位置:首页 > 蛋白库 > KAT2A_HUMAN
KAT2A_HUMAN
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   03-AUG-2022, entry version 224.
DE   RecName: Full=Histone acetyltransferase KAT2A;
DE            EC=2.3.1.48 {ECO:0000269|PubMed:27377381, ECO:0000269|PubMed:29211711, ECO:0000269|PubMed:31527837};
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 glutaryltransferase KAT2A {ECO:0000305};
DE            EC=2.3.1.- {ECO:0000269|PubMed:31542297};
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:0000303|PubMed:27796307, 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; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   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 yeast
RT   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., Berger S.L.,
RA   Nakatani Y., Allis C.D.;
RT   "Cloning of Drosophila GCN5: conserved features among metazoan GCN5 family
RT   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., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., 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 project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 362-837 (ISOFORM 1), AND TISSUE
RP   SPECIFICITY.
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 oncoprotein
RT   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 coactivator
RT   that interacts with pre-mRNA splicing and DNA damage-binding factors in
RT   vivo.";
RL   Mol. Cell. Biol. 21:6782-6795(2001).
RN   [7]
RP   IDENTIFICATION IN THE TFTC-HAT COMPLEX WITH TAF5L; TAF6L; TADA3L; SUPT3H;
RP   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 hGCN5
RT   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., Khochbin S.;
RT   "The histone acetyltransferase, hGCN5, interacts with and acetylates the
RT   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) are
RT   novel metazoan homologues of yeast TAFII47 containing a histone fold and a
RT   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 histone
RT   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 cells.";
RL   Nat. Biotechnol. 23:94-101(2005).
RN   [13]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=16753578; DOI=10.1016/j.cmet.2006.04.013;
RA   Lerin C., Rodgers J.T., Kalume D.E., Kim S.H., Pandey A., Puigserver P.;
RT   "GCN5 acetyltransferase complex controls glucose metabolism through
RT   transcriptional repression of PGC-1alpha.";
RL   Cell Metab. 3:429-438(2006).
RN   [14]
RP   FUNCTION, CATALYTIC ACTIVITY, 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 through
RT   acetylation of C/EBPbeta by GCN5.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:2703-2708(2007).
RN   [15]
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., Georgieva S.G.,
RA   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 silencing.";
RL   Mol. Cell 29:92-101(2008).
RN   [16]
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   [17]
RP   FUNCTION, CATALYTIC ACTIVITY, ACETYLATION AT LYS-549, PHOSPHORYLATION AT
RP   SER-307 AND THR-735, AND MUTAGENESIS OF SER-307; LYS-549; MET-567; TYR-601;
RP   621-TYR-PHE-622 AND THR-735.
RX   PubMed=23142079; DOI=10.1016/j.molcel.2012.09.030;
RA   Dominy J.E. Jr., Lee Y., Jedrychowski M.P., Chim H., Jurczak M.J.,
RA   Camporez J.P., Ruan H.B., Feldman J., Pierce K., Mostoslavsky R.,
RA   Denu J.M., Clish C.B., Yang X., Shulman G.I., Gygi S.P., Puigserver P.;
RT   "The deacetylase Sirt6 activates the acetyltransferase GCN5 and suppresses
RT   hepatic gluconeogenesis.";
RL   Mol. Cell 48:900-913(2012).
RN   [18]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [19]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, SUBCELLULAR LOCATION,
RP   INTERACTION WITH PLK4, AND MUTAGENESIS OF GLU-575 AND ASP-615.
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   [20]
RP   FUNCTION, CATALYTIC ACTIVITY, 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   [21]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-728; LYS-759 AND LYS-791, AND
RP   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-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [22]
RP   SUBUNIT.
RX   PubMed=30109122; DOI=10.1038/s41421-018-0048-8;
RA   Wang Y., Guo Y.R., Xing D., Tao Y.J., Lu Z.;
RT   "Supramolecular assembly of KAT2A with succinyl-CoA for histone
RT   succinylation.";
RL   Cell Discov. 4:47-47(2018).
