In as many as 1 in 10 cancers,42,43 and in common with several other oncotargets,25 K-Ras4B is seen to undergo a plethora of different mutations37,38,42 and/or PTMs38 that, in ways that are not always allosterically clear38,42 (bar steric disruption of the K-Ras4B–GAP interface, or catalyticinterference, e.g., through mutation of key residuesLys16 or Gln61; Figures S1b and 1),41 hinder GTP cleavageand thus trap the protein in a harmful hyperactive state. This evidence concerns the gene KRAS and cancer.