KAT8
entrez
84148
canonical
uniprot
Q9H7Z6
canonical
ensembl
ENSG00000103510
resolver
ensp
ENSP00000219797
resolver
ensp
ENSP00000406037
resolver
genesymbol
KAT8
resolver
genesymbol_syn
MOF
resolver
genesymbol_syn
MYST1
resolver
hgnc
HGNC:17933
resolver
uniprot
A8K4Z1
resolver
uniprot
G5E9P2
resolver
uniprot
Q659G0
resolver
uniprot
Q7LC17
resolver
uniprot
Q8IY59
resolver
uniprot
Q8WYB4
resolver
uniprot
Q8WZ14
resolver
uniprot
Q9HAC5
resolver
uniprot
Q9NR35
resolver
uniprot_entry
KAT8_HUMAN
resolver
uniprot_sec
A8K4Z1
resolver
uniprot_sec
G5E9P2
resolver
uniprot_sec
Q659G0
resolver
uniprot_sec
Q7LC17
resolver
uniprot_sec
Q8IY59
resolver
uniprot_sec
Q8WYB4
resolver
uniprot_sec
Q8WZ14
resolver
uniprot_sec
Q9HAC5
resolver
uniprot_sec
Q9NR35
resolver
activity_regulation
ACTIVITY REGULATION: The acetyltransferase activity is inhibited by anacardic acid derivatives. {ECO:0000269|PubMed:26505788}.
uniprot
proteins
amino_acid_sequence
MAAQGAAAAVAAGTSGVAGEGEPGPGENAAAEGTAPSPGRVSPPTPARGEPEVTVEIGETYLCRRPDSTWHSAEVIQSRVNDQEGREEFYVHYVGFNRRLDEWVDKNRLALTKTVKDAVQKNSEKYLSELAEQPERKITRNQKRKHDEINHVQKTYAEMDPTTAALEKEHEAITKVKYVDKIHIGNYEIDAWYFSPFPEDYGKQPKLWLCEYCLKYMKYEKSYRFHLGQCQWRQPPGKEIYRKSNISVYEVDGKDHKIYCQNLCLLAKLFLDHKTLYFDVEPFVFYILTEVDRQGAHIVGYFSKEKESPDGNNVACILTLPPYQRRGYGKFLIAFSYELSKLESTVGSPEKPLSDLGKLSYRSYWSWVLLEILRDFRGTLSIKDLSQMTSITQNDIISTLQSLNMVKYWKGQHVICVTPKLVEEHLKSAQYKKPPITVDSVCLKWAPPKHKQVKLSKK
uniprot
proteins
disease_involvement
DISEASE: Li-Ghorbani-Weisz-Hubshman syndrome (LIGOWS) [MIM:618974]: An autosomal dominant disorder characterized by global developmental delay, mild to moderate intellectual disability, speech and language impairment, and variable facial dysmorphism. Some patients have seizures and autistic features. Brain imaging abnormalities are observed in some patients and include decreased white matter volume, enlarged ventricles, thin corpus callosum, and gray matter nodular heterotopia. {ECO:0000269|PubMed:31794431}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
ec_number
2.3.1.-
uniprot
proteins
ec_number
2.3.1.48
uniprot
proteins
function
FUNCTION: Histone acetyltransferase that catalyzes histone H4 acetylation at 'Lys-5'- and 'Lys-8' (H4K5ac and H4K8ac) or 'Lys-16' (H4K16ac), depending on the context (PubMed:12397079, PubMed:16227571, PubMed:16543150, PubMed:20018852, PubMed:21217699, PubMed:22020126, PubMed:22547026, PubMed:31794431, PubMed:33837287). Catalytic component of the MSL histone acetyltransferase complex, a multiprotein complex that mediates the majority of histone H4 acetylation at 'Lys-16' (H4K16ac), an epigenetic mark that prevents chromatin compaction (PubMed:12397079, PubMed:16227571, PubMed:16543150, PubMed:21217699, PubMed:22020126, PubMed:22547026, PubMed:33657400, PubMed:33837287). H4K16ac