Chaperone
Cytoplasmic proteins of both prokaryotes and eukaryotes that bind to nascent or unfolded polypeptides and ensure correct folding or transport. Chaperone proteins do not covalently bind to their targets and do not form part of the finished product. Heat-shock proteins are an important sub set of chaperones. Three major families are recognised, the chaperonins (groEL and hsp60), the hsp70 family and the hsp90 family. Outside these major families are other proteins with similar functions including nucleoplasmin, secB and T-cell receptor associated protein. [ ]
Term info
Chaperone
- Chaperone
- Molecular Chaperone
Chaperone
Chaperone
Amino Acid, Peptide, or Protein
C0243041
C17764
Term relations
- Protein, Organized by Function
- Gene_Product_Has_Biochemical_Function some Regulatory Protein
- Gene_Product_Encoded_By_Gene some Chaperone Gene
- Gene_Product_Plays_Role_In_Biological_Process some Protein Folding
- Gene_Product_Plays_Role_In_Biological_Process some Subcellular Protein Targeting