HAT1
entrez
8520
canonical
uniprot
O14929
canonical
ensembl
ENSG00000128708
resolver
ensembl
ENSG00000292096
resolver
ensp
ENSP00000264108
resolver
ensp
ENSP00000517832
resolver
enst
ENST00000709700
resolver
genesymbol
HAT1
resolver
genesymbol_syn
KAT1
resolver
hgnc
HGNC:4821
resolver
uniprot
A0AAG2UVM1
resolver
uniprot
Q49A44
resolver
uniprot
Q53QF0
resolver
uniprot
Q53SU4
resolver
uniprot
Q6P594
resolver
uniprot
Q8WWB9
resolver
uniprot_entry
A0AAG2UVM1_HUMAN
resolver
uniprot_entry
HAT1_HUMAN
resolver
uniprot_sec
Q49A44
resolver
uniprot_sec
Q53QF0
resolver
uniprot_sec
Q53SU4
resolver
uniprot_sec
Q6P594
resolver
uniprot_sec
Q8WWB9
resolver
amino_acid_sequence
MAGFGAMEKFLVEYKSAVEKKLAEYKCNTNTAIELKLVRFPEDLENDIRTFFPEYTHQLFGDDETAFGYKGLKILLYYIAGSLSTMFRVEYASKVDENFDCVEADDVEGKIRQIIPPGFCTNTNDFLSLLEKEVDFKPFGTLLHTYSVLSPTGGENFTFQIYKADMTCRGFREYHERLQTFLMWFIETASFIDVDDERWHYFLVFEKYNKDGATLFATVGYMTVYNYYVYPDKTRPRVSQMLILTPFQGQGHGAQLLETVHRYYTEFPTVLDITAEDPSKSYVKLRDFVLVKLCQDLPCFSREKLMQGFNEDMVIEAQQKFKINKQHARRVYEILRLLVTDMSDAEQYRSYRLDIKRRLISPYKKKQRDLAKMRKCLRPEELTNQMNQIEISMQHEQLEESFQELVEDYRRVIERLAQE
uniprot
proteins
ec_number
2.3.1.-
uniprot
proteins
ec_number
2.3.1.48
uniprot
proteins
function
FUNCTION: Histone acetyltransferase that plays a role in different biological processes including cell cycle progression, glucose metabolism, histone production or DNA damage repair (PubMed:20953179, PubMed:23653357, PubMed:31278053, PubMed:32081014). Coordinates histone production and acetylation via H4 promoter binding (PubMed:31278053). Acetylates histone H4 at 'Lys-5' (H4K5ac) and 'Lys-12' (H4K12ac) and, to a lesser extent, histone H2A at 'Lys-5' (H2AK5ac) (PubMed:11585814, PubMed:22615379). Drives H4 production by chromatin binding to support chromatin replication and acetylation. Since transcription of H4 genes is tightly coupled to S-phase, plays an important role in S-phase entry and progression (PubMed:31278053). Promotes homologous recombination in DNA repair by facilitating histone turnover and incorporation of acetylated H3.3 at sites of double-strand breaks (PubMed:23653357). In addition, acetylates other substrates such as chromatin-related proteins (PubMed:32081014). Also acetylates RSAD2 which mediates the interaction of ubiquitin ligase UBE4A with RSAD2 leading to RSAD2 ubiquitination and subsequent degradation (PubMed:31812350). In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as 2-methylpropenoyl-CoA (methacryl-CoA), and is able to mediate histone methacrylation (PubMed:34961760). {ECO:0000269|PubMed:11585814, ECO:0000269|PubMed:20953179, ECO:0000269|PubMed:22615379, ECO:0000269|PubMed:23653357, ECO:0000269|PubMed:31278053, ECO:0000269|PubMed:31812350, ECO:0000269|PubMed:32081014, ECO:0000269|PubMed:34961760}.; FUNCTION: (Microbial infection) Contributes to hepatitis B virus (HBV) replication by acetylating histone H4 at the sites of 'Lys-5' and 'Lys-12' on the covalently closed circular DNA (cccDNA) minichromosome leading to its accumulation within the host cell. {ECO:0000269|PubMed:31695772}.
uniprot
proteins
mass_dalton
49541
uniprot
proteins
mutagenesis
MUTAGEN 62; /note="D->A: Strongly reduces HAT activity."; /evidence="ECO:0000269|PubMed:22615379"; MUTAGEN 64; /note="E->A: Strongly reduces HAT activity."; /evidence="ECO:0000269|PubMed:22615379"; MUTAGEN 187; /note="E->Q: Strongly reduces HAT activity."; /evidence="ECO:0000269|PubMed:22615379"; MUTAGEN 190; /note="S->A: Complete loss of activity after pulsatile shear stress."; /evidence="ECO:0000269|PubMed:28143904"; MUTAGEN 190; /note="S->D: No loss of activity after pulsatile shear stress."; /evidence="ECO:0000269|PubMed:28143904"; MUTAGEN 199; /note="W->A: Strongly reduces HAT activity."; /evidence="ECO:0000269|PubMed:22615379"; MUTAGEN 276; /note="E->Q: Strongly reduces HAT activity."; /evidence="ECO:0000269|PubMed:22615379"; MUTAGEN 277; /note="D->N: Strongly reduces HAT activity."; /evidence="ECO:0000269|PubMed:22615379
uniprot
proteins
post_translational_modification
PTM: Phosphorylated by AMPK at Ser-190; phosphorylation increases HAT1 activity. {ECO:0000269|PubMed:28143904}.
uniprot
proteins
protein_family
HAT1 family
uniprot
proteins
pubmed
11585814
uniprot
proteins
pubmed
12841681
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15815621
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
20148353
uniprot
proteins
pubmed
20953179
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22615379
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23653357
uniprot
proteins
pubmed
28143904
uniprot
proteins
pubmed
31278053
uniprot
proteins
pubmed
31695772
uniprot
proteins
pubmed
31812350
uniprot
proteins
pubmed
32081014
uniprot
proteins
pubmed
34961760
uniprot
proteins
pubmed
9427644
uniprot
proteins
sequence_length
419
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Isoform A]: Nucleus matrix {ECO:0000269|PubMed:20148353, ECO:0000269|PubMed:23653357}. Mitochondrion {ECO:0000269|PubMed:32081014}.; SUBCELLULAR LOCATION: [Isoform B]: Cytoplasm {ECO:0000269|PubMed:20148353}. Nucleus {ECO:0000269|PubMed:20148353}. Nucleus matrix {ECO:0000269|PubMed:20148353}. Nucleus, nucleoplasm {ECO:0000269|PubMed:20148353}. Note=Localization is predominantly nuclear in normal cells. Treatment with hydrogen peroxide or ionizing radiation enhances nuclear localization through redistribution of existing protein. {ECO:0000269|PubMed:20148353}.
uniprot
proteins