HSPD1 encodes Hsp60, the mitochondrial type I (GroEL-like) chaperonin. The 573-residue precursor carries an N-terminal matrix-targeting presequence. In the matrix, Hsp60 forms heptameric rings that associate with heptameric rings of the co-chaperonin HSPE1/Hsp10 to make single-ring half-football and double-ring football complexes. In an ATP-binding and hydrolysis cycle these complexes enclose newly imported or stress-denatured polypeptides and release them folded. Clients include matrix enzymes and respiratory-chain and ATP-synthase subunits. Hsp60 is essential, and its expression rises under mitochondrial proteotoxic stress. Missense variants that impair folding cause hereditary spastic paraplegia SPG13 and MitCHAP-60 hypomyelinating leukodystrophy. Smaller pools of Hsp60 occur in the cytosol, at the cell surface and in plasma or extracellular vesicles. There, context-dependent effects have been reported on caspase-3 activation and tumour-cell survival, binding of HDL and bacterial LPS, and costimulation of T cells through antigen-presenting cells; some TLR4-dependent effects of recombinant Hsp60 are attributable to bound LPS.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0001530 lipopolysaccharide binding | IDA PMID:17164250 Synergistic and differential modulation of immune responses ... | KEEP AS NON CORE | Summary: Extracellular Hsp60 binds bacterial LPS and enhances LPS signalling. Reason: Osterloh et al. showed specific binding of Hsp60 to LPS and Hsp60-specific, LPS-binding-dependent enhancement of APC responses. This may explain part of the controversy over Hsp60 as a TLR4 agonist. It is an extracellular, context-dependent activity, unrelated to the mitochondrial chaperonin function. The IEA row transfers the same claim from rodent orthologs. Supporting Evidence: PMID:17164250 Hsp60 specifically binds bacterial LPS PMID:17164250 This effect was Hsp60-specific and dependent on LPS-binding by Hsp60. |
| GO:0001530 lipopolysaccharide binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Extracellular Hsp60 binds bacterial LPS and enhances LPS signalling. Reason: Osterloh et al. showed specific binding of Hsp60 to LPS and Hsp60-specific, LPS-binding-dependent enhancement of APC responses. This may explain part of the controversy over Hsp60 as a TLR4 agonist. It is an extracellular, context-dependent activity, unrelated to the mitochondrial chaperonin function. The IEA row transfers the same claim from rodent orthologs. Supporting Evidence: PMID:17164250 Hsp60 specifically binds bacterial LPS PMID:17164250 This effect was Hsp60-specific and dependent on LPS-binding by Hsp60. |
| GO:0001819 positive regulation of cytokine production | IEA GO_REF:0000117 | MODIFY | Summary: ARBA-predicted, too broad; the supported cytokine effect is IFN-alpha induction. Reason: Positive regulation of cytokine production is true for extracellular Hsp60 but too general. The best-controlled cytokine effect of LPS-free Hsp60 is IFN-alpha induction in APC. Endotoxin-free Hsp60 does not induce IL-6, IL-12 or TNF in APC. Proposed replacements: positive regulation of interferon-alpha production Supporting Evidence: PMID:18256040 LPS-free Hsp60 enhances IFN alpha expression in APC PMID:18256040 LPS-free Hsp60 did not induce IL-6, IL-12 or tumor necrosis factor alpha production in APC |
| GO:0002039 p53 binding | IPI PMID:18086682 Hsp60 regulation of tumor cell apoptosis. | KEEP AS NON CORE | Summary: Hsp60 forms a complex with p53 in tumour cells and restrains p53 activity. Reason: Ghosh et al. identified an Hsp60-p53 complex whose disruption by Hsp60 knockdown stabilises p53 and triggers Bax-dependent apoptosis in tumour cells. This is a specific, experimentally supported interaction in a cancer-cell context, secondary to mitochondrial folding. Supporting Evidence: PMID:18086682 This response involves disruption of an Hsp60-p53 complex |
| GO:0002755 MyD88-dependent toll-like receptor signaling pathway | IDA PMID:16148103 Heat shock protein 60 activates B cells via the TLR4-MyD88 p... | MARK AS OVER ANNOTATED | Summary: TLR4/MyD88 dependence of Hsp60 effects is disputed by later endotoxin-free studies. Reason: Cohen-Sfady et al. reported that human HSP60 activates mouse B cells through TLR4/MyD88 and stated that LPS contamination was excluded (PMID:16148103). Later work found that Hsp60 binds LPS tightly (PMID:17164250), that it does not bind B or T lymphocytes (PMID:17164250), and that endotoxin-free Hsp60 acts independently of TLR4/MyD88 and does not induce IL-6, IL-12 or TNF in APC (PMID:18256040). TLR4-dependent activities of recombinant Hsp60 preparations are therefore at least partly attributable to bound LPS. The annotation is not removed, because the curators read the full paper with its controls, but it is likely an over-annotation of HSPD1 function. Supporting Evidence: PMID:16148103 The effects of HSP60 were found to be largely dependent on TLR4 and MyD88 signaling PMID:18256040 T cell co-stimulation induced by LPS-free Hsp60 was independent of TLR4 PMID:17164250 This effect was Hsp60-specific and dependent on LPS-binding by Hsp60. |
| GO:0002842 positive regulation of T cell mediated immune response to tumor cell | IDA PMID:10663613 gammadelta T cells lyse autologous and allogenic oesophageal... | KEEP AS NON CORE | Summary: Tumour-surface Hsp60 is recognised by cytotoxic gamma-delta T cells. Reason: Anti-Hsp60 antibody blocks gamma-delta T-cell lysis of oesophageal tumour cells that display surface Hsp60. Hsp60 here is the recognised target ligand that enables the response. This is a specific tumour-immunology context, not a recombinant-protein assay. Supporting Evidence: PMID:10663613 Anti-hsp60 and anti-hsp70 mAb significantly inhibited the cytotoxicity of gammadelta T cells to both autologous and allogenic oesophageal tumours PMID:10663613 Surface expression of hsp60 and hsp70 on oesophageal tumours and Daudi cells was demonstrated by flow cytometry |
| GO:0003688 DNA replication origin binding | ISS GO_REF:0000024 | UNDECIDED | Summary: Yeast Hsp60 binds mtDNA origin template single strands; human conservation is not shown. Reason: The ISS donor is yeast HSP60 (P19882), the mitochondrial Hsp60 ortholog in the same PANTHER family. Kaufman et al. showed crosslinking to mtDNA and specific single-stranded binding to the template strand of a putative yeast origin (PMID:10869431). Yeast ori elements have no direct counterpart in mammalian mtDNA, and no human binding assay was found. The activity is real in yeast but cannot yet be transferred, origin specificity least of all. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:P19882 Β· HSP60, Saccharomyces cerevisiae UNRESOLVED Direct source IDA is PMID:10869431. Human conservation requires binding or interface evidence; primary folding function is not exclusion. Supporting Evidence: PMID:10869431 Hsp60p binds to single-stranded DNA with high specificity for the template strand of a putative origin of mtDNA replication. |
| GO:0003697 single-stranded DNA binding | ISS GO_REF:0000024 | UNDECIDED | Summary: Yeast Hsp60 binds mtDNA origin template single strands; human conservation is not shown. Reason: The ISS donor is yeast HSP60 (P19882), the mitochondrial Hsp60 ortholog in the same PANTHER family. Kaufman et al. showed crosslinking to mtDNA and specific single-stranded binding to the template strand of a putative yeast origin (PMID:10869431). Yeast ori elements have no direct counterpart in mammalian mtDNA, and no human binding assay was found. The activity is real in yeast but cannot yet be transferred, origin specificity least of all. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:P19882 Β· HSP60, Saccharomyces cerevisiae UNRESOLVED Direct source IDA is PMID:10869431. Human conservation requires binding or interface evidence; primary folding function is not exclusion. Supporting Evidence: PMID:10869431 Hsp60p binds to single-stranded DNA with high specificity for the template strand of a putative origin of mtDNA replication. |
| GO:0003723 RNA binding | HDA PMID:22658674 Insights into RNA biology from an atlas of mammalian mRNA-bi... | KEEP AS NON CORE | Summary: Captured in a HeLa mRNA-interactome screen; no RNA-related function established. Reason: Covalent UV-crosslinking interactome capture identifies HSPD1 among mRNA-bound proteins in HeLa cells. This is HTP evidence of RNA association with no defined specificity or role, and it is unrelated to the chaperonin function. Supporting Evidence: PMID:22658674 Employing two complementary protocols for covalent UV crosslinking of RBPs to RNA |
| GO:0003725 double-stranded RNA binding | IDA PMID:21266579 Raftlin is involved in the nucleocapture complex to induce p... | UNDECIDED | Summary: dsRNA binding from a Raftlin/poly(I:C) uptake study; the HSPD1-specific result was not located. Reason: The cached full text of PMID:21266579 describes Raftlin-mediated poly(I:C) uptake but does not mention HSPD1 in the accessible text. The HSPD1 result is presumably in a supplementary proteomic list. The curator's annotation cannot be checked or refuted from what is available. |
| GO:0005515 protein binding | IPI PMID:15846844 Proteomic profiling of cellular proteins interacting with th... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:15846844 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:17110338 Hsp90 cochaperone Aha1 downregulation rescues misfolding of ... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:17110338 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:17823127 Cytosolic accumulation of HSP60 during apoptosis with or wit... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:17823127 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:18086682 Hsp60 regulation of tumor cell apoptosis. | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:18086682 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:21516116 Next-generation sequencing to generate interactome datasets. | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:21516116 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:21988832 Toward an understanding of the protein interaction network o... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:21988832 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:22664726 ATAD3B is a human embryonic stem cell specific mitochondrial... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:22664726 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:23349634 A newly uncovered group of distantly related lysine methyltr... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:23349634 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:23840630 Identification of Heat Shock Protein 60 as a Regulator of Ne... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:23840630 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:24286120 GTP binding controls complex formation by the human ROCO pro... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:24286120 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:25416956 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:25416956 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:25416956 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:25416956 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:25416956 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:25416956 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:25416956 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:25416956 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:25416956 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:25416956 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:25609649 Proteomic analyses reveal distinct chromatin-associated and ... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:25609649 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:25910212 Widespread macromolecular interaction perturbations in human... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:25910212 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:26618866 βF508 CFTR interactome remodelling promotes rescue of cystic... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:26618866 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:26871637 Widespread Expansion of Protein Interaction Capabilities by ... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:26871637 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:28514442 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:28514442 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:28514442 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:29568061 An AP-MS- and BioID-compatible MAC-tag enables comprehensive... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:29568061 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:29568061 An AP-MS- and BioID-compatible MAC-tag enables comprehensive... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:29568061 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:29924966 A Proteomic Variant Approach (ProVarA) for Personalized Medi... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:29924966 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:30021884 Histone Interaction Landscapes Visualized by Crosslinking Ma... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:30021884 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:31515488 Extensive disruption of protein interactions by genetic vari... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:31515488 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:32296183 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:32296183 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:32814053 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:32814053 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:32814053 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:32814053 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:32814053 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:32814053 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:32814053 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:32814053 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:32814053 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:32814053 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:32814053 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:32814053 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:32814053 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:32814053 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:32814053 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:32814053 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:32814053 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:32814053 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:32814053 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:32814053 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:33961781 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:33961781 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:33961781 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:33961781 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:35156780 CFTR interactome mapping using the mammalian membrane two-hy... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:35156780 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:36012204 Differential CFTR-Interactome Proximity Labeling Procedures ... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:36012204 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:40205054 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: Generic protein binding is uninformative and is removed under the protein-binding policy. Reason: The interaction reported in PMID:40205054 is not disputed, but bare 'protein binding' says nothing about function. Many HSPD1 interactome hits are folding clients or co-purifying mitochondrial proteins. The informative partner-specific functions (Hsp10 co-chaperonin binding, p53 binding, apolipoprotein binding) are captured by their own terms in this review. |
| GO:0005524 ATP binding | IEA GO_REF:0000002 | ACCEPT | Summary: ATP binding is part of the chaperonin cycle and is seen directly in the human structure. Reason: Human mHsp60 was crystallised with ATP mimic (ADP:BeF3) bound in the equatorial nucleotide pocket, and nucleotide binding drives ring formation and Hsp10 association. The InterPro2GO mapping is correct. Supporting Evidence: PMID:32317635 crystal structure of an ATP (ADP:BeF3-bound) ground-state mimic double-ring PMID:11422376 does not inhibit malate dehydrogenase refolding or ATP hydrolysis by mt-cpn60 in the presence of mt-cpn10 |
| GO:0005576 extracellular region | IDA PMID:18229457 Plasma heat shock protein 60 and cardiovascular disease risk... | KEEP AS NON CORE | Summary: Intact, presequence-free Hsp60 circulates in human plasma. Reason: Circulating Hsp60 in human plasma is mostly the intact mature protein lacking the mitochondrial import peptide, so it comes from mitochondria. Its release mechanism and function are unclear. It is a non-core extracellular location. Supporting Evidence: PMID:18229457 Mass spectrometric analysis of circulating immunoreactive Hsp60 reveal that it is predominantly the intact protein with no mitochondrial import peptide |
| GO:0005737 cytoplasm | IDA PMID:21328542 ZNF703 gene amplification at 8p12 specifies luminal B breast... | TOO GENERAL | Summary: Cytoplasm is entailed by mitochondrial matrix and cytosol, both kept in this review. Reason: The ZNF703 study saw HSP60 only in the cytoplasm (PMID:21328542), which is true but uninformative. Mitochondrial matrix and cytosol, both retained here, are part of the cytoplasm. Supporting Evidence: PMID:21328542 HSP60 was only present in the cytoplasm and may interact with the cytoplasmic form of ZNF703 |
| GO:0005737 cytoplasm | IEA GO_REF:0000107 | TOO GENERAL | Summary: Cytoplasm is entailed by mitochondrial matrix and cytosol, both kept in this review. Reason: The ZNF703 study saw HSP60 only in the cytoplasm (PMID:21328542), which is true but uninformative. Mitochondrial matrix and cytosol, both retained here, are part of the cytoplasm. Supporting Evidence: PMID:21328542 HSP60 was only present in the cytoplasm and may interact with the cytoplasmic form of ZNF703 |
| GO:0005739 mitochondrion | HTP PMID:34800366 Quantitative high-confidence human mitochondrial proteome an... | MODIFY | Summary: Correct but general; the supported location is the mitochondrial matrix. Reason: HSPD1 is mitochondrial in every proteomic and imaging dataset, and the specific compartment is the matrix. The review already accepts GO:0005759 mitochondrial matrix from IDA, IBA and TAS rows, so the general term is refined to that descendant. Proposed replacements: mitochondrial matrix Supporting Evidence: PMID:32317635 mHsp60-mHsp10 assists the folding of mitochondrial matrix proteins PMID:25918392 Human mitochondria harbor a single type I chaperonin system |
| GO:0005739 mitochondrion | IDA GO_REF:0000052 | MODIFY | Summary: Correct but general; the supported location is the mitochondrial matrix. Reason: HSPD1 is mitochondrial in every proteomic and imaging dataset, and the specific compartment is the matrix. The review already accepts GO:0005759 mitochondrial matrix from IDA, IBA and TAS rows, so the general term is refined to that descendant. Proposed replacements: mitochondrial matrix Supporting Evidence: PMID:32317635 mHsp60-mHsp10 assists the folding of mitochondrial matrix proteins PMID:25918392 Human mitochondria harbor a single type I chaperonin system |
| GO:0005739 mitochondrion | IDA PMID:17823127 Cytosolic accumulation of HSP60 during apoptosis with or wit... | MODIFY | Summary: Correct but general; the supported location is the mitochondrial matrix. Reason: HSPD1 is mitochondrial in every proteomic and imaging dataset, and the specific compartment is the matrix. The review already accepts GO:0005759 mitochondrial matrix from IDA, IBA and TAS rows, so the general term is refined to that descendant. Proposed replacements: mitochondrial matrix Supporting Evidence: PMID:32317635 mHsp60-mHsp10 assists the folding of mitochondrial matrix proteins PMID:25918392 Human mitochondria harbor a single type I chaperonin system |
| GO:0005739 mitochondrion | IDA PMID:18086682 Hsp60 regulation of tumor cell apoptosis. | MODIFY | Summary: Correct but general; the supported location is the mitochondrial matrix. Reason: HSPD1 is mitochondrial in every proteomic and imaging dataset, and the specific compartment is the matrix. The review already accepts GO:0005759 mitochondrial matrix from IDA, IBA and TAS rows, so the general term is refined to that descendant. Proposed replacements: mitochondrial matrix Supporting Evidence: PMID:32317635 mHsp60-mHsp10 assists the folding of mitochondrial matrix proteins PMID:25918392 Human mitochondria harbor a single type I chaperonin system |
| GO:0005739 mitochondrion | IDA PMID:21245038 Human 2'-phosphodiesterase localizes to the mitochondrial ma... | MODIFY | Summary: Correct but general; the supported location is the mitochondrial matrix. Reason: HSPD1 is mitochondrial in every proteomic and imaging dataset, and the specific compartment is the matrix. The review already accepts GO:0005759 mitochondrial matrix from IDA, IBA and TAS rows, so the general term is refined to that descendant. Proposed replacements: mitochondrial matrix Supporting Evidence: PMID:32317635 mHsp60-mHsp10 assists the folding of mitochondrial matrix proteins PMID:25918392 Human mitochondria harbor a single type I chaperonin system |
| GO:0005739 mitochondrion | IEA GO_REF:0000107 | MODIFY | Summary: Correct but general; the supported location is the mitochondrial matrix. Reason: HSPD1 is mitochondrial in every proteomic and imaging dataset, and the specific compartment is the matrix. The review already accepts GO:0005759 mitochondrial matrix from IDA, IBA and TAS rows, so the general term is refined to that descendant. Proposed replacements: mitochondrial matrix Supporting Evidence: PMID:32317635 mHsp60-mHsp10 assists the folding of mitochondrial matrix proteins PMID:25918392 Human mitochondria harbor a single type I chaperonin system |
| GO:0005743 mitochondrial inner membrane | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Peripheral inner-membrane association of the matrix chaperonin; ancillary. Reason: The IBA at PTN000143509 is seeded by experimental fly, rat and yeast inner-membrane annotations, and the ISS transfers mouse Hspd1 (P63038). Hsp60 is a soluble matrix protein that co-fractionates with the inner membrane and engages imported chains emerging from the TIM23 translocase. This supports peripheral association, not an integral membrane protein, and the location is secondary to the matrix. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000143509 Β· PTN000143509 SUPPORTS TRANSFER The cached IBD has experimental membrane-location sources; principal matrix residence is compatible with an associated membrane pool. |
| GO:0005743 mitochondrial inner membrane | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Peripheral inner-membrane association of the matrix chaperonin; ancillary. Reason: The IBA at PTN000143509 is seeded by experimental fly, rat and yeast inner-membrane annotations, and the ISS transfers mouse Hspd1 (P63038). Hsp60 is a soluble matrix protein that co-fractionates with the inner membrane and engages imported chains emerging from the TIM23 translocase. This supports peripheral association, not an integral membrane protein, and the location is secondary to the matrix. |
| GO:0005759 mitochondrial matrix | IBA GO_REF:0000033 | ACCEPT | Summary: Mitochondrial matrix is the principal location of the HSPD1-HSPE1 chaperonin. Reason: HSPD1 is imported via its N-terminal transit peptide (residues 1-26) and folds matrix proteins with Hsp10 in the matrix (PMID:32317635, PMID:11422376). Reactome places HSPD1 in the matrix as a substrate of LONP1 and CLPXP and as the product of ATF5/HSF1-driven expression. The IBA is seeded by yeast, fission yeast, zebrafish and human experimental rows. Supporting Evidence: PMID:32317635 mHsp60-mHsp10 assists the folding of mitochondrial matrix proteins PMID:11422376 Mitochondrial chaperonins are necessary for the folding of newly imported and stress-denatured mitochondrial proteins. |
