HSPD1/Hsp60 is a mitochondrial type I chaperonin that cooperates with HSPE1/Hsp10 to fold imported or stress-unfolded proteins. ATP-dependent conformational cycling of Hsp60 oligomers and the Hsp10 cochaperonin provides a protected folding chamber. Additional cytosolic and cell-surface pools have context-dependent roles in apoptosis and extracellular interactions. Studies using human Hsp60 and endotoxin controls support immune costimulation, including direct LPS binding and LPS-dependent or independent effects on antigen-presenting cells and lymphocyte responses; these activities are distinct contexts of a protein whose principal function is mitochondrial proteostasis.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0001530 lipopolysaccharide binding | IDA PMID:17164250 Synergistic and differential modulation of immune responses ... | KEEP AS NON CORE | Summary: Retain the experimentally supported extracellular immune context. Reason: PMID:17164250 directly reports Hsp60 binding to bacterial LPS and distinguishes LPS-independent IFN-alpha-linked costimulation from LPS-dependent enhancement of IL-12p40 and antigen-specific IFN-gamma. PMID:18256040 further tests endotoxin-free Hsp60. These specific positive assays support a context-dependent immune function; primary mitochondrial localization or hypothetical contamination alone is not a reason to withhold the annotation. Supporting Evidence: PMID:17164250 Hsp60 specifically binds bacterial LPS PMID:17164250 both molecules synergistically enhanced IL-12p40 production in APC and IFNgamma release |
| GO:0001530 lipopolysaccharide binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Retain the experimentally supported extracellular immune context. Reason: PMID:17164250 directly reports Hsp60 binding to bacterial LPS and distinguishes LPS-independent IFN-alpha-linked costimulation from LPS-dependent enhancement of IL-12p40 and antigen-specific IFN-gamma. PMID:18256040 further tests endotoxin-free Hsp60. These specific positive assays support a context-dependent immune function; primary mitochondrial localization or hypothetical contamination alone is not a reason to withhold the annotation. Supporting Evidence: PMID:17164250 Hsp60 specifically binds bacterial LPS PMID:17164250 both molecules synergistically enhanced IL-12p40 production in APC and IFNgamma release |
| GO:0001819 positive regulation of cytokine production | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: Retain the experimentally supported extracellular immune context. Reason: PMID:17164250 directly reports Hsp60 binding to bacterial LPS and distinguishes LPS-independent IFN-alpha-linked costimulation from LPS-dependent enhancement of IL-12p40 and antigen-specific IFN-gamma. PMID:18256040 further tests endotoxin-free Hsp60. These specific positive assays support a context-dependent immune function; primary mitochondrial localization or hypothetical contamination alone is not a reason to withhold the annotation. Supporting Evidence: PMID:17164250 Hsp60 specifically binds bacterial LPS PMID:17164250 both molecules synergistically enhanced IL-12p40 production in APC and IFNgamma release |
| GO:0002039 p53 binding | IPI PMID:18086682 Hsp60 regulation of tumor cell apoptosis. | KEEP AS NON CORE | Summary: Retain the context-dependent cytosolic/apoptotic interaction or effect as non-core. Reason: PMID:18086682 directly identifies Hsp60-associated survivin and an Hsp60-p53 complex in tumor cells. Acute Hsp60 loss destabilizes mitochondrial survivin and promotes p53/Bax-dependent apoptosis. This supports the specific binding, stabilization or survival context as ancillary to mitochondrial folding. Supporting Evidence: PMID:18086682 Hsp60 orchestrates a broad cell survival program centered on stabilization of mitochondrial survivin and restraining of p53 function |
| GO:0002755 MyD88-dependent toll-like receptor signaling pathway | IDA PMID:16148103 Heat shock protein 60 activates B cells via the TLR4-MyD88 p... | KEEP AS NON CORE | Summary: Retain the experimentally supported extracellular immune context. Reason: PMID:16148103 explicitly tests human HSP60 on naive mouse B cells, reports TLR4/MyD88 dependence, proliferation and IL-6/IL-10 production, and states that controls addressed LPS contamination. The responding cells are murine but the tested protein is human. The curated context is retained as non-core; the abstract supports these findings, while detailed control methods remain full-text dependent. 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. |
| 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: Retain the experimentally supported extracellular immune context. Reason: PMID:10663613 directly studies human tumor cells and gamma-delta T cells, shows cell-surface Hsp60, and reports that anti-Hsp60 antibody inhibits tumor-cell lysis. Retain this context-dependent immune recognition effect; it is not an assay of a recombinant preparation and should not inherit a generic endotoxin-contamination objection. Supporting Evidence: PMID:10663613 Anti-hsp60 and anti-hsp70 mAb significantly inhibited the cytotoxicity |
