These included: S351, which can be phosphorylated by Akt and is crucial for Nur77 tumor suppression activity (30, 31); L449W, which affects optimal occupation of an acyl chain in the bulky binding pocket and is required for the optimal trihydroxybenzene potency (32); S533, which can be phosphorylated by Akt2 (32); S553A, which alters the native surface feature of the LBD (33); and K577A, which alters a canonical SUMOylation consensus motif within the LBD (34). This evidence concerns the gene AKT2 and neoplasm.