Hspd1 heat shock protein 1 (chaperonin) [Mus musculus (house mouse)] - Gene

Summary

Official Symbol: Hspd1provided by MGI
Official Full Name: heat shock protein 1 (chaperonin)provided by MGI
Primary source: MGI:MGI:96242
See related: Ensembl:ENSMUSG00000025980 AllianceGenome:MGI:96242
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: 60kDa; CPN60; Hsp60; HSP-60; HSP-65
Summary: Enables lipopolysaccharide binding activity. Involved in positive regulation of T cell activation and positive regulation of type II interferon production. Acts upstream of or within T cell activation; cellular response to interleukin-7; and positive regulation of interferon-alpha production. Located in migrasome; secretory granule; and sperm plasma membrane. Is active in mitochondrion. Is expressed in several structures, including brain; eye; heart; and urinary system. Used to study hereditary spastic paraplegia 13. Human ortholog(s) of this gene implicated in several diseases, including artery disease (multiple); autistic disorder; glucose intolerance; hereditary spastic paraplegia (multiple); and hypomyelinating leukodystrophy 4. Orthologous to human HSPD1 (heat shock protein family D (Hsp60) member 1). [provided by Alliance of Genome Resources, Nov 2024]
Expression: Broad expression in placenta adult (RPKM 119.5), liver E14 (RPKM 114.0) and 21 other tissues See more
Orthologs: human all
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Genomic context

Location:: 1 C1.2; 1 28.01 cM

Exon count:: 13

Annotation release	Status	Assembly	Chr	Location
RS_2024_02	current	GRCm39 (GCF_000001635.27)	1	NC_000067.7 (55116992..55127402, complement)
108.20200622	previous assembly	GRCm38.p6 (GCF_000001635.26)	1	NC_000067.6 (55077833..55088243, complement)

Chromosome 1 - NC_000067.7 Genomic Context describing neighboring genes

Genomic regions, transcripts, and products

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Go to reference sequence details

Genomic Sequence:

Go to nucleotide: Graphics FASTA GenBank

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?

Cardiac-specific deletion of heat shock protein 60 induces mitochondrial stress and disrupts heart development in mice.
Title: Cardiac-specific deletion of heat shock protein 60 induces mitochondrial stress and disrupts heart development in mice.
Heat Shock Protein 60 Is Involved in Viral Replication Complex Formation and Facilitates Foot and Mouth Virus Replication by Stabilizing Viral Nonstructural Proteins 3A and 2C.
Title: Heat Shock Protein 60 Is Involved in Viral Replication Complex Formation and Facilitates Foot and Mouth Virus Replication by Stabilizing Viral Nonstructural Proteins 3A and 2C.
Heat shock protein 60 couples an oxidative stress-responsive p38/MK2 signaling and NF-kappaB survival machinery in cancer cells.
Title: Heat shock protein 60 couples an oxidative stress-responsive p38/MK2 signaling and NF-κB survival machinery in cancer cells.
HSP60 reduction protects against diet-induced obesity by modulating energy metabolism in adipose tissue.
Title: HSP60 reduction protects against diet-induced obesity by modulating energy metabolism in adipose tissue.
Heat Shock Protein 60 Restricts Release of Mitochondrial dsRNA to Suppress Hepatic Inflammation and Ameliorate Non-Alcoholic Fatty Liver Disease in Mice.
Title: Heat Shock Protein 60 Restricts Release of Mitochondrial dsRNA to Suppress Hepatic Inflammation and Ameliorate Non-Alcoholic Fatty Liver Disease in Mice.
HSP60 knockdown exerts differential response in endothelial cells and monocyte derived macrophages during atherogenic transformation.
Title: HSP60 knockdown exerts differential response in endothelial cells and monocyte derived macrophages during atherogenic transformation.
Heat shock protein 60 (HSP60) modulates adiponectin signaling by stabilizing adiponectin receptor.
Title: Heat shock protein 60 (HSP60) modulates adiponectin signaling by stabilizing adiponectin receptor.
Heat shock protein 60 regulates yolk sac erythropoiesis in mice.
Title: Heat shock protein 60 regulates yolk sac erythropoiesis in mice.
These results unravel a novel LOX-1-dependent pathway by which HSP60C can effectively activate macrophages.
Title: C-terminus of heat shock protein 60 can activate macrophages by lectin-like oxidized low-density lipoprotein receptor 1.
HSP65 and STEAP1 186-193 can significantly inhibit the growth of mouse RM-1 prostate cancer.
Title: Inhibition of mouse RM-1 prostate cancer and B16F10 melanoma by the fusion protein of HSP65 & STEAP1 (186-193).