| GO:0005759 mitochondrial matrix | IDA PMID:15784682 Detection of HSP60 on the membrane surface of stressed human... | ACCEPT | Summary: Mitochondrial matrix is the principal location of the HSPD1-HSPE1 chaperonin. Reason: HSPD1 is imported via its N-terminal transit peptide (residues 1-26) and folds matrix proteins with Hsp10 in the matrix (PMID:32317635, PMID:11422376). Reactome places HSPD1 in the matrix as a substrate of LONP1 and CLPXP and as the product of ATF5/HSF1-driven expression. The IBA is seeded by yeast, fission yeast, zebrafish and human experimental rows. Supporting Evidence: PMID:32317635 mHsp60-mHsp10 assists the folding of mitochondrial matrix proteins PMID:11422376 Mitochondrial chaperonins are necessary for the folding of newly imported and stress-denatured mitochondrial proteins. |
| GO:0005759 mitochondrial matrix | IDA PMID:19393246 Knockdown of human COX17 affects assembly and supramolecular... | ACCEPT | Summary: Mitochondrial matrix is the principal location of the HSPD1-HSPE1 chaperonin. Reason: HSPD1 is imported via its N-terminal transit peptide (residues 1-26) and folds matrix proteins with Hsp10 in the matrix (PMID:32317635, PMID:11422376). Reactome places HSPD1 in the matrix as a substrate of LONP1 and CLPXP and as the product of ATF5/HSF1-driven expression. The IBA is seeded by yeast, fission yeast, zebrafish and human experimental rows. Supporting Evidence: PMID:32317635 mHsp60-mHsp10 assists the folding of mitochondrial matrix proteins PMID:11422376 Mitochondrial chaperonins are necessary for the folding of newly imported and stress-denatured mitochondrial proteins. |
| GO:0005759 mitochondrial matrix | IDA PMID:24746669 Cyclin B1/Cdk1 coordinates mitochondrial respiration for cel... | ACCEPT | Summary: Mitochondrial matrix is the principal location of the HSPD1-HSPE1 chaperonin. Reason: HSPD1 is imported via its N-terminal transit peptide (residues 1-26) and folds matrix proteins with Hsp10 in the matrix (PMID:32317635, PMID:11422376). Reactome places HSPD1 in the matrix as a substrate of LONP1 and CLPXP and as the product of ATF5/HSF1-driven expression. The IBA is seeded by yeast, fission yeast, zebrafish and human experimental rows. Supporting Evidence: PMID:32317635 mHsp60-mHsp10 assists the folding of mitochondrial matrix proteins PMID:11422376 Mitochondrial chaperonins are necessary for the folding of newly imported and stress-denatured mitochondrial proteins. |
| GO:0005759 mitochondrial matrix | IDA PMID:7865888 PBP74, a new member of the mammalian 70-kDa heat shock prote... | ACCEPT | Summary: Mitochondrial matrix is the principal location of the HSPD1-HSPE1 chaperonin. Reason: HSPD1 is imported via its N-terminal transit peptide (residues 1-26) and folds matrix proteins with Hsp10 in the matrix (PMID:32317635, PMID:11422376). Reactome places HSPD1 in the matrix as a substrate of LONP1 and CLPXP and as the product of ATF5/HSF1-driven expression. The IBA is seeded by yeast, fission yeast, zebrafish and human experimental rows. Supporting Evidence: PMID:32317635 mHsp60-mHsp10 assists the folding of mitochondrial matrix proteins PMID:11422376 Mitochondrial chaperonins are necessary for the folding of newly imported and stress-denatured mitochondrial proteins. |
| GO:0005759 mitochondrial matrix | IEA GO_REF:0000044 | ACCEPT | Summary: Mitochondrial matrix is the principal location of the HSPD1-HSPE1 chaperonin. Reason: HSPD1 is imported via its N-terminal transit peptide (residues 1-26) and folds matrix proteins with Hsp10 in the matrix (PMID:32317635, PMID:11422376). Reactome places HSPD1 in the matrix as a substrate of LONP1 and CLPXP and as the product of ATF5/HSF1-driven expression. The IBA is seeded by yeast, fission yeast, zebrafish and human experimental rows. Supporting Evidence: PMID:32317635 mHsp60-mHsp10 assists the folding of mitochondrial matrix proteins PMID:11422376 Mitochondrial chaperonins are necessary for the folding of newly imported and stress-denatured mitochondrial proteins. |
| GO:0005759 mitochondrial matrix | TAS PMID:17823127 Cytosolic accumulation of HSP60 during apoptosis with or wit... | ACCEPT | Summary: Mitochondrial matrix is the principal location of the HSPD1-HSPE1 chaperonin. Reason: HSPD1 is imported via its N-terminal transit peptide (residues 1-26) and folds matrix proteins with Hsp10 in the matrix (PMID:32317635, PMID:11422376). Reactome places HSPD1 in the matrix as a substrate of LONP1 and CLPXP and as the product of ATF5/HSF1-driven expression. The IBA is seeded by yeast, fission yeast, zebrafish and human experimental rows. Supporting Evidence: PMID:32317635 mHsp60-mHsp10 assists the folding of mitochondrial matrix proteins PMID:11422376 Mitochondrial chaperonins are necessary for the folding of newly imported and stress-denatured mitochondrial proteins. |
| GO:0005759 mitochondrial matrix | TAS Reactome:R-HSA-8869558 | ACCEPT | Summary: Mitochondrial matrix is the principal location of the HSPD1-HSPE1 chaperonin. Reason: HSPD1 is imported via its N-terminal transit peptide (residues 1-26) and folds matrix proteins with Hsp10 in the matrix (PMID:32317635, PMID:11422376). Reactome places HSPD1 in the matrix as a substrate of LONP1 and CLPXP and as the product of ATF5/HSF1-driven expression. The IBA is seeded by yeast, fission yeast, zebrafish and human experimental rows. Supporting Evidence: PMID:32317635 mHsp60-mHsp10 assists the folding of mitochondrial matrix proteins PMID:11422376 Mitochondrial chaperonins are necessary for the folding of newly imported and stress-denatured mitochondrial proteins. |
| GO:0005759 mitochondrial matrix | TAS Reactome:R-HSA-9838035 | ACCEPT | Summary: Mitochondrial matrix is the principal location of the HSPD1-HSPE1 chaperonin. Reason: HSPD1 is imported via its N-terminal transit peptide (residues 1-26) and folds matrix proteins with Hsp10 in the matrix (PMID:32317635, PMID:11422376). Reactome places HSPD1 in the matrix as a substrate of LONP1 and CLPXP and as the product of ATF5/HSF1-driven expression. The IBA is seeded by yeast, fission yeast, zebrafish and human experimental rows. Supporting Evidence: PMID:32317635 mHsp60-mHsp10 assists the folding of mitochondrial matrix proteins PMID:11422376 Mitochondrial chaperonins are necessary for the folding of newly imported and stress-denatured mitochondrial proteins. |
| GO:0005759 mitochondrial matrix | TAS Reactome:R-HSA-9838081 | ACCEPT | Summary: Mitochondrial matrix is the principal location of the HSPD1-HSPE1 chaperonin. Reason: HSPD1 is imported via its N-terminal transit peptide (residues 1-26) and folds matrix proteins with Hsp10 in the matrix (PMID:32317635, PMID:11422376). Reactome places HSPD1 in the matrix as a substrate of LONP1 and CLPXP and as the product of ATF5/HSF1-driven expression. The IBA is seeded by yeast, fission yeast, zebrafish and human experimental rows. Supporting Evidence: PMID:32317635 mHsp60-mHsp10 assists the folding of mitochondrial matrix proteins PMID:11422376 Mitochondrial chaperonins are necessary for the folding of newly imported and stress-denatured mitochondrial proteins. |
| GO:0005759 mitochondrial matrix | TAS Reactome:R-HSA-9838093 | ACCEPT | Summary: Mitochondrial matrix is the principal location of the HSPD1-HSPE1 chaperonin. Reason: HSPD1 is imported via its N-terminal transit peptide (residues 1-26) and folds matrix proteins with Hsp10 in the matrix (PMID:32317635, PMID:11422376). Reactome places HSPD1 in the matrix as a substrate of LONP1 and CLPXP and as the product of ATF5/HSF1-driven expression. The IBA is seeded by yeast, fission yeast, zebrafish and human experimental rows. Supporting Evidence: PMID:32317635 mHsp60-mHsp10 assists the folding of mitochondrial matrix proteins PMID:11422376 Mitochondrial chaperonins are necessary for the folding of newly imported and stress-denatured mitochondrial proteins. |
| GO:0005759 mitochondrial matrix | TAS Reactome:R-HSA-9838289 | ACCEPT | Summary: Mitochondrial matrix is the principal location of the HSPD1-HSPE1 chaperonin. Reason: HSPD1 is imported via its N-terminal transit peptide (residues 1-26) and folds matrix proteins with Hsp10 in the matrix (PMID:32317635, PMID:11422376). Reactome places HSPD1 in the matrix as a substrate of LONP1 and CLPXP and as the product of ATF5/HSF1-driven expression. The IBA is seeded by yeast, fission yeast, zebrafish and human experimental rows. Supporting Evidence: PMID:32317635 mHsp60-mHsp10 assists the folding of mitochondrial matrix proteins PMID:11422376 Mitochondrial chaperonins are necessary for the folding of newly imported and stress-denatured mitochondrial proteins. |
| GO:0005759 mitochondrial matrix | TAS Reactome:R-HSA-9856666 | ACCEPT | Summary: Mitochondrial matrix is the principal location of the HSPD1-HSPE1 chaperonin. Reason: HSPD1 is imported via its N-terminal transit peptide (residues 1-26) and folds matrix proteins with Hsp10 in the matrix (PMID:32317635, PMID:11422376). Reactome places HSPD1 in the matrix as a substrate of LONP1 and CLPXP and as the product of ATF5/HSF1-driven expression. The IBA is seeded by yeast, fission yeast, zebrafish and human experimental rows. Supporting Evidence: PMID:32317635 mHsp60-mHsp10 assists the folding of mitochondrial matrix proteins PMID:11422376 Mitochondrial chaperonins are necessary for the folding of newly imported and stress-denatured mitochondrial proteins. |
| GO:0005769 early endosome | IDA PMID:11807771 Heat shock proteins 70 and 60 share common receptors which a... | MARK AS OVER ANNOTATED | Summary: Endocytic localisation of exogenously added Hsp60 in dendritic cells. Reason: PMID:11807771 followed recombinant Hsp60/Hsp70 internalised by receptor-mediated endocytosis into dendritic cells. Clathrin-coated pits, coated vesicles and early endosomes are the route of an exogenous ligand in a recipient cell, not compartments where endogenous HSPD1 resides or acts. Supporting Evidence: PMID:11807771 (hu)hsp60 share the same receptors on (hu)monocyte-derived DC |
| GO:0005829 cytosol | IDA PMID:17823127 Cytosolic accumulation of HSP60 during apoptosis with or wit... | KEEP AS NON CORE | Summary: A cytosolic pool of HSP60 accumulates during apoptosis and in tumour cells. Reason: HSP60 accumulates in the cytosol in many apoptotic systems (PMID:17823127), and a cytosolic pool interacts with survivin and p53 in tumour cells (PMID:18086682). This is a genuine extra-mitochondrial location in specific contexts. Supporting Evidence: PMID:17823127 in numerous apoptotic systems HSP60 protein accumulates in the cytosol |
| GO:0005829 cytosol | IDA PMID:18086682 Hsp60 regulation of tumor cell apoptosis. | KEEP AS NON CORE | Summary: A cytosolic pool of HSP60 accumulates during apoptosis and in tumour cells. Reason: HSP60 accumulates in the cytosol in many apoptotic systems (PMID:17823127), and a cytosolic pool interacts with survivin and p53 in tumour cells (PMID:18086682). This is a genuine extra-mitochondrial location in specific contexts. Supporting Evidence: PMID:17823127 in numerous apoptotic systems HSP60 protein accumulates in the cytosol |
| GO:0005886 plasma membrane | IDA PMID:11027668 Heat shock protein 60 is a high-affinity high-density lipopr... | KEEP AS NON CORE | Summary: Plasma-membrane pool of Hsp60 detected in hepatocyte membrane preparations. Reason: Hsp60 was purified from plasma-membrane preparations of human cell lines and primary hepatocytes as an HDL-binding protein (PMID:11027668). Surface Hsp60 has been reported on several cell types. It is a minor, context-dependent pool. Supporting Evidence: PMID:11027668 A new 55-kDa HDL/apolipoprotein binding protein was demonstrated in plasma membrane preparations of the human cell lines and primary cultured hepatocytes. |
| GO:0005886 plasma membrane | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Plasma-membrane pool of Hsp60 detected in hepatocyte membrane preparations. Reason: Hsp60 was purified from plasma-membrane preparations of human cell lines and primary hepatocytes as an HDL-binding protein (PMID:11027668). Surface Hsp60 has been reported on several cell types. It is a minor, context-dependent pool. Supporting Evidence: PMID:11027668 A new 55-kDa HDL/apolipoprotein binding protein was demonstrated in plasma membrane preparations of the human cell lines and primary cultured hepatocytes. |
