KAT7
entrez
11143
canonical
uniprot
O95251
canonical
ensembl
ENSG00000136504
resolver
ensp
ENSP00000259021
resolver
ensp
ENSP00000398961
resolver
ensp
ENSP00000413415
resolver
ensp
ENSP00000423385
resolver
ensp
ENSP00000424577
resolver
ensp
ENSP00000516479
resolver
enst
ENST00000706640
resolver
genesymbol
KAT7
resolver
genesymbol_syn
HBO1
resolver
genesymbol_syn
HBOa
resolver
genesymbol_syn
MYST2
resolver
hgnc
HGNC:17016
resolver
uniprot
A0A9L9PXR9
resolver
uniprot
B3KN74
resolver
uniprot
B4DF85
resolver
uniprot
B4DFB4
resolver
uniprot
B4DFE0
resolver
uniprot
B4DGY4
resolver
uniprot
E7ER15
resolver
uniprot
G5E9K7
resolver
uniprot_entry
A0A9L9PXR9_HUMAN
resolver
uniprot_entry
KAT7_HUMAN
resolver
uniprot_sec
B3KN74
resolver
uniprot_sec
B4DF85
resolver
uniprot_sec
B4DFB4
resolver
uniprot_sec
B4DFE0
resolver
uniprot_sec
B4DGY4
resolver
uniprot_sec
E7ER15
resolver
uniprot_sec
G5E9K7
resolver
activity_regulation
ACTIVITY REGULATION: Histone acetyltransferase activity is inhibited by GMNN in the context of a complex with CDT1, inhibiting histone H4 acetylation and DNA replication licensing (PubMed:20129055). Selectively inhibited by WM-3835 (N'-(4-fluoro-5-methyl-[1,1'-biphenyl]-3-carbonyl)-3- hydroxybenzenesulfonohydrazide) inhibitor (PubMed:31827282). {ECO:0000269|PubMed:20129055, ECO:0000269|PubMed:31827282}.
uniprot
proteins
amino_acid_sequence
MPRRKRNAGSSSDGTEDSDFSTDLEHTDSSESDGTSRRSARVTRSSARLSQSSQDSSPVRNLQSFGTEEPAYSTRRVTRSQQQPTPVTPKKYPLRQTRSSGSETEQVVDFSDRETKNTADHDESPPRTPTGNAPSSESDIDISSPNVSHDESIAKDMSLKDSGSDLSHRPKRRRFHESYNFNMKCPTPGCNSLGHLTGKHERHFSISGCPLYHNLSADECKVRAQSRDKQIEERMLSHRQDDNNRHATRHQAPTERQLRYKEKVAELRKKRNSGLSKEQKEKYMEHRQTYGNTREPLLENLTSEYDLDLFRRAQARASEDLEKLRLQGQITEGSNMIKTIAFGRYELDTWYHSPYPEEYARLGRLYMCEFCLKYMKSQTILRRHMAKCVWKHPPGDEIYRKGSISVFEVDGKKNKIYCQNLCLLAKLFLDHKTLYYDVEPFLFYVMTEADNTGCHLIGYFSKEKNSFLNYNVSCILTMPQYMRQGYGKMLIDFSYLLSKVEEKVGSPERPLSDLGLISYRSYWKEVLLRYLHNFQGKEISIKEISQETAVNPVDIVSTLQALQMLKYWKGKHLVLKRQDLIDEWIAKEAKRSNSNKTMDPSCLKWTPPKGT
uniprot
proteins
ec_number
2.3.1.48
uniprot
proteins
function
FUNCTION: Catalytic subunit of histone acetyltransferase HBO1 complexes, which specifically mediate acetylation of histone H3 at 'Lys-14' (H3K14ac), thereby regulating various processes, such as gene transcription, protein ubiquitination, immune regulation, stem cell pluripotent and self-renewal maintenance and embryonic development (PubMed:16387653, PubMed:21753189, PubMed:24065767, PubMed:26620551, PubMed:31767635, PubMed:31827282). Some complexes also catalyze acetylation of histone H4 at 'Lys-5', 'Lys-8' and 'Lys-12' (H4K5ac, H4K8ac and H4K12ac, respectively), regulating DNA replication initiation, regulating DNA replication initiation (PubMed:10438470, PubMed:19187766, PubMed:20129055, PubMed:24065767). Specificity