One HIP oligomer binds the ATPase domains of at least two HSC70 molecules dependent on activation of the HSC70 ATPase by HSP40. Stabilizes the ADP state of HSC70 that has a high affinity for substrate protein. Through its own chaperone activity, it may contribute to the interaction of HSC70 with various target proteins. Homotetramer. Interacts with HSC70 as well as DNAJ homologs and HSP90. Interacts (via the C-terminus 303- 319 AA) with GRK5. Belongs to the FAM10 family. Note: This description may include information from UniProtKB.
Cellular Component: cytoplasm; cytosol; protein complex
Molecular Function: chaperone binding; dATP binding; Hsp70 protein binding; identical protein binding; protein binding; protein binding, bridging; protein complex binding; protein domain specific binding; unfolded protein binding
Biological Process: protein folding; protein homooligomerization
LTP: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.