| GO:0003688 DNA replication origin binding | ISS GO_REF:0000024 | UNDECIDED | Summary: Direct yeast nucleoid-binding evidence is traced; conservation in human HSPD1 remains unresolved. Reason: The ISS donor is yeast Hsp60/P19882. QuickGO traces both DNA-binding activities to PMID:10869431, whose crosslinking and gel-shift experiments directly establish single-stranded origin-template binding. This is a real ancillary source function, not evidence inferred merely from chaperoning. Human conservation of the nucleoid-binding mechanism remains unresolved, especially for origin-specific recognition. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:P19882 · 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: Direct yeast nucleoid-binding evidence is traced; conservation in human HSPD1 remains unresolved. Reason: The ISS donor is yeast Hsp60/P19882. QuickGO traces both DNA-binding activities to PMID:10869431, whose crosslinking and gel-shift experiments directly establish single-stranded origin-template binding. This is a real ancillary source function, not evidence inferred merely from chaperoning. Human conservation of the nucleoid-binding mechanism remains unresolved, especially for origin-specific recognition. Propagation Review Root cause: UNRESOLVED Sources checked: UniProtKB:P19882 · 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: Retain the curated human RNA-association result as an ancillary activity. Reason: PMID:22658674 uses covalent UV-crosslinking and biochemical/statistical criteria to define the HeLa mRNA interactome. The HSPD1 HDA row records its inclusion; lack of a named folding-related RNA mechanism does not refute an independently curated RNA-binding observation. This screen does not establish sequence specificity or a core RNA-regulatory role. 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: The precise dsRNA assay needs recovery from the primary dataset. Reason: The accessible main text of PMID:21266579 establishes Raftlin-mediated poly(I:C) uptake but did not expose the HSPD1-specific binding result or supplementary protein list. A primary article focused on Raftlin does not prove that HSPD1 was not assayed. Preserve the curated IDA as unresolved while recovering its table/supplement evidence. |
| GO:0005515 protein binding | IPI PMID:15846844 Proteomic profiling of cellular proteins interacting with th... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:17110338 Hsp90 cochaperone Aha1 downregulation rescues misfolding of ... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:17823127 Cytosolic accumulation of HSP60 during apoptosis with or wit... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:18086682 Hsp60 regulation of tumor cell apoptosis. | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:21516116 Next-generation sequencing to generate interactome datasets. | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:21988832 Toward an understanding of the protein interaction network o... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:22664726 ATAD3B is a human embryonic stem cell specific mitochondrial... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:23349634 A newly uncovered group of distantly related lysine methyltr... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:23840630 Identification of Heat Shock Protein 60 as a Regulator of Ne... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:24286120 GTP binding controls complex formation by the human ROCO pro... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:25416956 A proteome-scale map of the human interactome network. | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:25609649 Proteomic analyses reveal distinct chromatin-associated and ... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:25910212 Widespread macromolecular interaction perturbations in human... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:26618866 ∆F508 CFTR interactome remodelling promotes rescue of cystic... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:26871637 Widespread Expansion of Protein Interaction Capabilities by ... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:29568061 An AP-MS- and BioID-compatible MAC-tag enables comprehensive... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:29568061 An AP-MS- and BioID-compatible MAC-tag enables comprehensive... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:29924966 A Proteomic Variant Approach (ProVarA) for Personalized Medi... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:30021884 Histone Interaction Landscapes Visualized by Crosslinking Ma... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:31515488 Extensive disruption of protein interactions by genetic vari... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:32296183 A reference map of the human binary protein interactome. | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:32814053 Interactome Mapping Provides a Network of Neurodegenerative ... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:35156780 CFTR interactome mapping using the mammalian membrane two-hy... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:36012204 Differential CFTR-Interactome Proximity Labeling Procedures ... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005515 protein binding | IPI PMID:40205054 Multimodal cell maps as a foundation for structural and func... | REMOVE | Summary: The observed interaction is retained as context, but generic protein binding is uninformative. Reason: Remove the generic term under project policy without declaring the curated interaction false. Hsp10 cooperation, ATP-dependent folding and any independently demonstrated partner-specific mechanisms provide the informative functions. |