RN   [23]
RP   FUNCTION, AND INTERACTION WITH XPC.
RX   PubMed=29973595; DOI=10.1038/s41467-018-05010-0;
RA   Bidon B., Iltis I., Semer M., Nagy Z., Larnicol A., Cribier A.,
RA   Benkirane M., Coin F., Egly J.M., Le May N.;
RT   "XPC is an RNA polymerase II cofactor recruiting ATAC to promoters by
RT   interacting with E2F1.";
RL   Nat. Commun. 9:2610-2610(2018).
RN   [24]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=31542297; DOI=10.1016/j.molcel.2019.08.018;
RA   Bao X., Liu Z., Zhang W., Gladysz K., Fung Y.M.E., Tian G., Xiong Y.,
RA   Wong J.W.H., Yuen K.W.Y., Li X.D.;
RT   "Glutarylation of histone H4 lysine 91 regulates chromatin dynamics.";
RL   Mol. Cell 0:0-0(2019).
RN   [25]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVE SITE, INTERACTION WITH XPC, AND
RP   MUTAGENESIS OF GLU-575 AND ASP-615.
RX   PubMed=31527837; DOI=10.1038/s41589-019-0354-y;
RA   Semer M., Bidon B., Larnicol A., Caliskan G., Catez P., Egly J.M., Coin F.,
RA   Le May N.;
RT   "DNA repair complex licenses acetylation of H2A.Z.1 by KAT2A during
RT   transcription.";
RL   Nat. Chem. Biol. 15:992-1000(2019).
RN   [26]
RP   INTERACTION WITH ERCC3.
RX   PubMed=30894545; DOI=10.1038/s41467-019-09270-2;
RA   Sandoz J., Nagy Z., Catez P., Caliskan G., Geny S., Renaud J.B.,
RA   Concordet J.P., Poterszman A., Tora L., Egly J.M., Le May N., Coin F.;
RT   "Functional interplay between TFIIH and KAT2A regulates higher-order
RT   chromatin structure and class II gene expression.";
RL   Nat. Commun. 10:1288-1288(2019).
RN   [27]
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   [28] {ECO:0007744|PDB:1Z4R}
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   [29]
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   [30] {ECO:0007744|PDB:5H84, ECO:0007744|PDB:5H86}
RP   X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 497-662 IN COMPLEX WITH
RP   BUTYRYL-COA AND PROPIONYL-COA, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RX   PubMed=27377381; DOI=10.1107/s2059798316007907;
RA   Ringel A.E., Wolberger C.;
RT   "Structural basis for acyl-group discrimination by human Gcn5L2.";
RL   Acta Crystallogr. D 72:841-848(2016).
RN   [31] {ECO:0007744|PDB:5TRL, ECO:0007744|PDB:5TRM}
RP   X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 497-662 IN COMPLEX WITH
RP   SUCCINYL-COA, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES,
RP   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., Xing D.,
RA   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 as a
CC       acetyltransferase, glutaryltransferase or succinyltransferase,
CC       depending on the context (PubMed:29211711). Acts as a histone lysine
CC       succinyltransferase: catalyzes succinylation of histone H3 on 'Lys-79'
CC       (H3K79succ), with a maximum frequency around the transcription start
CC       sites of genes (PubMed:29211711). Succinylation of histones gives a
CC       specific tag for epigenetic transcription activation (PubMed:29211711).