Submit: New GeneRIF Correction See all GeneRIFs (46)

Variation

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Alleles

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

Endonuclease-mediated (4)
Gene trapped (1)
Targeted (3) 1 citation

Interactions

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Products	Interactant	Other Gene	Complex	Source	Pubs	Description

General gene information

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Gene Ontology Provided by MGI

Function	Evidence Code	Pubs
enables ATP binding	IEA Inferred from Electronic Annotation more info
enables ATP-dependent protein folding chaperone	IEA Inferred from Electronic Annotation more info
enables apolipoprotein A-I binding	IEA Inferred from Electronic Annotation more info
enables apolipoprotein A-I binding	ISO Inferred from Sequence Orthology more info
enables apolipoprotein binding	ISO Inferred from Sequence Orthology more info
enables double-stranded RNA binding	ISO Inferred from Sequence Orthology more info	PubMed
enables enzyme binding	ISO Inferred from Sequence Orthology more info
enables high-density lipoprotein particle binding	IEA Inferred from Electronic Annotation more info
enables high-density lipoprotein particle binding	ISO Inferred from Sequence Orthology more info
enables isomerase activity	IEA Inferred from Electronic Annotation more info
enables lipopolysaccharide binding	IDA Inferred from Direct Assay more info	PubMed
enables lipopolysaccharide binding	ISO Inferred from Sequence Orthology more info
enables modification-dependent protein binding	ISO Inferred from Sequence Orthology more info
enables p53 binding	IEA Inferred from Electronic Annotation more info
enables p53 binding	ISO Inferred from Sequence Orthology more info
enables protein-containing complex binding	ISO Inferred from Sequence Orthology more info
enables protein-folding chaperone binding	IBA Inferred from Biological aspect of Ancestor more info
enables protein-folding chaperone binding	IEA Inferred from Electronic Annotation more info
enables protein-folding chaperone binding	ISO Inferred from Sequence Orthology more info
enables ubiquitin protein ligase binding	IEA Inferred from Electronic Annotation more info
enables ubiquitin protein ligase binding	ISO Inferred from Sequence Orthology more info

