Search Results
Overview
| Uniprot ID | O14929 |
|---|---|
| Protein Name | Histone acetyltransferase type B catalytic subunit |
| Gene Name | HAT1 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 15 | EKFLVEYKSAVEKKL |
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)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0000785 | chromatin |
| Cellular Component | GO:0000781 | chromosome, telomeric region |
| Cellular Component | GO:0005737 | cytoplasm |
| Cellular Component | GO:0005739 | mitochondrion |
| Cellular Component | GO:0016363 | nuclear matrix |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0032991 | protein-containing complex |
| Molecular Function | GO:0004402 | histone acetyltransferase activity |
| Molecular Function | GO:0042393 | histone binding |
| Molecular Function | GO:0010485 | histone H4 acetyltransferase activity |
| Molecular Function | GO:0043997 | histone H4K12 acetyltransferase activity |
| Molecular Function | GO:0140218 | histone methacryltransferase activity |
| Biological Process | GO:0051276 | chromosome organization |
| Biological Process | GO:0006475 | internal protein amino acid acetylation |
| Biological Process | GO:0006334 | nucleosome assembly |
| Biological Process | GO:0031509 | subtelomeric heterochromatin formation |
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] 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.
[3] Guo X, Ren X, Yan C, Huang H. Quantitative Proteomics Reveals the Role of Lysine Lactylation in Lenalidomide-Resistance in Multiple Myeloma Cells.. ACS Chem Biol 20(7):1728-1738. 2025 Jul 18. PMID: 40590393.
[4] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.
[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.