CC       Association with the 2-oxoglutarate dehydrogenase complex, which
CC       provides succinyl-CoA, is required for histone succinylation
CC       (PubMed:29211711). In different complexes, functions either as an
CC       acetyltransferase (HAT) or as a succinyltransferase: in the SAGA and
CC       ATAC complexes, acts as a histone acetyltransferase (PubMed:17301242,
CC       PubMed:19103755, PubMed:29211711). Has significant histone
CC       acetyltransferase activity with core histones, but not with nucleosome
CC       core particles (PubMed:17301242, PubMed:19103755). Acetylation of
CC       histones gives a specific tag for epigenetic transcription activation
CC       (PubMed:17301242, PubMed:19103755, PubMed:29211711). Recruited by the
CC       XPC complex at promoters, where it specifically mediates acetylation of
CC       histone variant H2A.Z.1/H2A.Z, thereby promoting expression of target
CC       genes (PubMed:29973595, PubMed:31527837). Involved in long-term memory
CC       consolidation and synaptic plasticity: acts by promoting expression of
CC       a hippocampal gene expression network linked to neuroactive receptor
CC       signaling (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 histone
CC       H3 at 'Lys-9' (H3K9ac), leading to promote IL2 expression (By
CC       similarity). Required for growth and differentiation of craniofacial
CC       cartilage and bone by regulating acetylation of histone H3 at 'Lys-9'
CC       (H3K9ac) (By similarity). Regulates embryonic stem cell (ESC)
CC       pluripotency and differentiation (By similarity). Also acetylates non-
CC       histone proteins, such as CEBPB, PPARGC1A, PLK4 and TBX5
CC       (PubMed:17301242, PubMed:16753578, PubMed:27796307, PubMed:29174768).
CC       Involved in heart and limb development by mediating acetylation of
CC       TBX5, acetylation regulating nucleocytoplasmic shuttling of TBX5
CC       (PubMed:29174768). Acts as a negative regulator of centrosome
CC       amplification by mediating acetylation of PLK4 (PubMed:27796307). Acts
CC       as a negative regulator of gluconeogenesis by mediating acetylation and
CC       subsequent inactivation of PPARGC1A (PubMed:16753578, PubMed:23142079).
CC       Also acts as a histone glutaryltransferase: catalyzes glutarylation of
CC       histone H4 on 'Lys-91' (H4K91glu), a mark that destabilizes nucleosomes
CC       by promoting dissociation of the H2A-H2B dimers from nucleosomes
CC       (PubMed:31542297). {ECO:0000250|UniProtKB:Q9JHD2,
CC       ECO:0000269|PubMed:16753578, ECO:0000269|PubMed:17301242,
CC       ECO:0000269|PubMed:19103755, ECO:0000269|PubMed:23142079,
CC       ECO:0000269|PubMed:27796307, ECO:0000269|PubMed:29174768,
CC       ECO:0000269|PubMed:29211711, ECO:0000269|PubMed:29973595,
CC       ECO:0000269|PubMed:31527837, ECO:0000269|PubMed:31542297}.
CC   -!- FUNCTION: (Microbial infection) In case of HIV-1 infection, it is
CC       recruited by the viral protein Tat. Regulates Tat's transactivating
CC       activity and may help inducing chromatin remodeling of proviral genes.
CC       {ECO:0000269|PubMed:11384967}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-acetyl-L-
CC         lysyl-[protein]; Xref=Rhea:RHEA:45948, Rhea:RHEA-COMP:9752,
CC         Rhea:RHEA-COMP:10731, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930;
CC         Evidence={ECO:0000269|PubMed:16753578, ECO:0000269|PubMed:17301242,
CC         ECO:0000269|PubMed:23142079, ECO:0000269|PubMed:27796307,
CC         ECO:0000269|PubMed:29174768};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=acetyl-CoA + L-lysyl-[histone] = CoA + H(+) + N(6)-acetyl-L-