| GO:0005524 ATP binding | IEA GO_REF:0000002 | ACCEPT | Summary: Conserved nucleotide-binding residues support ATP binding. Reason: The chaperonin fold and nucleotide-binding positions are conserved in the selected horse sequence, even though the internal deletion limits assessment of complete folding-cycle function. ATP binding is a narrower claim than efficient ATP-dependent substrate folding. Supporting Evidence: PMID:1346131 facilitates the formation of catalytically active ribulose-bisphosphate carboxylase from an unfolded state in the presence of K+ and MgATP. |
| GO:0005576 extracellular region | IDA PMID:18229457 Plasma heat shock protein 60 and cardiovascular disease risk... | KEEP AS NON CORE | Summary: Retain the detected secondary cellular compartment or assembly as non-core. Reason: Hsp60 can be detected outside its principal matrix pool, including stress-associated cytosolic, membrane and extracellular fractions. The curated observation is retained without inferring that Hsp60 is a constitutive secreted signal or a structural component of every detected vesicle. Physiological interpretation remains context-dependent. |
| GO:0005737 cytoplasm | IDA PMID:21328542 ZNF703 gene amplification at 8p12 specifies luminal B breast... | KEEP AS NON CORE | Summary: Retain the context-dependent cytosolic/apoptotic interaction or effect as non-core. Reason: The primary apoptosis study demonstrates cytosolic Hsp60 accumulation with either pro-death or pro-survival effects depending on the inducer and caspase-3 interaction. Opposite apoptotic-direction annotations need not conflict when contexts differ. These secondary roles do not replace the matrix folding function. Supporting Evidence: PMID:17823127 the cytosolically accumulated HSP60 possesses either pro-survival or pro-death functions, which involves differential interactions with caspase-3. |
| GO:0005737 cytoplasm | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Retain the context-dependent cytosolic/apoptotic interaction or effect as non-core. Reason: The primary apoptosis study demonstrates cytosolic Hsp60 accumulation with either pro-death or pro-survival effects depending on the inducer and caspase-3 interaction. Opposite apoptotic-direction annotations need not conflict when contexts differ. These secondary roles do not replace the matrix folding function. Supporting Evidence: PMID:17823127 the cytosolically accumulated HSP60 possesses either pro-survival or pro-death functions, which involves differential interactions with caspase-3. |
| GO:0005739 mitochondrion | HTP PMID:34800366 Quantitative high-confidence human mitochondrial proteome an... | ACCEPT | Summary: The mitochondrial matrix is the principal chaperonin compartment. Reason: The mammalian Hsp60/Hsp10 folding system acts in mitochondria. The selected horse sequence retains the N-terminal mitochondrial precursor region, supporting targeting independently of uncertain catalytic consequences of the internal deletion. Supporting Evidence: PMID:25918392 Human mitochondria harbor a single type I chaperonin system |
| GO:0005739 mitochondrion | IDA GO_REF:0000052 | ACCEPT | Summary: The mitochondrial matrix is the principal chaperonin compartment. Reason: The mammalian Hsp60/Hsp10 folding system acts in mitochondria. The selected horse sequence retains the N-terminal mitochondrial precursor region, supporting targeting independently of uncertain catalytic consequences of the internal deletion. Supporting Evidence: 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... | ACCEPT | Summary: The mitochondrial matrix is the principal chaperonin compartment. Reason: The mammalian Hsp60/Hsp10 folding system acts in mitochondria. The selected horse sequence retains the N-terminal mitochondrial precursor region, supporting targeting independently of uncertain catalytic consequences of the internal deletion. Supporting Evidence: PMID:25918392 Human mitochondria harbor a single type I chaperonin system |
| GO:0005739 mitochondrion | IDA PMID:18086682 Hsp60 regulation of tumor cell apoptosis. | ACCEPT | Summary: The mitochondrial matrix is the principal chaperonin compartment. Reason: The mammalian Hsp60/Hsp10 folding system acts in mitochondria. The selected horse sequence retains the N-terminal mitochondrial precursor region, supporting targeting independently of uncertain catalytic consequences of the internal deletion. Supporting Evidence: 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... | ACCEPT | Summary: The mitochondrial matrix is the principal chaperonin compartment. Reason: The mammalian Hsp60/Hsp10 folding system acts in mitochondria. The selected horse sequence retains the N-terminal mitochondrial precursor region, supporting targeting independently of uncertain catalytic consequences of the internal deletion. Supporting Evidence: PMID:25918392 Human mitochondria harbor a single type I chaperonin system |
