Suppression of tumorigenicity 13 protein (Hsp70-interacting protein) (ST13 (HIP))

Suppression of tumorigenicity 13 protein (Hsp70-interacting protein), commonly called **ST13** or **HIP**, is a cytosolic co-chaperone that interacts with the ATPase domain of the heat shock proteins HSP70 and Hsc70, stabilizing their ADP-bound state to facilitate high-affinity substrate binding, protein folding, and repair[1][2][3][4]. HIP acts by bridging HSP70 and HSP90 chaperone systems and participates in the assembly of steroid hormone receptor complexes, such as the glucocorticoid receptor[1][2]. While its name and some data suggest a tumor suppressor function, robust evidence for this is mainly limited to observed downregulation in specific tumor types (notably colorectal and gastric cancers)[1][2]. HIP's roles in neurodegeneration, endocrinological disorders, and other disease processes are potential but not conclusively established. There are currently no approved drugs targeting ST13/HIP directly, nor well-defined safety concerns, but its involvement in chaperone activity means that modulation could theoretically impact cell survival and proteostasis[1][2][3].

Other names

Hsp70-interacting proteinHIPHsc70-interacting proteinST13FAM10A1SNC6HSPABP1P48Aging-associated protein 2Progesterone receptor-associated p48 proteinRenal carcinoma antigen NY-REN-33Putative tumor suppressor ST13

Not drug-targeted in clinical pharmacology; mechanistically, supports and stabilizes Hsp70/HSC70 chaperone activity by binding their ATPase domain and promoting substrate protein folding[1][2][3].