CC         lysyl-[histone]; Xref=Rhea:RHEA:21992, Rhea:RHEA-COMP:9845,
CC         Rhea:RHEA-COMP:11338, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:61930; EC=2.3.1.48;
CC         Evidence={ECO:0000269|PubMed:27377381, ECO:0000269|PubMed:29211711,
CC         ECO:0000269|PubMed:31527837};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993;
CC         Evidence={ECO:0000269|PubMed:27377381, ECO:0000269|PubMed:29211711,
CC         ECO:0000269|PubMed:31527837};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-lysyl-[protein] + succinyl-CoA = CoA + H(+) + N(6)-succinyl-
CC         L-lysyl-[protein]; Xref=Rhea:RHEA:16261, Rhea:RHEA-COMP:9752,
CC         Rhea:RHEA-COMP:11877, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:87830;
CC         Evidence={ECO:0000269|PubMed:29211711};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glutaryl-CoA + L-lysyl-[protein] = CoA + H(+) + N(6)-glutaryl-
CC         L-lysyl-[protein]; Xref=Rhea:RHEA:18009, Rhea:RHEA-COMP:9752,
CC         Rhea:RHEA-COMP:11875, ChEBI:CHEBI:15378, ChEBI:CHEBI:29969,
CC         ChEBI:CHEBI:57287, ChEBI:CHEBI:57378, ChEBI:CHEBI:87828;
CC         Evidence={ECO:0000269|PubMed:31542297};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18010;
CC         Evidence={ECO:0000269|PubMed:31542297};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=0.83 uM for acetyl-CoA {ECO:0000269|PubMed:29211711};
CC         KM=0.91 uM for acetyl-CoA {ECO:0000269|PubMed:27377381};
CC         KM=0.36 uM for succinyl-CoA {ECO:0000269|PubMed:29211711};
CC   -!- SUBUNIT: Homooligomer; may form a tetramer of homodimers
CC       (PubMed:30109122). Interacts with EP300, CREBBP and ADA2. Component of
CC       the TFTC-HAT complex, at least composed of TAF5L, TAF6L, TAF3, TADA3L,
CC       SUPT3H/SPT3, TAF2/TAFII150, TAF4/TAFII135, TAF5/TAFII100, KAT2A/GCN5L2,
CC       TAF10 and TRRAP (PubMed:10373431, PubMed:10611234, PubMed:11438666).
CC       Component of the STAGA transcription coactivator-HAT complex, at least
CC       composed of SUPT3H, KAT2A, SUPT7L, TAF5L, TAF6L, TADA3L, TAD1L, TAF10,
CC       TAF12, TRRAP and TAF9 (PubMed:18206972). The STAGA core complex is
CC       associated with a subcomplex required for histone deubiquitination
CC       composed of ATXN7L3, ENY2 and USP22 (PubMed:18206972). Component of the
CC       ADA2A-containing complex (ATAC), composed of KAT14, KAT2A, TADA2L,
CC       TADA3L, ZZ3, MBIP, WDR5, YEATS2, CCDC101 and DR1 (PubMed:19103755). In
CC       the complex, it probably interacts directly with KAT14, MBIP and WDR5
CC       (PubMed:19103755). Interacts with PML (By similarity). Interacts with
CC       CEBPB (PubMed:17301242). Interacts with TACC1, TACC2 and TACC3
CC       (PubMed:14767476). Interacts with RELA (By similarity). Interacts with
CC       NFATC2 (By similarity). Interacts with TBX5 (PubMed:29174768).
CC       Interacts with PLK4 (PubMed:27796307). Associates with the 2-
CC       oxoglutarate dehydrogenase complex (PubMed:29211711). Interacts with
CC       XPC; leading to KAT2A recruitment to promoters and subsequent
CC       acetylation of histones (PubMed:29973595, PubMed:31527837). Interacts
CC       with ERCC3/XPB; leading to KAT2A recruitment to promoters and
CC       subsequent acetylation of histones (PubMed:30894545).
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, ECO:0000269|PubMed:29973595,
CC       ECO:0000269|PubMed:30109122, ECO:0000269|PubMed:30894545,
CC       ECO:0000269|PubMed:31527837}.
CC   -!- SUBUNIT: (Microbial infection) Interacts with and acetylates HIV-1 Tat.
CC       {ECO:0000269|PubMed:11384967}.
