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Database: UniProt
Entry: Q92830
LinkDB: Q92830
Original site: Q92830 
ID   KAT2A_HUMAN             Reviewed;         837 AA.
AC   Q92830; Q8N1A2; Q9UCW1;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 3.
DT   23-MAY-2018, entry version 197.
DE   RecName: Full=Histone acetyltransferase KAT2A;
DE            EC=2.3.1.48 {ECO:0000269|PubMed:29211711};
DE   AltName: Full=General control of amino acid synthesis protein 5-like 2 {ECO:0000250|UniProtKB:Q9JHD2};
DE   AltName: Full=Histone acetyltransferase GCN5 {ECO:0000303|PubMed:8552087, ECO:0000303|PubMed:9611240};
DE            Short=hGCN5 {ECO:0000303|PubMed:8552087, ECO:0000303|PubMed:9611240};
DE   AltName: Full=Histone succinyltransferase KAT2A {ECO:0000305};
DE            EC=2.3.1.- {ECO:0000269|PubMed:29211711};
DE   AltName: Full=Lysine acetyltransferase 2A {ECO:0000305};
DE   AltName: Full=STAF97 {ECO:0000303|PubMed:11564863};
GN   Name=KAT2A {ECO:0000312|HGNC:HGNC:4201};
GN   Synonyms=GCN5 {ECO:0000303|PubMed:8552087},
GN   GCN5L2 {ECO:0000250|UniProtKB:Q9JHD2};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 2), AND CHARACTERIZATION.
RC   TISSUE=Testis;
RX   PubMed=8552087; DOI=10.1128/MCB.16.2.593;
RA   Candau R., Moore P.A., Wang L., Barlev N., Ying C.Y., Rosen C.A.,
RA   Berger S.L.;
RT   "Identification of human proteins functionally conserved with the
RT   yeast putative adaptors ADA2 and GCN5.";
RL   Mol. Cell. Biol. 16:593-602(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], AND ALTERNATIVE SPLICING.
RC   TISSUE=Liver;
RX   PubMed=9611240; DOI=10.1093/nar/26.12.2948;
RA   Smith E.R., Belote J.M., Schlitz R.L., Yang X.-J., Moore P.A.,
RA   Berger S.L., Nakatani Y., Allis C.D.;
RT   "Cloning of Drosophila GCN5: conserved features among metazoan GCN5
RT   family members.";
RL   Nucleic Acids Res. 26:2948-2954(1998).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Eye, Skin, and Testis;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 362-837 (ISOFORM 1).
RC   TISSUE=Brain;
RX   PubMed=8684459; DOI=10.1038/382319a0;
RA   Yang X.-J., Ogryzko V.V., Nishikawa J., Howard B.H., Nakatani Y.;
RT   "A p300/CBP-associated factor that competes with the adenoviral
RT   oncoprotein E1A.";
RL   Nature 382:319-324(1996).
RN   [6]
RP   SUBCELLULAR LOCATION, IDENTIFICATION IN THE STAGA COMPLEX WITH SUPT3H;
RP   KIAA0764; TAF5L; TAF6L; TRRAP; TADA3L; TAF10; TAF12 AND TAF9, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY.
RX   PubMed=11564863; DOI=10.1128/MCB.21.20.6782-6795.2001;
RA   Martinez E., Palhan V.B., Tjernberg A., Lymar E.S., Gamper A.M.,
RA   Kundu T.K., Chait B.T., Roeder R.G.;
RT   "Human STAGA complex is a chromatin-acetylating transcription
RT   coactivator that interacts with pre-mRNA splicing and DNA damage-
RT   binding factors in vivo.";
RL   Mol. Cell. Biol. 21:6782-6795(2001).
RN   [7]
RP   IDENTIFICATION IN THE TFTC-HAT COMPLEX WITH TAF5L; TAF6L; TADA3L;
RP   SUPT3H; TAF2; TAF4; TAF5; TRRAP AND TAF10.
RX   PubMed=10373431; DOI=10.1074/jbc.274.26.18285;
RA   Brand M., Yamamoto K., Staub A., Tora L.;
RT   "Identification of TATA-binding protein-free TAFII-containing complex
RT   subunits suggests a role in nucleosome acetylation and signal
RT   transduction.";
RL   J. Biol. Chem. 274:18285-18289(1999).
RN   [8]
RP   INTERACTION WITH TRRAP.
RX   PubMed=10611234; DOI=10.1128/MCB.20.2.556-562.2000;
RA   McMahon S.B., Wood M.A., Cole M.D.;
RT   "The essential cofactor TRRAP recruits the histone acetyltransferase
RT   hGCN5 to c-Myc.";
RL   Mol. Cell. Biol. 20:556-562(2000).
