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HSPD1 heat shock 60kDa protein 1 (chaperonin) [ Homo sapiens (human) ]

Gene ID: 3329, updated on 18-Jan-2015
Official Symbol
HSPD1provided by HGNC
Official Full Name
heat shock 60kDa protein 1 (chaperonin)provided by HGNC
Primary source
HGNC:HGNC:5261
See related
Ensembl:ENSG00000144381; HPRD:00318; MIM:118190; Vega:OTTHUMG00000154463
Gene type
protein coding
RefSeq status
REVIEWED
Organism
Homo sapiens
Lineage
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo
Also known as
HLD4; CPN60; GROEL; HSP60; HSP65; SPG13; HSP-60; HuCHA60
Summary
This gene encodes a member of the chaperonin family. The encoded mitochondrial protein may function as a signaling molecule in the innate immune system. This protein is essential for the folding and assembly of newly imported proteins in the mitochondria. This gene is adjacent to a related family member and the region between the 2 genes functions as a bidirectional promoter. Several pseudogenes have been associated with this gene. Two transcript variants encoding the same protein have been identified for this gene. Mutations associated with this gene cause autosomal recessive spastic paraplegia 13. [provided by RefSeq, Jun 2010]
Orthologs
See HSPD1 in MapViewer
Location:
2q33.1
Exon count:
13
Annotation release Status Assembly Chr Location
106 current GRCh38 (GCF_000001405.26) 2 NC_000002.12 (197486584..197500274, complement)
105 previous assembly GRCh37.p13 (GCF_000001405.25) 2 NC_000002.11 (198351308..198364998, complement)

Chromosome 2 - NC_000002.12Genomic Context describing neighboring genes Neighboring gene splicing factor 3b, subunit 1, 155kDa Neighboring gene coenzyme Q10 homolog B (S. cerevisiae) Neighboring gene HSPE1-MOB4 readthrough Neighboring gene heat shock 10kDa protein 1 Neighboring gene MOB family member 4, phocein Neighboring gene raftlin family member 2

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

Replication interactions

Interaction Pubs
High levels of additive and synergic antiretroviral activity are obtained by using antiretroviral compounds (T1249, 3TC, RAL, or IDV) in PM1 cells stably expressing anti-host shRNAs (IPO7, HSPD1, or ATG16) or anti-HIV shRNAs (Pol, RT, or Nef) PubMed

Protein interactions

Protein Gene Interaction Pubs
Envelope surface glycoprotein gp120 env Tandem affinity purification and mass spectrometry analysis identify heat shock 60kDa protein 1 (HSPD1), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells PubMed
Envelope transmembrane glycoprotein gp41 env HIV-1 gp41 binds to heat-shock protein hsp60 through its extracellular domain (Env amino acids 539-684) PubMed
Gag-Pol gag-pol Tandem affinity purification and mass spectrometry analysis identify heat shock 60kDa protein 1 (HSPD1), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells PubMed
Nef nef High levels of additive and synergic antiretroviral activity are obtained by using antiretroviral compounds (T1249, 3TC, RAL, or IDV) in PM1 cells stably expressing anti-host shRNAs (IPO7, HSPD1, or ATG16) or anti-HIV shRNAs (Pol, RT, or Nef) PubMed
nef Tandem affinity purification and mass spectrometry analysis identify heat shock 60kDa protein 1 (HSPD1), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells PubMed
Pol gag-pol High levels of additive and synergic antiretroviral activity are obtained by using antiretroviral compounds (T1249, 3TC, RAL, or IDV) in PM1 cells stably expressing anti-host shRNAs (IPO7, HSPD1, or ATG16) or anti-HIV shRNAs (Pol, RT, or Nef) PubMed
Pr55(Gag) gag Tandem affinity purification and mass spectrometry analysis identify heat shock 60kDa protein 1 (HSPD1), HIV-1 Gag, Gag/Pol, gp120, and Nef incorporated into staufen1 RNP complexes isolated from HIV-1-expressing cells PubMed
gag Hsp60 is specifically incorporated into HIV-1 virions, similar to Hsp70 which is incorporated into virions through an interaction with HIV-1 Gag PubMed
Tat tat HIV-1 Tat upregulates the expression of heat shock 60kDa protein 1 (HSPD1; HSP60) in Jurkat cells PubMed
Vpr vpr A stable-isotope labeling by amino acids in cell culture coupled with mass spectrometry-based proteomics identifies downregulation of heat shock 60kDa protein 1 (HSPD1) expression by HIV-1 Vpr in Vpr transduced macrophages PubMed
integrase gag-pol HSP60 binds to the catalytic core domain (amino acids 48-212) of HIV-1 integrase (IN), stabilizing the IN active form and reducing thermal denaturation of the enzyme, thereby stimulating IN activity PubMed
retropepsin gag-pol Positional proteomics analysis identifies the cleavage of human heat shock 60kDa protein 1, mitochondria (HSPD1; chaperonin) at amino acid residues 431-432 by the HIV-1 protease PubMed
reverse transcriptase gag-pol High levels of additive and synergic antiretroviral activity are obtained by using antiretroviral compounds (T1249, 3TC, RAL, or IDV) in PM1 cells stably expressing anti-host shRNAs (IPO7, HSPD1, or ATG16) or anti-HIV shRNAs (Pol, RT, or Nef) PubMed

