Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Histone acetyltransferase KAT2A

Gene

Kat2a

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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).By similarity

Catalytic activityi

Acetyl-CoA + [histone] = CoA + acetyl-[histone].

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei568 – 5681Proton donor/acceptorBy similarity

GO - Molecular functioni

  1. acetyltransferase activity Source: UniProtKB
  2. chromatin binding Source: MGI
  3. H3 histone acetyltransferase activity Source: MGI
  4. histone acetyltransferase activity Source: MGI
  5. histone acetyltransferase activity (H4-K12 specific) Source: MGI
  6. histone deacetylase binding Source: MGI
  7. N-acetyltransferase activity Source: MGI
  8. transcription coactivator activity Source: MGI
  9. transcription factor binding Source: UniProtKB

GO - Biological processi

  1. cell proliferation Source: MGI
  2. histone deubiquitination Source: MGI
  3. histone H3 acetylation Source: MGI
  4. histone H3-K14 acetylation Source: MGI
  5. histone H4-K12 acetylation Source: MGI
  6. in utero embryonic development Source: MGI
  7. metencephalon development Source: MGI
  8. midbrain development Source: MGI
  9. multicellular organism growth Source: MGI
  10. nervous system development Source: MGI
  11. neural tube closure Source: MGI
  12. positive regulation of gluconeogenesis by positive regulation of transcription from RNA polymerase II promoter Source: MGI
  13. regulation of protein stability Source: MGI
  14. somitogenesis Source: MGI
  15. telencephalon development Source: MGI
  16. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Acyltransferase, Transferase

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiREACT_291621. HATs acetylate histones.

Names & Taxonomyi

Protein namesi
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:
MmGCN5
Lysine acetyltransferase 2A
Gene namesi
Name:Kat2a
Synonyms:Gcn5l2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Chromosome 11

Organism-specific databases

MGIiMGI:1343101. Kat2a.

Subcellular locationi

GO - Cellular componenti

  1. Ada2/Gcn5/Ada3 transcription activator complex Source: MGI
  2. extracellular space Source: MGI
  3. histone acetyltransferase complex Source: MGI
  4. mitotic spindle Source: MGI
  5. nucleus Source: MGI
  6. STAGA complex Source: MGI
  7. transcription factor TFTC complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 830829Histone acetyltransferase KAT2APRO_0000211203Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9JHD2.
PaxDbiQ9JHD2.
PRIDEiQ9JHD2.

PTM databases

PhosphoSiteiQ9JHD2.

Expressioni

Gene expression databases

BgeeiQ9JHD2.
ExpressionAtlasiQ9JHD2. baseline and differential.
GenevestigatoriQ9JHD2.

Interactioni

Subunit structurei

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.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
TrrapQ80YV33EBI-2943116,EBI-2942477

Protein-protein interaction databases

BioGridi199867. 10 interactions.
DIPiDIP-29180N.
IntActiQ9JHD2. 55 interactions.
MINTiMINT-4617449.
STRINGi10090.ENSMUSP00000099407.

Structurei

3D structure databases

ProteinModelPortaliQ9JHD2.
SMRiQ9JHD2. Positions 490-651, 723-828.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini496 – 649154N-acetyltransferasePROSITE-ProRule annotationAdd
BLAST
Domaini738 – 80871BromoPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni572 – 5743Acetyl-CoA bindingBy similarity
Regioni579 – 5857Acetyl-CoA bindingBy similarity
Regioni610 – 6134Acetyl-CoA bindingBy similarity

Sequence similaritiesi

Contains 1 bromo domain.PROSITE-ProRule annotation
Contains 1 N-acetyltransferase domain.PROSITE-ProRule annotation

Keywords - Domaini

Bromodomain

Phylogenomic databases

eggNOGiCOG5076.
GeneTreeiENSGT00760000119099.
HOGENOMiHOG000007151.
HOVERGENiHBG051710.
InParanoidiQ9JHD2.
KOiK06062.
OMAiNSPIWES.
TreeFamiTF105399.

