.

Sequence similarities

Belongs to the GCN5 family.

Contains 1 bromo domain.

Contains 1 N-acetyltransferase domain.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentNucleus
   DomainBromodomain
   Molecular functionTransferase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell proliferation

Inferred from mutant phenotype PubMed 17325035. Source: MGI

histone H3-K14 acetylation

Inferred from direct assay PubMed 17325035. Source: MGI

histone deubiquitination

Inferred from electronic annotation. Source: Compara

in utero embryonic development

Inferred from mutant phenotype PubMed 17325035. Source: MGI

metencephalon development

Inferred from mutant phenotype PubMed 17325035. Source: MGI

midbrain development

Inferred from mutant phenotype PubMed 17325035. Source: MGI

multicellular organism growth

Inferred from mutant phenotype PubMed 17325035. Source: MGI

neural tube closure

Inferred from mutant phenotype PubMed 17325035. Source: MGI

regulation of apoptotic process

Inferred from mutant phenotype PubMed 17325035. Source: MGI

regulation of protein stability

Inferred from electronic annotation. Source: Compara

regulation of transcription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

somitogenesis

Inferred from mutant phenotype PubMed 17325035. Source: MGI

telencephalon development

Inferred from mutant phenotype PubMed 17325035. Source: MGI

transcription, DNA-dependent

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentAda2/Gcn5/Ada3 transcription activator complex

Inferred from direct assay PubMed 20562830PubMed 20508642. Source: MGI

STAGA complex

Inferred from direct assay PubMed 19103755. Source: MGI

mitotic spindle

Inferred from direct assay PubMed 20562830. Source: MGI

transcription factor TFTC complex

Inferred from electronic annotation. Source: Compara

   Molecular_functionH3 histone acetyltransferase activity

Inferred from direct assay PubMed 17325035. Source: MGI

chromatin binding

Inferred from direct assay PubMed 16109736. Source: MGI

histone acetyltransferase activity

Inferred from direct assay Ref.1. Source: MGI

histone acetyltransferase activity (H4-K12 specific)

Inferred from direct assay PubMed 17325035. Source: MGI

transcription coactivator activity

Inferred from electronic annotation. Source: Compara

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 830830Histone acetyltransferase KAT2A
PRO_0000211203

Regions

Domain496 – 649154N-acetyltransferase
Domain738 – 80871Bromo

Experimental info

Sequence conflict8041D → N in AAF70497. Ref.1
Sequence conflict8151E → K in AAF70497. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q9JHD2 [UniParc].

Last modified July 27, 2011. Version 2.
Checksum: 7993CFFEA4734174

FASTA83093,394
        10         20         30         40         50         60 
MAEPSQAPNP VPAAQPRPLH SPAPAPTSTP APSPASASTP APTPAPAPAP AAAPAGSTGS 

        70         80         90        100        110        120 
GGAGVGSGGD PARPGLSQQQ RASQRKAQVR GLPRAKKLEK LGVFSACKAN ETCKCNGWKN 

       130        140        150        160        170        180 
PKPPTAPRMD LQQPAANLSE LCRSCEHPLA DHVSHLENVS EDEINRLLGM VVDVENLFMS 

       190        200        210        220        230        240 
VHKEEDTDTK QVYFYLFKLL RKCILQMTRP VVEGSLGSPP FEKPNIEQGV LNFVQYKFSH 

       250        260        270        280        290        300 
LAPRERQTMF ELSKMFLLCL NYWKLETPAQ FRQRSQSEDV ATYKVNYTRW LCYCHVPQSC 

       310        320        330        340        350        360 
DSLPRYETTH VFGRSLLRSI FTVTRRQLLE KFRVEKDKLV PEKRTLILTH FPKFLSMLEE 

       370        380        390        400        410        420 
EIYGANSPIW ESGFTMPPSE GTQLVPRPAT VSATVVPSFS PSMGGGSNSS LSLDSAGTEP 

