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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.
20-JUN-2018, entry version 153.
RecName: Full=Histone acetyltransferase KAT2A {ECO:0000305};
EC=2.3.1.48 {ECO:0000305|PubMed:28424240};
AltName: Full=General control of amino acid synthesis protein 5-like 2 {ECO:0000303|PubMed:11017084};
AltName: Full=Histone acetyltransferase GCN5 {ECO:0000303|PubMed:9742083};
Short=MmGCN5 {ECO:0000303|PubMed:9742083};
AltName: Full=Histone succinyltransferase KAT2A {ECO:0000250|UniProtKB:Q92830};
EC=2.3.1.- {ECO:0000250|UniProtKB:Q92830};
AltName: Full=Lysine acetyltransferase 2A {ECO:0000305};
Name=Kat2a {ECO:0000312|MGI:MGI:1343101};
Synonyms=Gcn5l2 {ECO:0000303|PubMed:11017084};
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]
DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
PubMed=11017084; DOI=10.1038/79973;
Xu W., Edmondson D.G., Evrard Y.A., Wakamiya M., Behringer R.R.,
Roth S.Y.;
"Loss of Gcn5l2 leads to increased apoptosis and mesodermal defects
during mouse development.";
Nat. Genet. 26:229-232(2000).
[6]
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).
[7]
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).
[8]
FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INTERACTION
WITH RELA.
PubMed=25024434; DOI=10.15252/embj.201487870;
Stilling R.M., Roenicke R., Benito E., Urbanke H., Capece V.,
Burkhardt S., Bahari-Javan S., Barth J., Sananbenesi F., Schuetz A.L.,
Dyczkowski J., Martinez-Hernandez A., Kerimoglu C., Dent S.Y.,
Bonn S., Reymann K.G., Fischer A.;
"K-Lysine acetyltransferase 2a regulates a hippocampal gene expression
network linked to memory formation.";
EMBO J. 33:1912-1927(2014).
[9]
FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DISRUPTION
PHENOTYPE, AND INTERACTION WITH NFATC2.
PubMed=28424240; DOI=10.4049/jimmunol.1600312;
Gao B., Kong Q., Zhang Y., Yun C., Dent S.Y.R., Song J., Zhang D.D.,
Wang Y., Li X., Fang D.;
"The histone acetyltransferase Gcn5 positively regulates T cell
activation.";
J. Immunol. 198:3927-3938(2017).
-!- FUNCTION: Protein lysine acyltransferase that can act both as a
acetyltransferase and succinyltransferase, depending on the
context (PubMed:28424240). Acts as a histone lysine
succinyltransferase: catalyzes succinylation of histone H3 on
'Lys-79' (H3K79succ), with a maximum frequency around the
transcription start sites of genes (By similarity). Succinylation
of histones gives a specific tag for epigenetic transcription
activation (By similarity). Association with the 2-oxoglutarate
dehydrogenase complex, which provides succinyl-CoA, is required
for histone succinylation (By similarity). In different complexes,
functions either as an acetyltransferase (HAT) or as a
succinyltransferase: in the SAGA and ATAC complexes, acts as a
histone acetyltransferase (By similarity). Has significant histone
acetyltransferase activity with core histones, but not with
nucleosome core particles (By similarity). Acetylation of histones
gives a specific tag for epigenetic transcription activation
(PubMed:28424240). Involved in long-term memory consolidation and
synaptic plasticity: acts by promoting expression of a hippocampal
gene expression network linked to neuroactive receptor signaling
(PubMed:25024434). Acts as a positive regulator of T-cell
activation: upon TCR stimulation, recruited to the IL2 promoter
following interaction with NFATC2 and catalyzes acetylation of
histone H3 at Lys-9 (H3K9ac), leading to promote IL2 expression
(PubMed:28424240). Also acetylates non-histone proteins, such as
CEBPB, PLK4 and TBX5 (PubMed:17301242). Involved in heart and limb
development by mediating acetylation of TBX5, acetylation
regulating nucleocytoplasmic shuttling of TBX5 (By similarity).
Acts as a negative regulator of centrosome amplification by
mediating acetylation of PLK4 (By similarity).
{ECO:0000250|UniProtKB:Q92830, ECO:0000269|PubMed:17301242,
ECO:0000269|PubMed:25024434, ECO:0000269|PubMed:28424240}.