RN   [9]
RP   FUNCTION (MICROBIAL INFECTION), AND INTERACTION WITH HIV-1 TAT.
RX   PubMed=11384967; DOI=10.1074/jbc.M101385200;
RA   Col E., Caron C., Seigneurin-Berny D., Gracia J., Favier A.,
RA   Khochbin S.;
RT   "The histone acetyltransferase, hGCN5, interacts with and acetylates
RT   the HIV transactivator, Tat.";
RL   J. Biol. Chem. 276:28179-28184(2001).
RN   [10]
RP   INTERACTION WITH TAF3.
RX   PubMed=11438666; DOI=10.1128/MCB.21.15.5109-5121.2001;
RA   Gangloff Y.G., Pointud J.-C., Thuault S., Carre L., Romier C.,
RA   Muratoglu S., Brand M., Tora L., Couderc J.-L., Davidson I.;
RT   "The TFIID components human TAFII140 and Drosophila BIP2 (TAFII155)
RT   are novel metazoan homologues of yeast TAFII47 containing a histone
RT   fold and a PHD finger.";
RL   Mol. Cell. Biol. 21:5109-5121(2001).
RN   [11]
RP   INTERACTION WITH TACC1; TACC2 AND TACC3.
RX   PubMed=14767476; DOI=10.1038/sj.onc.1207424;
RA   Gangisetty O., Lauffart B., Sondarva G.V., Chelsea D.M., Still I.H.;
RT   "The transforming acidic coiled coil proteins interact with nuclear
RT   histone acetyltransferases.";
RL   Oncogene 23:2559-2563(2004).
RN   [12]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=15592455; DOI=10.1038/nbt1046;
RA   Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA   Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT   "Immunoaffinity profiling of tyrosine phosphorylation in cancer
RT   cells.";
RL   Nat. Biotechnol. 23:94-101(2005).
RN   [13]
RP   FUNCTION, AND INTERACTION WITH CEBPB.
RX   PubMed=17301242; DOI=10.1073/pnas.0607378104;
RA   Wiper-Bergeron N., Salem H.A., Tomlinson J.J., Wu D., Hache R.J.;
RT   "Glucocorticoid-stimulated preadipocyte differentiation is mediated
RT   through acetylation of C/EBPbeta by GCN5.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2703-2708(2007).
RN   [14]
RP   IDENTIFICATION IN STAGA COMPLEX.
RX   PubMed=18206972; DOI=10.1016/j.molcel.2007.12.011;
RA   Zhao Y., Lang G., Ito S., Bonnet J., Metzger E., Sawatsubashi S.,
RA   Suzuki E., Le Guezennec X., Stunnenberg H.G., Krasnov A.,
RA   Georgieva S.G., Schuele R., Takeyama K., Kato S., Tora L., Devys D.;
RT   "A TFTC/STAGA module mediates histone H2A and H2B deubiquitination,
RT   coactivates nuclear receptors, and counteracts heterochromatin
RT   silencing.";
RL   Mol. Cell 29:92-101(2008).
RN   [15]
RP   FUNCTION, AND IDENTIFICATION IN ATAC COMPLEX.
RX   PubMed=19103755; DOI=10.1128/MCB.01599-08;
RA   Guelman S., Kozuka K., Mao Y., Pham V., Solloway M.J., Wang J., Wu J.,
RA   Lill J.R., Zha J.;
RT   "The double-histone-acetyltransferase complex ATAC is essential for
RT   mammalian development.";
RL   Mol. Cell. Biol. 29:1176-1188(2009).
RN   [16]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA   Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA   Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-
RT   terminal acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [17]
RP   FUNCTION, AND INTERACTION WITH TBX5.
RX   PubMed=29174768; DOI=10.1016/j.yjmcc.2017.11.013;
RA   Ghosh T.K., Aparicio-Sanchez J.J., Buxton S., Ketley A., Mohamed T.,
RA   Rutland C.S., Loughna S., Brook J.D.;
RT   "Acetylation of TBX5 by KAT2B and KAT2A regulates heart and limb
RT   development.";
RL   J. Mol. Cell. Cardiol. 114:185-198(2017).
RN   [18]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-728; LYS-759 AND LYS-791,
RP   AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-
RT   modification with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [19]
RP   STRUCTURE BY NMR OF 730-832.
RX   PubMed=11090279; DOI=10.1006/jmbi.2000.4207;
RA   Hudson B.P., Martinez-Yamout M.A., Dyson H.J., Wright P.E.;
RT   "Solution structure and acetyl-lysine binding activity of the GCN5
RT   bromodomain.";
RL   J. Mol. Biol. 304:355-370(2000).