| GO:0005739 mitochondrion | IEA GO_REF:0000107 | ACCEPT | Summary: The mitochondrial matrix is the principal chaperonin compartment. Reason: The mammalian Hsp60/Hsp10 folding system acts in mitochondria. The selected horse sequence retains the N-terminal mitochondrial precursor region, supporting targeting independently of uncertain catalytic consequences of the internal deletion. Supporting Evidence: 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: Retain mitochondrial inner-membrane association as ancillary to matrix proteostasis. Reason: Retain inner-membrane association as an ancillary location. The PAINT IBD PTN000143509 is seeded by experimental fly, rat and yeast membrane annotations; the separate ISS cites rat P63038. Matrix enrichment does not exclude peripheral membrane association, and this annotation does not assert an integral membrane-spanning chaperonin. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN000143509 · PTN000143509 SUPPORTS TRANSFER The cached IBD has experimental membrane-location sources; principal matrix residence is compatible with an associated membrane pool. Supporting Evidence: PMID:25918392 Human mitochondria harbor a single type I chaperonin system |
| GO:0005743 mitochondrial inner membrane | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Retain mitochondrial inner-membrane association as ancillary to matrix proteostasis. Reason: Retain inner-membrane association as an ancillary location. The PAINT IBD PTN000143509 is seeded by experimental fly, rat and yeast membrane annotations; the separate ISS cites rat P63038. Matrix enrichment does not exclude peripheral membrane association, and this annotation does not assert an integral membrane-spanning chaperonin. Supporting Evidence: PMID:25918392 Human mitochondria harbor a single type I chaperonin system |
| GO:0005759 mitochondrial matrix | IBA GO_REF:0000033 | ACCEPT | Summary: The mitochondrial matrix is the principal chaperonin compartment. Reason: The mammalian Hsp60/Hsp10 folding system acts in mitochondria. The selected horse sequence retains the N-terminal mitochondrial precursor region, supporting targeting independently of uncertain catalytic consequences of the internal deletion. Supporting Evidence: PMID:25918392 Human mitochondria harbor a single type I chaperonin system |
| GO:0005759 mitochondrial matrix | IDA PMID:15784682 Detection of HSP60 on the membrane surface of stressed human... | ACCEPT | Summary: The mitochondrial matrix is the principal chaperonin compartment. Reason: The mammalian Hsp60/Hsp10 folding system acts in mitochondria. The selected horse sequence retains the N-terminal mitochondrial precursor region, supporting targeting independently of uncertain catalytic consequences of the internal deletion. Supporting Evidence: PMID:25918392 Human mitochondria harbor a single type I chaperonin system |
| GO:0005759 mitochondrial matrix | IDA PMID:19393246 Knockdown of human COX17 affects assembly and supramolecular... | ACCEPT | Summary: The mitochondrial matrix is the principal chaperonin compartment. Reason: The mammalian Hsp60/Hsp10 folding system acts in mitochondria. The selected horse sequence retains the N-terminal mitochondrial precursor region, supporting targeting independently of uncertain catalytic consequences of the internal deletion. Supporting Evidence: PMID:25918392 Human mitochondria harbor a single type I chaperonin system |
| GO:0005759 mitochondrial matrix | IDA PMID:24746669 Cyclin B1/Cdk1 coordinates mitochondrial respiration for cel... | ACCEPT | Summary: The mitochondrial matrix is the principal chaperonin compartment. Reason: The mammalian Hsp60/Hsp10 folding system acts in mitochondria. The selected horse sequence retains the N-terminal mitochondrial precursor region, supporting targeting independently of uncertain catalytic consequences of the internal deletion. Supporting Evidence: PMID:25918392 Human mitochondria harbor a single type I chaperonin system |
| GO:0005759 mitochondrial matrix | IDA PMID:7865888 PBP74, a new member of the mammalian 70-kDa heat shock prote... | ACCEPT | Summary: The mitochondrial matrix is the principal chaperonin compartment. Reason: The mammalian Hsp60/Hsp10 folding system acts in mitochondria. The selected horse sequence retains the N-terminal mitochondrial precursor region, supporting targeting independently of uncertain catalytic consequences of the internal deletion. Supporting Evidence: PMID:25918392 Human mitochondria harbor a single type I chaperonin system |
| GO:0005759 mitochondrial matrix | IEA GO_REF:0000044 | ACCEPT | Summary: The mitochondrial matrix is the principal chaperonin compartment. Reason: The mammalian Hsp60/Hsp10 folding system acts in mitochondria. The selected horse sequence retains the N-terminal mitochondrial precursor region, supporting targeting independently of uncertain catalytic consequences of the internal deletion. Supporting Evidence: PMID:25918392 Human mitochondria harbor a single type I chaperonin system |
| GO:0005759 mitochondrial matrix | TAS PMID:17823127 Cytosolic accumulation of HSP60 during apoptosis with or wit... | ACCEPT | Summary: The mitochondrial matrix is the principal chaperonin compartment. Reason: The mammalian Hsp60/Hsp10 folding system acts in mitochondria. The selected horse sequence retains the N-terminal mitochondrial precursor region, supporting targeting independently of uncertain catalytic consequences of the internal deletion. Supporting Evidence: PMID:25918392 Human mitochondria harbor a single type I chaperonin system |
