Aliases for H2AFX Gene
External Ids for H2AFX Gene
Previous HGNC Symbols for H2AFX Gene
Previous GeneCards Identifiers for H2AFX Gene
Histones are basic nuclear proteins that are responsible for the nucleosome structure of the chromosomal fiber in eukaryotes. Two molecules of each of the four core histones (H2A, H2B, H3, and H4) form an octamer, around which approximately 146 bp of DNA is wrapped in repeating units, called nucleosomes. The linker histone, H1, interacts with linker DNA between nucleosomes and functions in the compaction of chromatin into higher order structures. This gene encodes a replication-independent histone that is a member of the histone H2A family, and generates two transcripts through the use of the conserved stem-loop termination motif, and the polyA addition motif. [provided by RefSeq, Oct 2015]
GeneCards Summary for H2AFX Gene
H2AFX (H2A Histone Family Member X) is a Protein Coding gene. Diseases associated with H2AFX include Nijmegen Breakage Syndrome and Ataxia-Telangiectasia. Among its related pathways are DNA Double-Strand Break Repair and Activated PKN1 stimulates transcription of AR (androgen receptor) regulated genes KLK2 and KLK3. GO annotations related to this gene include sequence-specific DNA binding and enzyme binding. An important paralog of this gene is HIST1H2AC.
UniProtKB/Swiss-Prot for H2AFX Gene
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.