KAT2A_MOUSE
ID KAT2A_MOUSE Reviewed; 830 AA.
AC Q9JHD2; Q3TZ59;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Histone acetyltransferase KAT2A {ECO:0000305};
DE EC=2.3.1.48 {ECO:0000305|PubMed:28424240};
DE AltName: Full=General control of amino acid synthesis protein 5-like 2 {ECO:0000303|PubMed:11017084};
DE AltName: Full=Histone acetyltransferase GCN5 {ECO:0000303|PubMed:9742083};
DE Short=MmGCN5 {ECO:0000303|PubMed:9742083};
DE AltName: Full=Histone glutaryltransferase KAT2A {ECO:0000305};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q92830};
DE AltName: Full=Histone succinyltransferase KAT2A {ECO:0000250|UniProtKB:Q92830};
DE EC=2.3.1.- {ECO:0000250|UniProtKB:Q92830};
DE AltName: Full=Lysine acetyltransferase 2A {ECO:0000305};
GN Name=Kat2a {ECO:0000312|MGI:MGI:1343101};
GN Synonyms=Gcn5l2 {ECO:0000303|PubMed:11017084};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9742083; DOI=10.1128/mcb.18.10.5659;
RA Xu W., Edmondson D.G., Roth S.Y.;
RT "Mammalian GCN5 and P/CAF acetyltransferases have homologous amino-terminal
RT domains important for recognition of nucleosomal substrates.";
RL Mol. Cell. Biol. 18:5659-5669(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Inner ear;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=11017084; DOI=10.1038/79973;
RA Xu W., Edmondson D.G., Evrard Y.A., Wakamiya M., Behringer R.R., Roth S.Y.;
RT "Loss of Gcn5l2 leads to increased apoptosis and mesodermal defects during
RT mouse development.";
RL Nat. Genet. 26:229-232(2000).
RN [6]
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 through
RT acetylation of C/EBPbeta by GCN5.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:2703-2708(2007).
RN [7]
RP INTERACTION WITH PML.
RX PubMed=22886304; DOI=10.1172/jci62129;
RA Carracedo A., Weiss D., Leliaert A.K., Bhasin M., de Boer V.C., Laurent G.,
RA Adams A.C., Sundvall M., Song S.J., Ito K., Finley L.S., Egia A.,
RA Libermann T., Gerhart-Hines Z., Puigserver P., Haigis M.C.,
RA Maratos-Flier E., Richardson A.L., Schafer Z.T., Pandolfi P.P.;
RT "A metabolic prosurvival role for PML in breast cancer.";
RL J. Clin. Invest. 122:3088-3100(2012).
RN [8]
RP FUNCTION, DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND INTERACTION WITH
RP RELA.
RX PubMed=25024434; DOI=10.15252/embj.201487870;
RA Stilling R.M., Roenicke R., Benito E., Urbanke H., Capece V., Burkhardt S.,
RA Bahari-Javan S., Barth J., Sananbenesi F., Schuetz A.L., Dyczkowski J.,
RA Martinez-Hernandez A., Kerimoglu C., Dent S.Y., Bonn S., Reymann K.G.,
RA Fischer A.;
RT "K-Lysine acetyltransferase 2a regulates a hippocampal gene expression
RT network linked to memory formation.";
RL EMBO J. 33:1912-1927(2014).
RN [9]
RP FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE,
RP AND INTERACTION WITH NFATC2.
RX PubMed=28424240; DOI=10.4049/jimmunol.1600312;
RA Gao B., Kong Q., Zhang Y., Yun C., Dent S.Y.R., Song J., Zhang D.D.,
RA Wang Y., Li X., Fang D.;
RT "The histone acetyltransferase Gcn5 positively regulates T cell
RT activation.";
RL J. Immunol. 198:3927-3938(2017).
RN [10]
RP FUNCTION.