Go to the HIV-1, Human Interaction Database

  • 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...
  • Metabolism of proteins, organism-specific biosystem (from REACTOME)
    Metabolism of proteins, organism-specific biosystemProtein metabolism comprises the pathways of translation, post-translational modification and protein folding.
  • Mitochondrial protein import, organism-specific biosystem (from REACTOME)
    Mitochondrial protein import, organism-specific biosystemA human mitochondrion contains about 1500 proteins, more than 99% of which are encoded in the nucleus, synthesized in the cytosol and imported into the mitochondrion. Proteins are targeted to four lo...
  • 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...
  • Validated targets of C-MYC transcriptional activation, organism-specific biosystem (from Pathway Interaction Database)
    Validated targets of C-MYC transcriptional activation, organism-specific biosystem
    Validated targets of C-MYC transcriptional activation
Products Interactant Other Gene Complex Source Pubs Description

Markers

Homology

Gene Ontology Provided by GOA

Function Evidence Code Pubs
ATP binding IEA
Inferred from Electronic Annotation
more info
 
ATPase activity ISS
Inferred from Sequence or Structural Similarity
more info
 
DNA replication origin binding ISS
Inferred from Sequence or Structural Similarity
more info
 
chaperone binding IPI
Inferred from Physical Interaction
more info
PubMed 
double-stranded RNA binding IDA
Inferred from Direct Assay
more info
PubMed 
lipopolysaccharide binding IDA
Inferred from Direct Assay
more info
PubMed 
p53 binding IPI
Inferred from Physical Interaction
more info
PubMed 
poly(A) RNA binding IDA
Inferred from Direct Assay
more info
PubMed 
protein binding IPI
Inferred from Physical Interaction
more info
PubMed 
single-stranded DNA binding ISS
Inferred from Sequence or Structural Similarity
more info
 
ubiquitin protein ligase binding IPI
Inferred from Physical Interaction
more info
PubMed 
unfolded protein binding IC
Inferred by Curator
more info
PubMed 
unfolded protein binding ISS
Inferred from Sequence or Structural Similarity
more info
 
Process Evidence Code Pubs
'de novo' protein folding ISS
Inferred from Sequence or Structural Similarity
more info
 
B cell activation IDA
Inferred from Direct Assay
more info
PubMed 
B cell cytokine production IDA
Inferred from Direct Assay
more info
PubMed 
B cell proliferation IDA
Inferred from Direct Assay
more info
PubMed 
MyD88-dependent toll-like receptor signaling pathway IDA
Inferred from Direct Assay
more info
PubMed 
T cell activation IDA
Inferred from Direct Assay
more info
PubMed 
activation of cysteine-type endopeptidase activity involved in apoptotic process IDA
Inferred from Direct Assay
more info
PubMed 
chaperone-mediated protein complex assembly ISS
Inferred from Sequence or Structural Similarity
more info
 
isotype switching to IgG isotypes IDA
Inferred from Direct Assay
more info
PubMed 
negative regulation of apoptotic process IMP
Inferred from Mutant Phenotype
more info
PubMed 
positive regulation of T cell activation IDA
Inferred from Direct Assay
more info
PubMed 
positive regulation of T cell activation ISS
Inferred from Sequence or Structural Similarity
more info
 
positive regulation of T cell mediated immune response to tumor cell IDA
Inferred from Direct Assay
more info
PubMed 
positive regulation of apoptotic process IMP
Inferred from Mutant Phenotype
more info
PubMed 
positive regulation of interferon-alpha production IDA
Inferred from Direct Assay
more info
PubMed 
positive regulation of interferon-gamma production IDA
Inferred from Direct Assay
more info
PubMed 
positive regulation of interferon-gamma production ISS
Inferred from Sequence or Structural Similarity
more info
 
positive regulation of interleukin-10 production IDA
Inferred from Direct Assay
more info
PubMed 
positive regulation of interleukin-12 production IDA
Inferred from Direct Assay
more info
PubMed 
positive regulation of interleukin-6 production IDA
Inferred from Direct Assay
more info
PubMed 
positive regulation of macrophage activation IDA
Inferred from Direct Assay
more info
PubMed 
protein maturation ISS
Inferred from Sequence or Structural Similarity
more info
 
protein refolding IDA
Inferred from Direct Assay
more info
PubMed 
protein stabilization IMP
Inferred from Mutant Phenotype
more info
PubMed 
protein stabilization ISS
Inferred from Sequence or Structural Similarity
more info
 
response to unfolded protein IDA
Inferred from Direct Assay
more info
PubMed 
viral process IEA
Inferred from Electronic Annotation
more info
 
