HSPE1: Polycystic Ovarian Syndrome Database

Gene Information

Gene Symbol

HSPE1

Aliases

CPN10, EPF, GROES, HSP10

Entrez Gene ID

3336

Gene Name

Heat shock protein family E (Hsp10) member 1

Chromosomal Location

2q33.1

HGNC ID

HGNC:5269

Summary

This gene 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. This gene and its co-chaperonin, HSPD1, are arranged in a head-to-head orientation on chromosome 2. Naturally occurring read-through transcription occurs between this locus and the neighboring locus MOBKL3.[provided by RefSeq, Feb 2011]

RefSeq DNA

NG_008914.1

RefSeq mRNA

NM_002157.3

e!Ensembl

Gene	ENSG00000115541
Transcript	ENST00000233893, ENST00000409729, ENST00000409468
Protein	ENSP00000233893, ENSP00000387101, ENSP00000386447

Gene Ontology (GO)

Show/Hide all(16 )

GO ID	Ontology	Function	Evidence	Reference
GO:0001649	Biological process	Osteoblast differentiation	HDA	16210410
GO:0006457	Biological process	Protein folding	TAS	7698325
GO:0006919	Biological process	Activation of cysteine-type endopeptidase activity involved in apoptotic process	NAS	10205158
GO:0006986	Biological process	Response to unfolded protein	TAS	7698325
GO:0051085	Biological process	Chaperone cofactor-dependent protein refolding	IBA	21873635
GO:0005739	Cellular component	Mitochondrion	IDA	10205158
GO:0005759	Cellular component	Mitochondrial matrix	IBA	21873635
GO:0016020	Cellular component	Membrane	HDA	16210410
GO:0070062	Cellular component	Extracellular exosome	HDA	20458337
GO:0003723	Molecular function	RNA binding	HDA	22658674
GO:0005515	Molecular function	Protein binding	IPI	9989505
GO:0046872	Molecular function	Metal ion binding	IBA	21873635
GO:0051082	Molecular function	Unfolded protein binding	IBA	21873635
GO:0051082	Molecular function	Unfolded protein binding	NAS	7916212, 12483302
GO:0051087	Molecular function	Chaperone binding	IBA	21873635
GO:0051087	Molecular function	Chaperone binding	IPI	10205158

Protein Information

Protein Name

10 kDa heat shock protein, mitochondrial, 10 kDa chaperonin, chaperonin 10, early-pregnancy factor, epididymis secretory sperm binding protein, heat shock 10kD protein 1 (chaperonin 10), heat shock 10kDa protein 1

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 (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).

Refseq Proteins

NP_002148.1

UniProt

P61604

PDB

4PJ1

Pfam

Pfam Accession	Pfam ID
PF00166	Cpn10