Process	Evidence Code	Pubs
involved_in B cell activation	ISO Inferred from Sequence Orthology more info
involved_in B cell proliferation	IEA Inferred from Electronic Annotation more info
involved_in B cell proliferation	ISO Inferred from Sequence Orthology more info
involved_in MyD88-dependent toll-like receptor signaling pathway	IEA Inferred from Electronic Annotation more info
involved_in MyD88-dependent toll-like receptor signaling pathway	ISO Inferred from Sequence Orthology more info
involved_in T cell activation	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within T cell activation	IDA Inferred from Direct Assay more info	PubMed
acts_upstream_of_or_within T cell activation	IGI Inferred from Genetic Interaction more info	PubMed
acts_upstream_of_or_within T cell activation	ISO Inferred from Sequence Orthology more info
NOT involved_in adhesion of symbiont to host	IDA Inferred from Direct Assay more info	PubMed
involved_in apoptotic mitochondrial changes	IBA Inferred from Biological aspect of Ancestor more info
involved_in apoptotic mitochondrial changes	ISO Inferred from Sequence Orthology more info
involved_in biological process involved in interaction with symbiont	IEA Inferred from Electronic Annotation more info
involved_in biological process involved in interaction with symbiont	ISO Inferred from Sequence Orthology more info
acts_upstream_of_or_within cellular response to interleukin-7	IDA Inferred from Direct Assay more info	PubMed
acts_upstream_of interferon-alpha production	IDA Inferred from Direct Assay more info	PubMed
involved_in isotype switching to IgG isotypes	IEA Inferred from Electronic Annotation more info
involved_in isotype switching to IgG isotypes	ISO Inferred from Sequence Orthology more info
involved_in mitochondrial unfolded protein response	IBA Inferred from Biological aspect of Ancestor more info
involved_in negative regulation of apoptotic process	IEA Inferred from Electronic Annotation more info
involved_in negative regulation of apoptotic process	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of apoptotic process in bone marrow cell	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of neuron apoptotic process	ISO Inferred from Sequence Orthology more info
involved_in negative regulation of reactive oxygen species biosynthetic process	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of T cell activation	IBA Inferred from Biological aspect of Ancestor more info
involved_in positive regulation of T cell activation	IDA Inferred from Direct Assay more info	PubMed
involved_in positive regulation of T cell activation	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of T cell mediated immune response to tumor cell	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of T cell mediated immune response to tumor cell	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of apoptotic process	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of apoptotic process	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of cysteine-type endopeptidase activity	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of interferon-alpha production	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within positive regulation of interferon-alpha production	IDA Inferred from Direct Assay more info	PubMed
involved_in positive regulation of interferon-alpha production	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of interleukin-10 production	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of interleukin-10 production	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of interleukin-12 production	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of interleukin-12 production	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of interleukin-6 production	IBA Inferred from Biological aspect of Ancestor more info
involved_in positive regulation of interleukin-6 production	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of interleukin-6 production	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of macrophage activation	IEA Inferred from Electronic Annotation more info
involved_in positive regulation of macrophage activation	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of tumor necrosis factor production	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of type II interferon production	IBA Inferred from Biological aspect of Ancestor more info
acts_upstream_of_or_within positive regulation of type II interferon production	IDA Inferred from Direct Assay more info	PubMed
involved_in positive regulation of type II interferon production	IDA Inferred from Direct Assay more info	PubMed
acts_upstream_of_or_within positive regulation of type II interferon production	IGI Inferred from Genetic Interaction more info	PubMed
acts_upstream_of_or_within positive regulation of type II interferon production	ISO Inferred from Sequence Orthology more info
involved_in positive regulation of type II interferon production	ISO Inferred from Sequence Orthology more info
involved_in protein folding	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein import into mitochondrial intermembrane space	IBA Inferred from Biological aspect of Ancestor more info
involved_in protein refolding	IEA Inferred from Electronic Annotation more info
involved_in protein refolding	ISO Inferred from Sequence Orthology more info
involved_in protein stabilization	IEA Inferred from Electronic Annotation more info
involved_in protein stabilization	ISO Inferred from Sequence Orthology more info
involved_in response to cold	ISS Inferred from Sequence or Structural Similarity more info
involved_in response to unfolded protein	IEA Inferred from Electronic Annotation more info
involved_in response to unfolded protein	ISO Inferred from Sequence Orthology more info
acts_upstream_of type II interferon production	IDA Inferred from Direct Assay more info	PubMed
acts_upstream_of type II interferon production	IGI Inferred from Genetic Interaction more info	PubMed