RN   [20]
RP   X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 497-662 IN COMPLEX WITH
RP   ACETYL-COA, AND ACTIVE SITE.
RX   PubMed=17410582; DOI=10.1002/prot.21407;
RA   Schuetz A., Bernstein G., Dong A., Antoshenko T., Wu H., Loppnau P.,
RA   Bochkarev A., Plotnikov A.N.;
RT   "Crystal structure of a binary complex between human GCN5 histone
RT   acetyltransferase domain and acetyl coenzyme A.";
RL   Proteins 68:403-407(2007).
RN   [21]
RP   X-RAY CRYSTALLOGRAPHY (2.06 ANGSTROMS) OF 729-837.
RX   PubMed=22464331; DOI=10.1016/j.cell.2012.02.013;
RA   Filippakopoulos P., Picaud S., Mangos M., Keates T., Lambert J.P.,
RA   Barsyte-Lovejoy D., Felletar I., Volkmer R., Muller S., Pawson T.,
RA   Gingras A.C., Arrowsmith C.H., Knapp S.;
RT   "Histone recognition and large-scale structural analysis of the human
RT   bromodomain family.";
RL   Cell 149:214-231(2012).
RN   [22]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH PLK4.
RX   PubMed=27796307; DOI=10.1038/ncomms13227;
RA   Fournier M., Orpinell M., Grauffel C., Scheer E., Garnier J.M., Ye T.,
RA   Chavant V., Joint M., Esashi F., Dejaegere A., Goenczy P., Tora L.;
RT   "KAT2A/KAT2B-targeted acetylome reveals a role for PLK4 acetylation in
RT   preventing centrosome amplification.";
RL   Nat. Commun. 7:13227-13227(2016).
RN   [23]
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 497-662 IN COMPLEX WITH
RP   SUCCINYL-COA, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP   PROPERTIES, DOMAIN, AND MUTAGENESIS OF TYR-645.
RX   PubMed=29211711; DOI=10.1038/nature25003;
RA   Wang Y., Guo Y.R., Liu K., Yin Z., Liu R., Xia Y., Tan L., Yang P.,
RA   Lee J.H., Li X.J., Hawke D., Zheng Y., Qian X., Lyu J., He J.,
RA   Xing D., Tao Y.J., Lu Z.;
RT   "KAT2A coupled with the alpha-KGDH complex acts as a histone H3
RT   succinyltransferase.";
RL   Nature 552:273-277(2017).
CC   -!- FUNCTION: Protein lysine acyltransferase that can act both as a
CC       acetyltransferase and succinyltransferase, depending on the
CC       context (PubMed:29211711). Acts as a histone lysine
CC       succinyltransferase: catalyzes succinylation of histone H3 on
CC       'Lys-79' (H3K79succ), with a maximum frequency around the
CC       transcription start sites of genes (PubMed:29211711).
CC       Succinylation of histones gives a specific tag for epigenetic
CC       transcription activation (PubMed:29211711). Association with the
CC       2-oxoglutarate dehydrogenase complex, which provides succinyl-CoA,
CC       is required for histone succinylation (PubMed:29211711). In
CC       different complexes, functions either as an acetyltransferase
CC       (HAT) or as a succinyltransferase: in the SAGA and ATAC complexes,
CC       acts as a histone acetyltransferase (PubMed:17301242,
CC       PubMed:19103755, PubMed:29211711). Has significant histone
CC       acetyltransferase activity with core histones, but not with
CC       nucleosome core particles (PubMed:17301242, PubMed:19103755).
CC       Acetylation of histones gives a specific tag for epigenetic
CC       transcription activation (PubMed:17301242, PubMed:19103755,
CC       PubMed:29211711). Involved in long-term memory consolidation and
CC       synaptic plasticity: acts by promoting expression of a hippocampal
CC       gene expression network linked to neuroactive receptor signaling
CC       (By similarity). Acts as a positive regulator of T-cell
CC       activation: upon TCR stimulation, recruited to the IL2 promoter
CC       following interaction with NFATC2 and catalyzes acetylation of
CC       histone H3 at Lys-9 (H3K9ac), leading to promote IL2 expression
CC       (By similarity). Also acetylates non-histone proteins, such as
CC       CEBPB, PLK4 and TBX5 (PubMed:17301242, PubMed:29174768,
CC       PubMed:27796307). Involved in heart and limb development by
CC       mediating acetylation of TBX5, acetylation regulating
CC       nucleocytoplasmic shuttling of TBX5 (PubMed:29174768). Acts as a
CC       negative regulator of centrosome amplification by mediating
CC       acetylation of PLK4 (PubMed:27796307).