| GO:0005905 clathrin-coated pit | IDA PMID:11807771 Heat shock proteins 70 and 60 share common receptors which a... | MARK AS OVER ANNOTATED | Summary: Endocytic localisation of exogenously added Hsp60 in dendritic cells. Reason: PMID:11807771 followed recombinant Hsp60/Hsp70 internalised by receptor-mediated endocytosis into dendritic cells. Clathrin-coated pits, coated vesicles and early endosomes are the route of an exogenous ligand in a recipient cell, not compartments where endogenous HSPD1 resides or acts. Supporting Evidence: PMID:11807771 (hu)hsp60 share the same receptors on (hu)monocyte-derived DC |
| GO:0006457 protein folding | IBA GO_REF:0000033 | ACCEPT | Summary: Protein folding is the core process carried out by the HSPD1-HSPE1 chaperonin. Reason: Human HSPD1 is the single mitochondrial type I (GroEL-like) chaperonin. With its HSPE1/Hsp10 co-chaperonin it encloses non-native polypeptides and folds them in an ATP-driven cycle (PMID:1346131, PMID:11422376, PMID:32317635). Disease variants D3G and V72I abolish refolding of malate dehydrogenase and the ATP synthase beta subunit (PMID:31444388). The PAINT node PTN000143677, seeded by E. coli GroEL, M. tuberculosis Cpn60s, yeast HSP60 and HSPD1 itself, places folding at the root of the type I chaperonin family, and HSPD1 is inside that clade (PANTHER PTHR45633:SF17). Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000143677 Β· PTN000143677 SUPPORTS TRANSFER Root type I chaperonin node seeded by GroEL, mycobacterial Cpn60, yeast HSP60 and HSPD1; human HSPD1 has direct folding assays of its own. Supporting Evidence: PMID:1346131 facilitates the formation of catalytically active ribulose-bisphosphate carboxylase from an unfolded state in the presence of K+ and MgATP. PMID:32317635 mHsp60-mHsp10 assists the folding of mitochondrial matrix proteins PMID:11422376 Mitochondrial chaperonins are necessary for the folding of newly imported and stress-denatured mitochondrial proteins. |
| GO:0006457 protein folding | IEA GO_REF:0000002 | ACCEPT | Summary: Protein folding is the core process carried out by the HSPD1-HSPE1 chaperonin. Reason: Human HSPD1 is the single mitochondrial type I (GroEL-like) chaperonin. With its HSPE1/Hsp10 co-chaperonin it encloses non-native polypeptides and folds them in an ATP-driven cycle (PMID:1346131, PMID:11422376, PMID:32317635). Disease variants D3G and V72I abolish refolding of malate dehydrogenase and the ATP synthase beta subunit (PMID:31444388). The PAINT node PTN000143677, seeded by E. coli GroEL, M. tuberculosis Cpn60s, yeast HSP60 and HSPD1 itself, places folding at the root of the type I chaperonin family, and HSPD1 is inside that clade (PANTHER PTHR45633:SF17). Supporting Evidence: PMID:1346131 facilitates the formation of catalytically active ribulose-bisphosphate carboxylase from an unfolded state in the presence of K+ and MgATP. PMID:32317635 mHsp60-mHsp10 assists the folding of mitochondrial matrix proteins PMID:11422376 Mitochondrial chaperonins are necessary for the folding of newly imported and stress-denatured mitochondrial proteins. |
| GO:0006458 'de novo' protein folding | ISS GO_REF:0000024 | ACCEPT | Summary: Folding of newly imported matrix proteins is de novo folding after translocation. Reason: Imported precursors arrive in the matrix unfolded and are folded for the first time by the Hsp60-Hsp10 chaperonin. The ISS donor is yeast HSP60 (P19882), the mitochondrial Hsp60 ortholog in PTHR45633, and the transfer agrees with the human data. Supporting Evidence: PMID:11422376 Mitochondrial chaperonins are necessary for the folding of newly imported and stress-denatured mitochondrial proteins. file:human/HSPD1/HSPD1-uniprot.txt Together with Hsp10, facilitates the correct folding of imported proteins. |
| GO:0006986 response to unfolded protein | IDA PMID:11050098 The importance of a mobile loop in regulating chaperonin/ co... | KEEP AS NON CORE | Summary: HSPD1 is a stress-induced effector chaperone that refolds unfolded proteins. Reason: HSPD1 acts on unfolded proteins as an effector, refolding them. It is not a sensor or signalling component of an unfolded-protein response. The cited paper (PMID:11050098) is a co-chaperonin specificity study. The term is defensible for an effector chaperone but is secondary to the folding activity itself. Supporting Evidence: PMID:11422376 Mitochondrial chaperonins are necessary for the folding of newly imported and stress-denatured mitochondrial proteins. PMID:11050098 its human homologue, Hsp60 functions specifically with its co-chaperonin partner, Hsp10 |
| GO:0008035 high-density lipoprotein particle binding | IDA PMID:11027668 Heat shock protein 60 is a high-affinity high-density lipopr... | KEEP AS NON CORE | Summary: Cell-surface Hsp60 was identified as a high-affinity HDL/apolipoprotein-binding protein. Reason: Ligand blotting of hepatocyte plasma-membrane preparations identified a 55-kDa HDL/apoA-I/apoA-II binding protein as Hsp60, and anti-Hsp60 antibody blocked apoA-II binding. This is a single study of a cell-surface pool. It is kept as a non-core, extra-mitochondrial binding activity. Supporting Evidence: PMID:11027668 Internal microprotein sequencing of the 55-kDa protein band revealed the binding protein as being heat shock protein 60 |
| GO:0008637 apoptotic mitochondrial changes | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Hsp60 is released from or redistributed outside mitochondria during apoptosis. Reason: The IBA at PTN000888030 is seeded by rat Hspd1 (RGD:621314). Human HSP60 accumulates in the cytosol during apoptosis, sometimes with mitochondrial release, and Hsp60/Hsp10 leave mitochondria with cytochrome c after staurosporine treatment (PMID:10205158). This is a context-dependent role, not the core function. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000888030 Β· PTN000888030 SUPPORTS TRANSFER Seeded by rat Hspd1 alone; consistent with independent human apoptosis studies. Supporting Evidence: PMID:17823127 in numerous apoptotic systems HSP60 protein accumulates in the cytosol PMID:10205158 pro-caspase-3 is present in the mitochondrial fraction of Jurkat T cells in a complex with the chaperone proteins Hsp60 and Hsp10 |
| GO:0009409 response to cold | ISS GO_REF:0000024 | MARK AS OVER ANNOTATED | Summary: Cold-induced expression of chicken Hsp60 does not show that HSPD1 executes a cold response. Reason: The ISS donor is chicken HSPD1 (Q5ZL72). The source study measured increased Hsp60 mRNA and protein in chicken hearts under cold stress (PMID:23636703). Stress-induced expression shows HSPD1 responds to the stimulus, not that it carries out a cold-specific process, and the same chaperone is induced by many stresses. The annotation is an over-reading of expression data. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:Q5ZL72 Β· HSPD1, Gallus gallus UNRESOLVED Ortholog relationship is sound; the donor annotation rests on expression change under cold stress, which supports regulation of HSPD1, not participation of HSPD1 in a cold response. Supporting Evidence: PMID:23636703 acute cold stress in 3-, 6-, and 12-h treatment groups significantly increased the protein levels of the Hsp60 gene in hearts of chickens |
| GO:0009986 cell surface | IDA PMID:10663613 gammadelta T cells lyse autologous and allogenic oesophageal... | KEEP AS NON CORE | Summary: Endogenous Hsp60 detected on the cell surface of stressed, tumour or lymphoid cells. Reason: PMID:10663613 detects endogenous Hsp60 on the surface of intact cells (immunogold, flow cytometry or AFM). This surface pool underlies the immune-recognition and lipoprotein-binding observations. It is secondary to the matrix location. Supporting Evidence: PMID:10663613 Surface expression of hsp60 and hsp70 on oesophageal tumours and Daudi cells was demonstrated by flow cytometry |
| GO:0009986 cell surface | IDA PMID:11807771 Heat shock proteins 70 and 60 share common receptors which a... | KEEP AS NON CORE | Summary: Exogenous Hsp60 bound to dendritic-cell surface receptors; the term holds via endogenous surface Hsp60. Reason: Lipsker et al. added human Hsp60/Hsp70 to monocyte-derived dendritic cells and followed receptor binding and internalisation. Surface signal there is exogenous ligand on another cell's receptors, not endogenous HSPD1 trafficked to the surface. Endogenous surface Hsp60 is supported by the other cell-surface rows, so the term is kept as non-core, but this row is weak support for it. Supporting Evidence: PMID:11807771 (hu)hsp60 share the same receptors on (hu)monocyte-derived DC |
| GO:0009986 cell surface | IDA PMID:15784682 Detection of HSP60 on the membrane surface of stressed human... | KEEP AS NON CORE | Summary: Endogenous Hsp60 detected on the cell surface of stressed, tumour or lymphoid cells. Reason: PMID:15784682 detects endogenous Hsp60 on the surface of intact cells (immunogold, flow cytometry or AFM). This surface pool underlies the immune-recognition and lipoprotein-binding observations. It is secondary to the matrix location. Supporting Evidence: PMID:15784682 we found clear evidence for the occurrence of HSP60 on the surface of stressed HUVECs |
| GO:0009986 cell surface | IDA PMID:9243807 Cell surface localization of the 60 kDa heat shock chaperoni... | KEEP AS NON CORE | Summary: Endogenous Hsp60 detected on the cell surface of stressed, tumour or lymphoid cells. Reason: PMID:9243807 detects endogenous Hsp60 on the surface of intact cells (immunogold, flow cytometry or AFM). This surface pool underlies the immune-recognition and lipoprotein-binding observations. It is secondary to the matrix location. Supporting Evidence: PMID:9243807 Labeling intensity was 250-800 gold particles per cell in Chinese hamster ovary cells and 600-2000 in CEM-SS human lymphoblasts. |
| GO:0016020 membrane | HDA PMID:19946888 Defining the membrane proteome of NK cells. | TOO GENERAL | Summary: Membrane is entailed by the more specific inner-membrane and plasma-membrane terms kept here. Reason: The NK-cell membrane proteome (HDA) and the IEA transfer place HSPD1 in membrane fractions. Mitochondrial inner membrane and plasma membrane are both retained as more specific non-core locations. |
| GO:0016020 membrane | IEA GO_REF:0000107 | TOO GENERAL | Summary: Membrane is entailed by the more specific inner-membrane and plasma-membrane terms kept here. Reason: The NK-cell membrane proteome (HDA) and the IEA transfer place HSPD1 in membrane fractions. Mitochondrial inner membrane and plasma membrane are both retained as more specific non-core locations. |
| GO:0016887 ATP hydrolysis activity | ISS GO_REF:0000024 | ACCEPT | Summary: ATP hydrolysis by Hsp60 drives the folding cycle. Reason: ATP hydrolysis by mt-cpn60 in the presence of mt-cpn10 was measured directly (PMID:11422376). It is the energy-coupling step of the ATP-dependent folding activity, and so is a component of the core function rather than an independent ATPase role. Supporting Evidence: PMID:11422376 does not inhibit malate dehydrogenase refolding or ATP hydrolysis by mt-cpn60 in the presence of mt-cpn10 |
| GO:0019899 enzyme binding | IPI PMID:20507888 LAP, an alcohol acetaldehyde dehydrogenase enzyme in Listeri... | KEEP AS NON CORE | Summary: Host-cell Hsp60 is the receptor bound by the Listeria adhesion protein LAP. Reason: LAP, a bifunctional alcohol acetaldehyde dehydrogenase, binds Hsp60 with nanomolar affinity; Hsp60 acts as its host-cell receptor on enterocytes. 'Enzyme binding' is accurate because LAP is an enzyme, but the biological role is pathogen adhesion. It is kept as a non-core, host-pathogen interaction. Supporting Evidence: PMID:20507888 interacts with host-cell receptor Hsp60 to promote bacterial adhesion PMID:20507888 displayed strong binding affinity (K(D) 2-31 nM) towards Hsp60 |
