O95251 · KAT7_HUMAN
- ProteinHistone acetyltransferase KAT7
- GeneKAT7
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids611 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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).
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).
Catalytic activity
- acetyl-CoA + L-lysyl-[histone] = CoA + H+ + N6-acetyl-L-lysyl-[histone]This reaction proceeds in the forward direction.
Activity regulation
Selectively inhibited by WM-3835 (N'-(4-fluoro-5-methyl-[1,1'-biphenyl]-3-carbonyl)-3- hydroxybenzenesulfonohydrazide) inhibitor (PubMed:31827282).
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 368 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 371 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 384 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 388 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 475-477 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: ILT | ||||||
Binding site | 483-488 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: RQGYGK | ||||||
Active site | 508 | Proton donor/acceptor | ||||
Sequence: E | ||||||
Binding site | 512 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: S | ||||||
Binding site | 521 | acetyl-CoA (UniProtKB | ChEBI) | ||||
Sequence: S |
GO annotations
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameHistone acetyltransferase KAT7
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionO95251
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
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).
Keywords
- Cellular component
Disease & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 50-53 | Impaired phosphorylation by ATR, leading to decreased ubiquitination and increased stability in response to DNA damage. | ||||
Sequence: SQSS → AQSA | ||||||
Mutagenesis | 57 | Leads to cell cycle arrest in the G1/S phase. | ||||
Sequence: S → A | ||||||
Mutagenesis | 338 | Decreases ubiquitination. | ||||
Sequence: K → R | ||||||
Mutagenesis | 371 | No interaction with MCM2 and ORC1. | ||||
Sequence: C → A | ||||||
Mutagenesis | 485 | Abolishes histone acetyltransferase activity. | ||||
Sequence: G → A | ||||||
Mutagenesis | 508 | Abolished histone acetyltransferase activity. | ||||
Sequence: E → A |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 398 variants from UniProt as well as other sources including ClinVar and dbSNP.
Organism-specific databases
Miscellaneous
Chemistry
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue, modified residue (large scale data), cross-link.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000051569 | 1-611 | UniProt | Histone acetyltransferase KAT7 | |||
Sequence: MPRRKRNAGSSSDGTEDSDFSTDLEHTDSSESDGTSRRSARVTRSSARLSQSSQDSSPVRNLQSFGTEEPAYSTRRVTRSQQQPTPVTPKKYPLRQTRSSGSETEQVVDFSDRETKNTADHDESPPRTPTGNAPSSESDIDISSPNVSHDESIAKDMSLKDSGSDLSHRPKRRRFHESYNFNMKCPTPGCNSLGHLTGKHERHFSISGCPLYHNLSADECKVRAQSRDKQIEERMLSHRQDDNNRHATRHQAPTERQLRYKEKVAELRKKRNSGLSKEQKEKYMEHRQTYGNTREPLLENLTSEYDLDLFRRAQARASEDLEKLRLQGQITEGSNMIKTIAFGRYELDTWYHSPYPEEYARLGRLYMCEFCLKYMKSQTILRRHMAKCVWKHPPGDEIYRKGSISVFEVDGKKNKIYCQNLCLLAKLFLDHKTLYYDVEPFLFYVMTEADNTGCHLIGYFSKEKNSFLNYNVSCILTMPQYMRQGYGKMLIDFSYLLSKVEEKVGSPERPLSDLGLISYRSYWKEVLLRYLHNFQGKEISIKEISQETAVNPVDIVSTLQALQMLKYWKGKHLVLKRQDLIDEWIAKEAKRSNSNKTMDPSCLKWTPPKGT | |||||||
Modified residue | 10 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 10 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 50 | UniProt | Phosphoserine; by ATR | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 50 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 52 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 53 | UniProt | Phosphoserine; by ATR | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 53 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 56 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 57 | UniProt | Phosphoserine; by PLK1 | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 57 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 64 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 64 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 73 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 80 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 85 | UniProt | Phosphothreonine; by CDK1 | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 85 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 88 | UniProt | Phosphothreonine; by CDK1 | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 88 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 97 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 99 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 100 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 102 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 102 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 104 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 104 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 111 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 111 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 118 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 124 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 124 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 128 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 128 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 130 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 138 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 158 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 158 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 162 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 162 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 164 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 164 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 167 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 178 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 178 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 187 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 192 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 199 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 205 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 216 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 277 | UniProt | N6-acetyllysine | ||||
Sequence: K | |||||||
Cross-link | 323 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2) | ||||
Sequence: K | |||||||
Cross-link | 338 | UniProt | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) | ||||
Sequence: K | |||||||
Modified residue (large scale data) | 403 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 432 | UniProt | N6-acetyllysine; by autocatalysis | ||||
Sequence: K | |||||||
Modified residue | 506 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 506 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 606 | PRIDE | Phosphothreonine | ||||
Sequence: T |
Post-translational modification
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).
