H2AX 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. Belongs to the histone H2A family. Note: This description may include information from UniProtKB.
Protein type: DNA repair, damage; DNA-binding; Helicase
Chromosomal Location of Human Ortholog: 9 A5.2|9 24.84 cM
Cellular Component:  centrosome; chromatin; chromosome; condensed nuclear chromosome; male germ cell nucleus; nuclear chromatin; nuclear speck; nucleoplasm; nucleosome; nucleus; replication fork; site of DNA damage; site of double-strand break; XY body
Molecular Function:  damaged DNA binding; DNA binding; enzyme binding; histone binding; protein binding; protein heterodimerization activity
Biological Process:  cell cycle; cellular response to DNA damage stimulus; cellular response to gamma radiation; chromatin organization; DNA recombination; DNA repair; double-strand break repair via homologous recombination; meiotic cell cycle; spermatogenesis
Reference #:  P27661 (UniProtKB)
Alt. Names/Synonyms: AW228881; H2A histone family, member X; H2a.x; H2a/x; H2afx; H2ax; Hist5-2ax; histone 5 protein 2ax; Histone H2A.x; Histone H2AX
Gene Symbols: H2afx
Molecular weight: 15,011 Da
Basal Isoelectric point: 10.74  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
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H2AX

Protein Structure Not Found.


Cross-references to other databases:  STRING  |  Reactome  |  BioGPS  |  Pfam  |  Phospho.ELM  |  NetworKIN  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene