EGFR-stimulated S37 phosphorylation of PKM2 promotes its nuclear translocation to support metabolic reprogramming in cancer cells [48]; Insulin growth factor 1 (IGF1)- activated AKT in the cytosol directly phosphorylates PKM2 at another serine residue (S202) to promote its nuclear translocation [49]; PKM2 phosphorylation at threonine T454 has been shown to promote its nuclear translocation and non-glycolytic function by an oncogenic proviral insertion in the gene for murine lymphomas 2 (PIM2), which is a serine/threonine protein kinase [50]. This evidence concerns the gene AKT1 and cancer.