KAT2A
entrez
2648
canonical
uniprot
Q92830
canonical
ensembl
ENSG00000108773
resolver
ensp
ENSP00000225916
resolver
ensp
ENSP00000543229
resolver
genesymbol
KAT2A
resolver
genesymbol_syn
GCN5
resolver
genesymbol_syn
GCN5L2
resolver
hgnc
HGNC:4201
resolver
uniprot
Q8N1A2
resolver
uniprot
Q9UCW1
resolver
uniprot_entry
KAT2A_HUMAN
resolver
uniprot_sec
Q8N1A2
resolver
uniprot_sec
Q9UCW1
resolver
amino_acid_sequence
MAEPSQAPTPAPAAQPRPLQSPAPAPTPTPAPSPASAPIPTPTPAPAPAPAAAPAGSTGTGGPGVGSGGAGSGGDPARPGLSQQQRASQRKAQVRGLPRAKKLEKLGVFSACKANETCKCNGWKNPKPPTAPRMDLQQPAANLSELCRSCEHPLADHVSHLENVSEDEINRLLGMVVDVENLFMSVHKEEDTDTKQVYFYLFKLLRKCILQMTRPVVEGSLGSPPFEKPNIEQGVLNFVQYKFSHLAPRERQTMFELSKMFLLCLNYWKLETPAQFRQRSQAEDVATYKVNYTRWLCYCHVPQSCDSLPRYETTHVFGRSLLRSIFTVTRRQLLEKFRVEKDKLVPEKRTLILTHFPKFLSMLEEEIYGANSPIWESGFTMPPSEGTQLVPRPASVSAAVVPSTPIFSPSMGGGSNSSLSLDSAGAEPMPGEKRTLPENLTLEDAKRLRVMGDIPMELVNEVMLTITDPAAMLGPETSLLSANAARDETARLEERRGIIEFHVIGNSLTPKANRRVLLWLVGLQNVFSHQLPRMPKEYIARLVFDPKHKTLALIKDGRVIGGICFRMFPTQGFTEIVFCAVTSNEQVKGYGTHLMNHLKEYHIKHNILYFLTYADEYAIGYFKKQGFSKDIKVPKSRYLGYIKDYEGATLMECELNPRIPYTELSHIIKKQKEIIKKLIERKQAQIRKVYPGLSCFKEGVRQIPVESVPGIRETGWKPLGKEKGKELKDPDQLYTTLKNLLAQIKSHPSAWPFMEPVKKSEAPDYYEVIRFPIDLKTMTERLRSRYYVTRKLFVADLQRVIANCREYNPPDSEYCRCASALEKFFYFKLKEGGLIDK
uniprot
proteins
ec_number
2.3.1.-
uniprot
proteins
ec_number
2.3.1.48
uniprot
proteins
function
FUNCTION: Protein lysine acyltransferase that catalyzes acetylation of histone and non-histone proteins using acetyl-CoA (PubMed:16753578, PubMed:17301242, PubMed:21131905, PubMed:22465951, PubMed:23142079, PubMed:27796307, PubMed:29174768, PubMed:31527837, PubMed:35995428, PubMed:38128537, PubMed:27377381, PubMed:29211711, PubMed:37040526, PubMed:39561764, PubMed:39694035). Also catalyzes acyl-CoA-dependent acylation of lysine residues in proteins using alternative acyl-CoA donors, including propionyl-CoA, butyryl-CoA, succinyl-CoA, glutaryl-CoA, crotonyl-CoA and lactoyl-CoA (PubMed:31542297, PubMed:29211711, PubMed:37040526, PubMed:39561764). Acts as a histone lysine succinyltransferase: catalyzes succinylation of histone H3 on 'Lys-79' (H3K79succ), with a maximum frequency around the transcription start sites of genes (PubMed:29211711). Succinylation of histones gives a specific tag for epigenetic transcription activation (PubMed:29211711). Association with the 2-oxoglutarate dehydrogenase complex, which provides succinyl-CoA, is required for histone succinylation (PubMed:29211711). In different complexes, functions either as an acetyltransferase (HAT) or as a succinyltransferase: in the SAGA and ATAC complexes, acts as a histone acetyltransferase (PubMed:17301242, PubMed:19103755, PubMed:29211711). Has significant histone acetyltransferase activity with core histones, but not with nucleosome core particles (PubMed:17301242, PubMed:19103755, PubMed:21131905). Has a a strong preference for acetylation of H3 at 'Lys-9' (H3K9ac) (PubMed:21131905). Also catalyzes acetylation of histone H1.4 (H1-4) at 'Lys-34' (H1.4K34ac), a