Hspe1 heat shock protein 1 (chaperonin 10) [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Hspe1provided by MGI
Official Full Name: heat shock protein 1 (chaperonin 10)provided by MGI
Primary source: MGI:MGI:104680
See related: Ensembl:ENSMUSG00000073676 AllianceGenome:MGI:104680
Gene type: protein coding
RefSeq status: VALIDATED
Organism: Mus musculus
Lineage: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; Murinae; Mus; Mus
Also known as: 10kDa; Hsp10; mt-cpn10
Summary: Predicted to enable metal ion binding activity; protein-folding chaperone binding activity; and unfolded protein binding activity. Predicted to be involved in chaperone cofactor-dependent protein refolding. Located in mitochondrion. Is expressed in brain; brainstem nucleus; early conceptus; and midbrain ventricular layer. Orthologous to human HSPE1 (heat shock protein family E (Hsp10) member 1). [provided by Alliance of Genome Resources, Nov 2024]
Expression: Broad expression in liver E14 (RPKM 162.7), placenta adult (RPKM 143.3) and 21 other tissues See more
Orthologs: human all
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Genomic context

Location:: 1 C1.2; 1 28.02 cM

Exon count:: 4

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	1	NC_000067.7 (55127307..55130476)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	1	NC_000067.6 (55088148..55091317)

Chromosome 1 - NC_000067.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Genomic Sequence:

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Expression

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See details

Project title: Mouse ENCODE transcriptome data
Description: RNA profiling data sets generated by the Mouse ENCODE project.
BioProject: PRJNA66167
Publication: PMID 25409824
Analysis date: n/a

Bibliography

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GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Tat-heat shock protein 10 ameliorates age-related phenotypes by facilitating neuronal plasticity and reducing age-related genes in the hippocampus.
Title: Tat-heat shock protein 10 ameliorates age-related phenotypes by facilitating neuronal plasticity and reducing age-related genes in the hippocampus.
heat shock protein 10 is a Sirtuin 3 substrate
Title: Prolonged fasting identifies heat shock protein 10 as a Sirtuin 3 substrate: elucidating a new mechanism linking mitochondrial protein acetylation to fatty acid oxidation enzyme folding and function.
expression increased as larger area and higher level of density during ovarian follicular development
Title: Involvement of HSP10 during the ovarian follicular development of polycystic ovary syndrome: Study in both human ovaries and cultured mouse follicles.
interaction between HSPE1 and HSPD1 in the reproductive tract and in capacitating spermatozoa
Title: Identification of the molecular chaperone, heat shock protein 1 (chaperonin 10), in the reproductive tract and in capacitating spermatozoa in the male mouse.
Hsp10 exerts anti-inflammatory activity by inhibiting Toll-like receptor signaling possibly by interacting with extracellular Hsp60
Title: Heat shock protein 10 inhibits lipopolysaccharide-induced inflammatory mediator production.

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Variation

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Alleles

Alleles of this type are documented at Mouse Genome Informatics (MGI)

Gene trapped (1)

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Markers

RH127488 (e-PCR)
- UniSTS:210798

AW108200 (e-PCR)
- UniSTS:181116

Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables metal ion binding	IBA Inferred from Biological aspect of Ancestor more info
enables protein folding chaperone	IEA Inferred from Electronic Annotation more info
enables protein-folding chaperone binding	IBA Inferred from Biological aspect of Ancestor more info
enables protein-folding chaperone binding	ISO Inferred from Sequence Orthology more info
enables protein-folding chaperone binding	ISS Inferred from Sequence or Structural Similarity more info
enables unfolded protein binding	IBA Inferred from Biological aspect of Ancestor more info

Process	Evidence Code	Pubs
involved_in chaperone cofactor-dependent protein refolding	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein folding	IEA Inferred from Electronic Annotation more info

Component	Evidence Code	Pubs
is_active_in mitochondrial matrix	IBA Inferred from Biological aspect of Ancestor more info
located_in mitochondrial matrix	IEA Inferred from Electronic Annotation more info
located_in mitochondrial matrix	ISO Inferred from Sequence Orthology more info
located_in mitochondrion	HDA more info	PubMed
is_active_in mitochondrion	IBA Inferred from Biological aspect of Ancestor more info
located_in mitochondrion	ISO Inferred from Sequence Orthology more info
located_in mitochondrion	ISS Inferred from Sequence or Structural Similarity more info

General protein information

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Preferred Names: 10 kDa heat shock protein, mitochondrial

Names: 10 kDa chaperonin; CPN10; chaperonin 10; heat shock 10 kDa protein 1 (chaperonin 10); mitochondrial chaperonin 10

NCBI Reference Sequences (RefSeq)

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RefSeqs maintained independently of Annotated Genomes

These reference sequences exist independently of genome builds. Explain

These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above.

mRNA and Protein(s)

NM_008303.4 → NP_032329.1 10 kDa heat shock protein, mitochondrial

See identical proteins and their annotated locations for NP_032329.1

Status: VALIDATED

Source sequence(s)

AV570511, BC099385, CJ238411

Consensus CDS

CCDS35570.1

UniProtKB/Swiss-Prot

Q64433

UniProtKB/TrEMBL

Q4KL76, Q9JI95

Related

ENSMUSP00000074724.7, ENSMUST00000075242.7

Conserved Domains (1) summary

cd00320
Location:8 → 100

cpn10; Chaperonin 10 Kd subunit (cpn10 or GroES); Cpn10 cooperates with chaperonin 60 (cpn60 or GroEL), an ATPase, to assist the folding and assembly of proteins and is found in eubacterial cytosol, as well as in the matrix of mitochondria and chloroplasts. It ...