| GO:0019899 enzyme binding | IPI PMID:20507888 LAP, an alcohol acetaldehyde dehydrogenase enzyme in Listeri... | KEEP AS NON CORE | Summary: Host-cell Hsp60 is the receptor bound by the Listeria adhesion protein LAP. Reason: LAP, a bifunctional alcohol acetaldehyde dehydrogenase, binds Hsp60 with nanomolar affinity; Hsp60 acts as its host-cell receptor on enterocytes. 'Enzyme binding' is accurate because LAP is an enzyme, but the biological role is pathogen adhesion. It is kept as a non-core, host-pathogen interaction. Supporting Evidence: PMID:20507888 interacts with host-cell receptor Hsp60 to promote bacterial adhesion PMID:20507888 displayed strong binding affinity (K(D) 2-31 nM) towards Hsp60 |
| GO:0019899 enzyme binding | IPI PMID:20507888 LAP, an alcohol acetaldehyde dehydrogenase enzyme in Listeri... | KEEP AS NON CORE | Summary: Host-cell Hsp60 is the receptor bound by the Listeria adhesion protein LAP. Reason: LAP, a bifunctional alcohol acetaldehyde dehydrogenase, binds Hsp60 with nanomolar affinity; Hsp60 acts as its host-cell receptor on enterocytes. 'Enzyme binding' is accurate because LAP is an enzyme, but the biological role is pathogen adhesion. It is kept as a non-core, host-pathogen interaction. Supporting Evidence: PMID:20507888 interacts with host-cell receptor Hsp60 to promote bacterial adhesion PMID:20507888 displayed strong binding affinity (K(D) 2-31 nM) towards Hsp60 |
| GO:0019899 enzyme binding | IPI PMID:20507888 LAP, an alcohol acetaldehyde dehydrogenase enzyme in Listeri... | KEEP AS NON CORE | Summary: Host-cell Hsp60 is the receptor bound by the Listeria adhesion protein LAP. Reason: LAP, a bifunctional alcohol acetaldehyde dehydrogenase, binds Hsp60 with nanomolar affinity; Hsp60 acts as its host-cell receptor on enterocytes. 'Enzyme binding' is accurate because LAP is an enzyme, but the biological role is pathogen adhesion. It is kept as a non-core, host-pathogen interaction. Supporting Evidence: PMID:20507888 interacts with host-cell receptor Hsp60 to promote bacterial adhesion PMID:20507888 displayed strong binding affinity (K(D) 2-31 nM) towards Hsp60 |
| GO:0030135 coated vesicle | IDA PMID:11807771 Heat shock proteins 70 and 60 share common receptors which a... | MARK AS OVER ANNOTATED | Summary: Endocytic localisation of exogenously added Hsp60 in dendritic cells. Reason: PMID:11807771 followed recombinant Hsp60/Hsp70 internalised by receptor-mediated endocytosis into dendritic cells. Clathrin-coated pits, coated vesicles and early endosomes are the route of an exogenous ligand in a recipient cell, not compartments where endogenous HSPD1 resides or acts. Supporting Evidence: PMID:11807771 (hu)hsp60 share the same receptors on (hu)monocyte-derived DC |
| GO:0030141 secretory granule | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Secretory-granule localisation transferred from rodent orthologs. Reason: The ISS/IEA rows transfer a mouse Hspd1 (P63038) observation of Hsp60 in secretory granules. This is compatible with the secreted/extracellular Hsp60 pool, but no human evidence was found and the location is peripheral to function. |
| GO:0030141 secretory granule | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Secretory-granule localisation transferred from rodent orthologs. Reason: The ISS/IEA rows transfer a mouse Hspd1 (P63038) observation of Hsp60 in secretory granules. This is compatible with the secreted/extracellular Hsp60 pool, but no human evidence was found and the location is peripheral to function. |
| GO:0031625 ubiquitin protein ligase binding | IPI PMID:19725078 Proteomic analysis of increased Parkin expression and its in... | KEEP AS NON CORE | Summary: HSPD1 co-purifies with the E3 ligase Parkin. Reason: PMID:19725078 identified HSPD1 among Parkin-associated proteins by tandem affinity purification. Parkin acts on mitochondria, and HSPD1 may be a chaperone client or co-purifying matrix protein rather than a functional Parkin adaptor. The specific binding term is retained as a non-core interaction. Supporting Evidence: PMID:19725078 Tandem affinity purification/MS revealed 14 potential interactants of Parkin; CKB, DBT, HSPD1 |
| GO:0031625 ubiquitin protein ligase binding | IPI PMID:21753002 Parkin interacts with Ambra1 to induce mitophagy. | KEEP AS NON CORE | Summary: HSPD1 co-purifies with the E3 ligase Parkin. Reason: PMID:21753002 identified HSPD1 among Parkin-associated proteins by tandem affinity purification. Parkin acts on mitochondria, and HSPD1 may be a chaperone client or co-purifying matrix protein rather than a functional Parkin adaptor. The specific binding term is retained as a non-core interaction. |
| GO:0032727 positive regulation of interferon-alpha production | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: LPS-free Hsp60 induces IFN-alpha in antigen-presenting cells. Reason: IFN-alpha induction is the best-controlled immune effect of extracellular Hsp60. It differs from LPS (PMID:17164250) and persists with endotoxin-free Hsp60 (PMID:18256040). It is a non-core activity of released Hsp60. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN002900230 Β· PTN002900230 SUPPORTS TRANSFER Vertebrate HSPD1 node seeded by mouse Hspd1 (MGI:96242) and human HSPD1 experimental annotations; the target among its own seeds marks experimental grounding, not circularity. The transferred claim is an extracellular, context-dependent immune effect. Supporting Evidence: PMID:17164250 in contrast to LPS Hsp60 induces IFNalpha production in professional APC PMID:18256040 LPS-free Hsp60 enhances IFN alpha expression in APC |
| GO:0032727 positive regulation of interferon-alpha production | IDA PMID:17164250 Synergistic and differential modulation of immune responses ... | KEEP AS NON CORE | Summary: LPS-free Hsp60 induces IFN-alpha in antigen-presenting cells. Reason: IFN-alpha induction is the best-controlled immune effect of extracellular Hsp60. It differs from LPS (PMID:17164250) and persists with endotoxin-free Hsp60 (PMID:18256040). It is a non-core activity of released Hsp60. Supporting Evidence: PMID:17164250 in contrast to LPS Hsp60 induces IFNalpha production in professional APC PMID:18256040 LPS-free Hsp60 enhances IFN alpha expression in APC |
| GO:0032729 positive regulation of type II interferon production | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Hsp60 enhances antigen-specific IFN-gamma release by T cells via APC. Reason: Hsp60 increases antigen-specific IFN-gamma release in APC-dependent T-cell activation. Part of the effect is IFN-alpha-mediated and LPS-independent (PMID:17164250, PMID:18256040). It is an indirect, context-dependent immune effect of extracellular Hsp60. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN002900230 Β· PTN002900230 SUPPORTS TRANSFER Vertebrate HSPD1 node seeded by mouse Hspd1 (MGI:96242) and human HSPD1 experimental annotations; the target among its own seeds marks experimental grounding, not circularity. The transferred claim is an extracellular, context-dependent immune effect. Supporting Evidence: PMID:17164250 both, Hsp60 and LPS, increase antigen-specific interferon (IFN) gamma release in T cells PMID:18256040 LPS-free Hsp60 enhances IFN alpha expression in APC |
| GO:0032729 positive regulation of type II interferon production | IDA PMID:17164250 Synergistic and differential modulation of immune responses ... | KEEP AS NON CORE | Summary: Hsp60 enhances antigen-specific IFN-gamma release by T cells via APC. Reason: Hsp60 increases antigen-specific IFN-gamma release in APC-dependent T-cell activation. Part of the effect is IFN-alpha-mediated and LPS-independent (PMID:17164250, PMID:18256040). It is an indirect, context-dependent immune effect of extracellular Hsp60. Supporting Evidence: PMID:17164250 both, Hsp60 and LPS, increase antigen-specific interferon (IFN) gamma release in T cells PMID:18256040 LPS-free Hsp60 enhances IFN alpha expression in APC |
| GO:0032729 positive regulation of type II interferon production | IDA PMID:17164250 Synergistic and differential modulation of immune responses ... | KEEP AS NON CORE | Summary: Hsp60 enhances antigen-specific IFN-gamma release by T cells via APC. Reason: Hsp60 increases antigen-specific IFN-gamma release in APC-dependent T-cell activation. Part of the effect is IFN-alpha-mediated and LPS-independent (PMID:17164250, PMID:18256040). It is an indirect, context-dependent immune effect of extracellular Hsp60. Supporting Evidence: PMID:17164250 both, Hsp60 and LPS, increase antigen-specific interferon (IFN) gamma release in T cells PMID:18256040 LPS-free Hsp60 enhances IFN alpha expression in APC |
| GO:0032729 positive regulation of type II interferon production | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Hsp60 enhances antigen-specific IFN-gamma release by T cells via APC. Reason: Hsp60 increases antigen-specific IFN-gamma release in APC-dependent T-cell activation. Part of the effect is IFN-alpha-mediated and LPS-independent (PMID:17164250, PMID:18256040). It is an indirect, context-dependent immune effect of extracellular Hsp60. Supporting Evidence: PMID:17164250 both, Hsp60 and LPS, increase antigen-specific interferon (IFN) gamma release in T cells PMID:18256040 LPS-free Hsp60 enhances IFN alpha expression in APC |
| GO:0032729 positive regulation of type II interferon production | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Hsp60 enhances antigen-specific IFN-gamma release by T cells via APC. Reason: Hsp60 increases antigen-specific IFN-gamma release in APC-dependent T-cell activation. Part of the effect is IFN-alpha-mediated and LPS-independent (PMID:17164250, PMID:18256040). It is an indirect, context-dependent immune effect of extracellular Hsp60. Supporting Evidence: PMID:17164250 both, Hsp60 and LPS, increase antigen-specific interferon (IFN) gamma release in T cells PMID:18256040 LPS-free Hsp60 enhances IFN alpha expression in APC |
| GO:0032733 positive regulation of interleukin-10 production | IDA PMID:16148103 Heat shock protein 60 activates B cells via the TLR4-MyD88 p... | MARK AS OVER ANNOTATED | Summary: IL-10 induction in B cells by Hsp60 rests on the contested TLR4 B-cell study. Reason: Cohen-Sfady et al. reported that human HSP60 activates mouse B cells through TLR4/MyD88 and stated that LPS contamination was excluded (PMID:16148103). Later work found that Hsp60 binds LPS tightly (PMID:17164250), that it does not bind B or T lymphocytes (PMID:17164250), and that endotoxin-free Hsp60 acts independently of TLR4/MyD88 and does not induce IL-6, IL-12 or TNF in APC (PMID:18256040). TLR4-dependent activities of recombinant Hsp60 preparations are therefore at least partly attributable to bound LPS. The annotation is not removed, because the curators read the full paper with its controls, but it is likely an over-annotation of HSPD1 function. Supporting Evidence: PMID:16148103 human HSP60 (but not the Escherichia coli GroEL or the Mycobacterial HSP65 molecules) induced naive mouse B cells to proliferate PMID:17164250 Hsp60 exclusively binds to macrophages and DC but not to T or B lymphocytes |
| GO:0032735 positive regulation of interleukin-12 production | IDA PMID:17164250 Synergistic and differential modulation of immune responses ... | KEEP AS NON CORE | Summary: Hsp60 enhances IL-12p40 only together with LPS, by binding it. Reason: Hsp60 and LPS synergistically enhance IL-12p40 production in APC, and the effect depends on Hsp60 binding LPS (PMID:17164250). LPS-free Hsp60 does not induce IL-12 (PMID:18256040). The annotation holds only in the presence of bacterial LPS and is kept as non-core with that restriction. Supporting Evidence: PMID:17164250 This effect was Hsp60-specific and dependent on LPS-binding by Hsp60. PMID:18256040 LPS-free Hsp60 did not induce IL-6, IL-12 or tumor necrosis factor alpha production in APC |