modification enriched at promoters of active genes (PubMed:22465951). Acetylation of histones gives a specific tag for epigenetic transcription activation (PubMed:17301242, PubMed:19103755, PubMed:29211711). Recruited by the XPC complex at promoters, where it specifically mediates acetylation of histone variant H2A.Z.1/H2A.Z, thereby promoting expression of target genes (PubMed:29973595, PubMed:31527837). Involved in long-term memory consolidation and synaptic plasticity: acts by promoting expression of a hippocampal gene expression network linked to neuroactive receptor signaling (By similarity). Acts as a positive regulator of T-cell activation: upon TCR stimulation, recruited to the IL2 promoter following interaction with NFATC2 and catalyzes acetylation of histone H3 at 'Lys-9' (H3K9ac), leading to promote IL2 expression (By similarity). Required for growth and differentiation of craniofacial cartilage and bone by regulating acetylation of histone H3 at 'Lys-9' (H3K9ac) (By similarity). Regulates embryonic stem cell (ESC) pluripotency and differentiation (By similarity). Also acetylates non-histone proteins, such as CEBPB, CGAS, MRE11, PPARGC1A, PLK4 and TBX5 (PubMed:16753578, PubMed:17301242, PubMed:27796307, PubMed:29174768, PubMed:38128537, PubMed:39694035). Involved in heart and limb development by mediating acetylation of TBX5, acetylation regulating nucleocytoplasmic shuttling of TBX5 (PubMed:29174768). Acts as a negative regulator of centrosome amplification by mediating acetylation of PLK4 (PubMed:27796307). Acts as a negative regulator of gluconeogenesis by mediating acetylation and subsequent inactivation of PPARGC1A (PubMed:16753578, PubMed:23142079). Acts as a positive regulator of cGAS-STING signaling by mediating acetylation and activation of CGAS (PubMed:39694035). Also acts as a histone glutaryltransferase: catalyzes glutarylation of histone H4 on 'Lys-91' (H4K91glu), a mark that destabilizes nucleosomes by promoting dissociation of the H2A-H2B dimers from nucleosomes (PubMed:31542297). Catalyzes histone H3 lactylation at 'Lys-14' and 'Lys-18' in a lactyl-CoA-dependent manner (PubMed:39561764). Lactyl-CoA for this reaction can be generated by ACSS2 (PubMed:39561764). {ECO:0000250|UniProtKB:Q9JHD2, ECO:0000269|PubMed:16753578, ECO:0000269|PubMed:17301242, ECO:0000269|PubMed:19103755, ECO:0000269|PubMed:21131905, ECO:0000269|PubMed:22465951, ECO:0000269|PubMed:23142079, ECO:0000269|PubMed:27377381, ECO:0000269|PubMed:27796307, ECO:0000269|PubMed:29174768, ECO:0000269|PubMed:29211711, ECO:0000269|PubMed:29973595, ECO:0000269|PubMed:31527837, ECO:0000269|PubMed:31542297, ECO:0000269|PubMed:35995428, ECO:0000269|PubMed:37040526, ECO:0000269|PubMed:38128537, ECO:0000269|PubMed:39561764, ECO:0000269|PubMed:39694035}.; FUNCTION: (Microbial infection) In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat's transactivating activity and may help inducing chromatin remodeling of proviral genes. {ECO:0000269|PubMed:11384967}.
