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

Gene ID: 15510, updated on 27-Nov-2024

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
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Genomic context

See Hspd1 in Genome Data Viewer
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_000067.7Genomic Context describing neighboring genes Neighboring gene splicing factor 3b, subunit 1 Neighboring gene STARR-seq mESC enhancer starr_00942 Neighboring gene STARR-seq mESC enhancer starr_00943 Neighboring gene coenzyme Q10B Neighboring gene ribosomal protein S2 pseudogene Neighboring gene STARR-positive B cell enhancer ABC_E7728 Neighboring gene heat shock protein 1 (chaperonin 10) Neighboring gene STARR-seq mESC enhancer starr_00944 Neighboring gene ribosomal protein L7A pseudogene Neighboring gene serine/arginine repetitive matrix 2 pseudogene

Genomic regions, transcripts, and products

Expression

  • 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

GeneRIFs: Gene References Into Functions

What's a GeneRIF?

Variation

Alleles

Alleles of this type are documented at Mouse Genome Informatics  (MGI)
  • Endonuclease-mediated (4) 
  • Gene trapped (1) 
  • Targeted (3)  1 citation

Pathways from PubChem

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

Markers

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 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 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 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

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
NP_034607.3

NCBI Reference Sequences (RefSeq)

NEW Try the new Transcript table

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)

  1. NM_001356512.1NP_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:28548
    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 ...
  2. NM_010477.4NP_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:28548
    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 ...

RefSeqs of Annotated Genomes: GCF_000001635.27-RS_2024_02

The following sections contain reference sequences that belong to a specific genome build. Explain

Reference GRCm39 C57BL/6J

Genomic

  1. NC_000067.7 Reference GRCm39 C57BL/6J

    Range
    55116992..55127402 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)