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

Gene ID: 15510, updated on 2-Oct-2018

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 Vega:OTTMUSG00000021770
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
Expression
Broad expression in placenta adult (RPKM 119.5), liver E14 (RPKM 114.0) and 21 other tissues See more
Orthologs

Genomic context

See Hspd1 in Genome Data Viewer
Location:
1; 1 C1.2
Exon count:
13
Annotation release Status Assembly Chr Location
106 current GRCm38.p4 (GCF_000001635.24) 1 NC_000067.6 (55077834..55088217, complement)
Build 37.2 previous assembly MGSCv37 (GCF_000001635.18) 1 NC_000067.5 (55134678..55144776, complement)

Chromosome 1 - NC_000067.6Genomic Context describing neighboring genes Neighboring gene splicing factor 3b, subunit 1 Neighboring gene coenzyme Q10B Neighboring gene ribosomal protein S2 pseudogene Neighboring gene heat shock protein 1 (chaperonin 10) 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 FunctionsWhat's a GeneRIF?

Variation

Alleles

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

Pathways from BioSystems

  • Legionellosis, organism-specific biosystem (from KEGG)
    Legionellosis, organism-specific biosystemLegionellosis is a potentially fatal infectious disease caused by the bacterium Legionella pneumophila and other legionella species. Two distinct clinical and epidemiological syndromes are associated...
  • Legionellosis, conserved biosystem (from KEGG)
    Legionellosis, conserved biosystemLegionellosis is a potentially fatal infectious disease caused by the bacterium Legionella pneumophila and other legionella species. Two distinct clinical and epidemiological syndromes are associated...
  • RNA degradation, organism-specific biosystem (from KEGG)
    RNA degradation, organism-specific biosystemThe correct processing, quality control and turnover of cellular RNA molecules are critical to many aspects in the expression of genetic information. In eukaryotes, two major pathways of mRNA decay e...
  • RNA degradation, conserved biosystem (from KEGG)
    RNA degradation, conserved biosystemThe correct processing, quality control and turnover of cellular RNA molecules are critical to many aspects in the expression of genetic information. In eukaryotes, two major pathways of mRNA decay e...
  • SIDS Susceptibility Pathways, organism-specific biosystem (from WikiPathways)
    SIDS Susceptibility Pathways, organism-specific biosystemIn this model, we provide an integrated view of Sudden Infant Death Syndrome (SIDS) at the level of implicated tissues, signaling networks and genetics. The purpose of this model is to serve as an ov...
  • Tuberculosis, organism-specific biosystem (from KEGG)
    Tuberculosis, organism-specific biosystemTuberculosis, or TB, is an infectious disease caused by Mycobacterium tuberculosis. One third of the world's population is thought to be infected with TB. About 90% of those infected result in latent...
  • Tuberculosis, conserved biosystem (from KEGG)
    Tuberculosis, conserved biosystemTuberculosis, or TB, is an infectious disease caused by Mycobacterium tuberculosis. One third of the world's population is thought to be infected with TB. About 90% of those infected result in latent...
  • Type I diabetes mellitus, organism-specific biosystem (from KEGG)
    Type I diabetes mellitus, organism-specific biosystemType I diabetes mellitus is a disease that results from autoimmune destruction of the insulin-producing beta-cells. Certain beta-cell proteins act as autoantigens after being processed by antigen-pre...
  • Type I diabetes mellitus, conserved biosystem (from KEGG)
    Type I diabetes mellitus, conserved biosystemType I diabetes mellitus is a disease that results from autoimmune destruction of the insulin-producing beta-cells. Certain beta-cell proteins act as autoantigens after being processed by antigen-pre...

Interactions

Products Interactant Other Gene Complex Source Pubs Description

General gene information

Markers

Homology

Gene Ontology Provided by MGI

Function Evidence Code Pubs
ATP binding IEA
Inferred from Electronic Annotation
more info
 
apolipoprotein A-I binding ISO
Inferred from Sequence Orthology
more info
 
apolipoprotein binding ISO
Inferred from Sequence Orthology
more info
 
chaperone binding ISO
Inferred from Sequence Orthology
more info
 
double-stranded RNA binding ISO
Inferred from Sequence Orthology
more info
PubMed 
enzyme binding ISO
Inferred from Sequence Orthology
more info
 
high-density lipoprotein particle binding ISO
Inferred from Sequence Orthology
more info
 
hydrolase activity IEA
Inferred from Electronic Annotation
more info
 
insulin binding ISO
Inferred from Sequence Orthology
more info
 
lipopolysaccharide binding IDA
Inferred from Direct Assay
more info
PubMed 
lipopolysaccharide binding ISO
Inferred from Sequence Orthology
more info
 
modification-dependent protein binding ISO
Inferred from Sequence Orthology
more info
 
nucleotide binding IEA
Inferred from Electronic Annotation
more info
 
p53 binding ISO
Inferred from Sequence Orthology
more info
 
protease binding ISO
Inferred from Sequence Orthology
more info
 
protein heterodimerization activity ISO
Inferred from Sequence Orthology
more info
 
protein-containing complex binding ISO
Inferred from Sequence Orthology
more info
 
ubiquitin protein ligase binding ISO
Inferred from Sequence Orthology
more info
 
unfolded protein binding IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
Process Evidence Code Pubs
'de novo' protein folding IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
B cell activation ISO
Inferred from Sequence Orthology
more info
 
B cell cytokine production ISO
Inferred from Sequence Orthology
more info
 
B cell proliferation ISO
Inferred from Sequence Orthology
more info
 
MyD88-dependent toll-like receptor signaling pathway ISO
Inferred from Sequence Orthology
more info
 
T cell activation IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
T cell activation IDA
Inferred from Direct Assay
more info
PubMed 
T cell activation IGI
Inferred from Genetic Interaction
more info
PubMed 
T cell activation ISO
Inferred from Sequence Orthology
more info
 
activation of cysteine-type endopeptidase activity involved in apoptotic process ISO
Inferred from Sequence Orthology
more info
 
NOT adhesion of symbiont to host IDA
Inferred from Direct Assay
more info
PubMed 
apoptotic mitochondrial changes IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
apoptotic mitochondrial changes ISO
Inferred from Sequence Orthology
more info
 
interaction with symbiont ISO
Inferred from Sequence Orthology
more info
 
isotype switching to IgG isotypes ISO
Inferred from Sequence Orthology
more info
 
mitochondrion organization IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
negative regulation of apoptotic process ISO
Inferred from Sequence Orthology
more info
 
negative regulation of apoptotic process in bone marrow ISO
Inferred from Sequence Orthology
more info
 
negative regulation of neuron apoptotic process ISO
Inferred from Sequence Orthology
more info
 
negative regulation of reactive oxygen species biosynthetic process ISO
Inferred from Sequence Orthology
more info
 
positive regulation of T cell activation IDA
Inferred from Direct Assay
more info
PubMed 
positive regulation of T cell activation ISO
Inferred from Sequence Orthology
more info
 
positive regulation of T cell mediated immune response to tumor cell ISO
Inferred from Sequence Orthology
more info
 
positive regulation of apoptotic process ISO
Inferred from Sequence Orthology
more info
 
positive regulation of inflammatory response ISO
Inferred from Sequence Orthology
more info
 
positive regulation of interferon-alpha production IDA
Inferred from Direct Assay
more info
PubMed 
positive regulation of interferon-alpha production ISO
Inferred from Sequence Orthology
more info
 
positive regulation of interferon-gamma production IDA
Inferred from Direct Assay
more info
PubMed 
positive regulation of interferon-gamma production IGI
Inferred from Genetic Interaction
more info
PubMed 
positive regulation of interferon-gamma production ISO
Inferred from Sequence Orthology
more info
 
