Pathway candidateNCBI-verifiedprotein-coding

HSPE1

heat shock protein family E (Hsp10) member 1

NCBI Gene: 3336 Ensembl GeneCards UniProt: P61604

Pathway candidate — not linked to PFS or PSSD by any record here

HSPE1 is in the library because it belongs to the receptor chaperones family. No study, report or commentary in the corpus names it, so a variant in HSPE1 is not, by itself, evidence of anything related to post-drug syndromes.

Gene summary

A protein-coding gene on chromosome 2 (steroid receptor chaperones). Encodes a major heat shock protein which functions as a chaperonin. Its structure consists of a heptameric ring which binds to another heat shock protein in order to form a symmetric, functional heterodimer which enhances protein folding in an ATP-dependent manner.

Source: NCBI Gene, accessed 2026-10-07.

Protein reference (UniProt)

Protein: 10 kDa heat shock protein, mitochondrial
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 (Probable).
Subcellular location: Mitochondrion matrix.

Source: UniProtKB/Swiss-Prot P61604, release 2026_03, licensed CC BY 4.0. This is the protein’s normal biology, not evidence about post-drug syndromes; associated conditions are inherited disorders of the gene, not PFS, PSSD or PRSD.

Why its pathway is in the library

Chaperone/co-chaperone control of steroid-receptor folding and sensitivity is a regulatory layer above the receptors themselves, tied to stress-axis signaling.

Written for the whole receptor chaperones family, not for HSPE1 specifically.

Mentioned in 0 corpus records

No corpus record names HSPE1 directly yet. It is in the library because it sits in a pathway the corpus tracks (Receptor chaperones).

Also in steroid receptor chaperones

All 14 genes

Browse by family on the gene families page.

Gene summary

Source: NCBI Gene, accessed 2026-10-07.

Protein reference (UniProt)

Protein: 10 kDa heat shock protein, mitochondrial
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 (Probable).
Subcellular location: Mitochondrion matrix.