In addition, it has been reported that the increased expression of AHA1 alters the activity of Hsp90 client proteins and the phosphorylation status of key signaling proteins, including Akt, resulting in enhanced kinase activity36–38, and affects the efficacy of Hsp90 inhibitors, such as Tanespimycin (17-N-allylamino-17-demethoxygeldanamycin, 17-AAG), in cancer cells. The gene discussed is HSP90AB1; the disease is cancer.