positive regulation of interleukin-10 production ISO
Inferred from Sequence Orthology
more info
 
positive regulation of interleukin-12 production ISO
Inferred from Sequence Orthology
more info
 
positive regulation of interleukin-6 production ISO
Inferred from Sequence Orthology
more info
 
positive regulation of interleukin-6 secretion ISO
Inferred from Sequence Orthology
more info
 
positive regulation of macrophage activation ISO
Inferred from Sequence Orthology
more info
 
positive regulation of tumor necrosis factor secretion ISO
Inferred from Sequence Orthology
more info
 
protein folding IEA
Inferred from Electronic Annotation
more info
 
protein import into mitochondrial intermembrane space IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
protein refolding ISO
Inferred from Sequence Orthology
more info
 
protein stabilization ISO
Inferred from Sequence Orthology
more info
 
response to unfolded protein ISO
Inferred from Sequence Orthology
more info
 
Component Evidence Code Pubs
Golgi apparatus ISO
Inferred from Sequence Orthology
more info
 
cell surface ISO
Inferred from Sequence Orthology
more info
 
clathrin-coated pit ISO
Inferred from Sequence Orthology
more info
 
coated vesicle ISO
Inferred from Sequence Orthology
more info
 
cytoplasm IDA
Inferred from Direct Assay
more info
PubMed 
cytoplasm ISO
Inferred from Sequence Orthology
more info
 
cytosol IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
cytosol ISO
Inferred from Sequence Orthology
more info
 
early endosome ISO
Inferred from Sequence Orthology
more info
 
extracellular exosome ISO
Inferred from Sequence Orthology
more info
 
extracellular space ISO
Inferred from Sequence Orthology
more info
 
intracellular membrane-bounded organelle IDA
Inferred from Direct Assay
more info
PubMed 
lipopolysaccharide receptor complex ISO
Inferred from Sequence Orthology
more info
 
membrane IMP
Inferred from Mutant Phenotype
more info
PubMed 
membrane raft ISO
Inferred from Sequence Orthology
more info
 
mitochondrial crista ISO
Inferred from Sequence Orthology
more info
 
mitochondrial inner membrane HDA PubMed 
mitochondrial inner membrane ISO
Inferred from Sequence Orthology
more info
 
mitochondrial matrix ISO
Inferred from Sequence Orthology
more info
 
mitochondrion HDA PubMed 
mitochondrion IBA
Inferred from Biological aspect of Ancestor
more info
PubMed 
mitochondrion IDA
Inferred from Direct Assay
more info
PubMed 
mitochondrion ISO
Inferred from Sequence Orthology
more info
 
myelin sheath IDA
Inferred from Direct Assay
more info
PubMed 
peroxisomal matrix ISO
Inferred from Sequence Orthology
more info
 
plasma membrane IDA
Inferred from Direct Assay
more info
PubMed 
plasma membrane ISO
Inferred from Sequence Orthology
more info
 
protein-containing complex ISO
Inferred from Sequence Orthology
more info
 
rough endoplasmic reticulum ISO
Inferred from Sequence Orthology
more info
 
secretory granule IDA
Inferred from Direct Assay
more info
PubMed 
secretory granule ISO
Inferred from Sequence Orthology
more info
 
colocalizes_with secretory granule ISO
Inferred from Sequence Orthology
more info
 
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_034607.3
XP_006495769.1

NCBI Reference Sequences (RefSeq)

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
    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
    P63038
    Related
    ENSMUSP00000027123.8, OTTMUSP00000024365, ENSMUST00000027123.14, OTTMUST00000051674
    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: Mus musculus Annotation Release 106

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

Reference GRCm38.p4 C57BL/6J

Genomic

  1. NC_000067.6 Reference GRCm38.p4 C57BL/6J

    Range
    55077834..55088217 complement
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_006495706.2XP_006495769.1  60 kDa heat shock protein, mitochondrial isoform X1

    UniProtKB/Swiss-Prot
    P63038
    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 ...
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