NP_002147.2
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NCBI GenBank Nucleotide #
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UniProt Primary Accession #
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UniProt Secondary Accession #
UniProt Related Accession #
NCBI Official Full Name
60 kDa heat shock protein, mitochondrial
NCBI Official Synonym Full Names
heat shock 60kDa protein 1 (chaperonin)
NCBI Official Synonym Symbols
HLD4; CPN60; GROEL; HSP60; HSP65; SPG13; HSP-60; HuCHA60 [Similar Products]
NCBI Protein Information
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
UniProt Protein Name
60 kDa heat shock protein, mitochondrial
UniProt Synonym Protein Names
60 kDa chaperonin; Chaperonin 60; CPN60; Heat shock protein 60; HSP-60; Hsp60; HuCHA60; Mitochondrial matrix protein P1; P60 lymphocyte protein
UniProt Synonym Gene Names
UniProt Entry Name
CH60_HUMAN
NCBI Summary for HSPD1
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]
UniProt Comments for HSPD1
HSP60: Implicated in mitochondrial protein import and macromolecular assembly. May facilitate the correct folding of imported proteins. May also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. Interacts with HRAS. Interacts with HBV protein X and HTLV-1 protein p40tax. Belongs to the chaperonin (HSP60) family.
Protein type: Mitochondrial; Chaperone
Chromosomal Location of Human Ortholog: 2q33.1
Cellular Component: extracellular space; protein complex; cell surface; mitochondrion; early endosome; coated pit; cytosol; secretory granule; membrane; mitochondrial matrix; mitochondrial inner membrane; cytoplasm; plasma membrane; lipopolysaccharide receptor complex; cyclin-dependent protein kinase activating kinase holoenzyme complex
Molecular Function: protein binding; p53 binding; lipopolysaccharide binding; ubiquitin protein ligase binding; chaperone binding; double-stranded RNA binding; ATPase activity; unfolded protein binding; DNA replication origin binding; ATP binding; single-stranded DNA binding
Biological Process: B cell proliferation; caspase activation; T cell activation; viral reproduction; protein stabilization; B cell activation; positive regulation of apoptosis; positive regulation of interleukin-12 production; protein maturation; isotype switching to IgG isotypes; positive regulation of interleukin-6 production; B cell cytokine production; response to unfolded protein; positive regulation of interleukin-10 production; MyD88-dependent toll-like receptor signaling pathway; positive regulation of interferon-gamma production; 'de novo' protein folding; protein refolding; positive regulation of T cell mediated immune response to tumor cell; positive regulation of T cell activation; chaperone-mediated protein complex assembly; positive regulation of interferon-alpha production; positive regulation of macrophage activation; negative regulation of apoptosis
Disease: Spastic Paraplegia 13, Autosomal Dominant; Leukodystrophy, Hypomyelinating, 4
Product References and Citations for anti-HSPD1 antibody
1. Hartl, F.U. (1996) Nature 381: 571-579. 2. Bukau, B. and Horwich, A.L. (1998) Cell 92: 351-366. 3. Hartl, F.U. and Hayer-Hartl, M. (2002) Science 295: 1852- 1858. 4. Jindal, S., et al. (1989) Molecular and Cellular Biology 9: 2279-2283. 5. La Verda, D., et al (1999) Infect Dis. Obstet. Gynecol. 7: 64-71. 6. Itoh, H. et al. (2002) Eur. J. Biochem. 269: 5931-5938. 7. Gupta, S. and Knowlton, A.A. J. Cell Mol Med. 9: 51-58. 8. Deocaris, C.C. et al. (2006) Cell Stress Chaperones 11: 116-128. 9. Lai, H.C. et al. (2007) Am. J. Physiol. Endocrinol. Metab. 292: E292-E297. 10. Gao, Y.L., et al (1995) J. of Immunology 154: 3548-3556. 11. Neuer, A., et al (1997) European Society for Human Reproduction and Embryology 12(5):925-929. 12. Bason, C., et al (2003) Lancet 362(9400): 1971-1977. 1. Ahgib, N. and Komatsu, S. (2009). Comparative analyses of the proteomes of leaves and flowers at various stages of development reveal organ-specific functional differentiation of proteins in soybean. Proteomes. 9 (21), 4889-4907. doi: 10.1002/pmic.200900308 2. Bayot A. et al. (2010). Identification of novel oxidized protein substrates and physiological partners of the mitochondrial ATP-dependent Lon-like protease Pim1. J Biol Chem. 285 (15), 11445-11457. doi: 10.1074/jbc.M109.065425 3. Ahsan, N., Donnart, T., Nouri, M.Z., and Komatsu, S. (2010). Tissue-specific defense and thermo-adaptive mechanisms of soybean seedlings under heat stress revealed by proteomic approach. J Proteome Res. 9 (8), 4189-4204. doi: 10.1021/pr100504j. 4. Dogan, S. A. et al. (2014). Tissue-Specific Loss of DARS2 Activates Stress Responses Independently of Respiratory Chain Deficiency in the Heart. Cell Metabolism. 19 (3), 458-469. doi.org/10.1016/j.cmet.2014.02.004
Research Articles on HSPD1
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Products associated with anti-HSPD1 antibody
Pathways associated with anti-HSPD1 antibody
Diseases associated with anti-HSPD1 antibody
Organs/Tissues associated with anti-HSPD1 antibody
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