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Histone acetyltransferase KAT2A (EC 2.3.1.48) (General control of amino acid synthesis protein 5-like 2) (Histone acetyltransferase GCN5) (MmGCN5) (Lysine acetyltransferase 2A)

 KAT2A_MOUSE             Reviewed;         830 AA.
Q9JHD2; Q3TZ59;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 2.
25-OCT-2017, entry version 149.
RecName: Full=Histone acetyltransferase KAT2A;
EC=2.3.1.48;
AltName: Full=General control of amino acid synthesis protein 5-like 2;
AltName: Full=Histone acetyltransferase GCN5;
Short=MmGCN5;
AltName: Full=Lysine acetyltransferase 2A;
Name=Kat2a; Synonyms=Gcn5l2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=9742083; DOI=10.1128/MCB.18.10.5659;
Xu W., Edmondson D.G., Roth S.Y.;
"Mammalian GCN5 and P/CAF acetyltransferases have homologous amino-
terminal domains important for recognition of nucleosomal
substrates.";
Mol. Cell. Biol. 18:5659-5669(1998).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
STRAIN=C57BL/6J; TISSUE=Inner ear;
PubMed=16141072; DOI=10.1126/science.1112014;
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.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
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., 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.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
FUNCTION, AND INTERACTION WITH CEBPB.
PubMed=17301242; DOI=10.1073/pnas.0607378104;
Wiper-Bergeron N., Salem H.A., Tomlinson J.J., Wu D., Hache R.J.;
"Glucocorticoid-stimulated preadipocyte differentiation is mediated
through acetylation of C/EBPbeta by GCN5.";
Proc. Natl. Acad. Sci. U.S.A. 104:2703-2708(2007).
[6]
INTERACTION WITH PML.
PubMed=22886304; DOI=10.1172/JCI62129;
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.;
"A metabolic prosurvival role for PML in breast cancer.";
J. Clin. Invest. 122:3088-3100(2012).
-!- 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). Also
acetylates non-histone proteins, such as CEBPB (PubMed:17301242).
Component of the ATAC complex, a complex with histone
acetyltransferase activity on histones H3 and H4 (By similarity).
{ECO:0000250|UniProtKB:Q92830, ECO:0000269|PubMed:17301242}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + [protein]-L-lysine = CoA +
[protein]-N(6)-acetyl-L-lysine.
-!- SUBUNIT: 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 KAT14, KAT2A, TADA2L,
TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1 (By similarity).
In the complex, it probably interacts directly with KAT14, MBIP
and WDR5 (By similarity). Interacts with PML. Interacts with CEBPB
(PubMed:17301242). {ECO:0000250|UniProtKB:Q92830,
ECO:0000269|PubMed:17301242, ECO:0000269|PubMed:22886304}.
-!- INTERACTION:
P28033:Cebpb; NbExp=5; IntAct=EBI-2943116, EBI-1029979;
Q80YV3:Trrap; NbExp=4; IntAct=EBI-2943116, EBI-2942477;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- SIMILARITY: Belongs to the acetyltransferase family. GCN5
subfamily. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF254441; AAF70497.1; -; mRNA.
EMBL; AK158079; BAE34351.1; -; mRNA.
EMBL; AL591469; CAM22909.1; -; Genomic_DNA.
EMBL; CH466662; EDL02541.1; -; Genomic_DNA.
CCDS; CCDS25433.1; -.
RefSeq; NP_064388.2; NM_020004.5.
UniGene; Mm.218837; -.
ProteinModelPortal; Q9JHD2; -.
SMR; Q9JHD2; -.
BioGrid; 199867; 12.
DIP; DIP-29180N; -.
IntAct; Q9JHD2; 58.
MINT; MINT-4617449; -.
STRING; 10090.ENSMUSP00000099407; -.
iPTMnet; Q9JHD2; -.
PhosphoSitePlus; Q9JHD2; -.
EPD; Q9JHD2; -.
MaxQB; Q9JHD2; -.
PaxDb; Q9JHD2; -.
PRIDE; Q9JHD2; -.
Ensembl; ENSMUST00000103118; ENSMUSP00000099407; ENSMUSG00000020918.
GeneID; 14534; -.
KEGG; mmu:14534; -.
UCSC; uc007lma.2; mouse.