-!- CATALYTIC ACTIVITY: Acetyl-CoA + [protein]-L-lysine = CoA +
[protein]-N(6)-acetyl-L-lysine. {ECO:0000305|PubMed:28424240}.
-!- CATALYTIC ACTIVITY: Succinyl-CoA + [protein]-L-lysine = CoA +
[protein]-N(6)-succinyl-L-lysine. {ECO:0000250|UniProtKB:Q92830}.
-!- SUBUNIT: Interacts with EP300, CREBBP and ADA2 (By similarity).
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 (By similarity).
Component of the STAGA transcription coactivator-HAT complex, at
least composed of SUPT3H, KAT2A, SUPT7L, TAF5L, TAF6L, TADA3L,
TAD1L, TAF10, TAF12, TRRAP and TAF9 (By similarity). 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 (PubMed:22886304). Interacts with CEBPB
(PubMed:17301242). Interacts with TACC1, TACC2 and TACC3 (By
similarity). Interacts with RELA (PubMed:25024434). Interacts with
NFATC2 (PubMed:28424240). Interacts with TBX5 (By similarity).
Interacts with PLK4 (By similarity). Associates with the 2-
oxoglutarate dehydrogenase complex (By similarity).
{ECO:0000250|UniProtKB:Q92830, ECO:0000269|PubMed:17301242,
ECO:0000269|PubMed:22886304, ECO:0000269|PubMed:25024434,
ECO:0000269|PubMed:28424240}.
-!- INTERACTION:
P28033:Cebpb; NbExp=5; IntAct=EBI-2943116, EBI-1029979;
Q80YV3:Trrap; NbExp=4; IntAct=EBI-2943116, EBI-2942477;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92830}.
Chromosome {ECO:0000269|PubMed:28424240}. Cytoplasm, cytoskeleton,
microtubule organizing center, centrosome
{ECO:0000250|UniProtKB:Q92830}. Note=Mainly localizes to the
nucleus. Also localizes to centrosomes in late G1 and around the
G1/S transition, coinciding with the onset of centriole formation.
{ECO:0000250|UniProtKB:Q92830}.
-!- TISSUE SPECIFICITY: In brain, highly expressed in the hippocampal
CA1 region (at protein level) (PubMed:25024434). Also expressed in
the hippocampal subregions CA3 and the dentate gyrus as well as in
the cortex and prefrontal cortex (PubMed:25024434). Expressed at
low level in the cerebellum (PubMed:25024434).
{ECO:0000269|PubMed:25024434}.
-!- DEVELOPMENTAL STAGE: Expressed uniformly throughout the embryo
from 7.5 to 9.0 dpc, except in the distal allantois and developing
heart. Gcn5l2 expression is down-regulated after 16.5 dpc, but is
later up-regulated in specific adult tissues.
{ECO:0000269|PubMed:11017084}.
-!- DOMAIN: Loop3 is required for substrate specificity and adopts
different structural conformations in succinyl-CoA-bound and
acetyl-CoA-bound forms. Tyr-638 has an important role in the
selective binding of succinyl-CoA over acetyl-CoA.
{ECO:0000250|UniProtKB:Q92830}.
-!- DISRUPTION PHENOTYPE: Lethality during embryogenesis: embryos
develop normally to 7.5 days post coitum (dpc), but growth is
severely retarded by 8.5 dpc and embryos fail to form dorsal
mesoderm lineages, including chordamesoderm and paraxial mesoderm
(PubMed:11017084). Differentiation of extra-embryonic and cardiac
mesoderm is not affected (PubMed:11017084). Loss of the dorsal
mesoderm lineages is due to a increased apoptosis
(PubMed:11017084). Conditional knockout mice lacking Kat2a in the
excitatory neurons of the adult forebrain display impaired
hippocampus-dependent memory consolidation as well as impaired
synaptic and nuclear plasticity (PubMed:25024434). Conditional
knockout mice lacking Kat2a in T lymphocytes show defects in T-
cell activation, T-cell proliferation, IL2 production and Th1/Th17
regulatory T-cell differentiation (PubMed:28424240). Th2
regulatory T-cell differentiation is not affected
(PubMed:28424240). {ECO:0000269|PubMed:11017084,
ECO:0000269|PubMed:25024434, ECO:0000269|PubMed:28424240}.