| GO:0005759 mitochondrial matrix | TAS Reactome:R-HSA-8869558 | ACCEPT | Summary: The mitochondrial matrix is the principal chaperonin compartment. Reason: The mammalian Hsp60/Hsp10 folding system acts in mitochondria. The selected horse sequence retains the N-terminal mitochondrial precursor region, supporting targeting independently of uncertain catalytic consequences of the internal deletion. Supporting Evidence: PMID:25918392 Human mitochondria harbor a single type I chaperonin system |
| GO:0005759 mitochondrial matrix | TAS Reactome:R-HSA-9838035 | ACCEPT | Summary: The mitochondrial matrix is the principal chaperonin compartment. Reason: The mammalian Hsp60/Hsp10 folding system acts in mitochondria. The selected horse sequence retains the N-terminal mitochondrial precursor region, supporting targeting independently of uncertain catalytic consequences of the internal deletion. Supporting Evidence: PMID:25918392 Human mitochondria harbor a single type I chaperonin system |
| GO:0005759 mitochondrial matrix | TAS Reactome:R-HSA-9838081 | ACCEPT | Summary: The mitochondrial matrix is the principal chaperonin compartment. Reason: The mammalian Hsp60/Hsp10 folding system acts in mitochondria. The selected horse sequence retains the N-terminal mitochondrial precursor region, supporting targeting independently of uncertain catalytic consequences of the internal deletion. Supporting Evidence: PMID:25918392 Human mitochondria harbor a single type I chaperonin system |
| GO:0005759 mitochondrial matrix | TAS Reactome:R-HSA-9838093 | ACCEPT | Summary: The mitochondrial matrix is the principal chaperonin compartment. Reason: The mammalian Hsp60/Hsp10 folding system acts in mitochondria. The selected horse sequence retains the N-terminal mitochondrial precursor region, supporting targeting independently of uncertain catalytic consequences of the internal deletion. Supporting Evidence: PMID:25918392 Human mitochondria harbor a single type I chaperonin system |
| GO:0005759 mitochondrial matrix | TAS Reactome:R-HSA-9838289 | ACCEPT | Summary: The mitochondrial matrix is the principal chaperonin compartment. Reason: The mammalian Hsp60/Hsp10 folding system acts in mitochondria. The selected horse sequence retains the N-terminal mitochondrial precursor region, supporting targeting independently of uncertain catalytic consequences of the internal deletion. Supporting Evidence: PMID:25918392 Human mitochondria harbor a single type I chaperonin system |
| GO:0005759 mitochondrial matrix | TAS Reactome:R-HSA-9856666 | ACCEPT | Summary: The mitochondrial matrix is the principal chaperonin compartment. Reason: The mammalian Hsp60/Hsp10 folding system acts in mitochondria. The selected horse sequence retains the N-terminal mitochondrial precursor region, supporting targeting independently of uncertain catalytic consequences of the internal deletion. Supporting Evidence: PMID:25918392 Human mitochondria harbor a single type I chaperonin system |
| GO:0005769 early endosome | IDA PMID:11807771 Heat shock proteins 70 and 60 share common receptors which a... | KEEP AS NON CORE | Summary: Retain the detected secondary cellular compartment or assembly as non-core. Reason: Hsp60 can be detected outside its principal matrix pool, including stress-associated cytosolic, membrane and extracellular fractions. The curated observation is retained without inferring that Hsp60 is a constitutive secreted signal or a structural component of every detected vesicle. Physiological interpretation remains context-dependent. |
| GO:0005829 cytosol | IDA PMID:17823127 Cytosolic accumulation of HSP60 during apoptosis with or wit... | KEEP AS NON CORE | Summary: Retain the context-dependent cytosolic/apoptotic interaction or effect as non-core. Reason: The primary apoptosis study demonstrates cytosolic Hsp60 accumulation with either pro-death or pro-survival effects depending on the inducer and caspase-3 interaction. Opposite apoptotic-direction annotations need not conflict when contexts differ. These secondary roles do not replace the matrix folding function. Supporting Evidence: PMID:17823127 the cytosolically accumulated HSP60 possesses either pro-survival or pro-death functions, which involves differential interactions with caspase-3. |
| GO:0005829 cytosol | IDA PMID:18086682 Hsp60 regulation of tumor cell apoptosis. | KEEP AS NON CORE | Summary: Retain the context-dependent cytosolic/apoptotic interaction or effect as non-core. Reason: The primary apoptosis study demonstrates cytosolic Hsp60 accumulation with either pro-death or pro-survival effects depending on the inducer and caspase-3 interaction. Opposite apoptotic-direction annotations need not conflict when contexts differ. These secondary roles do not replace the matrix folding function. Supporting Evidence: PMID:17823127 the cytosolically accumulated HSP60 possesses either pro-survival or pro-death functions, which involves differential interactions with caspase-3. |
| GO:0005886 plasma membrane | IDA PMID:11027668 Heat shock protein 60 is a high-affinity high-density lipopr... | KEEP AS NON CORE | Summary: Retain the detected secondary cellular compartment or assembly as non-core. Reason: Hsp60 can be detected outside its principal matrix pool, including stress-associated cytosolic, membrane and extracellular fractions. The curated observation is retained without inferring that Hsp60 is a constitutive secreted signal or a structural component of every detected vesicle. Physiological interpretation remains context-dependent. |
| GO:0005886 plasma membrane | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Retain the detected secondary cellular compartment or assembly as non-core. Reason: Hsp60 can be detected outside its principal matrix pool, including stress-associated cytosolic, membrane and extracellular fractions. The curated observation is retained without inferring that Hsp60 is a constitutive secreted signal or a structural component of every detected vesicle. Physiological interpretation remains context-dependent. |
| GO:0005905 clathrin-coated pit | IDA PMID:11807771 Heat shock proteins 70 and 60 share common receptors which a... | KEEP AS NON CORE | Summary: Retain the detected secondary cellular compartment or assembly as non-core. Reason: Hsp60 can be detected outside its principal matrix pool, including stress-associated cytosolic, membrane and extracellular fractions. The curated observation is retained without inferring that Hsp60 is a constitutive secreted signal or a structural component of every detected vesicle. Physiological interpretation remains context-dependent. |
| GO:0006457 protein folding | IBA GO_REF:0000033 | ACCEPT | Summary: Hsp60/Hsp10 ATP-dependent folding is established for the intact mammalian chaperonin. Reason: Purified mammalian Hsp60 with Hsp10 restores activity to unfolded substrate in an ATP-dependent reaction. This establishes folding/refolding, ATP-driven chaperoning and partner-assisted assembly. For the selected horse model, deletion of human 171–202 requires assessment of the apical-domain transition and oligomeric cycle before transferring full functional competence; conservation alone does not resolve that deletion. Supporting Evidence: PMID:1346131 facilitates the formation of catalytically active ribulose-bisphosphate carboxylase from an unfolded state in the presence of K+ and MgATP. |
| GO:0006457 protein folding | IEA GO_REF:0000002 | ACCEPT | Summary: Hsp60/Hsp10 ATP-dependent folding is established for the intact mammalian chaperonin. Reason: Purified mammalian Hsp60 with Hsp10 restores activity to unfolded substrate in an ATP-dependent reaction. This establishes folding/refolding, ATP-driven chaperoning and partner-assisted assembly. For the selected horse model, deletion of human 171–202 requires assessment of the apical-domain transition and oligomeric cycle before transferring full functional competence; conservation alone does not resolve that deletion. Supporting Evidence: PMID:1346131 facilitates the formation of catalytically active ribulose-bisphosphate carboxylase from an unfolded state in the presence of K+ and MgATP. |
| GO:0006458 'de novo' protein folding | ISS GO_REF:0000024 | ACCEPT | Summary: Hsp60/Hsp10 ATP-dependent folding is established for the intact mammalian chaperonin. Reason: Purified mammalian Hsp60 with Hsp10 restores activity to unfolded substrate in an ATP-dependent reaction. This establishes folding/refolding, ATP-driven chaperoning and partner-assisted assembly. For the selected horse model, deletion of human 171–202 requires assessment of the apical-domain transition and oligomeric cycle before transferring full functional competence; conservation alone does not resolve that deletion. Supporting Evidence: PMID:1346131 facilitates the formation of catalytically active ribulose-bisphosphate carboxylase from an unfolded state in the presence of K+ and MgATP. |
| GO:0006986 response to unfolded protein | IDA PMID:11050098 The importance of a mobile loop in regulating chaperonin/ co... | ACCEPT | Summary: Hsp60 participates in mitochondrial protein-folding stress responses. Reason: Its chaperonin activity restores folding of nonnative proteins and supports mitochondrial proteostasis. The stress-response term is mechanistically grounded, while HSPD1 is not itself the transcriptional sensor of every unfolded-protein-response pathway. Supporting Evidence: PMID:1346131 facilitates the formation of catalytically active ribulose-bisphosphate carboxylase from an unfolded state in the presence of K+ and MgATP. |
| 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: Retain the source-specific interaction or host-associated effect as non-core. Reason: The curated source PMID:11027668 reports this ancillary interaction or biological context. It is not sufficient to replace ATP-dependent folding as the core function, and no generalized ligand/receptor or symbiont function is inferred beyond the reported observation. |
| GO:0008637 apoptotic mitochondrial changes | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Retain the context-dependent cytosolic/apoptotic interaction or effect as non-core. Reason: The primary apoptosis study demonstrates cytosolic Hsp60 accumulation with either pro-death or pro-survival effects depending on the inducer and caspase-3 interaction. Opposite apoptotic-direction annotations need not conflict when contexts differ. These secondary roles do not replace the matrix folding function. Supporting Evidence: PMID:17823127 the cytosolically accumulated HSP60 possesses either pro-survival or pro-death functions, which involves differential interactions with caspase-3. |
