Fraction of the 2000 identified somatic mutations in cancer that involve histidine subsitutions

Value 15 %
Organism Human Homo sapiens
Reference Damaghi M, Wojtkowiak JW, Gillies RJ. pH sensing and regulation in cancer. Front Physiol. 2013 Dec 17 4 :370. doi: 10.3389/fphys.2013.00370. p.2 left column 2nd paragraphPubMed ID24381558
Primary Source Kan, Z. et al., (2010). Diverse somatic mutation patterns and pathway alterations in human cancers. Nature 466, 869–873.doi:10.1038/nature09208PubMed ID20668451
Comments p.2 left column 2nd paragraph:"Although under-represented in the human proteome with ~2% frequency (Webb et al., 2011), histidines are found in critical regions of G-protein coupled receptors, GPCRs (OGR1 and GPR4), intracellular molecules involved in actin assembly (Talin and Cofilin), membrane proton pumps and acid-sensing ion channels, ASICs (Schonichen et al., 2013b). Protonation and de-protonation has been experimentally shown to change protein structure and thus, alter protein-protein binding affinity, change protein stability, modify protein function, and alter subcellular localization (Schonichen et al., 2013b). Evolutionarily, histidines must confer some selective advantage for cancers, as 15% of the 2000 identified somatic mutations in cancer involve histidine subsitutions, with Arg-to-His being the most frequent (primary source)."
Entered by Uri M
ID 112179