CC       {ECO:0000250|UniProtKB:Q9JHD2, ECO:0000269|PubMed:17301242,
CC       ECO:0000269|PubMed:19103755, ECO:0000269|PubMed:27796307,
CC       ECO:0000269|PubMed:29174768, ECO:0000269|PubMed:29211711}.
CC   -!- FUNCTION: (Microbial infection) In case of HIV-1 infection, it is
CC       recruited by the viral protein Tat. Regulates Tat's
CC       transactivating activity and may help inducing chromatin
CC       remodeling of proviral genes. {ECO:0000269|PubMed:11384967}.
CC   -!- CATALYTIC ACTIVITY: Acetyl-CoA + [protein]-L-lysine = CoA +
CC       [protein]-N(6)-acetyl-L-lysine. {ECO:0000269|PubMed:29211711}.
CC   -!- CATALYTIC ACTIVITY: Succinyl-CoA + [protein]-L-lysine = CoA +
CC       [protein]-N(6)-succinyl-L-lysine. {ECO:0000269|PubMed:29211711}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.83 uM for acetyl-CoA {ECO:0000269|PubMed:29211711};
CC         KM=0.36 uM for succinyl-CoA {ECO:0000269|PubMed:29211711};
CC   -!- SUBUNIT: Interacts with EP300, CREBBP and ADA2. Component of the
CC       TFTC-HAT complex, at least composed of TAF5L, TAF6L, TAF3, TADA3L,
CC       SUPT3H/SPT3, TAF2/TAFII150, TAF4/TAFII135, TAF5/TAFII100,
CC       KAT2A/GCN5L2, TAF10 and TRRAP (PubMed:10373431, PubMed:10611234,
CC       PubMed:11438666). Component of the STAGA transcription
CC       coactivator-HAT complex, at least composed of SUPT3H, KAT2A,
CC       SUPT7L, TAF5L, TAF6L, TADA3L, TAD1L, TAF10, TAF12, TRRAP and TAF9
CC       (PubMed:18206972). The STAGA core complex is associated with a
CC       subcomplex required for histone deubiquitination composed of
CC       ATXN7L3, ENY2 and USP22 (PubMed:18206972). Component of the ADA2A-
CC       containing complex (ATAC), composed of KAT14, KAT2A, TADA2L,
CC       TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1
CC       (PubMed:19103755). In the complex, it probably interacts directly
CC       with KAT14, MBIP and WDR5 (PubMed:19103755). Interacts with PML
CC       (By similarity). Interacts with CEBPB (PubMed:17301242). Interacts
CC       with TACC1, TACC2 and TACC3 (PubMed:14767476). Interacts with RELA
CC       (By similarity). Interacts with NFATC2 (By similarity). Interacts
CC       with TBX5 (PubMed:29174768). Interacts with PLK4
CC       (PubMed:27796307). Associates with the 2-oxoglutarate
CC       dehydrogenase complex (PubMed:29211711).
CC       {ECO:0000250|UniProtKB:Q9JHD2, ECO:0000269|PubMed:10373431,
CC       ECO:0000269|PubMed:10611234, ECO:0000269|PubMed:11438666,
CC       ECO:0000269|PubMed:14767476, ECO:0000269|PubMed:17301242,
CC       ECO:0000269|PubMed:18206972, ECO:0000269|PubMed:19103755,
CC       ECO:0000269|PubMed:27796307, ECO:0000269|PubMed:29174768,
CC       ECO:0000269|PubMed:29211711}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with and acetylates HIV-1
CC       Tat. {ECO:0000269|PubMed:11384967}.
CC   -!- INTERACTION:
CC       O75717:WDHD1; NbExp=5; IntAct=EBI-477622, EBI-3951691;
CC       Q8IYH5:ZZZ3; NbExp=2; IntAct=EBI-477622, EBI-2795524;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11564863,
CC       ECO:0000269|PubMed:27796307, ECO:0000269|PubMed:29211711}.
CC       Chromosome {ECO:0000269|PubMed:29211711}. Cytoplasm, cytoskeleton,
CC       microtubule organizing center, centrosome
CC       {ECO:0000269|PubMed:27796307}. Note=Mainly localizes to the
CC       nucleus. Also localizes to centrosomes in late G1 and around the
CC       G1/S transition, coinciding with the onset of centriole formation.