       430        440        450        460        470        480 
MPAGEKRKLP ENLTLEDAKR LRVMGDIPME LVNEVMLTIT DPAAMLGPET SLLSANAARD 

       490        500        510        520        530        540 
ETARLEERRG IIEFHVIGNS LTPKANRRVL LWLVGLQNVF SHQLPRMPKE YIARLVFDPK 

       550        560        570        580        590        600 
HKTLALIKDG RVIGGICFRM FPTQGFTEIV FCAVTSNEQV KGYGTHLMNH LKEYHIKHSI 

       610        620        630        640        650        660 
LYFLTYADEY AIGYFKKQGF SKDIKVPKSR YLGYIKDYEG ATLMECELNP RIPYTELSHI 

       670        680        690        700        710        720 
IKKQKEIIKK LIERKQAQIR KVYPGLSCFK EGVRQIPVES VPGIRETGWK PLGKEKGKEL 

       730        740        750        760        770        780 
KDPDQLYTTL KNLLAQIKSH PSAWPFMEPV KKSEAPDYYE VIRFPIDLKT MTERLRSRYY 

       790        800        810        820        830 
VTRKLFVADL QRVIANCREY NPPDSEYCRC ASALEKFFYF KLKEGGLIDK

« Hide

References

« Hide 'large scale' references
[1]"Mammalian GCN5 and P/CAF acetyltransferases have homologous amino-terminal domains important for recognition of nucleosomal substrates."
Xu W., Edmondson D.G., Roth S.Y.
Mol. Cell. Biol. 18:5659-5669(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: C57BL/6J.
Tissue: Inner ear.
[3]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[4]Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"A metabolic prosurvival role for PML in breast cancer."
Carracedo A., Weiss D., Leliaert A.K., Bhasin M., de Boer V.C., Laurent G., Adams A.C., Sundvall M., Song S.J., Ito K., Finley L.S., Egia A., Libermann T., Gerhart-Hines Z., Puigserver P., Haigis M.C., Maratos-Flier E., Richardson A.L., Schafer Z.T., Pandolfi P.P.
J. Clin. Invest. 122:3088-3100(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH PML.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AF254441 mRNA. Translation: AAF70497.1.
AK158079 mRNA. Translation: BAE34351.1.
AL591469 Genomic DNA. Translation: CAM22909.1.
CH466662 Genomic DNA. Translation: EDL02541.1.
IPIIPI00119270.
RefSeqNP_064388.2. NM_020004.5.
UniGeneMm.218837.

3D structure databases

ProteinModelPortalQ9JHD2.
SMRQ9JHD2. Positions 490-828.
ModBaseSearch...

Protein-protein interaction databases

DIPDIP-29180N.
IntActQ9JHD2. 15 interactions.
STRING10090.ENSMUSP00000099407.

PTM databases

PhosphoSiteQ9JHD2.

Proteomic databases

PaxDbQ9JHD2.
PRIDEQ9JHD2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000103118; ENSMUSP00000099407; ENSMUSG00000020918.
GeneID14534.
KEGGmmu:14534.

Organism-specific databases

CTD2648.
MGIMGI:1343101. Kat2a.

Phylogenomic databases

eggNOGCOG5076.
GeneTreeENSGT00660000095339.
HOGENOMHOG000007151.
HOVERGENHBG051710.
KOK06062.
OMAGENSPIW.

Gene expression databases

ArrayExpressQ9JHD2.
BgeeQ9JHD2.
GenevestigatorQ9JHD2.
GermOnlineENSMUSG00000020918. Mus musculus.

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]
PfamPF13508. Acetyltransf_7. 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]
SUPFAMSSF55729. Acyl_CoA_acyltransferase. 1 hit.
SSF47370. Bromodomain. 1 hit.
PROSITEPS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSKAT2A. mouse.
NextBio286188.
SOURCESearch...

Entry information

Entry nameKAT2A_MOUSE
AccessionPrimary (citable) accession number: Q9JHD2
Secondary accession number(s): Q3TZ59
Entry history
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: July 27, 2011
Last modified: May 1, 2013
This is version 108 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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