constitutes the only acetylation mark intergenerationally transmitted and regulates key biological processes, such as oogenesis, embryonic stem cell pluripotency, hematopoiesis or glucose metabolism (By similarity). The MSL complex is required for chromosome stability and genome integrity by maintaining homeostatic levels of H4K16ac (PubMed:33837287). The MSL complex is also involved in gene dosage by promoting up-regulation of genes expressed by the X chromosome (By similarity). X up-regulation is required to compensate for autosomal biallelic expression (By similarity). The MSL complex also participates in gene dosage compensation by promoting expression of Tsix non-coding RNA (By similarity). As part of the NSL histone acetyltransferase complex, catalyzes histone H4 acetylation at 'Lys-5'- and 'Lys-8' (H4K5ac and H4K8ac) at transcription start sites and promotes transcription initiation (PubMed:20018852, PubMed:22547026, PubMed:33657400). The NSL complex also acts as a regulator of gene expression in mitochondria: KAT8 associates with mitochondrial DNA and controls expression of respiratory genes in an acetyltransferase-dependent mechanism (PubMed:27768893). Also functions as an acetyltransferase for non-histone targets, such as ALKBH5, COX17, IRF3, KDM1A/LSD1, LMNA, PAX7 or TP53/p53 (PubMed:17189187, PubMed:19854137, PubMed:37369679). Acts as an inhibitor of antiviral immunity by acetylating IRF3, preventing IRF3 recruitment to promoters (By similarity). Acts as a regulator of asymmetric division in muscle stem cells by mediating acetylation of PAX7 (By similarity). As part of the NSL complex, acetylates TP53/p53 at 'Lys-120' (PubMed:17189187, PubMed:19854137). Acts as a regulator of epithelial-to-mesenchymal transition as part of the NSL complex by mediating acetylation of KDM1A/LSD1 (PubMed:27292636). The NSL complex is required for nuclear architecture maintenance by mediating acetylation of LMNA (By similarity). Promotes mitochondrial integrity by catalyzing acetylation of COX17 (By similarity). In addition to protein acetyltransferase activity, able to mediate protein propionylation (PubMed:29321206). {ECO:0000250|UniProtKB:Q9D1P2, ECO:0000269|PubMed:12397079, ECO:0000269|PubMed:16227571, ECO:0000269|PubMed:16543150, ECO:0000269|PubMed:17189187, ECO:0000269|PubMed:19854137, ECO:0000269|PubMed:20018852, ECO:0000269|PubMed:21217699, ECO:0000269|PubMed:22020126, ECO:0000269|PubMed:22547026, ECO:0000269|PubMed:27292636, ECO:0000269|PubMed:27768893, ECO:0000269|PubMed:29321206, ECO:0000269|PubMed:31794431, ECO:0000269|PubMed:33657400, ECO:0000269|PubMed:33837287, ECO:0000269|PubMed:37369679}.
