Search Results
Overview
| Uniprot ID | P26772 |
|---|---|
| Protein Name | 10 kDa heat shock protein, mitochondrial |
| Gene Name | Hspe1 |
| Organism | Rattus norvegicus |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 28 | SAAETVTKGGIMLPE |
| 36 | GGIMLPEKSQGKVLQ |
| 40 | LPEKSQGKVLQATVV |
| 54 | VAVGSGGKGKGGEIQ |
| 56 | VGSGGKGKGGEIQPV |
| 66 | EIQPVSVKVGDKVLL |
| 70 | VSVKVGDKVLLPEYG |
| 8 | MAGQAFRKFLPLFDR |
| 86 | TKVVLDDKDYFLFRD |
Function
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
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005759 | mitochondrial matrix |
| Cellular Component | GO:0005739 | mitochondrion |
| Molecular Function | GO:0005524 | ATP binding |
| Molecular Function | GO:0046872 | metal ion binding |
| Molecular Function | GO:0044183 | protein folding chaperone |
| Molecular Function | GO:0051087 | protein-folding chaperone binding |
| Molecular Function | GO:0051082 | unfolded protein binding |
| Biological Process | GO:0006457 | protein folding |
Reference
[1] Sheng L, Xu H, Wang Y, Ni J, Xiang T et al.. Systematic analysis of lysine lactylation in nucleus pulposus cells.. iScience 27(11):111157. 2024 Nov 15. PMID: 39524337.
[2] Chen Y, Sun W, Sun Z, Zhao H, Wu T et al.. Effect of electroacupuncture on hippocampal protein lactylation in a rat model of vascular dementia.. Front Neurol 16:1629474. 2025. PMID: 40963935.