RX PubMed=30424580; DOI=10.3390/jdb6040027;
RA Sen R., Pezoa S.A., Carpio Shull L., Hernandez-Lagunas L., Niswander L.A.,
RA Artinger K.B.;
RT "Kat2a and Kat2b acetyltransferase activity regulates craniofacial
RT cartilage and bone differentiation in zebrafish and mice.";
RL J. Dev. Biol. 6:0-0(2018).
RN [11]
RP FUNCTION.
RX PubMed=30270482; DOI=10.1002/stem.2919;
RA Moris N., Edri S., Seyres D., Kulkarni R., Domingues A.F., Balayo T.,
RA Frontini M., Pina C.;
RT "Histone acetyltransferase KAT2A stabilizes pluripotency with control of
RT transcriptional heterogeneity.";
RL Stem Cells 36:1828-1838(2018).
CC -!- FUNCTION: Protein lysine acyltransferase that can act as a
CC acetyltransferase, glutaryltransferase or succinyltransferase,
CC depending on the context (PubMed:28424240). 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 (By similarity). Succinylation of histones gives a
CC specific tag for epigenetic transcription activation (By similarity).
CC Association with the 2-oxoglutarate dehydrogenase complex, which
CC provides succinyl-CoA, is required for histone succinylation (By
CC similarity). 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 (By similarity).
CC Has significant histone acetyltransferase activity with core histones,
CC but not with nucleosome core particles (By similarity). Acetylation of
CC histones gives a specific tag for epigenetic transcription activation
CC (PubMed:28424240). Recruited by the XPC complex at promoters, where it
CC specifically mediates acetylation of histone variant H2A.Z.1/H2A.Z,
CC thereby promoting expression of target genes (By similarity). Involved
CC in long-term memory consolidation and synaptic plasticity: acts by
CC promoting expression of a hippocampal gene expression network linked to
CC neuroactive receptor signaling (PubMed:25024434). Acts as a positive
CC regulator of T-cell activation: upon TCR stimulation, recruited to the
CC IL2 promoter following interaction with NFATC2 and catalyzes
CC acetylation of histone H3 at 'Lys-9' (H3K9ac), leading to promote IL2
CC expression (PubMed:28424240). Required for growth and differentiation
CC of craniofacial cartilage and bone by regulating acetylation of histone
CC H3 at 'Lys-9' (H3K9ac) (PubMed:30424580). Regulates embryonic stem cell
CC (ESC) pluripotency and differentiation (PubMed:30270482). Also
CC acetylates non-histone proteins, such as CEBPB, PPARGC1A, PLK4 and TBX5
CC (PubMed:17301242). Involved in heart and limb development by mediating
CC acetylation of TBX5, acetylation regulating nucleocytoplasmic shuttling
CC of TBX5 (By similarity). Acts as a negative regulator of centrosome
CC amplification by mediating acetylation of PLK4 (By similarity). Acts as
CC a negative regulator of gluconeogenesis by mediating acetylation and
CC subsequent inactivation of PPARGC1A (By similarity). Also acts as a
CC histone glutaryltransferase: catalyzes glutarylation of histone H4 on
CC 'Lys-91' (H4K91glu), a mark that destabilizes nucleosomes by promoting
CC dissociation of the H2A-H2B dimers from nucleosomes (By similarity).
CC {ECO:0000250|UniProtKB:Q92830, ECO:0000269|PubMed:17301242,
CC ECO:0000269|PubMed:25024434, ECO:0000269|PubMed:28424240,
CC ECO:0000269|PubMed:30270482, ECO:0000269|PubMed:30424580}.
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:0000305|PubMed:28424240};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:45949;
CC Evidence={ECO:0000305|PubMed:28424240};
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:0000305|PubMed:28424240};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:21993;
CC Evidence={ECO:0000305|PubMed:28424240};
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:0000250|UniProtKB:Q92830};
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:0000250|UniProtKB:Q92830};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:18010;
CC Evidence={ECO:0000250|UniProtKB:Q92830};
CC -!- SUBUNIT: Interacts with EP300, CREBBP and ADA2 (By similarity).