CC       {ECO:0000269|PubMed:27796307}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=GCN5-L;
CC         IsoId=Q92830-1; Sequence=Displayed;
CC       Name=2; Synonyms=GCN5-S;
CC         IsoId=Q92830-2; Sequence=VSP_000556;
CC   -!- TISSUE SPECIFICITY: Expressed in all tissues tested, with most
CC       abundant expression in ovary.
CC   -!- DOMAIN: Loop3 is required for substrate specificity and adopts
CC       different structural conformations in succinyl-CoA-bound and
CC       acetyl-CoA-bound forms. Tyr-645 has an important role in the
CC       selective binding of succinyl-CoA over acetyl-CoA.
CC       {ECO:0000269|PubMed:29211711}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. GCN5
CC       subfamily. {ECO:0000305}.
DR   EMBL; AF029777; AAC39769.1; -; mRNA.
DR   EMBL; CH471152; EAW60803.1; -; Genomic_DNA.
DR   EMBL; BC032743; AAH32743.1; -; mRNA.
DR   EMBL; BC039907; AAH39907.1; -; mRNA.
DR   EMBL; BC105977; AAI05978.1; -; mRNA.
DR   EMBL; U57316; AAC50641.1; -; Genomic_DNA.
DR   CCDS; CCDS11417.1; -. [Q92830-1]
DR   PIR; S71789; S71789.
DR   RefSeq; NP_066564.2; NM_021078.2. [Q92830-1]
DR   RefSeq; XP_016879937.1; XM_017024448.1.
DR   UniGene; Hs.463045; -.
DR   PDB; 1F68; NMR; -; A=730-832.
DR   PDB; 1Z4R; X-ray; 1.74 A; A=497-662.
DR   PDB; 3D7C; X-ray; 2.06 A; A/B=729-837.
DR   PDB; 5H84; X-ray; 2.00 A; A=497-662.
DR   PDB; 5H86; X-ray; 2.08 A; A=497-662.
DR   PDB; 5MLJ; X-ray; 1.80 A; A/B=729-837.
DR   PDB; 5TRL; X-ray; 2.30 A; A/B/C/D/E/F/G/H=497-662.
DR   PDB; 5TRM; X-ray; 2.90 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T/U/V/W/X=497-662.
DR   PDBsum; 1F68; -.
DR   PDBsum; 1Z4R; -.
DR   PDBsum; 3D7C; -.
DR   PDBsum; 5H84; -.
DR   PDBsum; 5H86; -.
DR   PDBsum; 5MLJ; -.
DR   PDBsum; 5TRL; -.
DR   PDBsum; 5TRM; -.
DR   ProteinModelPortal; Q92830; -.
DR   SMR; Q92830; -.
DR   BioGrid; 108918; 114.
DR   CORUM; Q92830; -.
DR   DIP; DIP-28146N; -.
DR   IntAct; Q92830; 38.
DR   MINT; Q92830; -.
DR   STRING; 9606.ENSP00000225916; -.
DR   BindingDB; Q92830; -.
DR   ChEMBL; CHEMBL5501; -.
DR   DrugBank; DB01992; Coenzyme A.
DR   iPTMnet; Q92830; -.
DR   PhosphoSitePlus; Q92830; -.
DR   BioMuta; KAT2A; -.
DR   DMDM; 209572743; -.
DR   EPD; Q92830; -.
DR   MaxQB; Q92830; -.
DR   PaxDb; Q92830; -.
DR   PeptideAtlas; Q92830; -.
DR   PRIDE; Q92830; -.
DR   Ensembl; ENST00000225916; ENSP00000225916; ENSG00000108773. [Q92830-1]
DR   GeneID; 2648; -.
DR   KEGG; hsa:2648; -.
DR   UCSC; uc002hyx.3; human. [Q92830-1]
DR   CTD; 2648; -.
DR   DisGeNET; 2648; -.
DR   EuPathDB; HostDB:ENSG00000108773.10; -.
DR   GeneCards; KAT2A; -.
DR   HGNC; HGNC:4201; KAT2A.
DR   HPA; HPA048958; -.
DR   MIM; 602301; gene.
DR   neXtProt; NX_Q92830; -.
DR   OpenTargets; ENSG00000108773; -.
DR   PharmGKB; PA162392664; -.
DR   eggNOG; KOG1472; Eukaryota.
DR   eggNOG; COG5076; LUCA.
DR   GeneTree; ENSGT00760000119099; -.
DR   HOGENOM; HOG000007151; -.
DR   InParanoid; Q92830; -.
DR   KO; K06062; -.
DR   OMA; NHLKDYS; -.
DR   OrthoDB; EOG091G03ZO; -.
DR   PhylomeDB; Q92830; -.
DR   TreeFam; TF105399; -.