CC   -!- INTERACTION:
CC       Q92830; Q9NY61: AATF; NbExp=4; IntAct=EBI-477622, EBI-372428;
CC       Q92830; Q01094: E2F1; NbExp=3; IntAct=EBI-477622, EBI-448924;
CC       Q92830; O75717: WDHD1; NbExp=5; IntAct=EBI-477622, EBI-3951691;
CC       Q92830; Q8IYH5: ZZZ3; NbExp=2; IntAct=EBI-477622, EBI-2795524;
CC       Q92830; P0DTC9: N; Xeno; NbExp=2; IntAct=EBI-477622, EBI-25475856;
CC       Q92830; P59595: N; Xeno; NbExp=2; IntAct=EBI-477622, EBI-7602718;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11564863,
CC       ECO:0000269|PubMed:27796307, ECO:0000269|PubMed:29211711}. Chromosome
CC       {ECO:0000269|PubMed:29211711}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome {ECO:0000269|PubMed:27796307}.
CC       Note=Mainly localizes to the nucleus (PubMed:27796307). Also localizes
CC       to centrosomes in late G1 and around the G1/S transition, coinciding
CC       with the onset of centriole formation (PubMed:27796307).
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.
CC       {ECO:0000269|PubMed:8684459}.
CC   -!- DOMAIN: Loop3 is required for substrate specificity and adopts
CC       different structural conformations in succinyl-CoA-bound and acetyl-
CC       CoA-bound forms. Tyr-645 has an important role in the selective binding
CC       of succinyl-CoA over acetyl-CoA. {ECO:0000269|PubMed:29211711}.
CC   -!- PTM: Acetylated at Lys-549, inhibiting the protein acetyltransferase
CC       activity (PubMed:23142079). Deacetylation at Lys-549 by SIRT6 promotes
CC       phosphorylation at Ser-307 and Thr-735 and subsequent activation of the
CC       protein acetyltransferase activity, leading to acetylation and
CC       inactivation of PPARGC1A (PubMed:23142079).
CC       {ECO:0000269|PubMed:23142079}.
CC   -!- SIMILARITY: Belongs to the acetyltransferase family. GCN5 subfamily.
CC       {ECO:0000305}.
CC   -!- CAUTION: According to a report, has weak protein acyltransferase
CC       activity compared to protein acetyltransferase activity
CC       (PubMed:27377381). These conclusions are however not supported by
CC       subsequent studies (PubMed:29211711, PubMed:31542297).
CC       {ECO:0000269|PubMed:27377381, ECO:0000269|PubMed:29211711,
CC       ECO:0000269|PubMed:31542297}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
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   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   PDB; 6J3P; X-ray; 1.60 A; A/B=726-837.
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   PDBsum; 6J3P; -.
DR   AlphaFoldDB; Q92830; -.
DR   SMR; Q92830; -.
DR   BioGRID; 108918; 166.
DR   ComplexPortal; CPX-900; SAGA complex, KAT2A variant.
DR   ComplexPortal; CPX-903; TFTC histone acetylation complex.
DR   ComplexPortal; CPX-997; GCN5-containing ATAC complex.
DR   CORUM; Q92830; -.
DR   DIP; DIP-28146N; -.
DR   IntAct; Q92830; 64.
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   jPOST; Q92830; -.
DR   MassIVE; Q92830; -.
DR   MaxQB; Q92830; -.
DR   PaxDb; Q92830; -.
DR   PeptideAtlas; Q92830; -.
DR   PRIDE; Q92830; -.
DR   ProteomicsDB; 75506; -. [Q92830-1]
DR   ProteomicsDB; 75507; -. [Q92830-2]
DR   Antibodypedia; 29117; 363 antibodies from 34 providers.
DR   DNASU; 2648; -.
DR   Ensembl; ENST00000225916.10; ENSP00000225916.5; ENSG00000108773.11. [Q92830-1]
DR   GeneID; 2648; -.
DR   KEGG; hsa:2648; -.
DR   MANE-Select; ENST00000225916.10; ENSP00000225916.5; NM_021078.3; NP_066564.2.
DR   UCSC; uc002hyx.3; human. [Q92830-1]
DR   CTD; 2648; -.
DR   DisGeNET; 2648; -.
DR   GeneCards; KAT2A; -.
DR   HGNC; HGNC:4201; KAT2A.
DR   HPA; ENSG00000108773; Low tissue specificity.