of the HBO1 complexes is determined by the scaffold subunit: complexes containing BRPF scaffold (BRPF1, BRD1/BRPF2 or BRPF3) direct KAT7/HBO1 specificity towards H3K14ac, while complexes containing JADE (JADE1, JADE2 and JADE3) scaffold direct KAT7/HBO1 specificity towards histone H4 (PubMed:19187766, PubMed:20129055, PubMed:24065767, PubMed:26620551). H3K14ac promotes transcriptional elongation by facilitating the processivity of RNA polymerase II (PubMed:31827282). Acts as a key regulator of hematopoiesis by forming a complex with BRD1/BRPF2, directing KAT7/HBO1 specificity towards H3K14ac and promoting erythroid differentiation (PubMed:21753189). H3K14ac is also required for T-cell development (By similarity). KAT7/HBO1-mediated acetylation facilitates two consecutive steps, licensing and activation, in DNA replication initiation: H3K14ac facilitates the activation of replication origins, and histone H4 acetylation (H4K5ac, H4K8ac and H4K12ac) facilitates chromatin loading of MCM complexes, promoting DNA replication licensing (PubMed:10438470, PubMed:11278932, PubMed:18832067, PubMed:19187766, PubMed:20129055, PubMed:21856198, PubMed:24065767, PubMed:26620551). Acts as a positive regulator of centromeric CENPA assembly: recruited to centromeres and mediates histone acetylation, thereby preventing centromere inactivation mediated by SUV39H1, possibly by increasing histone turnover/exchange (PubMed:27270040). Involved in nucleotide excision repair: phosphorylation by ATR in response to ultraviolet irradiation promotes its localization to DNA damage sites, where it mediates histone acetylation to facilitate recruitment of XPC at the damaged DNA sites (PubMed:28719581). Acts as an inhibitor of NF-kappa-B independently of its histone acetyltransferase activity (PubMed:16997280). {ECO:0000250|UniProtKB:Q5SVQ0, ECO:0000269|PubMed:10438470, ECO:0000269|PubMed:11278932, ECO:0000269|PubMed:16387653, ECO:0000269|PubMed:16997280, ECO:0000269|PubMed:18832067, ECO:0000269|PubMed:19187766, ECO:0000269|PubMed:20129055, ECO:0000269|PubMed:21753189, ECO:0000269|PubMed:21856198, ECO:0000269|PubMed:24065767, ECO:0000269|PubMed:26620551, ECO:0000269|PubMed:27270040, ECO:0000269|PubMed:28719581, ECO:0000269|PubMed:31767635, ECO:0000269|PubMed:31827282}.; FUNCTION: Plays a central role in the maintenance of leukemia stem cells in acute myeloid leukemia (AML) (PubMed:31827282). Acts by mediating acetylation of histone H3 at 'Lys-14' (H3K14ac), thereby facilitating the processivity of RNA polymerase II to maintain the high expression of key genes, such as HOXA9 and HOXA10 that help to sustain the functional properties of leukemia stem cells (PubMed:31827282). {ECO:0000269|PubMed:31827282}.