-!- 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.
ComplexPortal; CPX-1025; GCN5-containing ATAC complex.
ComplexPortal; CPX-916; TFTC histone acetylation complex.
ComplexPortal; CPX-920; SAGA complex.
DIP; DIP-29180N; -.
IntAct; Q9JHD2; 58.
MINT; Q9JHD2; -.
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; ENSGT00920000149009; -.
HOGENOM; HOG000007151; -.
HOVERGEN; HBG051710; -.
InParanoid; Q9JHD2; -.
KO; K06062; -.
OMA; NHLKDYS; -.
OrthoDB; EOG091G03ZO; -.
TreeFam; TF105399; -.
Reactome; R-MMU-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
Reactome; R-MMU-350054; Notch-HLH transcription pathway.
Reactome; R-MMU-5250924; B-WICH complex positively regulates rRNA expression.
Reactome; R-MMU-5689880; Ub-specific processing proteases.
Reactome; R-MMU-8941856; RUNX3 regulates NOTCH signaling.
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:0005813; C:centrosome; ISS:UniProtKB.
GO; GO:0000123; C:histone acetyltransferase complex; IDA:MGI.
GO; GO:0072686; C:mitotic spindle; IDA:MGI.
GO; GO:0000790; C:nuclear chromatin; ISO:MGI.
GO; GO:0005634; C:nucleus; IDA:MGI.
GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:Ensembl.
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:UniProtKB.
GO; GO:0043997; F:histone acetyltransferase activity (H4-K12 specific); IDA:MGI.
GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
GO; GO:0106078; F:histone succinyltransferase activity; ISS:UniProtKB.
GO; GO:0008080; F:N-acetyltransferase activity; IDA:MGI.
GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; ISO:MGI.
GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
GO; GO:0071929; P:alpha-tubulin acetylation; ISO:MGI.
GO; GO:0055007; P:cardiac muscle cell differentiation; ISO:MGI.
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:0001816; P:cytokine production; IMP:UniProtKB.
GO; GO:0007507; P:heart development; ISS:UniProtKB.
GO; GO:0016578; P:histone deubiquitination; ISO:MGI.
GO; GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
GO; GO:0044154; P:histone H3-K14 acetylation; IDA:MGI.
GO; GO:0043983; P:histone H4-K12 acetylation; IDA:MGI.
GO; GO:0106077; P:histone succinylation; ISS:UniProtKB.
GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
GO; GO:0018393; P:internal peptidyl-lysine acetylation; ISO:MGI.
GO; GO:0048312; P:intracellular distribution of mitochondria; ISO:MGI.
GO; GO:0060173; P:limb development; ISS:UniProtKB.
GO; GO:0007616; P:long-term memory; IMP:UniProtKB.
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:0046600; P:negative regulation of centriole replication; ISO: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; ISO:MGI.
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; ISO:MGI.
GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; ISO:MGI.
GO; GO:0031647; P:regulation of protein stability; ISO:MGI.
GO; GO:0045589; P:regulation of regulatory T cell differentiation; IMP:UniProtKB.
GO; GO:0048167; P:regulation of synaptic plasticity; IMP:UniProtKB.
GO; GO:0050863; P:regulation of T cell activation; IMP:UniProtKB.
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; IPR037800; GCN5.
InterPro; IPR016376; GCN5/PCAF.
InterPro; IPR000182; GNAT_dom.
InterPro; IPR009464; PCAF_N.
PANTHER; PTHR22880:SF124; PTHR22880:SF124; 1.
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; Chromosome;
Complete proteome; Cytoplasm; Cytoskeleton; 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 and succinyl-CoA binding.
{ECO:0000250|UniProtKB:Q92830}.
REGION 579 585 Acetyl-CoA and succinyl-CoA binding.
{ECO:0000250|UniProtKB:Q92830}.
REGION 610 613 Acetyl-CoA and succinyl-CoA binding.
{ECO:0000250|UniProtKB:Q92830}.
ACT_SITE 568 568 Proton donor/acceptor.
{ECO:0000250|UniProtKB:Q92830}.
BINDING 638 638 Succinyl-CoA.
{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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