| Modification Notes |
The heat shock proteins (HSPs) comprise a group of highly conserved, abundantly expressed proteins with diverse functions, which include the assembly and sequestering of multiprotein complexes, transportation of nascent polypeptide chains across cellular membranes and regulation of protein folding. Heat shock proteins (also known as molecular chaperones) fall into six general families: HSP 90, HSP 70, HSP 60, the low molecular weight HSPs, the immunophilins and the HSP 105 family. STCH, also known as HSPA13 (heat shock 70 kDa protein, member 13) or microsomal stress 70 protein ATPase core, is a 471 amino acid protein belonging to the HSP 70 protein family. Localized to the Endoplasmic Reticulum, STCH has peptide-independent ATPase activity. Fundamentally expressed in all tissues, STCH has been found to interact with PLIC-1 and PLIC-2, proteins involved in the signaling connection between the membrane receptors for Thrombospondin and the cytoskeleton. |