DR   MIM; 602301; gene.
DR   neXtProt; NX_Q92830; -.
DR   OpenTargets; ENSG00000108773; -.
DR   PharmGKB; PA162392664; -.
DR   VEuPathDB; HostDB:ENSG00000108773; -.
DR   eggNOG; KOG1472; Eukaryota.
DR   GeneTree; ENSGT00940000158799; -.
DR   HOGENOM; CLU_015901_0_0_1; -.
DR   InParanoid; Q92830; -.
DR   OMA; NHLKDYS; -.
DR   OrthoDB; 349249at2759; -.
DR   PhylomeDB; Q92830; -.
DR   TreeFam; TF105399; -.
DR   BRENDA; 2.3.1.48; 2681.
DR   PathwayCommons; Q92830; -.
DR   Reactome; R-HSA-1912408; Pre-NOTCH Transcription and Translation.
DR   Reactome; R-HSA-210744; Regulation of gene expression in late stage (branching morphogenesis) pancreatic bud precursor cells.
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   Reactome; R-HSA-9013695; NOTCH4 Intracellular Domain Regulates Transcription.
DR   SignaLink; Q92830; -.
DR   SIGNOR; Q92830; -.
DR   BioGRID-ORCS; 2648; 96 hits in 1096 CRISPR screens.
DR   ChiTaRS; KAT2A; human.
DR   EvolutionaryTrace; Q92830; -.
DR   GeneWiki; GCN5L2; -.
DR   GenomeRNAi; 2648; -.
DR   Pharos; Q92830; Tchem.
DR   PRO; PR:Q92830; -.
DR   Proteomes; UP000005640; Chromosome 17.
DR   RNAct; Q92830; protein.
DR   Bgee; ENSG00000108773; Expressed in right uterine tube and 184 other tissues.
DR   ExpressionAtlas; Q92830; baseline and differential.
DR   Genevisible; Q92830; HS.
DR   GO; GO:0140672; C:ATAC complex; IDA:BHF-UCL.
DR   GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR   GO; GO:0000785; C:chromatin; IEA:Ensembl.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR   GO; GO:0000123; C:histone acetyltransferase complex; IDA:UniProtKB.
DR   GO; GO:0072686; C:mitotic spindle; IC:ComplexPortal.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0000124; C:SAGA 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:0140297; F:DNA-binding transcription factor binding; IPI: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:0106229; F:histone glutaryltransferase activity; IDA: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:0019903; F:protein phosphatase binding; IEA:Ensembl.
DR   GO; GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
DR   GO; GO:0071929; P:alpha-tubulin acetylation; 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; IBA:GO_Central.
DR   GO; GO:0048144; P:fibroblast proliferation; IEA:Ensembl.
DR   GO; GO:0006094; P:gluconeogenesis; IEA:Ensembl.
DR   GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR   GO; GO:0016573; P:histone acetylation; IDA: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; IDA:ComplexPortal.
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:0035521; P:monoubiquitinated histone deubiquitination; IDA:ComplexPortal.
DR   GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; IDA:ComplexPortal.
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:0106227; P:peptidyl-lysine glutarylation; IDA:UniProtKB.
DR   GO; GO:2000727; P:positive regulation of cardiac muscle cell differentiation; IEA:Ensembl.
DR   GO; GO:0031346; P:positive regulation of cell projection organization; IEA:Ensembl.
DR   GO; GO:0001819; P:positive regulation of cytokine production; ISS:UniProtKB.
DR   GO; GO:0045722; P:positive regulation of gluconeogenesis; 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:0045893; P:positive regulation of transcription, DNA-templated; IDA:UniProtKB.
DR   GO; GO:1903010; P:regulation of bone development; ISS:UniProtKB.
DR   GO; GO:0061035; P:regulation of cartilage development; ISS:UniProtKB.
DR   GO; GO:0051726; P:regulation of cell cycle; IMP:ComplexPortal.
DR   GO; GO:0051302; P:regulation of cell division; IDA:ComplexPortal.