| GO:0032755 positive regulation of interleukin-6 production | IBA GO_REF:0000033 | MARK AS OVER ANNOTATED | Summary: IL-6 induction by Hsp60 is contradicted for endotoxin-free protein. Reason: Cohen-Sfady et al. reported that human HSP60 activates mouse B cells through TLR4/MyD88 and stated that LPS contamination was excluded (PMID:16148103). Later work found that Hsp60 binds LPS tightly (PMID:17164250), that it does not bind B or T lymphocytes (PMID:17164250), and that endotoxin-free Hsp60 acts independently of TLR4/MyD88 and does not induce IL-6, IL-12 or TNF in APC (PMID:18256040). TLR4-dependent activities of recombinant Hsp60 preparations are therefore at least partly attributable to bound LPS. The annotation is not removed, because the curators read the full paper with its controls, but it is likely an over-annotation of HSPD1 function. For IL-6 specifically, LPS-free Hsp60 did not induce IL-6 in APC (PMID:18256040). Propagation Review Root cause: UNRESOLVED Sources checked: PANTHER:PTN002900230 Β· PTN002900230 UNRESOLVED Seeded by rat Hspd1 and human HSPD1 (PMID:16148103). The phylogenetic placement is fine; the seed experiments are disputed by endotoxin-free studies showing no IL-6 induction. Supporting Evidence: PMID:16148103 The effects of HSP60 were found to be largely dependent on TLR4 and MyD88 signaling PMID:18256040 LPS-free Hsp60 did not induce IL-6, IL-12 or tumor necrosis factor alpha production in APC |
| GO:0032755 positive regulation of interleukin-6 production | IDA PMID:16148103 Heat shock protein 60 activates B cells via the TLR4-MyD88 p... | MARK AS OVER ANNOTATED | Summary: IL-6 induction by Hsp60 is contradicted for endotoxin-free protein. Reason: Cohen-Sfady et al. reported that human HSP60 activates mouse B cells through TLR4/MyD88 and stated that LPS contamination was excluded (PMID:16148103). Later work found that Hsp60 binds LPS tightly (PMID:17164250), that it does not bind B or T lymphocytes (PMID:17164250), and that endotoxin-free Hsp60 acts independently of TLR4/MyD88 and does not induce IL-6, IL-12 or TNF in APC (PMID:18256040). TLR4-dependent activities of recombinant Hsp60 preparations are therefore at least partly attributable to bound LPS. The annotation is not removed, because the curators read the full paper with its controls, but it is likely an over-annotation of HSPD1 function. For IL-6 specifically, LPS-free Hsp60 did not induce IL-6 in APC (PMID:18256040). Supporting Evidence: PMID:16148103 The effects of HSP60 were found to be largely dependent on TLR4 and MyD88 signaling PMID:18256040 LPS-free Hsp60 did not induce IL-6, IL-12 or tumor necrosis factor alpha production in APC |
| GO:0032991 protein-containing complex | IDA PMID:21328542 ZNF703 gene amplification at 8p12 specifies luminal B breast... | MARK AS OVER ANNOTATED | Summary: Generic complex term from co-immunoprecipitation; not informative. Reason: PMID:21328542 recovers HSPD1 with a bait protein (ZNF703 or a METTL methyltransferase). Co-purification shows an interaction but not a defined stable complex. Many such baits are chaperonin clients. The informative complex for HSPD1 is the Hsp60-Hsp10 chaperonin, which is not what these experiments describe. Supporting Evidence: PMID:21328542 HSP60 was only present in the cytoplasm and may interact with the cytoplasmic form of ZNF703 |
| GO:0032991 protein-containing complex | IDA PMID:23349634 A newly uncovered group of distantly related lysine methyltr... | MARK AS OVER ANNOTATED | Summary: Generic complex term from co-immunoprecipitation; not informative. Reason: PMID:23349634 recovers HSPD1 with a bait protein (ZNF703 or a METTL methyltransferase). Co-purification shows an interaction but not a defined stable complex. Many such baits are chaperonin clients. The informative complex for HSPD1 is the Hsp60-Hsp10 chaperonin, which is not what these experiments describe. Supporting Evidence: PMID:23349634 chaperonins HSPD1 and CCT (see METTL18, CAMKMT, METTL20, and METTL21B) |
| GO:0034185 apolipoprotein binding | IPI PMID:11027668 Heat shock protein 60 is a high-affinity high-density lipopr... | KEEP AS NON CORE | Summary: Cell-surface Hsp60 was identified as a high-affinity HDL/apolipoprotein-binding protein. Reason: Ligand blotting of hepatocyte plasma-membrane preparations identified a 55-kDa HDL/apoA-I/apoA-II binding protein as Hsp60, and anti-Hsp60 antibody blocked apoA-II binding. This is a single study of a cell-surface pool. It is kept as a non-core, extra-mitochondrial binding activity. Supporting Evidence: PMID:11027668 Internal microprotein sequencing of the 55-kDa protein band revealed the binding protein as being heat shock protein 60 |
| GO:0034186 apolipoprotein A-I binding | IPI PMID:11027668 Heat shock protein 60 is a high-affinity high-density lipopr... | KEEP AS NON CORE | Summary: Cell-surface Hsp60 was identified as a high-affinity HDL/apolipoprotein-binding protein. Reason: Ligand blotting of hepatocyte plasma-membrane preparations identified a 55-kDa HDL/apoA-I/apoA-II binding protein as Hsp60, and anti-Hsp60 antibody blocked apoA-II binding. This is a single study of a cell-surface pool. It is kept as a non-core, extra-mitochondrial binding activity. Supporting Evidence: PMID:11027668 Internal microprotein sequencing of the 55-kDa protein band revealed the binding protein as being heat shock protein 60 |
| GO:0034514 mitochondrial unfolded protein response | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: HSPD1 is a downstream effector and reporter of the mitochondrial UPR, not a signalling component. Reason: The PAINT IBD at PTN000143510 is seeded by C. elegans hsp-60 (WBGene00002025). hsp-60 is the classic transcriptional target and reporter of the UPRmt. Human HSPD1 transcription is likewise activated by ATF5/HSF1 (Reactome R-HSA-9856666). The chaperonin then refolds matrix proteins as the effector arm of the response. This is real but secondary to the constitutive folding function. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000143510 Β· PTN000143510 SUPPORTS TRANSFER Seeded by worm hsp-60; transfer is reasonable for the effector-chaperone role, not for sensing or signalling. Supporting Evidence: PMID:11422376 Mitochondrial chaperonins are necessary for the folding of newly imported and stress-denatured mitochondrial proteins. |
| GO:0042026 protein refolding | IDA PMID:11050098 The importance of a mobile loop in regulating chaperonin/ co... | ACCEPT | Summary: HSPD1-HSPE1 refolds denatured substrates such as malate dehydrogenase. Reason: Human HSPD1 is the single mitochondrial type I (GroEL-like) chaperonin. With its HSPE1/Hsp10 co-chaperonin it encloses non-native polypeptides and folds them in an ATP-driven cycle (PMID:1346131, PMID:11422376, PMID:32317635). Disease variants D3G and V72I abolish refolding of malate dehydrogenase and the ATP synthase beta subunit (PMID:31444388). The PAINT node PTN000143677, seeded by E. coli GroEL, M. tuberculosis Cpn60s, yeast HSP60 and HSPD1 itself, places folding at the root of the type I chaperonin family, and HSPD1 is inside that clade (PANTHER PTHR45633:SF17). Refolding of chemically denatured enzymes is the standard assay of this activity, and stress-denatured matrix proteins are physiological substrates. Supporting Evidence: PMID:11422376 Mitochondrial chaperonins are necessary for the folding of newly imported and stress-denatured mitochondrial proteins. PMID:11422376 does not inhibit malate dehydrogenase refolding or ATP hydrolysis by mt-cpn60 in the presence of mt-cpn10 PMID:31444388 unable to fold denatured substrates such as Ξ±-lactalbumin, malate dehydrogenase (MDH), and the Ξ²-subunit of ATP synthase |
| GO:0042026 protein refolding | IEA GO_REF:0000002 | ACCEPT | Summary: HSPD1-HSPE1 refolds denatured substrates such as malate dehydrogenase. Reason: Human HSPD1 is the single mitochondrial type I (GroEL-like) chaperonin. With its HSPE1/Hsp10 co-chaperonin it encloses non-native polypeptides and folds them in an ATP-driven cycle (PMID:1346131, PMID:11422376, PMID:32317635). Disease variants D3G and V72I abolish refolding of malate dehydrogenase and the ATP synthase beta subunit (PMID:31444388). The PAINT node PTN000143677, seeded by E. coli GroEL, M. tuberculosis Cpn60s, yeast HSP60 and HSPD1 itself, places folding at the root of the type I chaperonin family, and HSPD1 is inside that clade (PANTHER PTHR45633:SF17). Refolding of chemically denatured enzymes is the standard assay of this activity, and stress-denatured matrix proteins are physiological substrates. Supporting Evidence: PMID:11422376 Mitochondrial chaperonins are necessary for the folding of newly imported and stress-denatured mitochondrial proteins. PMID:11422376 does not inhibit malate dehydrogenase refolding or ATP hydrolysis by mt-cpn60 in the presence of mt-cpn10 PMID:31444388 unable to fold denatured substrates such as Ξ±-lactalbumin, malate dehydrogenase (MDH), and the Ξ²-subunit of ATP synthase |
| GO:0042100 B cell proliferation | IDA PMID:16148103 Heat shock protein 60 activates B cells via the TLR4-MyD88 p... | MARK AS OVER ANNOTATED | Summary: Reported B-cell activation by Hsp60 is contested; Hsp60 does not bind B cells. Reason: Cohen-Sfady et al. reported that human HSP60 activates mouse B cells through TLR4/MyD88 and stated that LPS contamination was excluded (PMID:16148103). Later work found that Hsp60 binds LPS tightly (PMID:17164250), that it does not bind B or T lymphocytes (PMID:17164250), and that endotoxin-free Hsp60 acts independently of TLR4/MyD88 and does not induce IL-6, IL-12 or TNF in APC (PMID:18256040). TLR4-dependent activities of recombinant Hsp60 preparations are therefore at least partly attributable to bound LPS. The annotation is not removed, because the curators read the full paper with its controls, but it is likely an over-annotation of HSPD1 function. If the effect is accepted, the right term is the regulation term (Hsp60 is an exogenous stimulus, not part of the B cell's proliferation machinery). Supporting Evidence: PMID:16148103 human HSP60 (but not the Escherichia coli GroEL or the Mycobacterial HSP65 molecules) induced naive mouse B cells to proliferate PMID:16148103 Care was taken to rule out contamination of the HSP60 with LPS as a causative factor. PMID:17164250 Hsp60 exclusively binds to macrophages and DC but not to T or B lymphocytes |
| GO:0042110 T cell activation | IBA GO_REF:0000033 | MODIFY | Summary: Hsp60 costimulates rather than executes T-cell activation; use the regulation term. Reason: The experiments add Hsp60 to APC/T-cell cultures and measure enhanced antigen-specific T-cell activation. Hsp60 is an extracellular costimulatory signal, not a component of the T cell's activation machinery, so 'positive regulation of T cell activation' (GO:0050870, already annotated by IBA and IDA) describes the claim correctly. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN002900230 Β· PTN002900230 SUPPORTS TRANSFER Vertebrate node seeded by mouse and human experimental rows. The transfer is sound, but the term should be the regulation term GO:0050870, which the same node also carries. Proposed replacements: positive regulation of T cell activation Supporting Evidence: PMID:15371451 the Hsp60-mediated enhancement of antigen-specific T cell activation does not correlate with endotoxin contamination PMID:18256040 T cell co-stimulation induced by LPS-free Hsp60 was independent of TLR4 |
| GO:0042110 T cell activation | IDA PMID:15371451 Lipopolysaccharide-free heat shock protein 60 activates T ce... | MODIFY | Summary: Hsp60 costimulates rather than executes T-cell activation; use the regulation term. Reason: The experiments add Hsp60 to APC/T-cell cultures and measure enhanced antigen-specific T-cell activation. Hsp60 is an extracellular costimulatory signal, not a component of the T cell's activation machinery, so 'positive regulation of T cell activation' (GO:0050870, already annotated by IBA and IDA) describes the claim correctly. Proposed replacements: positive regulation of T cell activation Supporting Evidence: PMID:15371451 the Hsp60-mediated enhancement of antigen-specific T cell activation does not correlate with endotoxin contamination PMID:18256040 T cell co-stimulation induced by LPS-free Hsp60 was independent of TLR4 |