Family and domain databases

Gene3Di1.20.920.10. 1 hit.
3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR000182. GNAT_dom.
IPR016376. Hist_acetylase_PCAF.
IPR009464. PCAF_N.
[Graphical view]
PfamiPF13508. Acetyltransf_7. 1 hit.
PF00439. Bromodomain. 1 hit.
PF06466. PCAF_N. 1 hit.
[Graphical view]
PIRSFiPIRSF003048. Histone_acetylase_PCAF. 1 hit.
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00297. BROMO. 1 hit.
[Graphical view]
SUPFAMiSSF47370. SSF47370. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEiPS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS51186. GNAT. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9JHD2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAEPSQAPNP VPAAQPRPLH SPAPAPTSTP APSPASASTP APTPAPAPAP
60 70 80 90 100
AAAPAGSTGS GGAGVGSGGD PARPGLSQQQ RASQRKAQVR GLPRAKKLEK
110 120 130 140 150
LGVFSACKAN ETCKCNGWKN PKPPTAPRMD LQQPAANLSE LCRSCEHPLA
160 170 180 190 200
DHVSHLENVS EDEINRLLGM VVDVENLFMS VHKEEDTDTK QVYFYLFKLL
210 220 230 240 250
RKCILQMTRP VVEGSLGSPP FEKPNIEQGV LNFVQYKFSH LAPRERQTMF
260 270 280 290 300
ELSKMFLLCL NYWKLETPAQ FRQRSQSEDV ATYKVNYTRW LCYCHVPQSC
310 320 330 340 350
DSLPRYETTH VFGRSLLRSI FTVTRRQLLE KFRVEKDKLV PEKRTLILTH
360 370 380 390 400
FPKFLSMLEE EIYGANSPIW ESGFTMPPSE GTQLVPRPAT VSATVVPSFS
410 420 430 440 450
PSMGGGSNSS LSLDSAGTEP MPAGEKRKLP ENLTLEDAKR LRVMGDIPME
460 470 480 490 500
LVNEVMLTIT DPAAMLGPET SLLSANAARD ETARLEERRG IIEFHVIGNS
510 520 530 540 550
LTPKANRRVL LWLVGLQNVF SHQLPRMPKE YIARLVFDPK HKTLALIKDG
560 570 580 590 600
RVIGGICFRM FPTQGFTEIV FCAVTSNEQV KGYGTHLMNH LKEYHIKHSI
610 620 630 640 650
LYFLTYADEY AIGYFKKQGF SKDIKVPKSR YLGYIKDYEG ATLMECELNP
660 670 680 690 700
RIPYTELSHI IKKQKEIIKK LIERKQAQIR KVYPGLSCFK EGVRQIPVES
710 720 730 740 750
VPGIRETGWK PLGKEKGKEL KDPDQLYTTL KNLLAQIKSH PSAWPFMEPV
760 770 780 790 800
KKSEAPDYYE VIRFPIDLKT MTERLRSRYY VTRKLFVADL QRVIANCREY
810 820 830
NPPDSEYCRC ASALEKFFYF KLKEGGLIDK
Length:830
Mass (Da):93,394
Last modified:July 27, 2011 - v2
Checksum:i7993CFFEA4734174
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti804 – 8041D → N in AAF70497 (PubMed:9742083).Curated
Sequence conflicti815 – 8151E → K in AAF70497 (PubMed:9742083).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF254441 mRNA. Translation: AAF70497.1.
AK158079 mRNA. Translation: BAE34351.1.
AL591469 Genomic DNA. Translation: CAM22909.1.
CH466662 Genomic DNA. Translation: EDL02541.1.
CCDSiCCDS25433.1.
RefSeqiNP_064388.2. NM_020004.5.
UniGeneiMm.218837.

Genome annotation databases

EnsembliENSMUST00000103118; ENSMUSP00000099407; ENSMUSG00000020918.
GeneIDi14534.
KEGGimmu:14534.
UCSCiuc007lma.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF254441 mRNA. Translation: AAF70497.1.
AK158079 mRNA. Translation: BAE34351.1.
AL591469 Genomic DNA. Translation: CAM22909.1.
CH466662 Genomic DNA. Translation: EDL02541.1.
CCDSiCCDS25433.1.
RefSeqiNP_064388.2. NM_020004.5.
UniGeneiMm.218837.

3D structure databases

ProteinModelPortaliQ9JHD2.
SMRiQ9JHD2. Positions 490-651, 723-828.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi199867. 10 interactions.
DIPiDIP-29180N.
IntActiQ9JHD2. 55 interactions.
MINTiMINT-4617449.
STRINGi10090.ENSMUSP00000099407.

PTM databases

PhosphoSiteiQ9JHD2.

Proteomic databases

MaxQBiQ9JHD2.
PaxDbiQ9JHD2.
PRIDEiQ9JHD2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000103118; ENSMUSP00000099407; ENSMUSG00000020918.
GeneIDi14534.
KEGGimmu:14534.
UCSCiuc007lma.2. mouse.

Organism-specific databases

CTDi2648.
MGIiMGI:1343101. Kat2a.

Phylogenomic databases

eggNOGiCOG5076.
GeneTreeiENSGT00760000119099.
HOGENOMiHOG000007151.
HOVERGENiHBG051710.
InParanoidiQ9JHD2.
KOiK06062.
OMAiNSPIWES.
TreeFamiTF105399.

Enzyme and pathway databases

ReactomeiREACT_291621. HATs acetylate histones.

Miscellaneous databases

ChiTaRSiKat2a. mouse.
NextBioi286188.
PROiQ9JHD2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JHD2.
ExpressionAtlasiQ9JHD2. baseline and differential.
GenevestigatoriQ9JHD2.

Family and domain databases

Gene3Di1.20.920.10. 1 hit.
3.40.630.30. 1 hit.
InterProiIPR016181. Acyl_CoA_acyltransferase.
IPR001487. Bromodomain.
IPR018359. Bromodomain_CS.
IPR000182. GNAT_dom.
IPR016376. Hist_acetylase_PCAF.
IPR009464. PCAF_N.
[Graphical view]
PfamiPF13508. Acetyltransf_7. 1 hit.
PF00439. Bromodomain. 1 hit.
PF06466. PCAF_N. 1 hit.
[Graphical view]
PIRSFiPIRSF003048. Histone_acetylase_PCAF. 1 hit.
PRINTSiPR00503. BROMODOMAIN.
SMARTiSM00297. BROMO. 1 hit.
[Graphical view]
SUPFAMiSSF47370. SSF47370. 1 hit.
SSF55729. SSF55729. 1 hit.
PROSITEiPS00633. BROMODOMAIN_1. 1 hit.
PS50014. BROMODOMAIN_2. 1 hit.
PS51186. GNAT. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. Cited for: INTERACTION WITH PML.

Entry informationi

Entry nameiKAT2A_MOUSE
AccessioniPrimary (citable) accession number: Q9JHD2
Secondary accession number(s): Q3TZ59
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: July 27, 2011
Last modified: April 29, 2015
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.