HSPD1
Sign in to saveAlso known as CPN60, GROEL, HLD4, HSP-60, HSP60, HSP65, HuCHA60, SPG13
GroEL is a protein which belongs to the chaperonin family of molecular chaperones, and is found in many bacteria. It is required for the proper folding of many proteins. To function properly, GroEL requires the lid-like cochaperonin protein complex GroES. In eukaryotes the organellar proteins Hsp60 and Hsp10 are structurally and functionally nearly identical to GroEL and GroES, respectively, due to their endosymbiotic origin.
Gene data
HSPD1- Name
- heat shock protein family D (Hsp60) member 1
- Type
- protein-coding
- Position
- 197,486,580–197,516,737 (−)
- Aliases
- CPN60, GROEL, HLD4, HSP-60, HSP60, HSP65, HuCHA60, SPG13
- Ensembl
- ENSG00000144381
- RefSeq RNA
- NM_002156.5, NM_199440.2
- RefSeq protein
- NP_002147.2, NP_955472.1
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].
Gene Ontology
Biological process
Molecular function
Pathways
via MyGene.info
Wikidata facts
- Image
- Protein CD44 PDB 1poz.png
Show 6 more facts
- HomoloGene ID
- 1626
- exact match
- identifiers.org/ncbigene/3329
- genomic end
- 198381461
- genomic start
- 197486584
- cytogenetic location
- 2q33.1
- Commons category
- GroEL
Sources (7)
via Wikidata · CC0
~24 min read
Article
20 sectionsContents
- Discovery
- Structure
- Function
- Common
- Mitochondrial protein transport
- DNA metabolism
- Cytoplasmic vs mitochondrial HSP60
- Synthesis and assembly
- Immunological role
- Stress response
- Relationship to cancer
- Mechanism
- Thermodynamics
- Structure
- Interactions
- Phage T4 morphogenesis
- See also
- References
- Further reading
- External links
GroEL is a protein which belongs to the chaperonin family of molecular chaperones, and is found in many bacteria. It is required for the proper folding of many proteins. To function properly, GroEL requires the lid-like cochaperonin protein complex GroES. In eukaryotes the organellar proteins Hsp60 and Hsp10 are structurally and functionally nearly identical to GroEL and GroES, respectively, due to their endosymbiotic origin.
HSP60 is implicated in mitochondrial protein import and macromolecular assembly. It may facilitate the correct folding of imported proteins, and may also prevent misfolding and promote the refolding and proper assembly of unfolded polypeptides generated under stress conditions in the mitochondrial matrix. HSP60 interacts with HRAS and with HBV protein X and HTLV-1 protein p40tax. HSP60 belongs to the chaperonin (HSP60) family. Note: This description may include information from UniProtKB.