DR   GO; GO:0006282; P:regulation of DNA repair; IC:ComplexPortal.
DR   GO; GO:0045995; P:regulation of embryonic development; IEA:Ensembl.
DR   GO; GO:0031063; P:regulation of histone deacetylation; IMP:ComplexPortal.
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:0043484; P:regulation of RNA splicing; IC:ComplexPortal.
DR   GO; GO:2000036; P:regulation of stem cell population maintenance; 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; IDA:ComplexPortal.
DR   GO; GO:0006355; P:regulation of transcription, DNA-templated; IMP:ComplexPortal.
DR   GO; GO:0090043; P:regulation of tubulin deacetylation; IMP:ComplexPortal.
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   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; PTHR45750; PTHR45750; 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; Cytoplasm; Cytoskeleton; Host-virus interaction;
KW   Isopeptide bond; Nucleus; Phosphoprotein; Reference proteome;
KW   Transcription; Transcription regulation; Transferase; Ubl conjugation.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   CHAIN           2..837
FT                   /note="Histone acetyltransferase KAT2A"
FT                   /id="PRO_0000211202"
FT   DOMAIN          503..656
FT                   /note="N-acetyltransferase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT   DOMAIN          745..815
FT                   /note="Bromo"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT   REGION          1..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          407..434
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          639..648
FT                   /note="Loop 3"
FT                   /evidence="ECO:0000269|PubMed:29211711"
FT   COMPBIAS        9..51
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        407..423
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        575
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000269|PubMed:27796307,
FT                   ECO:0000269|PubMed:31527837"
FT   BINDING         579..581
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000269|PubMed:17410582,
FT                   ECO:0007744|PDB:1Z4R"
FT   BINDING         579..581
FT                   /ligand="succinyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57292"
FT                   /evidence="ECO:0000269|PubMed:29211711,
FT                   ECO:0007744|PDB:5TRL"
FT   BINDING         586..592
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000269|PubMed:17410582,
FT                   ECO:0007744|PDB:1Z4R"
FT   BINDING         586..592
FT                   /ligand="succinyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57292"
FT                   /evidence="ECO:0000269|PubMed:29211711,
FT                   ECO:0007744|PDB:5TRL"
FT   BINDING         617
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000269|PubMed:17410582,
FT                   ECO:0007744|PDB:1Z4R"
FT   BINDING         617
FT                   /ligand="succinyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57292"
FT                   /evidence="ECO:0000269|PubMed:29211711,
FT                   ECO:0007744|PDB:5TRL"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0007744|PubMed:22814378"
FT   MOD_RES         307
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:23142079"
FT   MOD_RES         549
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000269|PubMed:23142079"
FT   MOD_RES         735
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0000269|PubMed:23142079"
FT   CROSSLNK        728
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        759
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   CROSSLNK        791
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VAR_SEQ         1..410
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_000556"
FT   MUTAGEN         307
FT                   /note="S->A: Slightly reduced ability to acetylate and
FT                   inhibit PPARGC1A. Strongly reduced ability to acetylate and
FT                   inhibit PPARGC1A; when associated with A-307 and Q-549."
FT                   /evidence="ECO:0000269|PubMed:23142079"
FT   MUTAGEN         549
FT                   /note="K->Q: Mimics acetylation; reduced ability to
FT                   acetylate and inhibit PPARGC1A. Strongly reduced ability to
FT                   acetylate and inhibit PPARGC1A; when associated with A-307
FT                   and A-735."
FT                   /evidence="ECO:0000269|PubMed:23142079"
FT   MUTAGEN         567
FT                   /note="M->A: Reduced ability to acetylate and inhibit
FT                   PPARGC1A."
FT                   /evidence="ECO:0000269|PubMed:23142079"
FT   MUTAGEN         575
FT                   /note="E->A: Catalytically dead mutant; abolished
FT                   acyltransferase activity; when associated with A-615."
FT                   /evidence="ECO:0000269|PubMed:27796307,
FT                   ECO:0000269|PubMed:31527837"
FT   MUTAGEN         601
FT                   /note="Y->F: Reduced ability to acetylate and inhibit
FT                   PPARGC1A."
