heat shock protein [hsp] 70, HSP70A or HSP-A

Function

• involved in preventing misfolding of polypeptide chains
• in cooperation with other chaperones, Hsp70s stabilize preexistent proteins against aggregation & mediate folding of newly translated polypeptides in the cytosol as well as within organelles
• these chaperones participate in all these processes through their ability to recognize nonnative conformations of other proteins.
• they bind extended peptide segments with a net hydrophobic character exposed by polypeptides during translation & membrane translocation, or following stress-induced damage
• may be required to maintain protein precursors in translocation-competent form

Compartment

-localizes on lysosomal membrane

Expression

• heat or stress induced protein

Pathology

• overexpression of HSP70 protects fragile lysosomal membranes of cancer cells against lysosomal membrane permeabilization by enhancing activity of acid sphingomyelinase

More general terms

• heat shock protein [hsp]-70 family
• PEST protein
• chaperonin; chaperone

More specific terms

• heat shock 70 kD protein 12A (HSPA12A, KIAA0417)
• heat shock 70 kD protein 12B (HSPA12B, C20orf60)
• heat shock protein [hsp] 70-3 or HSPA3
• heat shock-related 70 kD protein 2; heat shock 70 kD protein 2 (HSPA2)

Component of

• TCP1 ring complex (T-complex protein 1, chaperonin containing T-complex polypeptide 1)