HSPE1 Co-chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp60, facilitates the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. The functional units of these chaperonins consist of heptameric rings of the large subunit Hsp60, which function as a back-to-back double ring. In a cyclic reaction, Hsp60 ring complexes bind one unfolded substrate protein per ring, followed by the binding of ATP and association with 2 heptameric rings of the co-chaperonin Hsp10. This leads to sequestration of the substrate protein in the inner cavity of Hsp60 where, for a certain period of time, it can fold undisturbed by other cell components. Synchronous hydrolysis of ATP in all Hsp60 subunits results in the dissociation of the chaperonin rings and the release of ADP and the folded substrate protein. Belongs to the GroES chaperonin family. Note: This description may include information from UniProtKB.
Protein type: Mitochondrial
Chromosomal Location of Human Ortholog: 2q33.1
Cellular Component:  mitochondrion
Molecular Function:  ATP binding; chaperone binding; protein binding; unfolded protein binding
Biological Process:  activation of cysteine-type endopeptidase activity involved in apoptotic process; protein folding; response to unfolded protein
Reference #:  P61604 (UniProtKB)
Alt. Names/Synonyms: 10 kDa chaperonin; 10 kDa heat shock protein, mitochondrial; CH10; Chaperonin 10; CPN10; Early-pregnancy factor; EPF; epididymis secretory sperm binding protein; GROES; heat shock 10kD protein 1 (chaperonin 10); heat shock 10kDa protein 1; heat shock 10kDa protein 1 (chaperonin 10); heat shock protein family E (Hsp10) member 1; Hsp10; HSPE1
Gene Symbols: HSPE1
Molecular weight: 10,932 Da
Basal Isoelectric point: 8.89  Predict pI for various phosphorylation states
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HSPE1

Protein Structure Not Found.


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