CC Component of the TFTC-HAT complex, at least composed of TAF5L, TAF6L,
CC TAF3, TADA3L, SUPT3H/SPT3, TAF2/TAFII150, TAF4/TAFII135, TAF5/TAFII100,
CC KAT2A/GCN5L2, TAF10 and TRRAP (By similarity). Component of the STAGA
CC transcription coactivator-HAT complex, at least composed of SUPT3H,
CC KAT2A, SUPT7L, TAF5L, TAF6L, TADA3L, TAD1L, TAF10, TAF12, TRRAP and
CC TAF9 (By similarity). The STAGA core complex is associated with a
CC subcomplex required for histone deubiquitination composed of ATXN7L3,
CC ENY2 and USP22 (By similarity). Component of the ADA2A-containing
CC complex (ATAC), composed of KAT14, KAT2A, TADA2L, TADA3L, ZZ3, MBIP,
CC WDR5, YEATS2, CCDC101 and DR1 (By similarity). In the complex, it
CC probably interacts directly with KAT14, MBIP and WDR5 (By similarity).
CC Interacts with PML (PubMed:22886304). Interacts with CEBPB
CC (PubMed:17301242). Interacts with TACC1, TACC2 and TACC3 (By
CC similarity). Interacts with RELA (PubMed:25024434). Interacts with
CC NFATC2 (PubMed:28424240). Interacts with TBX5 (By similarity).
CC Interacts with PLK4 (By similarity). Associates with the 2-oxoglutarate
CC dehydrogenase complex (By similarity). Interacts with XPC; leading to
CC KAT2A recruitment to promoters and subsequent acetylation of histones
CC (By similarity). Interacts with ERCC3/XPB; leading to KAT2A recruitment
CC to promoters and subsequent acetylation of histones (By similarity).
CC {ECO:0000250|UniProtKB:Q92830, ECO:0000269|PubMed:17301242,
CC ECO:0000269|PubMed:22886304, ECO:0000269|PubMed:25024434,
CC ECO:0000269|PubMed:28424240}.
CC -!- INTERACTION:
CC Q9JHD2; P28033: Cebpb; NbExp=5; IntAct=EBI-2943116, EBI-1029979;
CC Q9JHD2; Q80YV3: Trrap; NbExp=4; IntAct=EBI-2943116, EBI-2942477;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q92830}.
CC Chromosome {ECO:0000269|PubMed:28424240}. Cytoplasm, cytoskeleton,
CC microtubule organizing center, centrosome
CC {ECO:0000250|UniProtKB:Q92830}. Note=Mainly localizes to the nucleus.
CC Also localizes to centrosomes in late G1 and around the G1/S
CC transition, coinciding with the onset of centriole formation.
CC {ECO:0000250|UniProtKB:Q92830}.
CC -!- TISSUE SPECIFICITY: In brain, highly expressed in the hippocampal CA1
CC region (at protein level) (PubMed:25024434). Also expressed in the
CC hippocampal subregions CA3 and the dentate gyrus as well as in the
CC cortex and prefrontal cortex (PubMed:25024434). Expressed at low level
CC in the cerebellum (PubMed:25024434). {ECO:0000269|PubMed:25024434}.
CC -!- DEVELOPMENTAL STAGE: Expressed uniformly throughout the embryo from 7.5
CC to 9.0 dpc, except in the distal allantois and developing heart. Gcn5l2
CC expression is down-regulated after 16.5 dpc, but is later up-regulated
CC in specific adult tissues. {ECO:0000269|PubMed:11017084}.
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-638 has an important role in the selective binding
CC of succinyl-CoA over acetyl-CoA. {ECO:0000250|UniProtKB:Q92830}.
CC -!- PTM: Acetylated at Lys-542, inhibiting the protein acetyltransferase
CC activity (By similarity). Deacetylation at Lys-542 by SIRT6 promotes
CC phosphorylation at Ser-302 and Thr-728 and subsequent activation of the
CC protein acetyltransferase activity, leading to acetylation and
CC inactivation of PPARGC1A (By similarity).
CC {ECO:0000250|UniProtKB:Q92830}.