FT                   /evidence="ECO:0000269|PubMed:23142079"
FT   MUTAGEN         615
FT                   /note="D->A: Catalytically dead mutant; abolished
FT                   acyltransferase activity; when associated with A-575."
FT                   /evidence="ECO:0000269|PubMed:27796307,
FT                   ECO:0000269|PubMed:31527837"
FT   MUTAGEN         621..622
FT                   /note="YF->AA: Abolised protein acetyltransferase
FT                   activity."
FT                   /evidence="ECO:0000269|PubMed:23142079"
FT   MUTAGEN         645
FT                   /note="Y->A: Reduced histone succinylation without
FT                   affecting histone acetylation. Reduced gene expression."
FT                   /evidence="ECO:0000269|PubMed:29211711"
FT   MUTAGEN         735
FT                   /note="T->A: Slightly reduced ability to acetylate and
FT                   inhibit PPARGC1A. Strongly reduced ability to acetylate and
FT                   inhibit PPARGC1A; when associated with Q-549 and A-735."
FT                   /evidence="ECO:0000269|PubMed:23142079"
FT   CONFLICT        116
FT                   /note="E -> G (in Ref. 1; AAC39769)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        134
FT                   /note="M -> I (in Ref. 1; AAC39769)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        269
FT                   /note="K -> E (in Ref. 1; AAC39769)"
FT                   /evidence="ECO:0000305"
FT   STRAND          498..504
FT                   /evidence="ECO:0007829|PDB:1Z4R"
FT   HELIX           514..530
FT                   /evidence="ECO:0007829|PDB:1Z4R"
FT   HELIX           536..543
FT                   /evidence="ECO:0007829|PDB:1Z4R"
FT   STRAND          549..555
FT                   /evidence="ECO:0007829|PDB:1Z4R"
FT   STRAND          558..568
FT                   /evidence="ECO:0007829|PDB:1Z4R"
FT   TURN            569..572
FT                   /evidence="ECO:0007829|PDB:1Z4R"
FT   STRAND          573..581
FT                   /evidence="ECO:0007829|PDB:1Z4R"
FT   HELIX           583..585
FT                   /evidence="ECO:0007829|PDB:1Z4R"
FT   STRAND          587..589
FT                   /evidence="ECO:0007829|PDB:1Z4R"
FT   HELIX           590..604
FT                   /evidence="ECO:0007829|PDB:1Z4R"
FT   STRAND          609..614
FT                   /evidence="ECO:0007829|PDB:1Z4R"
FT   HELIX           616..618
FT                   /evidence="ECO:0007829|PDB:1Z4R"
FT   HELIX           619..624
FT                   /evidence="ECO:0007829|PDB:1Z4R"
FT   STRAND          627..629
FT                   /evidence="ECO:0007829|PDB:1Z4R"
FT   HELIX           635..638
FT                   /evidence="ECO:0007829|PDB:1Z4R"
FT   TURN            639..641
FT                   /evidence="ECO:0007829|PDB:1Z4R"
FT   STRAND          649..654
FT                   /evidence="ECO:0007829|PDB:1Z4R"
FT   HELIX           730..746
FT                   /evidence="ECO:0007829|PDB:6J3P"
FT   HELIX           748..753
FT                   /evidence="ECO:0007829|PDB:6J3P"
FT   TURN            759..761
FT                   /evidence="ECO:0007829|PDB:6J3P"
FT   HELIX           765..768
FT                   /evidence="ECO:0007829|PDB:6J3P"
FT   HELIX           775..783
FT                   /evidence="ECO:0007829|PDB:6J3P"
FT   HELIX           790..807
FT                   /evidence="ECO:0007829|PDB:6J3P"
FT   STRAND          810..812
FT                   /evidence="ECO:0007829|PDB:6J3P"
FT   HELIX           813..831
FT                   /evidence="ECO:0007829|PDB:6J3P"
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
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024