Search Results
Overview
| Uniprot ID | O95251 |
|---|---|
| Protein Name | Histone acetyltransferase KAT7 |
| Gene Name | KAT7 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 263 | RQLRYKEKVAELRKK |
| 323 | RASEDLEKLRLQGQI |
| 90 | QPTPVTPKKYPLRQT |
| 91 | PTPVTPKKYPLRQTR |
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)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Molecular Function | GO:0008270 | zinc ion binding |
| Cellular Component | GO:0000785 | chromatin |
| Cellular Component | GO:0005694 | chromosome |
| Cellular Component | GO:0000775 | chromosome, centromeric region |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0000123 | histone acetyltransferase complex |
| Cellular Component | GO:0036409 | histone H3-K14 acetyltransferase complex |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0090734 | site of DNA damage |
| Molecular Function | GO:0003682 | chromatin binding |
| Molecular Function | GO:0003688 | DNA replication origin binding |
| Molecular Function | GO:0004402 | histone acetyltransferase activity |
| Molecular Function | GO:0010484 | histone H3 acetyltransferase activity |
| Molecular Function | GO:0036408 | histone H3K14 acetyltransferase activity |
| Molecular Function | GO:0043994 | histone H3K23 acetyltransferase activity |
| Molecular Function | GO:0044016 | histone H3K4 acetyltransferase activity |
| Molecular Function | GO:0010485 | histone H4 acetyltransferase activity |
| Molecular Function | GO:0043997 | histone H4K12 acetyltransferase activity |
| Molecular Function | GO:0043995 | histone H4K5 acetyltransferase activity |
| Molecular Function | GO:0043996 | histone H4K8 acetyltransferase activity |
| Molecular Function | GO:0003712 | transcription coregulator activity |
| Biological Process | GO:0006281 | DNA repair |
| Biological Process | GO:0006260 | DNA replication |
| Biological Process | GO:0140889 | DNA replication-dependent chromatin disassembly |
| Biological Process | GO:0018393 | internal peptidyl-lysine acetylation |
| Biological Process | GO:0001779 | natural killer cell differentiation |
| Biological Process | GO:0045740 | positive regulation of DNA replication |
| Biological Process | GO:0032786 | positive regulation of DNA-templated transcription, elongation |
| Biological Process | GO:0045648 | positive regulation of erythrocyte differentiation |
| Biological Process | GO:1902035 | positive regulation of hematopoietic stem cell proliferation |
| Biological Process | GO:1900182 | positive regulation of protein localization to nucleus |
| Biological Process | GO:0045944 | positive regulation of transcription by RNA polymerase II |
| Biological Process | GO:0051726 | regulation of cell cycle |
| Biological Process | GO:0001558 | regulation of cell growth |
| Biological Process | GO:2000278 | regulation of DNA biosynthetic process |
| Biological Process | GO:0006275 | regulation of DNA replication |
| Biological Process | GO:0030174 | regulation of DNA-templated DNA replication initiation |
| Biological Process | GO:0006355 | regulation of DNA-templated transcription |
| Biological Process | GO:2000819 | regulation of nucleotide-excision repair |
| Biological Process | GO:0006357 | regulation of transcription by RNA polymerase II |
| Biological Process | GO:0072716 | response to actinomycin D |
| Biological Process | GO:0072739 | response to anisomycin |
| Biological Process | GO:0072720 | response to dithiothreitol |
| Biological Process | GO:0072710 | response to hydroxyurea |
| Biological Process | GO:0072708 | response to sorbitol |
| Biological Process | GO:0031098 | stress-activated protein kinase signaling cascade |
| Biological Process | GO:0030217 | T cell differentiation |
| Biological Process | GO:0045815 | transcription initiation-coupled chromatin remodeling |
Reference
[1] Yang D, Yin J, Shan L, Yi X, Zhang W et al.. Identification of lysine-lactylated substrates in gastric cancer cells.. iScience 25(7):104630. 2022 Jul 15. PMID: 35800753.
[2] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[3] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.
[4] He C, Zhang J, Bai X, Lu C, Zhang K. Lysine lactylation-based insight to understanding the characterization of cervical cancer.. Biochim Biophys Acta Mol Basis Dis 1870(7):167356. 2024 Oct. PMID: 39025375.
[5] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.