Early pregnancy factor

HSPE1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4PJ1
Identifiers
Aliases	HSPE1, heat shock 10kDa protein 1, CPN10, EPF, GROES, HSP10, heat shock protein family E (Hsp10) member 1
External IDs	OMIM: 600141 MGI: 104680 HomoloGene: 20500 GeneCards: HSPE1
Gene ontology Molecular function • chaperone binding • protein binding • ATP binding • metal ion binding • unfolded protein binding • RNA binding Cellular component • cytoplasm • extracellular exosome • membrane • mitochondrion • mitochondrial matrix Biological process • response to unfolded protein • activation of cysteine-type endopeptidase activity involved in apoptotic process • protein folding • osteoblast differentiation • chaperone mediated protein folding requiring cofactor Sources:Amigo / QuickGO
RNA expression pattern
More reference expression data
Orthologs
Species	Human	Mouse
Entrez	3336	15528
Ensembl	ENSG00000115541	ENSMUSG00000073676
UniProt	P61604	Q64433
RefSeq (mRNA)	NM_002157	NM_008303
RefSeq (protein)	NP_002148	NP_032329.1 NP_032329
Location (UCSC)	Chr 2: 197.5 – 197.5 Mb	Chr 1: 55.09 – 55.09 Mb
PubMed search

Cpn10
gp31 co-chaperonin from bacteriophage t4
Identifiers
Symbol	Cpn10
Pfam	PF00166
Pfam clan	CL0296
InterPro	IPR020818
PROSITE	PDOC00576
SCOP	1lep
SUPERFAMILY	1lep
Available protein structures: Pfam structures PDB RCSB PDB; PDBe; PDBj PDBsum structure summary

4PJ1

3336

15528

ENSG00000115541

ENSMUSG00000073676

P61604

Q64433

NM_002157

NM_008303

NP_002148

NP_032329.1
NP_032329

Heat shock 10 kDa protein 1 (Hsp10) also known as chaperonin 10 (cpn10) or early-pregnancy factor (EPF) is a protein that in humans is encoded by the HSPE1 gene. The homolog in E. coli is GroES that is a chaperonin which usually works in conjunction with GroEL.

GroES exists as a ring-shaped oligomer of between six and eight identical subunits, while the 60 kDa chaperonin (cpn60 - or groEL in bacteria) forms a structure comprising 2 stacked rings, each ring containing 7 identical subunits. These ring structures assemble by self-stimulation in the presence of Mg²⁺-ATP. The central cavity of the cylindrical cpn60 tetradecamer provides an isolated environment for protein folding whilst cpn-10 binds to cpn-60 and synchronizes the release of the folded protein in an Mg²⁺-ATP dependent manner. The binding of cpn10 to cpn60 inhibits the weak ATPase activity of cpn60.