HSPE1 report

I. Expression across cell types

II. Expression across tissues

III. Associated gene sets

GO_0006457Biological processprotein folding
GO_0006919Biological processactivation of cysteine-type endopeptidase activity involved in apoptotic process
GO_0006986Biological processresponse to unfolded protein
GO_0001649Biological processosteoblast differentiation
GO_0051085Biological processchaperone cofactor-dependent protein refolding
GO_0070062Cellular componentextracellular exosome
GO_0005739Cellular componentmitochondrion
GO_0016020Cellular componentmembrane
GO_0005759Cellular componentmitochondrial matrix
GO_0044183Molecular functionprotein folding chaperone
GO_0051087Molecular functionprotein-folding chaperone binding
GO_0005515Molecular functionprotein binding
GO_0046872Molecular functionmetal ion binding
GO_0005524Molecular functionATP binding
GO_0051082Molecular functionunfolded protein binding
GO_0003723Molecular functionRNA binding

IV. Literature review

[source]
Gene nameHSPE1
Protein nameHeat shock 10kDa protein 1 (Chaperonin 10), isoform CRA_h (Heat shock protein family E (Hsp10) member 1)
10 kDa heat shock protein, mitochondrial (Hsp10) (10 kDa chaperonin) (Chaperonin 10) (CPN10) (Early-pregnancy factor) (EPF)
10 kDa heat shock protein, mitochondrial (10 kDa chaperonin) (Chaperonin 10)
SynonymshCG_21429
DescriptionFUNCTION: 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 (Probable). .

AccessionsENST00000409729.1
ENST00000233893.10
ENST00000409468.1
B8ZZ54
B8ZZL8
P61604