CC -!- DISRUPTION PHENOTYPE: Lethality during embryogenesis: embryos develop
CC normally to 7.5 days post coitum (dpc), but growth is severely retarded
CC by 8.5 dpc and embryos fail to form dorsal mesoderm lineages, including
CC chordamesoderm and paraxial mesoderm (PubMed:11017084). Differentiation
CC of extra-embryonic and cardiac mesoderm is not affected
CC (PubMed:11017084). Loss of the dorsal mesoderm lineages is due to an
CC increased apoptosis (PubMed:11017084). Conditional knockout mice
CC lacking Kat2a in the excitatory neurons of the adult forebrain display
CC impaired hippocampus-dependent memory consolidation as well as impaired
CC synaptic and nuclear plasticity (PubMed:25024434). Conditional knockout
CC mice lacking Kat2a in T lymphocytes show defects in T-cell activation,
CC T-cell proliferation, IL2 production and Th1/Th17 regulatory T-cell
CC differentiation (PubMed:28424240). Th2 regulatory T-cell
CC differentiation is not affected (PubMed:28424240).
CC {ECO:0000269|PubMed:11017084, ECO:0000269|PubMed:25024434,
CC ECO:0000269|PubMed:28424240}.
CC -!- SIMILARITY: Belongs to the acetyltransferase family. GCN5 subfamily.
CC {ECO:0000305}.
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DR EMBL; AF254441; AAF70497.1; -; mRNA.
DR EMBL; AK158079; BAE34351.1; -; mRNA.
DR EMBL; AL591469; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466662; EDL02541.1; -; Genomic_DNA.
DR CCDS; CCDS25433.1; -.
DR RefSeq; NP_064388.2; NM_020004.5.
DR PDB; 7BY1; X-ray; 1.80 A; A/B=67-378.
DR PDBsum; 7BY1; -.
DR AlphaFoldDB; Q9JHD2; -.
DR SMR; Q9JHD2; -.
DR BioGRID; 199867; 15.
DR ComplexPortal; CPX-1025; GCN5-containing ATAC complex.
DR ComplexPortal; CPX-916; TFTC histone acetylation complex.
DR ComplexPortal; CPX-920; SAGA complex, KAT2A variant.
DR DIP; DIP-29180N; -.
DR IntAct; Q9JHD2; 58.
DR MINT; Q9JHD2; -.
DR STRING; 10090.ENSMUSP00000099407; -.
DR iPTMnet; Q9JHD2; -.
DR PhosphoSitePlus; Q9JHD2; -.
DR EPD; Q9JHD2; -.
DR MaxQB; Q9JHD2; -.
DR PaxDb; Q9JHD2; -.
DR PRIDE; Q9JHD2; -.
DR ProteomicsDB; 301732; -.
DR Antibodypedia; 29117; 363 antibodies from 34 providers.
DR DNASU; 14534; -.
DR Ensembl; ENSMUST00000103118; ENSMUSP00000099407; ENSMUSG00000020918.
DR GeneID; 14534; -.
DR KEGG; mmu:14534; -.
DR UCSC; uc007lma.2; mouse.
DR CTD; 2648; -.
DR MGI; MGI:1343101; Kat2a.
DR VEuPathDB; HostDB:ENSMUSG00000020918; -.
DR eggNOG; KOG1472; Eukaryota.
DR GeneTree; ENSGT00940000158799; -.
DR InParanoid; Q9JHD2; -.
DR OMA; NHLKDYS; -.
DR OrthoDB; 349249at2759; -.
DR PhylomeDB; Q9JHD2; -.
DR TreeFam; TF105399; -.
DR BRENDA; 2.3.1.48; 3474.
DR Reactome; R-MMU-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
DR Reactome; R-MMU-350054; Notch-HLH transcription pathway.
DR Reactome; R-MMU-5250924; B-WICH complex positively regulates rRNA expression.
DR Reactome; R-MMU-5689880; Ub-specific processing proteases.
