Search Results
Overview
| Uniprot ID | P16104 |
|---|---|
| Protein Name | Histone H2AX |
| Gene Name | H2AX |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 10 | GRGKTGGKARAKAKS |
| 119 | IQAVLLPKKTSATVG |
| 120 | QAVLLPKKTSATVGP |
| 128 | TSATVGPKAPSGGKK |
| 135 | KAPSGGKKATQASQE |
| 6 | **MSGRGKTGGKARA |
Function
Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling. Required for checkpoint-mediated arrest of cell cycle progression in response to low doses of ionizing radiation and for efficient repair of DNA double strand breaks (DSBs) specifically when modified by C-terminal phosphorylation
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005813 | centrosome |
| Cellular Component | GO:0000794 | condensed nuclear chromosome |
| Cellular Component | GO:0070062 | extracellular exosome |
| Cellular Component | GO:0001673 | male germ cell nucleus |
| Cellular Component | GO:0016607 | nuclear speck |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0000786 | nucleosome |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0005657 | replication fork |
| Cellular Component | GO:0090734 | site of DNA damage |
| Cellular Component | GO:0035861 | site of double-strand break |
| Cellular Component | GO:0001741 | XY body |
| Molecular Function | GO:0140463 | chromatin-protein adaptor activity |
| Molecular Function | GO:0003684 | damaged DNA binding |
| Molecular Function | GO:0003677 | DNA binding |
| Molecular Function | GO:0019899 | enzyme binding |
| Molecular Function | GO:0042393 | histone binding |
| Molecular Function | GO:0046982 | protein heterodimerization activity |
| Molecular Function | GO:0030527 | structural constituent of chromatin |
| Biological Process | GO:0000077 | DNA damage checkpoint signaling |
| Biological Process | GO:0006974 | DNA damage response |
| Biological Process | GO:0006310 | DNA recombination |
| Biological Process | GO:0006302 | double-strand break repair |
| Biological Process | GO:0031507 | heterochromatin formation |
| Biological Process | GO:0051321 | meiotic cell cycle |
| Biological Process | GO:0006334 | nucleosome assembly |
| Biological Process | GO:0045739 | positive regulation of DNA repair |
| Biological Process | GO:1990166 | protein localization to site of double-strand break |
| Biological Process | GO:0010212 | response to ionizing radiation |
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] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.
[5] 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.
[6] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.
[7] 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.
[8] 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.
[9] 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.