UniProt Summary: N-alpha-acetyltransferase that specifically mediates the acetylation of the N-terminal residues of histones H4 and H2A (PubMed:21935442, PubMed:25619998). In contrast to other N-alpha- acetyltransferase, has a very specific selectivity for histones H4 and H2A N-terminus and specifically recognizes the 'Ser-Gly-Arg- Gly sequence' (PubMed:21935442, PubMed:25619998). Acts as a negative regulator of apoptosis (PubMed:26666750). May play a role in hepatic lipid metabolism (By similarity). {ECO:0000250|UniProtKB:Q8VE10, ECO:0000269|PubMed:21935442, ECO:0000269|PubMed:25619998, ECO:0000269|PubMed:26666750}.
Pfam DomainsGO Terms
Pfam Domains
Acetyltransf 1
GO Terms
H2A histone acetyltransferase activity
peptide-serine-N-acetyltransferase activity
regulation of chromatin silencing at rDNA
H4 histone acetyltransferase activity
N-terminal protein amino acid acetylation
histone H2A acetylation
N-terminal protein amino acid modification
regulation of chromatin silencing
histone H4 acetylation
histone acetylation
internal peptidyl-lysine acetylation
peptidyl-lysine acetylation
internal protein amino acid acetylation
regulation of gene silencing
protein acetylation
protein acylation
regulation of chromatin organization
protein maturation
peptidyl-lysine modification
regulation of chromosome organization
histone modification
covalent chromatin modification
chromatin organization
peptidyl-amino acid modification
chromosome organization
lipid metabolic process
regulation of organelle organization
gene expression
CRISPR Data
Compound HitMost Correlated Genes in ChemogenomicsTissues where Essential in the Avana Dataset (DepMap 20Q1)