DR Reactome; R-MMU-8941856; RUNX3 regulates NOTCH signaling.
DR BioGRID-ORCS; 14534; 3 hits in 79 CRISPR screens.
DR ChiTaRS; Kat2a; mouse.
DR PRO; PR:Q9JHD2; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q9JHD2; protein.
DR Bgee; ENSMUSG00000020918; Expressed in internal carotid artery and 258 other tissues.
DR ExpressionAtlas; Q9JHD2; baseline and differential.
DR Genevisible; Q9JHD2; MM.
DR GO; GO:0140672; C:ATAC complex; IDA:MGI.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0000123; C:histone acetyltransferase complex; IDA:MGI.
DR GO; GO:0072686; C:mitotic spindle; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; ISO:MGI.
DR GO; GO:0000124; C:SAGA complex; IDA:MGI.
DR GO; GO:0033276; C:transcription factor TFTC complex; ISO:MGI.
DR GO; GO:0016407; F:acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0140297; F:DNA-binding transcription factor binding; IPI:UniProtKB.
DR GO; GO:0010484; F:H3 histone acetyltransferase activity; IDA:MGI.
DR GO; GO:0004402; F:histone acetyltransferase activity; IDA:UniProtKB.
DR GO; GO:0043997; F:histone acetyltransferase activity (H4-K12 specific); IDA:MGI.
DR GO; GO:0042826; F:histone deacetylase binding; ISO:MGI.
DR GO; GO:0106229; F:histone glutaryltransferase activity; ISS:UniProtKB.
DR GO; GO:0106078; F:histone succinyltransferase activity; ISS:UniProtKB.
DR GO; GO:0008080; F:N-acetyltransferase activity; IDA:MGI.
DR GO; GO:0061733; F:peptide-lysine-N-acetyltransferase activity; ISO:MGI.
DR GO; GO:0019903; F:protein phosphatase binding; ISO:MGI.
DR GO; GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
DR GO; GO:0071929; P:alpha-tubulin acetylation; ISO:MGI.
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; IMP:MGI.
DR GO; GO:0006094; P:gluconeogenesis; IGI:MGI.
DR GO; GO:0007507; P:heart development; ISS:UniProtKB.
DR GO; GO:0016573; P:histone acetylation; ISO:MGI.
DR GO; GO:0016578; P:histone deubiquitination; ISO:MGI.
DR GO; GO:0043966; P:histone H3 acetylation; IDA:UniProtKB.
DR GO; GO:0044154; P:histone H3-K14 acetylation; IDA:MGI.
DR GO; GO:0043983; P:histone H4-K12 acetylation; IDA:MGI.
DR GO; GO:0106077; P:histone succinylation; ISS:UniProtKB.
DR GO; GO:0001701; P:in utero embryonic development; IMP:MGI.
DR GO; GO:0018393; P:internal peptidyl-lysine acetylation; ISO:MGI.
DR GO; GO:0048312; P:intracellular distribution of mitochondria; ISO:MGI.
DR GO; GO:0060173; P:limb development; ISS:UniProtKB.
DR GO; GO:0007616; P:long-term memory; IMP:UniProtKB.
DR GO; GO:0022037; P:metencephalon development; IMP:MGI.
DR GO; GO:0030901; P:midbrain development; IMP:MGI.
DR GO; GO:0035521; P:monoubiquitinated histone deubiquitination; ISO:MGI.
DR GO; GO:0035522; P:monoubiquitinated histone H2A deubiquitination; ISO:MGI.
DR GO; GO:0035264; P:multicellular organism growth; IMP:MGI.
DR GO; GO:0046600; P:negative regulation of centriole replication; ISO:MGI.
DR GO; GO:0007399; P:nervous system development; IMP:MGI.
DR GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR GO; GO:0106227; P:peptidyl-lysine glutarylation; ISS:UniProtKB.
DR GO; GO:2000727; P:positive regulation of cardiac muscle cell differentiation; ISO:MGI.
DR GO; GO:0031346; P:positive regulation of cell projection organization; ISO:MGI.
