GroEL

HSPD1
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 4PJ1
Identifiers
Aliases	HSPD1, CPN60, GROEL, HLD4, HSP-60, HSP60, HSP65, HuCHA60, SPG13, heat shock protein family D (Hsp60) member 1
External IDs	OMIM: 118190; MGI: 96242; HomoloGene: 1626; GeneCards: HSPD1; OMA:HSPD1 - orthologs
Gene location (Human) Chr. Chromosome 2 (human)[1] Band 2q33.1 Start 197,486,584 bp[1] End 197,516,737 bp[1]
Gene location (Mouse) Chr. Chromosome 1 (mouse)[2] Band 1|1 C1.2 Start 55,116,994 bp[2] End 55,127,402 bp[2]
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in right adrenal gland right adrenal cortex left adrenal gland left adrenal cortex ventricular zone body of pancreas epithelium of colon mucosa of transverse colon ganglionic eminence rectum Top expressed in tail of embryo epiblast ovary genital tubercle adrenal gland right kidney proximal tubule embryo blastocyst yolk sac More reference expression data BioGPS More reference expression data
Gene ontology Molecular function nucleotide binding chaperone binding p53 binding single-stranded DNA binding ATPase activity protein binding double-stranded RNA binding DNA replication origin binding ATP binding ubiquitin protein ligase binding protein folding chaperone activity unfolded protein binding RNA binding hydrolase activity high-density lipoprotein particle binding enzyme binding apolipoprotein binding apolipoprotein A-I binding lipopolysaccharide binding isomerase activity Cellular component cytoplasm cyclin-dependent protein kinase activating kinase holoenzyme complex lipopolysaccharide receptor complex early endosome mitochondrion clathrin-coated pit coated vesicle extracellular exosome extracellular matrix mitochondrial matrix extracellular space mitochondrial inner membrane cytosol plasma membrane cell surface membrane secretory granule protein-containing complex Biological process chaperone-mediated protein complex assembly positive regulation of interleukin-12 production positive regulation of interleukin-10 production protein stabilization protein maturation positive regulation of macrophage activation MyD88-dependent toll-like receptor signaling pathway isotype switching to IgG isotypes B cell activation B cell cytokine production response to unfolded protein B cell proliferation protein folding positive regulation of T cell mediated immune response to tumor cell protein refolding positive regulation of interleukin-6 production positive regulation of apoptotic process response to cold viral process activation of cysteine-type endopeptidase activity involved in apoptotic process regulation of transcription by RNA polymerase II 'de novo' protein folding protein import into mitochondrial intermembrane space chaperone-mediated protein folding apoptotic mitochondrial changes positive regulation of interferon-alpha production positive regulation of interferon-gamma production T cell activation negative regulation of apoptotic process positive regulation of T cell activation mitochondrion organization Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 3329 15510 Ensembl ENSG00000144381 ENSMUSG00000025980 UniProt P10809 P63038 RefSeq (mRNA) NM_002156 NM_199440 NM_010477 NM_001356512 RefSeq (protein) NP_002147 NP_955472 NP_034607 NP_001343441 Location (UCSC) Chr 2: 197.49 – 197.52 Mb Chr 1: 55.12 – 55.13 Mb PubMed search [3] [4]
Wikidata
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This article is missing information about action in bacteria and chloroplasts. Please expand the article to include this information. Further details may exist on the talk page. (December 2020)

GroEL is a protein which belongs to the chaperonin family of molecular chaperones, and is found in many bacteria.^[5] 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.

Alternate Names: 60 kDa chaperonin, Chaperonin 60, CPN60, Heat shock protein 60, HSP-60, HuCHA60, Mitochondrial matrix protein P1, P60 lymphocyte protein, HSPD1

Heat shock protein 60 (HSP60) is a mitochondrial chaperonin that is typically held responsible for the transportation and refolding of proteins from the cytoplasm into the mitochondrial matrix. In addition to its role as a heat shock protein, HSP60 functions as a chaperonin to assist in folding linear amino acid chains into their respective three-dimensional structure. Through the extensive study of groEL, HSP60’s bacterial homolog, HSP60 has been deemed essential in the synthesis and transportation of essential mitochondrial proteins from the cell's cytoplasm into the mitochondrial matrix. Further studies have linked HSP60 to diabetes, stress response, cancer and certain types of immunological disorders.