XB-FEAT-22066189: Difference between revisions
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as ''Xenopus'' has a gene duplication, this genes'root name changed but kept the gene 2 suffix [.2], so is now ''h2ax.2'' H2A.X variant histone gene 2 | as ''Xenopus'' has a gene duplication, this genes'root name changed but kept the gene 2 suffix [.2], so is now ''h2ax.2'' H2A.X variant histone gene 2 | ||
=summary from NCBI fro human H2AX= | |||
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] | |||
Latest revision as of 11:33, 2 July 2020
nomenclature changes
06.30.2020 Human symbol has changed for genepage ID: 22066189 From h2afx to h2ax (H2A.X variant histone)
as Xenopus has a gene duplication, this genes'root name changed but kept the gene 2 suffix [.2], so is now h2ax.2 H2A.X variant histone gene 2
summary from NCBI fro human H2AX
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]