H2AFX

H2AFX (H2A histone family, member X) is one of several is_associated_with::genes coding for is_associated_with::histone H2A. In humans and other is_associated_with::eukaryotes, the is_associated_with::DNA is wrapped around is_associated_with::histone-groups, consisting of is_associated_with::core histones H2A, H2B, H3 and H4. Thus, the H2AX contributes to the nucleosome-formation and therefore the structure of DNA.

H2AX becomes phosphorylated on serine 139, then called gamma-H2AX, as a reaction on DNA Double-strand breaks (DSB). The kinases of the PI3-family (is_associated_with::Ataxia telangiectasia mutated, ATR and DNA-PKcs) are responsible for this phosphorylation, especially ATM. The modification can happen accidentally during replication fork collapse or in the response to ionizing radiation but also during controlled physiological processes such as V(D)J recombination. Gamma-H2AX is a sensitive target for looking at DSBs in cells. The role of the phosphorylated form of the histone in DNA repair is under discussion but it is known that because of the modification the DNA becomes less condensed, potentially allowing space for the recruitment of proteins necessary during repair of DSBs. Mutagenesis experiments have shown that the modification is necessary for the proper formation of ionizing radiation induced foci in response to double strand breaks, but is not required for the recruitment of proteins to the site of DSBs.

Interactions
H2AX has been shown to interact with is_associated_with::MDC1, is_associated_with::Nibrin, is_associated_with::TP53BP1,   is_associated_with::Bloom syndrome protein, is_associated_with::BRCA1   and is_associated_with::BARD1.