CTD; 2648; -.
MGI; MGI:1343101; Kat2a.
eggNOG; KOG1472; Eukaryota.
eggNOG; COG5076; LUCA.
GeneTree; ENSGT00760000119099; -.
HOGENOM; HOG000007151; -.
HOVERGEN; HBG051710; -.
InParanoid; Q9JHD2; -.
KO; K06062; -.
OMA; NHLKDYS; -.
OrthoDB; EOG091G03ZO; -.
TreeFam; TF105399; -.
Reactome; R-MMU-5250924; B-WICH complex positively regulates rRNA expression.
Reactome; R-MMU-5689880; Ub-specific processing proteases.
ChiTaRS; Kat2a; mouse.
PRO; PR:Q9JHD2; -.
Proteomes; UP000000589; Chromosome 11.
Bgee; ENSMUSG00000020918; -.
ExpressionAtlas; Q9JHD2; baseline and differential.
Genevisible; Q9JHD2; MM.
GO; GO:0005671; C:Ada2/Gcn5/Ada3 transcription activator complex; IDA:MGI.
GO; GO:0005615; C:extracellular space; ISO:MGI.
GO; GO:0000123; C:histone acetyltransferase complex; IDA:MGI.
GO; GO:0072686; C:mitotic spindle; IDA:MGI.
GO; GO:0000790; C:nuclear chromatin; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0030914; C:STAGA complex; IDA:MGI.
GO; GO:0033276; C:transcription factor TFTC complex; ISO:MGI.
GO; GO:0016407; F:acetyltransferase activity; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; IDA:MGI.
GO; GO:0010484; F:H3 histone acetyltransferase activity; IDA:MGI.
GO; GO:0004402; F:histone acetyltransferase activity; IDA:MGI.
GO; GO:0043997; F:histone acetyltransferase activity (H4-K12 specific); IDA:MGI.
GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
GO; GO:0008080; F:N-acetyltransferase activity; IDA:MGI.
GO; GO:0019903; F:protein phosphatase binding; IEA:Ensembl.
GO; GO:0003713; F:transcription coactivator activity; ISO:MGI.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0071929; P:alpha-tubulin acetylation; IEA:Ensembl.
GO; GO:0055007; P:cardiac muscle cell differentiation; IEA:Ensembl.
GO; GO:0008283; P:cell proliferation; IMP:MGI.
GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEA:Ensembl.
GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
GO; GO:0016578; P:histone deubiquitination; ISO:MGI.
GO; GO:0043966; P:histone H3 acetylation; ISO:MGI.
GO; GO:0044154; P:histone H3-K14 acetylation; IDA:MGI.
GO; GO:0043983; P:histone H4-K12 acetylation; IDA:MGI.
GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
GO; GO:0048312; P:intracellular distribution of mitochondria; IEA:Ensembl.
GO; GO:0022037; P:metencephalon development; IMP:MGI.
GO; GO:0030901; P:midbrain development; IMP:MGI.
GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
GO; GO:0007399; P:nervous system development; IMP:MGI.
GO; GO:0001843; P:neural tube closure; IMP:MGI.
GO; GO:0031346; P:positive regulation of cell projection organization; IEA:Ensembl.
GO; GO:0035948; P:positive regulation of gluconeogenesis by positive regulation of transcription from RNA polymerase II promoter; IGI:MGI.
GO; GO:0035066; P:positive regulation of histone acetylation; IEA:Ensembl.
GO; GO:1903955; P:positive regulation of protein targeting to mitochondrion; ISO:MGI.
GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; IEA:Ensembl.
GO; GO:1903146; P:regulation of autophagy of mitochondrion; ISO:MGI.
GO; GO:0031647; P:regulation of protein stability; ISO:MGI.
GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
GO; GO:0001756; P:somitogenesis; IMP:MGI.
GO; GO:0021537; P:telencephalon development; IMP:MGI.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
Gene3D; 1.20.920.10; -; 1.
InterPro; IPR016181; Acyl_CoA_acyltransferase.
InterPro; IPR001487; Bromodomain.
InterPro; IPR036427; Bromodomain-like_sf.
InterPro; IPR018359; Bromodomain_CS.
InterPro; IPR016376; GCN5/PCAF.
InterPro; IPR000182; GNAT_dom.
InterPro; IPR009464; PCAF_N.
Pfam; PF00583; Acetyltransf_1; 1.
Pfam; PF00439; Bromodomain; 1.
Pfam; PF06466; PCAF_N; 1.
PIRSF; PIRSF003048; Histone_acetylase_PCAF; 1.
PRINTS; PR00503; BROMODOMAIN.
SMART; SM00297; BROMO; 1.
SUPFAM; SSF47370; SSF47370; 1.
SUPFAM; SSF55729; SSF55729; 1.
PROSITE; PS00633; BROMODOMAIN_1; 1.
PROSITE; PS50014; BROMODOMAIN_2; 1.
PROSITE; PS51186; GNAT; 1.
1: Evidence at protein level;
Acetylation; Acyltransferase; Bromodomain; Complete proteome;
Isopeptide bond; Nucleus; Reference proteome; Transcription;
Transcription regulation; Transferase; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000250|UniProtKB:Q92830}.
CHAIN 2 830 Histone acetyltransferase KAT2A.
/FTId=PRO_0000211203.
DOMAIN 496 649 N-acetyltransferase.
{ECO:0000255|PROSITE-ProRule:PRU00532}.
DOMAIN 738 808 Bromo. {ECO:0000255|PROSITE-
ProRule:PRU00035}.
REGION 572 574 Acetyl-CoA binding.
{ECO:0000250|UniProtKB:Q92830}.
REGION 579 585 Acetyl-CoA binding.
{ECO:0000250|UniProtKB:Q92830}.
REGION 610 613 Acetyl-CoA binding.
{ECO:0000250|UniProtKB:Q92830}.
ACT_SITE 568 568 Proton donor/acceptor.
{ECO:0000250|UniProtKB:Q92830}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000250|UniProtKB:Q92830}.
CROSSLNK 721 721 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q92830}.
CROSSLNK 752 752 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q92830}.
CROSSLNK 784 784 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000250|UniProtKB:Q92830}.
CONFLICT 804 804 D -> N (in Ref. 1; AAF70497).
{ECO:0000305}.
CONFLICT 815 815 E -> K (in Ref. 1; AAF70497).
{ECO:0000305}.
SEQUENCE 830 AA; 93394 MW; 7993CFFEA4734174 CRC64;
MAEPSQAPNP VPAAQPRPLH SPAPAPTSTP APSPASASTP APTPAPAPAP AAAPAGSTGS
GGAGVGSGGD PARPGLSQQQ RASQRKAQVR GLPRAKKLEK LGVFSACKAN ETCKCNGWKN
PKPPTAPRMD LQQPAANLSE LCRSCEHPLA DHVSHLENVS EDEINRLLGM VVDVENLFMS
VHKEEDTDTK QVYFYLFKLL RKCILQMTRP VVEGSLGSPP FEKPNIEQGV LNFVQYKFSH
LAPRERQTMF ELSKMFLLCL NYWKLETPAQ FRQRSQSEDV ATYKVNYTRW LCYCHVPQSC
DSLPRYETTH VFGRSLLRSI FTVTRRQLLE KFRVEKDKLV PEKRTLILTH FPKFLSMLEE
EIYGANSPIW ESGFTMPPSE GTQLVPRPAT VSATVVPSFS PSMGGGSNSS LSLDSAGTEP
MPAGEKRKLP ENLTLEDAKR LRVMGDIPME LVNEVMLTIT DPAAMLGPET SLLSANAARD
ETARLEERRG IIEFHVIGNS LTPKANRRVL LWLVGLQNVF SHQLPRMPKE YIARLVFDPK
HKTLALIKDG RVIGGICFRM FPTQGFTEIV FCAVTSNEQV KGYGTHLMNH LKEYHIKHSI
LYFLTYADEY AIGYFKKQGF SKDIKVPKSR YLGYIKDYEG ATLMECELNP RIPYTELSHI
IKKQKEIIKK LIERKQAQIR KVYPGLSCFK EGVRQIPVES VPGIRETGWK PLGKEKGKEL
KDPDQLYTTL KNLLAQIKSH PSAWPFMEPV KKSEAPDYYE VIRFPIDLKT MTERLRSRYY
VTRKLFVADL QRVIANCREY NPPDSEYCRC ASALEKFFYF KLKEGGLIDK


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