10 kDa heat shock protein, mitochondrial (HSPE1)
The protein contains 102 amino acids for an estimated molecular weight of 10932 Da.
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 (PubMed:7912672, PubMed:1346131, PubMed:11422376). 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). (updated: Oct. 10, 2018)
Protein identification was indicated in the following studies:
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- Chu and co-workers. (2018) Quantitative mass spectrometry of human reticulocytes reveal proteome-wide modifications during maturation. Br J Haematol. 180(1), 118-133.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
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Biological Process
Activation of cysteine-type endopeptidase activity involved in apoptotic process
Chaperone cofactor-dependent protein refolding
Osteoblast differentiation
Protein folding
Response to unfolded protein
Molecular Function
ATP binding
ATPase
Chaperone binding
Metal ion binding
RNA binding
Unfolded protein binding
The reference OMIM entry for this protein is 600141
Heat-shock 10-kd protein; hspe1
Chaperonin 10 homolog
Cpn10 homolog
Groes homolog; groes
Hsp10
DESCRIPTION
Chaperonins are ubiquitous, indispensable proteins that facilitate protein folding in an ATP-dependent manner (Todd et al., 1994), enhancing the yield of properly folded substrate protein under conditions where spontaneous folding does not occur. Chaperonins are typified by the E. coli heat-shock proteins GroEL (cpn60; 118190) and GroES (cpn10). GroES is a heptameric ring of identical 10.4-kD subunits that binds to each end of GroEL to form a symmetric, functional heterodimer.CLONING
Monzini et al. (1994) found complete identity of human and bovine chaperonin 10 cDNA. See reviews by Zeilstra-Ryalls et al. (1991) and Georgopoulos and Welch (1993). Hansen et al. (2003) presented the full sequence of the HSP60 (GroEL) and HSP10 genes.GENE FUNCTION
Using a luciferase-reporter assay, Hansen et al. (2003) demonstrated that the region between the HSP10 and HSP60 (118190) genes functions as a bidirectional promoter. The transcriptional activity of the promoter fragment in the HSP60 direction is approximately twice that in the HSP10 direction under normal growth conditions; upon heat shock, promoter activity in either direction increased by a factor of approximately 12. Tokuriki and Tawfik (2009) examined the ability of the E. coli GroEL/GroES chaperonins to buffer destabilizing and adaptive mutations. Mutational drifts performed in vitro with 4 different enzymes indicated the GroEL/GroES overexpression doubled the number of accumulating mutations, and promoted the folding of enzyme variants carrying mutations in the protein core and/or mutations with higher destabilizing effects. The divergence of modified enzymatic specificity occurred much faster under GroEL/GroES overexpression, in terms of the number of adapted variants (greater than or equal to 2-fold) and their improved specificity and activity (greater than or equal to 10-fold). Tokuriki and Tawfik (2009) concluded that protein stability is a major constraint in protein evolution, and that buffering mechanisms such as chaperonins are key in alleviating this constraint.GENE STRUCTURE
Hansen et al. (2003) found that the HSP10 gene consists of 4 exons. The authors demonstrated that the 2 genes are linked head to head. The first exon of HSP60 is noncoding, and the first exon of HSP10 ends with the start codon.MAPPING
By radiation hybrid analysis, Hansen et al. (2003) mapped the mitochondrial chaperonin HSP60 (HSPD1; 118190) and its co-chaperonin HSP10 (heat-shock protein 10) between markers AFMA121YH1 and WI-10756 on chromosome 2. This localization and the position of 2 homologous fragments in the human genome assembly were consistent with the cytogenetic location 2q33.1. ... More on the omim web site
June 29, 2020: Protein entry updated
Automatic update: OMIM entry 600141 was added.
Oct. 19, 2018: Additional information
Initial protein addition to the database. This entry was referenced in Bryk and co-workers. (2017).