DR GO; GO:0001819; P:positive regulation of cytokine production; IMP:UniProtKB.
DR GO; GO:0045722; P:positive regulation of gluconeogenesis; IGI:MGI.
DR GO; GO:0035066; P:positive regulation of histone acetylation; ISO:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; ISS:UniProtKB.
DR GO; GO:1903010; P:regulation of bone development; IMP:UniProtKB.
DR GO; GO:0061035; P:regulation of cartilage development; IMP: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; IDA:ComplexPortal.
DR GO; GO:0031063; P:regulation of histone deacetylation; ISO:MGI.
DR GO; GO:0031647; P:regulation of protein stability; ISO:MGI.
DR GO; GO:0045589; P:regulation of regulatory T cell differentiation; IMP:UniProtKB.
DR GO; GO:0043484; P:regulation of RNA splicing; IC:ComplexPortal.
DR GO; GO:2000036; P:regulation of stem cell population maintenance; IMP:UniProtKB.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IMP:UniProtKB.
DR GO; GO:0050863; P:regulation of T cell activation; IMP:UniProtKB.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; ISO:MGI.
DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISO:MGI.
DR GO; GO:0090043; P:regulation of tubulin deacetylation; ISO:MGI.
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; IMP:MGI.
DR GO; GO:0021537; P:telencephalon development; IMP:MGI.
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; Bromodomain; Chromosome;
KW Cytoplasm; Cytoskeleton; Isopeptide bond; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation; Transferase;
KW Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT CHAIN 2..830
FT /note="Histone acetyltransferase KAT2A"
FT /id="PRO_0000211203"
FT DOMAIN 496..649
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00532"
FT DOMAIN 738..808
FT /note="Bromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00035"
FT REGION 1..94
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..426
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..51
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 568
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT BINDING 572..574
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT BINDING 572..574
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT BINDING 579..585
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT BINDING 579..585
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT BINDING 610
FT /ligand="acetyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57288"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT BINDING 610
FT /ligand="succinyl-CoA"
FT /ligand_id="ChEBI:CHEBI:57292"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT MOD_RES 542
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT MOD_RES 728
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT CROSSLNK 721
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT CROSSLNK 752
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT CROSSLNK 784
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q92830"
FT CONFLICT 804
FT /note="D -> N (in Ref. 1; AAF70497)"
FT /evidence="ECO:0000305"
FT CONFLICT 815
FT /note="E -> K (in Ref. 1; AAF70497)"
FT /evidence="ECO:0000305"
FT HELIX 84..90
FT /evidence="ECO:0007829|PDB:7BY1"
FT HELIX 94..102
FT /evidence="ECO:0007829|PDB:7BY1"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:7BY1"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:7BY1"
FT HELIX 150..153
FT /evidence="ECO:0007829|PDB:7BY1"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:7BY1"
FT HELIX 161..183
FT /evidence="ECO:0007829|PDB:7BY1"
FT HELIX 187..206
FT /evidence="ECO:0007829|PDB:7BY1"
FT STRAND 222..225
FT /evidence="ECO:0007829|PDB:7BY1"
FT HELIX 226..238
FT /evidence="ECO:0007829|PDB:7BY1"
FT HELIX 243..262
FT /evidence="ECO:0007829|PDB:7BY1"
FT HELIX 268..274
FT /evidence="ECO:0007829|PDB:7BY1"
FT HELIX 277..293
FT /evidence="ECO:0007829|PDB:7BY1"
FT HELIX 295..299
FT /evidence="ECO:0007829|PDB:7BY1"
FT HELIX 308..311
FT /evidence="ECO:0007829|PDB:7BY1"
FT HELIX 314..335
FT /evidence="ECO:0007829|PDB:7BY1"
FT HELIX 336..338
FT /evidence="ECO:0007829|PDB:7BY1"
FT HELIX 341..363
FT /evidence="ECO:0007829|PDB:7BY1"
FT HELIX 368..370
FT /evidence="ECO:0007829|PDB:7BY1"
SQ 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