DR   BRENDA; 2.3.1.48; 2681.
DR   Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation.
DR   Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
DR   Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
DR   Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
DR   Reactome; R-HSA-3214847; HATs acetylate histones.
DR   Reactome; R-HSA-350054; Notch-HLH transcription pathway.
DR   Reactome; R-HSA-5250924; B-WICH complex positively regulates rRNA expression.
DR   Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR   Reactome; R-HSA-73762; RNA Polymerase I Transcription Initiation.
DR   Reactome; R-HSA-8941856; RUNX3 regulates NOTCH signaling.
DR   Reactome; R-HSA-9013508; NOTCH3 Intracellular Domain Regulates Transcription.
DR   SignaLink; Q92830; -.
DR   SIGNOR; Q92830; -.
DR   ChiTaRS; KAT2A; human.
DR   EvolutionaryTrace; Q92830; -.
DR   GeneWiki; GCN5L2; -.
DR   GenomeRNAi; 2648; -.
DR   PRO; PR:Q92830; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   Bgee; ENSG00000108773; -.
DR   CleanEx; HS_KAT2A; -.
DR   ExpressionAtlas; Q92830; baseline and differential.
DR   Genevisible; Q92830; HS.
DR   GO; GO:0005671; C:Ada2/Gcn5/Ada3 transcription activator complex; IDA:BHF-UCL.
DR   GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR   GO; GO:0072686; C:mitotic spindle; IEA:Ensembl.
DR   GO; GO:0000790; C:nuclear chromatin; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0030914; C:STAGA complex; IDA:UniProtKB.
DR   GO; GO:0033276; C:transcription factor TFTC complex; IDA:UniProtKB.
DR   GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
DR   GO; GO:0010484; F:H3 histone acetyltransferase activity; IDA:BHF-UCL.
DR   GO; GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0043997; F:histone acetyltransferase activity (H4-K12 specific); IEA:Ensembl.
DR   GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
DR   GO; GO:0106078; F:histone succinyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; IDA:UniProtKB.
DR   GO; GO:0036459; F:thiol-dependent ubiquitinyl hydrolase activity; TAS:Reactome.
DR   GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR   GO; GO:0008134; F:transcription factor binding; IPI:UniProtKB.
DR   GO; GO:0071929; P:alpha-tubulin acetylation; IEA:Ensembl.
DR   GO; GO:0055007; P:cardiac muscle cell differentiation; IEA:Ensembl.
DR   GO; GO:0008283; P:cell proliferation; IEA:Ensembl.
DR   GO; GO:1990090; P:cellular response to nerve growth factor stimulus; IEA:Ensembl.
DR   GO; GO:0071356; P:cellular response to tumor necrosis factor; IEA:Ensembl.
DR   GO; GO:0006338; P:chromatin remodeling; TAS:ProtInc.
DR   GO; GO:0001816; P:cytokine production; ISS:UniProtKB.
DR   GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR   GO; GO:0016578; P:histone deubiquitination; IDA:UniProtKB.
DR   GO; GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
DR   GO; GO:0044154; P:histone H3-K14 acetylation; IEA:Ensembl.
DR   GO; GO:0106077; P:histone succinylation; IDA:UniProtKB.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0018393; P:internal peptidyl-lysine acetylation; IDA:UniProtKB.
DR   GO; GO:0048312; P:intracellular distribution of mitochondria; IEA:Ensembl.
DR   GO; GO:0060173; P:limb development; ISS:UniProtKB.
DR   GO; GO:0007616; P:long-term memory; ISS:UniProtKB.
DR   GO; GO:0022037; P:metencephalon development; IEA:Ensembl.
DR   GO; GO:0030901; P:midbrain development; IEA:Ensembl.
DR   GO; GO:0035264; P:multicellular organism growth; IEA:Ensembl.
DR   GO; GO:0046600; P:negative regulation of centriole replication; IDA:UniProtKB.
DR   GO; GO:0001843; P:neural tube closure; IEA:Ensembl.
DR   GO; GO:0031346; P:positive regulation of cell projection organization; IEA:Ensembl.
DR   GO; GO:0045815; P:positive regulation of gene expression, epigenetic; TAS:Reactome.
DR   GO; GO:0035948; P:positive regulation of gluconeogenesis by positive regulation of transcription from RNA polymerase II promoter; IEA:Ensembl.
DR   GO; GO:0035066; P:positive regulation of histone acetylation; IEA:Ensembl.
DR   GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR   GO; GO:2000679; P:positive regulation of transcription regulatory region DNA binding; IEA:Ensembl.
DR   GO; GO:0016579; P:protein deubiquitination; TAS:Reactome.