uniprot
proteins
mass_dalton
70642
uniprot
proteins
mutagenesis
MUTAGEN 50..53; /note="SQSS->AQSA: Impaired phosphorylation by ATR, leading to decreased ubiquitination and increased stability in response to DNA damage."; /evidence="ECO:0000269|PubMed:26572825"; MUTAGEN 57; /note="S->A: Leads to cell cycle arrest in the G1/S phase."; /evidence="ECO:0000269|PubMed:18250300"; MUTAGEN 338; /note="K->R: Decreases ubiquitination."; /evidence="ECO:0000269|PubMed:23319590"; MUTAGEN 371; /note="C->A: No interaction with MCM2 and ORC1."; /evidence="ECO:0000269|PubMed:11278932"; MUTAGEN 485; /note="G->A: Abolishes histone acetyltransferase activity."; /evidence="ECO:0000269|PubMed:17954561, ECO:0000269|PubMed:20129055"; MUTAGEN 508; /note="E->A: Abolished histone acetyltransferase activity."; /evidence="ECO:0000269|PubMed:31827282
uniprot
proteins
post_translational_modification
PTM: Phosphorylated at Ser-50 and Ser-53 by ATR in response to DNA damage, promoting its ubiquitination by the CRL4(DDB2) complex and subsequent degradation (PubMed:26572825). Phosphorylation at Ser-50 and Ser-53 by ATR in response to ultraviolet-induced DNA, promotes localization to DNA damage sites (PubMed:28719581). Phosphorylation at Ser-57 by PLK1 during mitosis seems important for prereplicative complex formation and DNA replication licensing, and requires prior phosphorylation at Thr-85 and Thr-88 by CDK1 (PubMed:18250300). Phosphorylated by MAP2K1, which accelerates its degradation (By similarity). {ECO:0000250|UniProtKB:Q5SVQ0, ECO:0000269|PubMed:18250300, ECO:0000269|PubMed:26572825, ECO:0000269|PubMed:28719581}.; PTM: Ubiquitinated at Lys-338, leading to proteasomal degradation (PubMed:23319590). Ubiquitinated by the CRL4(DDB2) complex following phosphorylation by ATR, leading to its subsequent degradation (PubMed:26572825). {ECO:0000269|PubMed:23319590, ECO:0000269|PubMed:26572825}.; PTM: Autoacetylation at Lys-432 is required for proper function. {ECO:0000250|UniProtKB:Q9H7Z6}.
uniprot
proteins
protein_family
MYST (SAS/MOZ) family
uniprot
proteins
pubmed
10438470
uniprot
proteins
pubmed
10930412
uniprot
proteins
pubmed
11278932
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16387653
uniprot
proteins
pubmed
16625196
uniprot
proteins
pubmed
16964243
uniprot
proteins
pubmed
16997280
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
17525332
uniprot
proteins
pubmed
17954561
uniprot
proteins
pubmed
18250300
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18832067
uniprot
proteins
pubmed
19187766
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20129055
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21753189
uniprot
proteins
pubmed
21856198
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
23319590
uniprot
proteins
pubmed
24065767
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
26572825
uniprot
proteins
pubmed
26620551
uniprot
proteins
pubmed
27270040
uniprot
proteins
pubmed
28112733
uniprot
proteins
pubmed
28334966
uniprot
proteins
pubmed
28719581
uniprot
proteins
pubmed
29382722
uniprot
proteins
pubmed
31767635
uniprot
proteins
pubmed
31827282
uniprot
proteins
sequence_length
611
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10930412, ECO:0000269|PubMed:11278932, ECO:0000269|PubMed:16387653, ECO:0000269|PubMed:24065767, ECO:0000269|PubMed:28719581}. Chromosome {ECO:0000269|PubMed:18832067, ECO:0000269|PubMed:19187766, ECO:0000269|PubMed:20129055, ECO:0000269|PubMed:21753189, ECO:0000269|PubMed:24065767, ECO:0000269|PubMed:28719581}. Chromosome, centromere {ECO:0000269|PubMed:27270040}. Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q5SVQ0}. Note=Associates with replication origins specifically during the G1 phase of the cell cycle (PubMed:18832067, PubMed:20129055). Localizes to transcription start sites (PubMed:21753189, PubMed:24065767). Localizes to ultraviolet-induced DNA damage sites following phosphorylation by ATR (PubMed:28719581). Localizes to centromeres in G1 phase (PubMed:27270040). {ECO:0000269|PubMed:18832067, ECO:0000269|PubMed:20129055, ECO:0000269|PubMed:21753189, ECO:0000269|PubMed:24065767, ECO:0000269|PubMed:27270040, ECO:0000269|PubMed:28719581}.
uniprot
proteins