| GO:0009409 response to cold | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Retain the cold-response transfer from its resolved vertebrate experiment. Reason: The ISS donor Q5ZL72 is chicken HSPD1. PMID:23636703 reports increased Hsp60 expression during acute/chronic cold stress in chicken hearts. This is a conserved stress-response context, not a claim of a unique human or horse cold-sensing mechanism. The previous reference to unexamined horse experiments was irrelevant to the human annotation. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: UniProtKB:Q5ZL72 · HSPD1, Gallus gallus SUPPORTS TRANSFER QuickGO resolves the source IDA to PMID:23636703, a chicken heart cold-stress study; the broad vertebrate response is compatible with conserved Hsp60 proteostasis. Supporting Evidence: PMID:23636703 the mRNA levels of Hsps (70, 60, 40, and 27) increased significantly |
| GO:0009986 cell surface | IDA PMID:10663613 gammadelta T cells lyse autologous and allogenic oesophageal... | KEEP AS NON CORE | Summary: Retain the detected secondary cellular compartment or assembly as non-core. Reason: Hsp60 can be detected outside its principal matrix pool, including stress-associated cytosolic, membrane and extracellular fractions. The curated observation is retained without inferring that Hsp60 is a constitutive secreted signal or a structural component of every detected vesicle. Physiological interpretation remains context-dependent. |
| GO:0009986 cell surface | IDA PMID:11807771 Heat shock proteins 70 and 60 share common receptors which a... | KEEP AS NON CORE | Summary: Retain the detected secondary cellular compartment or assembly as non-core. Reason: Hsp60 can be detected outside its principal matrix pool, including stress-associated cytosolic, membrane and extracellular fractions. The curated observation is retained without inferring that Hsp60 is a constitutive secreted signal or a structural component of every detected vesicle. Physiological interpretation remains context-dependent. |
| GO:0009986 cell surface | IDA PMID:15784682 Detection of HSP60 on the membrane surface of stressed human... | KEEP AS NON CORE | Summary: Retain the detected secondary cellular compartment or assembly as non-core. Reason: Hsp60 can be detected outside its principal matrix pool, including stress-associated cytosolic, membrane and extracellular fractions. The curated observation is retained without inferring that Hsp60 is a constitutive secreted signal or a structural component of every detected vesicle. Physiological interpretation remains context-dependent. |
| GO:0009986 cell surface | IDA PMID:9243807 Cell surface localization of the 60 kDa heat shock chaperoni... | KEEP AS NON CORE | Summary: Retain the detected secondary cellular compartment or assembly as non-core. Reason: Hsp60 can be detected outside its principal matrix pool, including stress-associated cytosolic, membrane and extracellular fractions. The curated observation is retained without inferring that Hsp60 is a constitutive secreted signal or a structural component of every detected vesicle. Physiological interpretation remains context-dependent. |
| GO:0016020 membrane | HDA PMID:19946888 Defining the membrane proteome of NK cells. | KEEP AS NON CORE | Summary: Retain the detected secondary cellular compartment or assembly as non-core. Reason: Hsp60 can be detected outside its principal matrix pool, including stress-associated cytosolic, membrane and extracellular fractions. The curated observation is retained without inferring that Hsp60 is a constitutive secreted signal or a structural component of every detected vesicle. Physiological interpretation remains context-dependent. |
| GO:0016020 membrane | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Retain the detected secondary cellular compartment or assembly as non-core. Reason: Hsp60 can be detected outside its principal matrix pool, including stress-associated cytosolic, membrane and extracellular fractions. The curated observation is retained without inferring that Hsp60 is a constitutive secreted signal or a structural component of every detected vesicle. Physiological interpretation remains context-dependent. |
| GO:0016887 ATP hydrolysis activity | ISS GO_REF:0000024 | ACCEPT | Summary: Hsp60/Hsp10 ATP-dependent folding is established for the intact mammalian chaperonin. Reason: Purified mammalian Hsp60 with Hsp10 restores activity to unfolded substrate in an ATP-dependent reaction. This establishes folding/refolding, ATP-driven chaperoning and partner-assisted assembly. For the selected horse model, deletion of human 171–202 requires assessment of the apical-domain transition and oligomeric cycle before transferring full functional competence; conservation alone does not resolve that deletion. Supporting Evidence: PMID:1346131 facilitates the formation of catalytically active ribulose-bisphosphate carboxylase from an unfolded state in the presence of K+ and MgATP. |