Component Evidence Code Pubs
cell surface IDA
Inferred from Direct Assay
more info
PubMed 
coated pit IDA
Inferred from Direct Assay
more info
PubMed 
coated vesicle IDA
Inferred from Direct Assay
more info
PubMed 
colocalizes_with cyclin-dependent protein kinase activating kinase holoenzyme complex IDA
Inferred from Direct Assay
more info
PubMed 
cytoplasm IDA
Inferred from Direct Assay
more info
PubMed 
cytosol IDA
Inferred from Direct Assay
more info
PubMed 
early endosome IDA
Inferred from Direct Assay
more info
PubMed 
extracellular space IDA
Inferred from Direct Assay
more info
PubMed 
extracellular vesicular exosome IDA
Inferred from Direct Assay
more info
PubMed 
lipopolysaccharide receptor complex IDA
Inferred from Direct Assay
more info
PubMed 
membrane IDA
Inferred from Direct Assay
more info
PubMed 
mitochondrial inner membrane ISS
Inferred from Sequence or Structural Similarity
more info
 
mitochondrial matrix TAS
Traceable Author Statement
more info
PubMed 
mitochondrion IDA
Inferred from Direct Assay
more info
 
plasma membrane IEA
Inferred from Electronic Annotation
more info
 
protein complex IDA
Inferred from Direct Assay
more info
PubMed 
secretory granule ISS
Inferred from Sequence or Structural Similarity
more info
 
Preferred Names
60 kDa heat shock protein, mitochondrial
Names
60 kDa heat shock protein, mitochondrial
chaperonin 60
60 kDa chaperonin
heat shock protein 65
P60 lymphocyte protein
mitochondrial matrix protein P1
short heat shock protein 60 Hsp60s1

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.

Genomic

  1. NG_008915.1 

    Range
    5001..18691
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. NM_002156.4NP_002147.2  60 kDa heat shock protein, mitochondrial

    See proteins identical to NP_002147.2

    Status: REVIEWED

    Description
    Transcript Variant: This variant (1) represents the longer transcript. Both variants 1 and 2 encode the same protein.
    Source sequence(s)
    AU098504, BC002676
    Consensus CDS
    CCDS33357.1
    UniProtKB/TrEMBL
    A0A024R3X4
    UniProtKB/Swiss-Prot
    P10809
    Related
    ENSP00000373620, OTTHUMP00000205744, ENST00000388968, OTTHUMT00000335324
    Conserved Domains (2) summary
    PRK12850
    Location:27553
    groEL; chaperonin GroEL; Reviewed
    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_199440.1NP_955472.1  60 kDa heat shock protein, mitochondrial

    See proteins identical to NP_955472.1

    Status: REVIEWED

    Description
    Transcript Variant: This variant (2) differs in the 5' UTR compared to variant 1. Both variants 1 and 2 encode the same isoform.
    Source sequence(s)
    BC002676, BG701476
    Consensus CDS
    CCDS33357.1
    UniProtKB/TrEMBL
    A0A024R3X4
    UniProtKB/Swiss-Prot
    P10809
    Related
    ENSP00000340019, ENST00000345042
    Conserved Domains (2) summary
    PRK12850
    Location:27553
    groEL; chaperonin GroEL; Reviewed
    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: Homo sapiens Annotation Release 106

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

Reference GRCh38 Primary Assembly

Genomic

  1. NC_000002.12 

    Range
    197486584..197500274
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

mRNA and Protein(s)

  1. XM_005246518.1XP_005246575.1  

    See proteins identical to XP_005246575.1

    UniProtKB/TrEMBL
    A0A024R3X4
    UniProtKB/Swiss-Prot
    P10809
    Conserved Domains (2) summary
    PRK12850
    Location:27553
    groEL; chaperonin GroEL; Reviewed
    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 ...

Alternate CHM1_1.1

Genomic

  1. NC_018913.2 

    Range
    198357144..198370838
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)

Alternate HuRef

Genomic

  1. AC_000134.1 

    Range
    190203711..190217402
    Download
    GenBank, FASTA, Sequence Viewer (Graphics)