DR   GO; GO:0031647; P:regulation of protein stability; IMP:MGI.
DR   GO; GO:0045589; P:regulation of regulatory T cell differentiation; ISS:UniProtKB.
DR   GO; GO:0048167; P:regulation of synaptic plasticity; ISS:UniProtKB.
DR   GO; GO:0050863; P:regulation of T cell activation; ISS:UniProtKB.
DR   GO; GO:0006357; P:regulation of transcription by RNA polymerase II; TAS:ProtInc.
DR   GO; GO:0031667; P:response to nutrient levels; IEA:Ensembl.
DR   GO; GO:0014070; P:response to organic cyclic compound; IEA:Ensembl.
DR   GO; GO:0001756; P:somitogenesis; IEA:Ensembl.
DR   GO; GO:0021537; P:telencephalon development; IEA:Ensembl.
DR   GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
DR   GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.920.10; -; 1.
DR   InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR   InterPro; IPR001487; Bromodomain.
DR   InterPro; IPR036427; Bromodomain-like_sf.
DR   InterPro; IPR018359; Bromodomain_CS.
DR   InterPro; IPR037800; GCN5.
DR   InterPro; IPR016376; GCN5/PCAF.
DR   InterPro; IPR000182; GNAT_dom.
DR   InterPro; IPR009464; PCAF_N.
DR   PANTHER; PTHR22880:SF124; PTHR22880:SF124; 1.
DR   Pfam; PF00583; Acetyltransf_1; 1.
DR   Pfam; PF00439; Bromodomain; 1.
DR   Pfam; PF06466; PCAF_N; 1.
DR   PIRSF; PIRSF003048; Histone_acetylase_PCAF; 1.
DR   PRINTS; PR00503; BROMODOMAIN.
DR   SMART; SM00297; BROMO; 1.
DR   SUPFAM; SSF47370; SSF47370; 1.
DR   SUPFAM; SSF55729; SSF55729; 1.
DR   PROSITE; PS00633; BROMODOMAIN_1; 1.
DR   PROSITE; PS50014; BROMODOMAIN_2; 1.
DR   PROSITE; PS51186; GNAT; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Acetylation; Acyltransferase; Alternative splicing;
KW   Bromodomain; Chromosome; Complete proteome; Cytoplasm; Cytoskeleton;
KW   Host-virus interaction; Isopeptide bond; Nucleus; Reference proteome;
KW   Transcription; Transcription regulation; Transferase; Ubl conjugation.
FT   INIT_MET      1      1       Removed. {ECO:0000244|PubMed:22814378}.
FT   CHAIN         2    837       Histone acetyltransferase KAT2A.
FT                                /FTId=PRO_0000211202.
FT   DOMAIN      503    656       N-acetyltransferase.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00532}.
FT   DOMAIN      745    815       Bromo. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00035}.
FT   REGION      579    581       Acetyl-CoA and succinyl-CoA binding.
FT                                {ECO:0000244|PDB:5TRL,
FT                                ECO:0000269|PubMed:17410582,
FT                                ECO:0000269|PubMed:29211711}.
FT   REGION      586    592       Acetyl-CoA and succinyl-CoA binding.
FT                                {ECO:0000244|PDB:5TRL,
FT                                ECO:0000269|PubMed:17410582,
FT                                ECO:0000269|PubMed:29211711}.
FT   REGION      617    620       Acetyl-CoA and succinyl-CoA binding.
FT                                {ECO:0000244|PDB:5TRL,
FT                                ECO:0000269|PubMed:17410582,
FT                                ECO:0000269|PubMed:29211711}.
FT   REGION      639    648       Loop 3. {ECO:0000269|PubMed:29211711}.
FT   ACT_SITE    575    575       Proton donor/acceptor.
FT                                {ECO:0000303|PubMed:17410582}.
FT   BINDING     645    645       Succinyl-CoA. {ECO:0000244|PDB:5TRL,
FT                                ECO:0000269|PubMed:29211711}.
FT   MOD_RES       2      2       N-acetylalanine.
FT                                {ECO:0000244|PubMed:22814378}.
FT   CROSSLNK    728    728       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    759    759       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   CROSSLNK    791    791       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in SUMO2).
FT                                {ECO:0000244|PubMed:28112733}.
FT   VAR_SEQ       1    410       Missing (in isoform 2). {ECO:0000305}.
FT                                /FTId=VSP_000556.
FT   MUTAGEN     645    645       Y->A: Reduced histone succinylation
FT                                without affecting histone acetylation.
FT                                Reduced gene expression.
FT                                {ECO:0000269|PubMed:29211711}.