Ubiquitinated by the CRL4(DDB2) complex following phosphorylation by ATR, leading to its subsequent degradation (PubMed:26572825).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
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).
Binary interactions
Type | Entry 1 | Entry 2 | Number of experiments | Intact | |
---|---|---|---|---|---|
BINARY | O95251 | AR P10275 | 5 | EBI-473199, EBI-608057 | |
BINARY | O95251 | BARD1 Q99728 | 2 | EBI-473199, EBI-473181 | |
BINARY | O95251 | CEP126 Q9P2H0 | 2 | EBI-473199, EBI-473176 | |
BINARY | O95251 | JADE1 Q6IE81 | 4 | EBI-473199, EBI-954672 | |
BINARY | O95251 | MCRS1 Q96EZ8 | 3 | EBI-473199, EBI-348259 | |
BINARY | O95251 | PLK1 P53350 | 6 | EBI-473199, EBI-476768 | |
BINARY | O95251 | VIM P08670 | 4 | EBI-473199, EBI-353844 |
Protein-protein interaction databases
Chemistry
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, compositional bias, zinc finger, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-173 | Disordered | ||||
Sequence: MPRRKRNAGSSSDGTEDSDFSTDLEHTDSSESDGTSRRSARVTRSSARLSQSSQDSSPVRNLQSFGTEEPAYSTRRVTRSQQQPTPVTPKKYPLRQTRSSGSETEQVVDFSDRETKNTADHDESPPRTPTGNAPSSESDIDISSPNVSHDESIAKDMSLKDSGSDLSHRPKRR | ||||||
Compositional bias | 19-38 | Basic and acidic residues | ||||
Sequence: DFSTDLEHTDSSESDGTSRR | ||||||
Compositional bias | 39-106 | Polar residues | ||||
Sequence: SARVTRSSARLSQSSQDSSPVRNLQSFGTEEPAYSTRRVTRSQQQPTPVTPKKYPLRQTRSSGSETEQ | ||||||
Compositional bias | 107-123 | Basic and acidic residues | ||||
Sequence: VVDFSDRETKNTADHDE | ||||||
Compositional bias | 124-151 | Polar residues | ||||
Sequence: SPPRTPTGNAPSSESDIDISSPNVSHDE | ||||||
Compositional bias | 153-173 | Basic and acidic residues | ||||
Sequence: IAKDMSLKDSGSDLSHRPKRR | ||||||
Zinc finger | 176-219 | CCHHC-type | ||||
Sequence: HESYNFNMKCPTPGCNSLGHLTGKHERHFSISGCPLYHNLSADE | ||||||
Domain | 332-607 | MYST-type HAT | ||||
Sequence: EGSNMIKTIAFGRYELDTWYHSPYPEEYARLGRLYMCEFCLKYMKSQTILRRHMAKCVWKHPPGDEIYRKGSISVFEVDGKKNKIYCQNLCLLAKLFLDHKTLYYDVEPFLFYVMTEADNTGCHLIGYFSKEKNSFLNYNVSCILTMPQYMRQGYGKMLIDFSYLLSKVEEKVGSPERPLSDLGLISYRSYWKEVLLRYLHNFQGKEISIKEISQETAVNPVDIVSTLQALQMLKYWKGKHLVLKRQDLIDEWIAKEAKRSNSNKTMDPSCLKWTP | ||||||
Zinc finger | 365-390 | C2HC MYST-type | ||||
Sequence: LYMCEFCLKYMKSQTILRRHMAKCVW |
Domain
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 5 isoforms produced by Alternative splicing.
