CH60_HUMAN

Evidence for PS localization

GO

G2C

SynGO

SynaptomeDB

HPA (protein expression in neurons)

Functions

Chaperonin implicated in mitochondrial protein import and macromolecular assembly. Together with Hsp10, 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 (PubMed, PubMed). 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 (Probable). [View more on UniProt]

Protein features

Binary interactions with known binding regions

To display all evidence describing the interaction with a partner, click on the protein name left to the bars.

Network

Isoforms

Disease-causing germline mutations

No data found.

Linear motifs

No annotated instance was found. To search for linear motifs, use the ELM prediction server.

Fingerprint

Molecular function

Biological process

Disease

No data found.

All partners