FT   CONFLICT    116    116       E -> G (in Ref. 1; AAC39769).
FT                                {ECO:0000305}.
FT   CONFLICT    134    134       M -> I (in Ref. 1; AAC39769).
FT                                {ECO:0000305}.
FT   CONFLICT    269    269       K -> E (in Ref. 1; AAC39769).
FT                                {ECO:0000305}.
FT   STRAND      498    504       {ECO:0000244|PDB:1Z4R}.
FT   HELIX       514    530       {ECO:0000244|PDB:1Z4R}.
FT   HELIX       536    543       {ECO:0000244|PDB:1Z4R}.
FT   STRAND      549    555       {ECO:0000244|PDB:1Z4R}.
FT   STRAND      558    568       {ECO:0000244|PDB:1Z4R}.
FT   TURN        569    572       {ECO:0000244|PDB:1Z4R}.
FT   STRAND      573    581       {ECO:0000244|PDB:1Z4R}.
FT   HELIX       583    585       {ECO:0000244|PDB:1Z4R}.
FT   STRAND      587    589       {ECO:0000244|PDB:1Z4R}.
FT   HELIX       590    604       {ECO:0000244|PDB:1Z4R}.
FT   STRAND      609    614       {ECO:0000244|PDB:1Z4R}.
FT   HELIX       616    618       {ECO:0000244|PDB:1Z4R}.
FT   HELIX       619    624       {ECO:0000244|PDB:1Z4R}.
FT   STRAND      627    629       {ECO:0000244|PDB:1Z4R}.
FT   HELIX       635    638       {ECO:0000244|PDB:1Z4R}.
FT   TURN        639    641       {ECO:0000244|PDB:1Z4R}.
FT   STRAND      649    654       {ECO:0000244|PDB:1Z4R}.
FT   HELIX       730    746       {ECO:0000244|PDB:5MLJ}.
FT   HELIX       748    753       {ECO:0000244|PDB:5MLJ}.
FT   TURN        759    761       {ECO:0000244|PDB:5MLJ}.
FT   HELIX       765    768       {ECO:0000244|PDB:5MLJ}.
FT   HELIX       775    783       {ECO:0000244|PDB:5MLJ}.
FT   HELIX       790    807       {ECO:0000244|PDB:5MLJ}.
FT   STRAND      810    812       {ECO:0000244|PDB:5MLJ}.
FT   HELIX       813    831       {ECO:0000244|PDB:5MLJ}.
SQ   SEQUENCE   837 AA;  93926 MW;  728CC8ACF08600EA CRC64;
     MAEPSQAPTP APAAQPRPLQ SPAPAPTPTP APSPASAPIP TPTPAPAPAP AAAPAGSTGT
     GGPGVGSGGA GSGGDPARPG LSQQQRASQR KAQVRGLPRA KKLEKLGVFS ACKANETCKC
     NGWKNPKPPT APRMDLQQPA ANLSELCRSC EHPLADHVSH LENVSEDEIN RLLGMVVDVE
     NLFMSVHKEE DTDTKQVYFY LFKLLRKCIL QMTRPVVEGS LGSPPFEKPN IEQGVLNFVQ
     YKFSHLAPRE RQTMFELSKM FLLCLNYWKL ETPAQFRQRS QAEDVATYKV NYTRWLCYCH
     VPQSCDSLPR YETTHVFGRS LLRSIFTVTR RQLLEKFRVE KDKLVPEKRT LILTHFPKFL
     SMLEEEIYGA NSPIWESGFT MPPSEGTQLV PRPASVSAAV VPSTPIFSPS MGGGSNSSLS
     LDSAGAEPMP GEKRTLPENL TLEDAKRLRV MGDIPMELVN EVMLTITDPA AMLGPETSLL
     SANAARDETA RLEERRGIIE FHVIGNSLTP KANRRVLLWL VGLQNVFSHQ LPRMPKEYIA
     RLVFDPKHKT LALIKDGRVI GGICFRMFPT QGFTEIVFCA VTSNEQVKGY GTHLMNHLKE
     YHIKHNILYF LTYADEYAIG YFKKQGFSKD IKVPKSRYLG YIKDYEGATL MECELNPRIP
     YTELSHIIKK QKEIIKKLIE RKQAQIRKVY PGLSCFKEGV RQIPVESVPG IRETGWKPLG
     KEKGKELKDP DQLYTTLKNL LAQIKSHPSA WPFMEPVKKS EAPDYYEVIR FPIDLKTMTE
     RLRSRYYVTR KLFVADLQRV IANCREYNPP DSEYCRCASA LEKFFYFKLK EGGLIDK
//
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