Overview
| Uniprot ID | P27661 |
| Protein Name | Histone H2AX |
| Gene Name | H2ax |
| Organism | Mus musculus |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 128 |
SSATVGPKAPAVGKK |
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
10
MSGRGKTGGK
20
ARAKAKSRSS
30
RAGLQFPVGR
40
VHRLLRKGHY
50
AERVGAGAPV
60
YLAAVLEYLT
70
AEILELAGNA
80
ARDNKKTRII
90
PRHLQLAIRN
100
DEELNKLLGG
110
VTIAQGGVLP
120
NIQAVLLPKK
130
SSATVGPKAP
140
AVGKKASQAS
QEY
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005813 |
centrosome |
| Cellular Component |
GO:0000785 |
chromatin |
| Cellular Component |
GO:0005694 |
chromosome |
| Cellular Component |
GO:0000781 |
chromosome, telomeric region |
| Cellular Component |
GO:0000794 |
condensed nuclear chromosome |
| 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: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:0071480 |
cellular response to gamma radiation |
| Biological Process |
GO:0000077 |
DNA damage checkpoint signaling |
| Biological Process |
GO:0006974 |
DNA damage response |
| Biological Process |
GO:0006281 |
DNA repair |
| Biological Process |
GO:0000724 |
double-strand break repair via homologous recombination |
| Biological Process |
GO:0031507 |
heterochromatin formation |
| Biological Process |
GO:0051321 |
meiotic cell cycle |
| Biological Process |
GO:1905168 |
positive regulation of double-strand break repair via homologous recombination |
| Biological Process |
GO:0070534 |
protein K63-linked ubiquitination |
| Biological Process |
GO:1990166 |
protein localization to site of double-strand break |
| Biological Process |
GO:0007283 |
spermatogenesis |
Reference
[1] Zhuo W, Zhang M, Tan J, Gao Y, Wang Y et al.. Lysine lactylation analysis of proteins in the heart of the Kawasaki disease mouse model.. Front Cell Dev Biol 13:1550220. 2025. PMID: 40114965.