{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O95251","secondaryAccessions":["B3KN74","B4DF85","B4DFB4","B4DFE0","B4DGY4","E7ER15","G5E9K7"],"uniProtkbId":"KAT7_HUMAN","entryAudit":{"firstPublicDate":"2005-07-05","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1999-05-01","entryVersion":211,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Homo sapiens","commonName":"Human","taxonId":9606,"lineage":["Eukaryota","Metazoa","Chordata","Craniata","Vertebrata","Euteleostomi","Mammalia","Eutheria","Euarchontoglires","Primates","Haplorrhini","Catarrhini","Hominidae","Homo"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Histone acetyltransferase KAT7"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10438470"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17954561"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24065767"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26620551"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31827282"}],"value":"2.3.1.48"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10438470"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10930412"}],"value":"Histone acetyltransferase binding to ORC1"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"31767635"}],"value":"Lysine acetyltransferase 7"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"Reference","id":"Ref.4"}],"value":"MOZ, YBF2/SAS3, SAS2 and TIP60 protein 2"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"Reference","id":"Ref.4"}],"value":"MYST-2"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"31767635"},{"evidenceCode":"ECO:0000312","source":"HGNC","id":"HGNC:17016"}],"value":"KAT7"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10438470"},{"evidenceCode":"ECO:0000303","source":"PubMed","id":"10930412"}],"value":"HBO1"},{"evidences":[{"evidenceCode":"ECO:0000303","source":"Reference","id":"Ref.3"}],"value":"HBOa"},{"evidences":[{"evidenceCode":"ECO:0000303","source":"Reference","id":"Ref.4"}],"value":"MYST2"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q5SVQ0"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10438470"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11278932"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16387653"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16997280"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18832067"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19187766"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20129055"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21753189"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21856198"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24065767"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26620551"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27270040"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28719581"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31767635"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31827282"}],"value":"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)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31827282"}],"value":"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)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-[histone] + acetyl-CoA = N(6)-acetyl-L-lysyl-[histone] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21992"},{"database":"Rhea","id":"RHEA-COMP:9845"},{"database":"Rhea","id":"RHEA-COMP:11338"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:61930"}],"ecNumber":"2.3.1.48","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10438470"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17954561"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24065767"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26620551"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31827282"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:21993"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10438470"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17954561"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24065767"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26620551"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31827282"}]}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20129055"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31827282"}],"value":"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)"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q5SVQ0"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10438470"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10930412"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11278932"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16387653"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17954561"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18832067"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19187766"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20129055"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21753189"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24065767"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26620551"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27270040"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"29382722"}],"value":"Component of the HBO1 complex composed of KAT7/HBO1, MEAF6, ING4 or ING5, and one scaffold subunit: complexes containing BRPF scaffold (BRPF1, BRD1/BRPF2 or BRPF3) direct KAT7/HBO1 specificity towards H3K14ac, while complexes containing JADE scaffold (JADE1, JADE2 and JADE3) mediate acetylation of histone H4 (PubMed:16387653, PubMed:19187766, PubMed:20129055, PubMed:21753189, PubMed:24065767, PubMed:26620551, PubMed:29382722). Interacts with MCM2 and ORC1 (PubMed:10438470, PubMed:11278932, PubMed:16387653). Interacts with the androgen receptor (AR); in the presence of dihydrotestosterone (PubMed:10930412). Interacts with CDT1 (PubMed:18832067). Interacts with MAP2K1 and CUL1 (By similarity). Interacts with p53/TP53; leading to inhibit histone acetyltransferase activity (PubMed:17954561). Interacts with MIS18BP1 (PubMed:27270040)"}],"commentType":"SUBUNIT"},{"commentType":"INTERACTION","interactions":[{"interactantOne":{"uniProtKBAccession":"O95251","intActId":"EBI-473199"},"interactantTwo":{"uniProtKBAccession":"P10275","geneName":"AR","intActId":"EBI-608057"},"numberOfExperiments":5,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O95251","intActId":"EBI-473199"},"interactantTwo":{"uniProtKBAccession":"Q99728","geneName":"BARD1","intActId":"EBI-473181"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O95251","intActId":"EBI-473199"},"interactantTwo":{"uniProtKBAccession":"Q9P2H0","geneName":"CEP126","intActId":"EBI-473176"},"numberOfExperiments":2,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O95251","intActId":"EBI-473199"},"interactantTwo":{"uniProtKBAccession":"Q6IE81","geneName":"JADE1","intActId":"EBI-954672"},"numberOfExperiments":4,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O95251","intActId":"EBI-473199"},"interactantTwo":{"uniProtKBAccession":"Q96EZ8","geneName":"MCRS1","intActId":"EBI-348259"},"numberOfExperiments":3,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O95251","intActId":"EBI-473199"},"interactantTwo":{"uniProtKBAccession":"P53350","geneName":"PLK1","intActId":"EBI-476768"},"numberOfExperiments":6,"organismDiffer":false},{"interactantOne":{"uniProtKBAccession":"O95251","intActId":"EBI-473199"},"interactantTwo":{"uniProtKBAccession":"P08670","geneName":"VIM","intActId":"EBI-353844"},"numberOfExperiments":4,"organismDiffer":false}]},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18832067"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20129055"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21753189"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24065767"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27270040"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28719581"}],"value":"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)"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10930412"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11278932"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16387653"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24065767"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28719581"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18832067"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19187766"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20129055"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"21753189"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"24065767"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28719581"}],"value":"Chromosome","id":"SL-0468"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"27270040"}],"value":"Chromosome, centromere","id":"SL-0047"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q5SVQ0"}],"value":"Cytoplasm, cytosol","id":"SL-0091"}}]},{"commentType":"ALTERNATIVE PRODUCTS","events":["Alternative splicing"],"isoforms":[{"name":{"value":"1"},"isoformIds":["O95251-1"],"isoformSequenceStatus":"Displayed"},{"name":{"value":"2"},"isoformIds":["O95251-2"],"sequenceIds":["VSP_042553","VSP_042554"],"isoformSequenceStatus":"Described"},{"name":{"value":"3"},"isoformIds":["O95251-3"],"sequenceIds":["VSP_042552","VSP_042553","VSP_042554"],"isoformSequenceStatus":"Described"},{"name":{"value":"4"},"isoformIds":["O95251-4"],"sequenceIds":["VSP_042554"],"isoformSequenceStatus":"Described"},{"name":{"value":"5"},"isoformIds":["O95251-5"],"sequenceIds":["VSP_042552","VSP_042553"],"isoformSequenceStatus":"Described"}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10438470"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10930412"}],"value":"Ubiquitously expressed, with highest levels in testis"}],"commentType":"TISSUE SPECIFICITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11278932"}],"value":"The C2HC MYST-type zinc finger is required for interaction with MCM2 and ORC1"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"10930412"}],"value":"The N-terminus is involved in transcriptional repression, while the C-terminus mediates AR-interaction"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q5SVQ0"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18250300"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26572825"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28719581"}],"value":"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)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23319590"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"26572825"}],"value":"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)"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9H7Z6"}],"value":"Autoacetylation at Lys-432 is required for proper function"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the MYST (SAS/MOZ) family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":611,"modifier":"EXACT"}},"description":"Histone acetyltransferase KAT7","featureId":"PRO_0000051569"},{"type":"Domain","location":{"start":{"value":332,"modifier":"EXACT"},"end":{"value":607,"modifier":"EXACT"}},"description":"MYST-type HAT","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01063"}]},{"type":"Zinc 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