| GO:0042110 T cell activation | IDA PMID:17164250 Synergistic and differential modulation of immune responses ... | MODIFY | Summary: Hsp60 costimulates rather than executes T-cell activation; use the regulation term. Reason: The experiments add Hsp60 to APC/T-cell cultures and measure enhanced antigen-specific T-cell activation. Hsp60 is an extracellular costimulatory signal, not a component of the T cell's activation machinery, so 'positive regulation of T cell activation' (GO:0050870, already annotated by IBA and IDA) describes the claim correctly. Proposed replacements: positive regulation of T cell activation Supporting Evidence: PMID:15371451 the Hsp60-mediated enhancement of antigen-specific T cell activation does not correlate with endotoxin contamination PMID:18256040 T cell co-stimulation induced by LPS-free Hsp60 was independent of TLR4 |
| GO:0042110 T cell activation | IDA PMID:18256040 Hsp60-mediated T cell stimulation is independent of TLR4 and... | MODIFY | Summary: Hsp60 costimulates rather than executes T-cell activation; use the regulation term. Reason: The experiments add Hsp60 to APC/T-cell cultures and measure enhanced antigen-specific T-cell activation. Hsp60 is an extracellular costimulatory signal, not a component of the T cell's activation machinery, so 'positive regulation of T cell activation' (GO:0050870, already annotated by IBA and IDA) describes the claim correctly. Proposed replacements: positive regulation of T cell activation Supporting Evidence: PMID:15371451 the Hsp60-mediated enhancement of antigen-specific T cell activation does not correlate with endotoxin contamination PMID:18256040 T cell co-stimulation induced by LPS-free Hsp60 was independent of TLR4 |
| GO:0042113 B cell activation | IDA PMID:16148103 Heat shock protein 60 activates B cells via the TLR4-MyD88 p... | MARK AS OVER ANNOTATED | Summary: Reported B-cell activation by Hsp60 is contested; Hsp60 does not bind B cells. Reason: Cohen-Sfady et al. reported that human HSP60 activates mouse B cells through TLR4/MyD88 and stated that LPS contamination was excluded (PMID:16148103). Later work found that Hsp60 binds LPS tightly (PMID:17164250), that it does not bind B or T lymphocytes (PMID:17164250), and that endotoxin-free Hsp60 acts independently of TLR4/MyD88 and does not induce IL-6, IL-12 or TNF in APC (PMID:18256040). TLR4-dependent activities of recombinant Hsp60 preparations are therefore at least partly attributable to bound LPS. The annotation is not removed, because the curators read the full paper with its controls, but it is likely an over-annotation of HSPD1 function. If the effect is accepted, the right term is the regulation term (Hsp60 is an exogenous stimulus, not part of the B cell's proliferation machinery). Supporting Evidence: PMID:16148103 human HSP60 (but not the Escherichia coli GroEL or the Mycobacterial HSP65 molecules) induced naive mouse B cells to proliferate PMID:16148103 Care was taken to rule out contamination of the HSP60 with LPS as a causative factor. PMID:17164250 Hsp60 exclusively binds to macrophages and DC but not to T or B lymphocytes |
| GO:0043032 positive regulation of macrophage activation | IDA PMID:17164250 Synergistic and differential modulation of immune responses ... | MARK AS OVER ANNOTATED | Summary: Macrophage activation by recombinant Hsp60 is largely an endotoxin effect. Reason: Macrophage TNF induction by recombinant Hsp60 disappears after endotoxin removal and is not produced by eukaryotically expressed Hsp60 (PMID:15371451). Endotoxin-free Hsp60 does not induce IL-6, IL-12 or TNF in APC (PMID:18256040). The positive macrophage effects in PMID:17164250 depend on Hsp60-bound LPS. Calling HSPD1 itself a positive regulator of macrophage activation therefore overstates the evidence. Supporting Evidence: PMID:15371451 The induction of tumor necrosis factor-alpha secretion in mouse macrophages is lost after endotoxin removal PMID:18256040 LPS-free Hsp60 did not induce IL-6, IL-12 or tumor necrosis factor alpha production in APC PMID:17164250 This effect was Hsp60-specific and dependent on LPS-binding by Hsp60. |
| GO:0043066 negative regulation of apoptotic process | IMP PMID:18086682 Hsp60 regulation of tumor cell apoptosis. | KEEP AS NON CORE | Summary: Hsp60 knockdown destabilises survivin and triggers apoptosis in tumour cells. Reason: Acute Hsp60 ablation in tumour cells destabilises mitochondrial survivin, releases p53 and induces caspase-dependent apoptosis; normal cells tolerate the knockdown. HSPD1 acts here as a chaperone of survival factors. The effect is real but specific to tumour cells and secondary to core folding. Supporting Evidence: PMID:18086682 Acute ablation of Hsp60 by small interfering RNA destabilizes the mitochondrial pool of survivin PMID:18086682 This response involves disruption of an Hsp60-p53 complex |
| GO:0044406 adhesion of symbiont to host | IDA NOT PMID:20633027 Mycobacterium tuberculosis employs Cpn60.2 as an adhesin tha... | KEEP AS NON CORE | Summary: NOT annotation: human Hsp60, unlike mycobacterial Cpn60.2 and GroEL, does not mediate M. tuberculosis adhesion. Reason: In competition assays, mouse and human Hsp60 did not inhibit mycobacterial binding to macrophages, unlike bacterial Cpn60.2/GroEL. The negative result is retained as recorded. It concerns a pathogen-side adhesin activity that HSPD1 does not share. Supporting Evidence: PMID:20633027 is shared by the Escherichia coli homologue, GroEL, but not by the mouse and human Hsp60 homologues |
| GO:0045041 protein import into mitochondrial intermembrane space | IBA GO_REF:0000033 | UNDECIDED | Summary: Contested yeast-derived claim about conservative sorting of cytochrome b2; left unresolved. Reason: The IBA at PTN000143510 is seeded only by yeast HSP60 (SGD:S000004249). The yeast evidence is that matrix Hsp60 holds imported cytochrome b2 unfolded before re-export across the inner membrane (PMID:1347713). Rospert et al. found that a b2-presequence fusion is sorted by stop-transfer and never meets Hsp60 (PMID:7911803). Which route authentic b2 takes was therefore disputed in the source organism. No human experiment addresses it, and the dedicated intermembrane-space import machinery (MIA40/CHCHD4) is unrelated. A focused OpenScientist audit reached the same conclusion. HSPD1 is inside the mitochondrial Hsp60 clade that inherited the node, so the transfer is not phylogenetically wrong; the source biology is contested. Propagation Review Root cause: UNRESOLVED Sources checked: PANTHER:PTN000143510 Β· PTN000143510 UNRESOLVED The yeast HSP60-seeded IBD is confirmed; antifolding/export and stop-transfer source experiments need route-specific comparison and human conservation assessment. Supporting Evidence: PMID:1347713 While in the matrix, the protein interacts with hsp60, which arrests its folding prior to export. PMID:7911803 the cytochrome b2 presequence arrests import through the inner membrane, with the result that the attached passenger protein is never exposed to hsp60. file:human/HSPD1/HSPD1-hypotheses/function-hypothesis-go-0045041/openscientist.md The human annotation to GO:0045041 is **IBA-only** (phylogenetically inferred from a yeast ancestor via GO_Central) |
| GO:0046696 lipopolysaccharide receptor complex | IDA PMID:17164250 Synergistic and differential modulation of immune responses ... | MARK AS OVER ANNOTATED | Summary: Co-localisation with CD14 does not establish membership of the LPS receptor complex. Reason: Hsp60 bound at the APC surface co-localises with CD14 and binds LPS. Hsp60 is an LPS-binding extracellular protein that can deliver LPS, not an established subunit of the CD14/TLR4/MD-2 receptor complex. LPS binding (GO:0001530) captures the supported claim. Supporting Evidence: PMID:17164250 Hsp60 bound to the cell surface of APC colocalizes with the LPS co-receptor CD14 PMID:17164250 Hsp60 specifically binds bacterial LPS |
| GO:0048291 isotype switching to IgG isotypes | IDA PMID:16148103 Heat shock protein 60 activates B cells via the TLR4-MyD88 p... | UNDECIDED | Summary: IgG isotype switching assay not described in the available abstract. Reason: The abstract of PMID:16148103 describes proliferation, IL-6/IL-10 and activation-marker induction but not the isotype-switching experiment, and the B-cell findings of this study are contested (see the B-cell rows). The claim cannot be assessed without the full text. |
| GO:0050821 protein stabilization | IMP PMID:18086682 Hsp60 regulation of tumor cell apoptosis. | KEEP AS NON CORE | Summary: Hsp60 knockdown destabilises survivin and triggers apoptosis in tumour cells. Reason: Acute Hsp60 ablation in tumour cells destabilises mitochondrial survivin, releases p53 and induces caspase-dependent apoptosis; normal cells tolerate the knockdown. HSPD1 acts here as a chaperone of survival factors. The effect is real but specific to tumour cells and secondary to core folding. Supporting Evidence: PMID:18086682 Acute ablation of Hsp60 by small interfering RNA destabilizes the mitochondrial pool of survivin PMID:18086682 This response involves disruption of an Hsp60-p53 complex |
| GO:0050821 protein stabilization | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Protein stabilisation (survivin) transferred by similarity; consistent with the human IMP. Reason: The ISS donor is yeast HSP60 (P19882). Human HSPD1 itself has IMP evidence that it stabilises the mitochondrial pool of survivin (PMID:18086682). The ISS row restates a context-specific chaperone-client effect and is kept as non-core. Supporting Evidence: PMID:18086682 Acute ablation of Hsp60 by small interfering RNA destabilizes the mitochondrial pool of survivin |
| GO:0050870 positive regulation of T cell activation | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Endotoxin-free Hsp60 costimulates T cells through APC. Reason: Low-endotoxin and eukaryotically expressed Hsp60 still enhances antigen-specific T-cell activation (PMID:15371451), independently of TLR4/MyD88 (PMID:18256040). This is the best-supported extracellular immune function of Hsp60. The PMID:16148103 row (B-cell-mediated T-cell enhancement) is weaker, because Hsp60 does not bind B cells and T-cell stimulation by Hsp60 is not B-cell-mediated (PMID:17164250). The term itself holds. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN002900230 Β· PTN002900230 SUPPORTS TRANSFER Vertebrate HSPD1 node seeded by mouse Hspd1 (MGI:96242) and human HSPD1 experimental annotations; the target among its own seeds marks experimental grounding, not circularity. The transferred claim is an extracellular, context-dependent immune effect. Supporting Evidence: PMID:15371451 the Hsp60-mediated enhancement of antigen-specific T cell activation does not correlate with endotoxin contamination PMID:18256040 T cell co-stimulation induced by LPS-free Hsp60 was independent of TLR4 |
| GO:0050870 positive regulation of T cell activation | IDA PMID:16148103 Heat shock protein 60 activates B cells via the TLR4-MyD88 p... | KEEP AS NON CORE | Summary: Endotoxin-free Hsp60 costimulates T cells through APC. Reason: Low-endotoxin and eukaryotically expressed Hsp60 still enhances antigen-specific T-cell activation (PMID:15371451), independently of TLR4/MyD88 (PMID:18256040). This is the best-supported extracellular immune function of Hsp60. The PMID:16148103 row (B-cell-mediated T-cell enhancement) is weaker, because Hsp60 does not bind B cells and T-cell stimulation by Hsp60 is not B-cell-mediated (PMID:17164250). The term itself holds. Supporting Evidence: PMID:15371451 the Hsp60-mediated enhancement of antigen-specific T cell activation does not correlate with endotoxin contamination PMID:18256040 T cell co-stimulation induced by LPS-free Hsp60 was independent of TLR4 |
| GO:0050870 positive regulation of T cell activation | IDA PMID:17164250 Synergistic and differential modulation of immune responses ... | KEEP AS NON CORE | Summary: Endotoxin-free Hsp60 costimulates T cells through APC. Reason: Low-endotoxin and eukaryotically expressed Hsp60 still enhances antigen-specific T-cell activation (PMID:15371451), independently of TLR4/MyD88 (PMID:18256040). This is the best-supported extracellular immune function of Hsp60. The PMID:16148103 row (B-cell-mediated T-cell enhancement) is weaker, because Hsp60 does not bind B cells and T-cell stimulation by Hsp60 is not B-cell-mediated (PMID:17164250). The term itself holds. Supporting Evidence: PMID:15371451 the Hsp60-mediated enhancement of antigen-specific T cell activation does not correlate with endotoxin contamination PMID:18256040 T cell co-stimulation induced by LPS-free Hsp60 was independent of TLR4 |