O95251-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length611
- Mass (Da)70,642
- Last updated1999-05-01 v1
- Checksum8368E7C4F07D8D7C
O95251-2
- Name2
O95251-3
- Name3
O95251-4
- Name4
- Differences from canonical
- 222-251: Missing
O95251-5
- Name5
Computationally mapped potential isoform sequences
There are 16 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
E7EUP3 | E7EUP3_HUMAN | KAT7 | 425 | ||
A0A6Q8PHH2 | A0A6Q8PHH2_HUMAN | KAT7 | 524 | ||
D6RFZ5 | D6RFZ5_HUMAN | KAT7 | 455 | ||
B4DGH8 | B4DGH8_HUMAN | KAT7 | 166 | ||
A0AA34QVH8 | A0AA34QVH8_HUMAN | KAT7 | 637 | ||
A0A9L9PXR9 | A0A9L9PXR9_HUMAN | KAT7 | 531 | ||
A0A9L9PY29 | A0A9L9PY29_HUMAN | KAT7 | 517 | ||
A0A9L9PXP8 | A0A9L9PXP8_HUMAN | KAT7 | 455 | ||
A0A9L9PXR4 | A0A9L9PXR4_HUMAN | KAT7 | 577 | ||
A0A9L9PXJ9 | A0A9L9PXJ9_HUMAN | KAT7 | 580 | ||
A0A9L9PXL5 | A0A9L9PXL5_HUMAN | KAT7 | 627 | ||
A0A9L9PXM0 | A0A9L9PXM0_HUMAN | KAT7 | 264 | ||
A0A9L9PXC5 | A0A9L9PXC5_HUMAN | KAT7 | 548 | ||
A0A9L9PWZ9 | A0A9L9PWZ9_HUMAN | KAT7 | 547 | ||
A0A9L9PX81 | A0A9L9PX81_HUMAN | KAT7 | 508 | ||
A0A9L9PX04 | A0A9L9PX04_HUMAN | KAT7 | 264 |
Features
Showing features for compositional bias, sequence conflict, alternative sequence.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 19-38 | Basic and acidic residues | ||||
Sequence: DFSTDLEHTDSSESDGTSRR | ||||||
Sequence conflict | 38-44 | in Ref. 5; BAG57945 | ||||
Sequence: Missing | ||||||
Compositional bias | 39-106 | Polar residues | ||||
Sequence: SARVTRSSARLSQSSQDSSPVRNLQSFGTEEPAYSTRRVTRSQQQPTPVTPKKYPLRQTRSSGSETEQ | ||||||
Sequence conflict | 41 | in Ref. 5; BAG57346 | ||||
Sequence: R → Q | ||||||
Alternative sequence | VSP_042552 | 55-113 | in isoform 3 and isoform 5 | |||
Sequence: Missing | ||||||
Compositional bias | 107-123 | Basic and acidic residues | ||||
Sequence: VVDFSDRETKNTADHDE | ||||||
Alternative sequence | VSP_042553 | 114-193 | in isoform 2, isoform 3 and isoform 5 | |||
Sequence: Missing | ||||||
Compositional bias | 124-151 | Polar residues | ||||
Sequence: SPPRTPTGNAPSSESDIDISSPNVSHDE | ||||||
Compositional bias | 153-173 | Basic and acidic residues | ||||
Sequence: IAKDMSLKDSGSDLSHRPKRR | ||||||
Alternative sequence | VSP_042554 | 222-251 | in isoform 2, isoform 3 and isoform 4 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF074606 EMBL· GenBank· DDBJ | AAC99368.1 EMBL· GenBank· DDBJ | mRNA | ||
AF140360 EMBL· GenBank· DDBJ | AAD42348.1 EMBL· GenBank· DDBJ | mRNA | ||
AF217502 EMBL· GenBank· DDBJ | AAL56649.1 EMBL· GenBank· DDBJ | mRNA | ||
AK023890 EMBL· GenBank· DDBJ | BAG51236.1 EMBL· GenBank· DDBJ | mRNA | ||
AK293976 EMBL· GenBank· DDBJ | BAG57346.1 EMBL· GenBank· DDBJ | mRNA | ||
AK294014 EMBL· GenBank· DDBJ | BAG57375.1 EMBL· GenBank· DDBJ | mRNA | ||
AK294052 EMBL· GenBank· DDBJ | BAG57401.1 EMBL· GenBank· DDBJ | mRNA | ||
AK294836 EMBL· GenBank· DDBJ | BAG57945.1 EMBL· GenBank· DDBJ | mRNA | ||
AC015795 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
AC027801 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
CH471109 EMBL· GenBank· DDBJ | EAW94658.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
CH471109 EMBL· GenBank· DDBJ | EAW94659.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
BC032640 EMBL· GenBank· DDBJ | AAH32640.1 EMBL· GenBank· DDBJ | mRNA |