Component	Evidence Code	Pubs
located_in Golgi cisterna	ISO Inferred from Sequence Orthology more info
located_in cell surface	IEA Inferred from Electronic Annotation more info
located_in cell surface	ISO Inferred from Sequence Orthology more info
located_in clathrin-coated pit	IEA Inferred from Electronic Annotation more info
located_in clathrin-coated pit	ISO Inferred from Sequence Orthology more info
located_in coated vesicle	IEA Inferred from Electronic Annotation more info
located_in coated vesicle	ISO Inferred from Sequence Orthology more info
located_in cytoplasm	IDA Inferred from Direct Assay more info	PubMed
located_in cytoplasm	ISO Inferred from Sequence Orthology more info
located_in cytosol	IEA Inferred from Electronic Annotation more info
located_in cytosol	ISO Inferred from Sequence Orthology more info
located_in early endosome	IEA Inferred from Electronic Annotation more info
located_in early endosome	ISO Inferred from Sequence Orthology more info
located_in extracellular exosome	IEA Inferred from Electronic Annotation more info
located_in extracellular exosome	ISO Inferred from Sequence Orthology more info
located_in extracellular space	ISO Inferred from Sequence Orthology more info
located_in intracellular membrane-bounded organelle	IDA Inferred from Direct Assay more info	PubMed
part_of lipopolysaccharide receptor complex	IEA Inferred from Electronic Annotation more info
part_of lipopolysaccharide receptor complex	ISO Inferred from Sequence Orthology more info
located_in membrane	IMP Inferred from Mutant Phenotype more info	PubMed
located_in migrasome	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrial crista	ISO Inferred from Sequence Orthology more info
located_in mitochondrial inner membrane	HDA more info	PubMed
is_active_in mitochondrial inner membrane	IBA Inferred from Biological aspect of Ancestor more info
located_in mitochondrial inner membrane	ISO Inferred from Sequence Orthology more info
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
is_active_in mitochondrial matrix	ISO Inferred from Sequence Orthology more info
located_in mitochondrial matrix	ISO Inferred from Sequence Orthology more info
located_in mitochondrion	HDA more info	PubMed
is_active_in mitochondrion	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrion	IDA Inferred from Direct Assay more info	PubMed
located_in mitochondrion	ISO Inferred from Sequence Orthology more info
located_in myelin sheath	HDA more info	PubMed
located_in peroxisomal matrix	ISO Inferred from Sequence Orthology more info
located_in plasma membrane	ISO Inferred from Sequence Orthology more info
part_of protein-containing complex	ISO Inferred from Sequence Orthology more info
part_of protein-containing complex	ISS Inferred from Sequence or Structural Similarity more info
located_in secretory granule	IDA Inferred from Direct Assay more info	PubMed
located_in secretory granule	ISO Inferred from Sequence Orthology more info
located_in sperm midpiece	IEA Inferred from Electronic Annotation more info
located_in sperm plasma membrane	IDA Inferred from Direct Assay more info	PubMed
located_in zymogen granule	ISO Inferred from Sequence Orthology more info

General protein information

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Preferred Names: 60 kDa heat shock protein, mitochondrial

Names: 60 kDa chaperonin; chaperonin 60; heat shock 60kDa protein 1 (chaperonin); heat shock protein 60; heat shock protein, 60 kDa; mitochondrial matrix protein P1

NP_001343441.1

EC 5.6.1.7

NP_034607.3

EC 5.6.1.7

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_001356512.1 → NP_001343441.1 60 kDa heat shock protein, mitochondrial

Status: VALIDATED

Source sequence(s)

AC108391

Consensus CDS

CCDS35569.1

UniProtKB/Swiss-Prot

P19226, P19227, P63038, P97602, Q3KQP2, Q3UIP0, Q8C2C7, Q8VEF4

Conserved Domains (1) summary

cd03344
Location:28 → 548

GroEL; GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. The symmetry of type I is seven-fold and they are found ...
NM_010477.4 → NP_034607.3 60 kDa heat shock protein, mitochondrial

See identical proteins and their annotated locations for NP_034607.3

Status: VALIDATED

Source sequence(s)

AK143882, BF607107, BY014148

Consensus CDS

CCDS35569.1

UniProtKB/Swiss-Prot

P19226, P19227, P63038, P97602, Q3KQP2, Q3UIP0, Q8C2C7, Q8VEF4

Related

ENSMUSP00000027123.9, ENSMUST00000027123.15

Conserved Domains (1) summary

cd03344
Location:28 → 548

GroEL; GroEL_like type I chaperonin. Chaperonins are involved in productive folding of proteins. They share a common general morphology, a double toroid of 2 stacked rings, each composed of 7-9 subunits. The symmetry of type I is seven-fold and they are found ...