PKM2 activity is also regulated by phosphorylation; in particular, phosphorylation at Tyr105 disturbs the binding of PKM2 to its allosteric activator fructose-1,6-bisphosphate (FBP), thereby inhibiting tetramer formation and promoting aerobic glycolysis as a metabolic advantage to tumor cells [48]. The gene discussed is PKM; the disease is neoplasm.