InterPro domain: IPR034649

The Hsc70/Hsp70-interacting protein (Hip, also p48 or suppressor of tumorigenicity ST13) functions as a regulator of the cyclic action of Hsp70. Hip forms homodimers, and this entry represents the N-terminal dimerization domain, which may not be directly involved in its regulatory function. A central domain of Hip that contains TPR repeats binds the ATPase domain of Hsp70 and slows the release of ADP [ 1 , 2 , 3 , 4 ].

1. Structure and function of Hip, an attenuator of the Hsp70 chaperone cycle. Nat. Struct. Mol. Biol. 20, 929-35
2. Low resolution structural characterization of the Hsp70-interacting protein - Hip - from Leishmania braziliensis emphasizes its high asymmetry. Arch. Biochem. Biophys. 520, 88-98
3. Mutational analysis of the hsp70-interacting protein Hip. Mol. Cell. Biol. 16, 6200-7
4. Orthologs in Arabidopsis thaliana of the Hsp70 interacting protein Hip. Cell Stress Chaperones 6, 247-55