| GO:0050870 positive regulation of T cell activation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Endotoxin-free Hsp60 costimulates T cells through APC. Reason: Low-endotoxin and eukaryotically expressed Hsp60 still enhances antigen-specific T-cell activation (PMID:15371451), independently of TLR4/MyD88 (PMID:18256040). This is the best-supported extracellular immune function of Hsp60. The PMID:16148103 row (B-cell-mediated T-cell enhancement) is weaker, because Hsp60 does not bind B cells and T-cell stimulation by Hsp60 is not B-cell-mediated (PMID:17164250). The term itself holds. Supporting Evidence: PMID:15371451 the Hsp60-mediated enhancement of antigen-specific T cell activation does not correlate with endotoxin contamination PMID:18256040 T cell co-stimulation induced by LPS-free Hsp60 was independent of TLR4 |
| GO:0050870 positive regulation of T cell activation | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Endotoxin-free Hsp60 costimulates T cells through APC. Reason: Low-endotoxin and eukaryotically expressed Hsp60 still enhances antigen-specific T-cell activation (PMID:15371451), independently of TLR4/MyD88 (PMID:18256040). This is the best-supported extracellular immune function of Hsp60. The PMID:16148103 row (B-cell-mediated T-cell enhancement) is weaker, because Hsp60 does not bind B cells and T-cell stimulation by Hsp60 is not B-cell-mediated (PMID:17164250). The term itself holds. Supporting Evidence: PMID:15371451 the Hsp60-mediated enhancement of antigen-specific T cell activation does not correlate with endotoxin contamination PMID:18256040 T cell co-stimulation induced by LPS-free Hsp60 was independent of TLR4 |
| GO:0051087 protein-folding chaperone binding | IBA GO_REF:0000033 | ACCEPT | Summary: HSPD1 binds its co-chaperonin HSPE1/Hsp10, an obligate part of the folding cycle. Reason: Human Hsp60 works only with Hsp10, and specificity lies in the Hsp10 mobile loop (PMID:11050098). Hsp60 and Hsp10 co-purify as a complex in mitochondria (PMID:10205158). The IBA from PTN000143509 is seeded by yeast HSP60 and HSPD1 itself. Propagation Review Root cause: NO FAILURE CORE Sources checked: PANTHER:PTN000143509 Β· PTN000143509 SUPPORTS TRANSFER Mitochondrial Hsp60 node; co-chaperonin binding is the conserved Hsp60-Hsp10 interaction and HSPD1 has its own experimental support. Supporting Evidence: PMID:11050098 its human homologue, Hsp60 functions specifically with its co-chaperonin partner, Hsp10 PMID:10205158 pro-caspase-3 is present in the mitochondrial fraction of Jurkat T cells in a complex with the chaperone proteins Hsp60 and Hsp10 |
| GO:0051087 protein-folding chaperone binding | IPI PMID:10205158 Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 ... | ACCEPT | Summary: HSPD1 binds its co-chaperonin HSPE1/Hsp10, an obligate part of the folding cycle. Reason: Human Hsp60 works only with Hsp10, and specificity lies in the Hsp10 mobile loop (PMID:11050098). Hsp60 and Hsp10 co-purify as a complex in mitochondria (PMID:10205158). The IBA from PTN000143509 is seeded by yeast HSP60 and HSPD1 itself. Supporting Evidence: PMID:11050098 its human homologue, Hsp60 functions specifically with its co-chaperonin partner, Hsp10 PMID:10205158 pro-caspase-3 is present in the mitochondrial fraction of Jurkat T cells in a complex with the chaperone proteins Hsp60 and Hsp10 |
| GO:0051131 chaperone-mediated protein complex assembly | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Chaperonin-assisted assembly of imported oligomeric proteins is a secondary aspect of folding. Reason: Mitochondrial Hsp60 was first identified as required for the assembly of imported oligomeric matrix proteins, and UniProt describes HSPD1 as implicated in macromolecular assembly. Folding of subunits precedes and enables assembly. The term is as precise as the ISS warrants, but the core activity is folding. Supporting Evidence: file:human/HSPD1/HSPD1-uniprot.txt Chaperonin implicated in mitochondrial protein import and macromolecular assembly. |
| GO:0051604 protein maturation | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Broad process; folding of imported proteins is one step of their maturation. Reason: Hsp60-mediated folding completes the maturation of imported matrix proteins after presequence removal. Protein folding is not an is_a child of protein maturation in GO, so this is kept as a peripheral parallel description rather than replaced. Supporting Evidence: PMID:11422376 Mitochondrial chaperonins are necessary for the folding of newly imported and stress-denatured mitochondrial proteins. |
| GO:0051702 biological process involved in interaction with symbiont | IMP PMID:20507888 LAP, an alcohol acetaldehyde dehydrogenase enzyme in Listeri... | KEEP AS NON CORE | Summary: Hsp60 mediates Listeria adhesion to host cells as the LAP receptor. Reason: Pre-treatment of pathogenic Listeria with Hsp60 reduced adhesion to Caco-2 cells. This supports host Hsp60 as a receptor in this interaction with a symbiont. It is a non-core role. Supporting Evidence: PMID:20507888 interacts with host-cell receptor Hsp60 to promote bacterial adhesion |
| GO:0070062 extracellular exosome | HDA PMID:19056867 Large-scale proteomics and phosphoproteomics of urinary exos... | KEEP AS NON CORE | Summary: Detected in exosome proteomes; a passenger in extracellular vesicles. Reason: HSPD1 recurs in exosome proteomes (urine, B-cell, extravillous trophoblast). This is a reproducible location but carries no evidence of a vesicle-specific function. Kept as non-core. |
| GO:0070062 extracellular exosome | HDA PMID:20458337 MHC class II-associated proteins in B-cell exosomes and pote... | KEEP AS NON CORE | Summary: Detected in exosome proteomes; a passenger in extracellular vesicles. Reason: HSPD1 recurs in exosome proteomes (urine, B-cell, extravillous trophoblast). This is a reproducible location but carries no evidence of a vesicle-specific function. Kept as non-core. |
| GO:0070062 extracellular exosome | IDA PMID:21276792 Morphologic and proteomic characterization of exosomes relea... | KEEP AS NON CORE | Summary: Detected in exosome proteomes; a passenger in extracellular vesicles. Reason: HSPD1 recurs in exosome proteomes (urine, B-cell, extravillous trophoblast). This is a reproducible location but carries no evidence of a vesicle-specific function. Kept as non-core. |
| GO:0097225 sperm midpiece | IMP PMID:32791035 Bi-allelic Loss-of-function Variants in CFAP58 Cause Flagell... | KEEP AS NON CORE | Summary: Hsp60 marks the mitochondrial sheath of the sperm midpiece. Reason: In the CFAP58 study, HSP60 staining was used to visualise the mitochondrial sheath, which is disrupted in mutant sperm. The location is correct because sperm mitochondria are in the midpiece, but it is a cell-type-specific rendering of the mitochondrial location. |
| GO:0140494 migrasome | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Migrasome localisation transferred electronically from orthologs. Reason: The IEA transfers a mouse Hspd1 (P63038) migrasome observation. Like the exosome rows, it records a vesicle location without a demonstrated role, and is kept as non-core. |
| GO:0140608 cysteine-type endopeptidase activator activity | IDA PMID:17823127 Cytosolic accumulation of HSP60 during apoptosis with or wit... | KEEP AS NON CORE | Summary: Hsp60-Hsp10 accelerates pro-caspase-3 activation in vitro and in BMD188-induced death. Reason: Recombinant Hsp60/Hsp10 accelerates cytochrome c/dATP-driven pro-caspase-3 activation in an ATP-dependent manner (PMID:10205158). In BMD188-induced apoptosis the pro-death role of cytosolic HSP60 involves caspase-3 maturation (PMID:17823127). The activator term describes a chaperone action on procaspase-3. It is kept as a non-core, apoptosis-specific function. Supporting Evidence: PMID:10205158 recombinant Hsp60 and Hsp10 accelerated the activation of pro-caspase-3 by cytochrome c and dATP in an ATP-dependent manner PMID:17823127 HSP60 has a pro-death function and that the pro-death role of HSP60 seems to involve caspase-3 maturation and activation in the cytosol |
| GO:0140662 ATP-dependent protein folding chaperone | IDA PMID:1346131 Mammalian mitochondrial chaperonin 60 functions as a single ... | ACCEPT | Summary: Core activity: HSPD1 is the ATP-dependent type I chaperonin of the mitochondrial matrix. Reason: Human HSPD1 is the single mitochondrial type I (GroEL-like) chaperonin. With its HSPE1/Hsp10 co-chaperonin it encloses non-native polypeptides and folds them in an ATP-driven cycle (PMID:1346131, PMID:11422376, PMID:32317635). Disease variants D3G and V72I abolish refolding of malate dehydrogenase and the ATP synthase beta subunit (PMID:31444388). The PAINT node PTN000143677, seeded by E. coli GroEL, M. tuberculosis Cpn60s, yeast HSP60 and HSPD1 itself, places folding at the root of the type I chaperonin family, and HSPD1 is inside that clade (PANTHER PTHR45633:SF17). Supporting Evidence: PMID:1346131 facilitates the formation of catalytically active ribulose-bisphosphate carboxylase from an unfolded state in the presence of K+ and MgATP. PMID:11422376 does not inhibit malate dehydrogenase refolding or ATP hydrolysis by mt-cpn60 in the presence of mt-cpn10 PMID:32317635 Refolding assays demonstrate obligate single- and double-ring mHsp60 variants are active PMID:31444388 unable to fold denatured substrates such as Ξ±-lactalbumin, malate dehydrogenase (MDH), and the Ξ²-subunit of ATP synthase |
| GO:0140662 ATP-dependent protein folding chaperone | IEA GO_REF:0000002 | ACCEPT | Summary: Core activity: HSPD1 is the ATP-dependent type I chaperonin of the mitochondrial matrix. Reason: Human HSPD1 is the single mitochondrial type I (GroEL-like) chaperonin. With its HSPE1/Hsp10 co-chaperonin it encloses non-native polypeptides and folds them in an ATP-driven cycle (PMID:1346131, PMID:11422376, PMID:32317635). Disease variants D3G and V72I abolish refolding of malate dehydrogenase and the ATP synthase beta subunit (PMID:31444388). The PAINT node PTN000143677, seeded by E. coli GroEL, M. tuberculosis Cpn60s, yeast HSP60 and HSPD1 itself, places folding at the root of the type I chaperonin family, and HSPD1 is inside that clade (PANTHER PTHR45633:SF17). Supporting Evidence: PMID:1346131 facilitates the formation of catalytically active ribulose-bisphosphate carboxylase from an unfolded state in the presence of K+ and MgATP. PMID:11422376 does not inhibit malate dehydrogenase refolding or ATP hydrolysis by mt-cpn60 in the presence of mt-cpn10 PMID:32317635 Refolding assays demonstrate obligate single- and double-ring mHsp60 variants are active PMID:31444388 unable to fold denatured substrates such as Ξ±-lactalbumin, malate dehydrogenase (MDH), and the Ξ²-subunit of ATP synthase |
| GO:1900118 negative regulation of execution phase of apoptosis | IMP PMID:17823127 Cytosolic accumulation of HSP60 during apoptosis with or wit... | KEEP AS NON CORE | Summary: Pro-survival role of cytosolic HSP60 in other apoptotic systems. Reason: In apoptosis induced by inducers other than BMD188, HSP60 knockdown promotes death and HSP60 does not associate with active caspase-3. This is the opposite of the BMD188 result, but the contexts differ and both are kept as non-core. Supporting Evidence: PMID:17823127 HSP60 appears to play a pro-survival role in other apoptotic systems |
| GO:1900119 positive regulation of execution phase of apoptosis | IMP PMID:17823127 Cytosolic accumulation of HSP60 during apoptosis with or wit... | KEEP AS NON CORE | Summary: Pro-death role of cytosolic HSP60 in BMD188-induced apoptosis. Reason: siRNA knockdown shows HSP60 promotes caspase-3 maturation and cell death in the BMD188 system. The opposite-direction annotation (GO:1900118) from the same paper reflects a different apoptotic inducer, so both are kept as context-dependent, non-core roles. Supporting Evidence: PMID:17823127 HSP60 has a pro-death function and that the pro-death role of HSP60 seems to involve caspase-3 maturation and activation in the cytosol |
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