uniprot
proteins
mass_dalton
93926
uniprot
proteins
mutagenesis
MUTAGEN 307; /note="S->A: Slightly reduced ability to acetylate and inhibit PPARGC1A. Strongly reduced ability to acetylate and inhibit PPARGC1A; when associated with A-307 and Q-549."; /evidence="ECO:0000269|PubMed:23142079"; MUTAGEN 533; /note="R->A: Reduced activity towards lactyl-CoA but no effect on its activity towards acetyl-CoA, succinyl-CoA or crotonyl-CoA."; /evidence="ECO:0000269|PubMed:39561764"; MUTAGEN 549; /note="K->Q: Mimics acetylation; reduced ability to acetylate and inhibit PPARGC1A. Strongly reduced ability to acetylate and inhibit PPARGC1A; when associated with A-307 and A-735."; /evidence="ECO:0000269|PubMed:23142079"; MUTAGEN 567; /note="M->A: Reduced ability to acetylate and inhibit PPARGC1A."; /evidence="ECO:0000269|PubMed:23142079"; MUTAGEN 575; /note="E->A: Catalytically dead mutant; abolished acyltransferase activity; when associated with A-615."; /evidence="ECO:0000269|PubMed:27796307, ECO:0000269|PubMed:31527837"; MUTAGEN 601; /note="Y->F: Reduced ability to acetylate and inhibit PPARGC1A."; /evidence="ECO:0000269|PubMed:23142079"; MUTAGEN 615; /note="D->A: Catalytically dead mutant; abolished acyltransferase activity; when associated with A-575."; /evidence="ECO:0000269|PubMed:27796307, ECO:0000269|PubMed:31527837"; MUTAGEN 621..622; /note="YF->AA: Abolised protein acetyltransferase activity."; /evidence="ECO:0000269|PubMed:23142079"; MUTAGEN 645; /note="Y->A: Reduced histone succinylation without affecting histone acetylation. Reduced gene expression. Reduced binding to succinyl-CoA and butyryl-CoA."; /evidence="ECO:0000269|PubMed:29211711, ECO:0000269|PubMed:37040526"; MUTAGEN 735; /note="T->A: Slightly reduced ability to acetylate and inhibit PPARGC1A. Strongly reduced ability to acetylate and inhibit PPARGC1A; when associated with Q-549 and A-735."; /evidence="ECO:0000269|PubMed:23142079
uniprot
proteins
post_translational_modification
PTM: Acetylated at Lys-549, inhibiting the protein acetyltransferase activity (PubMed:23142079). Deacetylation at Lys-549 by SIRT6 promotes phosphorylation at Ser-307 and Thr-735 and subsequent activation of the protein acetyltransferase activity, leading to acetylation and inactivation of PPARGC1A (PubMed:23142079). {ECO:0000269|PubMed:23142079}.
uniprot
proteins
protein_family
Acetyltransferase family
uniprot
proteins
protein_family
GCN5 subfamily
uniprot
proteins
pubmed
10373431
uniprot
proteins
pubmed
10611234
uniprot
proteins
pubmed
11090279
uniprot
proteins
pubmed
11384967
uniprot
proteins
pubmed
11438666
uniprot
proteins
pubmed
11564863
uniprot
proteins
pubmed
14767476
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15592455
uniprot
proteins
pubmed
16753578
uniprot
proteins
pubmed
17301242
uniprot
proteins
pubmed
17410582
uniprot
proteins
pubmed
18206972
uniprot
proteins
pubmed
19103755
uniprot
proteins
pubmed
21131905
uniprot
proteins
pubmed
22464331
uniprot
proteins
pubmed
22465951
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
23142079
uniprot
proteins
pubmed
25593309
uniprot
proteins
pubmed
27377381
uniprot
proteins
pubmed
27796307
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
29174768
uniprot
proteins
pubmed
29211711
uniprot
proteins
pubmed
29973595
uniprot
proteins
pubmed
30109122
uniprot
proteins
pubmed
30894545
uniprot
proteins
pubmed
31527837
uniprot
proteins
pubmed
31542297
uniprot
proteins
pubmed
35995428
uniprot
proteins
pubmed
37040526
uniprot
proteins
pubmed
38128537
uniprot
proteins
pubmed
39561764
uniprot
proteins
pubmed
39694035
uniprot
proteins
pubmed
8552087
uniprot
proteins
pubmed
8684459
uniprot
proteins
pubmed
9611240
uniprot
proteins
sequence_length
837
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11564863, ECO:0000269|PubMed:25593309, ECO:0000269|PubMed:27796307, ECO:0000269|PubMed:29211711}. Chromosome {ECO:0000269|PubMed:29211711}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:27796307}. Note=Mainly localizes to the nucleus (PubMed:27796307). Localizes to sites of DNA damage (PubMed:25593309). Also localizes to centrosomes in late G1 and around the G1/S transition, coinciding with the onset of centriole formation (PubMed:27796307). {ECO:0000269|PubMed:27796307}.
uniprot
proteins