uniprot
proteins
mass_dalton
52403
uniprot
proteins
mutagenesis
MUTAGEN 143; /note="K->A: Abolished association with importin-alpha-1 (KPNA2) and translocation into the nucleus."; /evidence="ECO:0000269|PubMed:28991411"; MUTAGEN 144; /note="R->A: Abolished association with importin-alpha-1 (KPNA2) and translocation into the nucleus."; /evidence="ECO:0000269|PubMed:28991411"; MUTAGEN 145; /note="K->A: Abolished association with importin-alpha-1 (KPNA2) and translocation into the nucleus."; /evidence="ECO:0000269|PubMed:28991411"; MUTAGEN 268; /note="K->M: Does not affect non-enzymatic 'autoacetylation'."; /evidence="ECO:0000269|PubMed:27382063"; MUTAGEN 274; /note="K->A,D,Q,G,N,F,V,I,W,T,M,P,S,C,H,E,R,Y,L: Loss of acetylation, leading to abolished histone acetyltransferase activity."; /evidence="ECO:0000269|PubMed:21217699, ECO:0000269|PubMed:22020126, ECO:0000269|PubMed:27382063"; MUTAGEN 316; /note="C->S: Strongly reduces histone acetyltransferase activity without abolishing non-enzymatic 'autoacetylation'."; /evidence="ECO:0000269|PubMed:21217699, ECO:0000269|PubMed:22918831, ECO:0000269|PubMed:27382063"; MUTAGEN 350; /note="E->Q: Abolishes histone acetyltransferase activity without abolishing non-enzymatic 'autoacetylation'. Abolished ability to regulate mitochondrial gene expression."; /evidence="ECO:0000269|PubMed:21217699, ECO:0000269|PubMed:22918831, ECO:0000269|PubMed:27382063, ECO:0000269|PubMed:27768893, ECO:0000269|PubMed:33657400
uniprot
proteins
post_translational_modification
PTM: Acetylation at Lys-274 facilitates cognate substrate Lys-binding and acetylation (PubMed:22020126, PubMed:27382063). Although considered as an autoacetylation event, acetylation at Lys-274 probably takes place via a non-enzymatic process following acetyl-CoA-binding, which primes KAT8 for cognate protein-lysine acetylation (PubMed:27382063). Deacetylated by SIRT1 (PubMed:22918831). {ECO:0000269|PubMed:22020126, ECO:0000269|PubMed:22918831, ECO:0000269|PubMed:27382063}.
uniprot
proteins
protein_family
MYST (SAS/MOZ) family
uniprot
proteins
pubmed
10786633
uniprot
proteins
pubmed
12397079
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15498874
uniprot
proteins
pubmed
15616553
uniprot
proteins
pubmed
15923642
uniprot
proteins
pubmed
15960975
uniprot
proteins
pubmed
16227571
uniprot
proteins
pubmed
16543150
uniprot
proteins
pubmed
17189187
uniprot
proteins
pubmed
17974005
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19854137
uniprot
proteins
pubmed
20018852
uniprot
proteins
pubmed
20620954
uniprot
proteins
pubmed
21217699
uniprot
proteins
pubmed
21691301
uniprot
proteins
pubmed
22020126
uniprot
proteins
pubmed
22547026
uniprot
proteins
pubmed
22814378
uniprot
proteins
pubmed
22918831
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
26505788
uniprot
proteins
pubmed
27292636
uniprot
proteins
pubmed
27382063
uniprot
proteins
pubmed
27768893
uniprot
proteins
pubmed
28991411
uniprot
proteins
pubmed
29321206
uniprot
proteins
pubmed
30224647
uniprot
proteins
pubmed
31794431
uniprot
proteins
pubmed
33467728
uniprot
proteins
pubmed
33657400
uniprot
proteins
pubmed
33837287
uniprot
proteins
pubmed
37369679
uniprot
proteins
sequence_length
458
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10786633, ECO:0000269|PubMed:20018852, ECO:0000269|PubMed:27768893, ECO:0000269|PubMed:28991411, ECO:0000269|PubMed:31794431}. Chromosome {ECO:0000269|PubMed:33657400, ECO:0000305|PubMed:10786633}. Mitochondrion {ECO:0000269|PubMed:27768893}. Note=Translocated into the nucleus via its association with importin-alpha-1 (KPNA2) (PubMed:28991411). As part of the NSL complex, associates with the proximal part of promoters and transcription start sites (PubMed:33657400). As part of the MSL complex, associates with gene bodies (By similarity). Also localizes to mitochondria; associates with mitochondrial DNA and regulates mitochondrial gene expression (PubMed:27768893). {ECO:0000250|UniProtKB:Q9D1P2, ECO:0000269|PubMed:27768893, ECO:0000269|PubMed:28991411, ECO:0000269|PubMed:33657400}.
uniprot
proteins