| GO:0019899 enzyme binding | IPI PMID:20507888 LAP, an alcohol acetaldehyde dehydrogenase enzyme in Listeri... | KEEP AS NON CORE | Summary: Retain the source-specific interaction or host-associated effect as non-core. Reason: The curated source PMID:20507888 reports this ancillary interaction or biological context. It is not sufficient to replace ATP-dependent folding as the core function, and no generalized ligand/receptor or symbiont function is inferred beyond the reported observation. |
| GO:0019899 enzyme binding | IPI PMID:20507888 LAP, an alcohol acetaldehyde dehydrogenase enzyme in Listeri... | KEEP AS NON CORE | Summary: Retain the source-specific interaction or host-associated effect as non-core. Reason: The curated source PMID:20507888 reports this ancillary interaction or biological context. It is not sufficient to replace ATP-dependent folding as the core function, and no generalized ligand/receptor or symbiont function is inferred beyond the reported observation. |
| GO:0019899 enzyme binding | IPI PMID:20507888 LAP, an alcohol acetaldehyde dehydrogenase enzyme in Listeri... | KEEP AS NON CORE | Summary: Retain the source-specific interaction or host-associated effect as non-core. Reason: The curated source PMID:20507888 reports this ancillary interaction or biological context. It is not sufficient to replace ATP-dependent folding as the core function, and no generalized ligand/receptor or symbiont function is inferred beyond the reported observation. |
| GO:0019899 enzyme binding | IPI PMID:20507888 LAP, an alcohol acetaldehyde dehydrogenase enzyme in Listeri... | KEEP AS NON CORE | Summary: Retain the source-specific interaction or host-associated effect as non-core. Reason: The curated source PMID:20507888 reports this ancillary interaction or biological context. It is not sufficient to replace ATP-dependent folding as the core function, and no generalized ligand/receptor or symbiont function is inferred beyond the reported observation. |
| GO:0030135 coated vesicle | IDA PMID:11807771 Heat shock proteins 70 and 60 share common receptors which a... | KEEP AS NON CORE | Summary: Retain the detected secondary cellular compartment or assembly as non-core. Reason: Hsp60 can be detected outside its principal matrix pool, including stress-associated cytosolic, membrane and extracellular fractions. The curated observation is retained without inferring that Hsp60 is a constitutive secreted signal or a structural component of every detected vesicle. Physiological interpretation remains context-dependent. |
| GO:0030141 secretory granule | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Retain the detected secondary cellular compartment or assembly as non-core. Reason: Hsp60 can be detected outside its principal matrix pool, including stress-associated cytosolic, membrane and extracellular fractions. The curated observation is retained without inferring that Hsp60 is a constitutive secreted signal or a structural component of every detected vesicle. Physiological interpretation remains context-dependent. |
| GO:0030141 secretory granule | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Retain the detected secondary cellular compartment or assembly as non-core. Reason: Hsp60 can be detected outside its principal matrix pool, including stress-associated cytosolic, membrane and extracellular fractions. The curated observation is retained without inferring that Hsp60 is a constitutive secreted signal or a structural component of every detected vesicle. Physiological interpretation remains context-dependent. |
| GO:0031625 ubiquitin protein ligase binding | IPI PMID:19725078 Proteomic analysis of increased Parkin expression and its in... | KEEP AS NON CORE | Summary: Retain the source-specific interaction or host-associated effect as non-core. Reason: The curated source PMID:19725078 reports this ancillary interaction or biological context. It is not sufficient to replace ATP-dependent folding as the core function, and no generalized ligand/receptor or symbiont function is inferred beyond the reported observation. |
| GO:0031625 ubiquitin protein ligase binding | IPI PMID:21753002 Parkin interacts with Ambra1 to induce mitophagy. | KEEP AS NON CORE | Summary: Retain the source-specific interaction or host-associated effect as non-core. Reason: The curated source PMID:21753002 reports this ancillary interaction or biological context. It is not sufficient to replace ATP-dependent folding as the core function, and no generalized ligand/receptor or symbiont function is inferred beyond the reported observation. |
| GO:0032727 positive regulation of interferon-alpha production | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Retain the experimentally supported extracellular immune context. Reason: PMID:17164250 directly reports Hsp60 binding to bacterial LPS and distinguishes LPS-independent IFN-alpha-linked costimulation from LPS-dependent enhancement of IL-12p40 and antigen-specific IFN-gamma. PMID:18256040 further tests endotoxin-free Hsp60. These specific positive assays support a context-dependent immune function; primary mitochondrial localization or hypothetical contamination alone is not a reason to withhold the annotation. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN002900230 · PTN002900230 SUPPORTS TRANSFER The vertebrate IBD includes human HSPD1 itself among experimentally supported descendants; that is target experimental grounding, not circularity. Preparation-specific studies distinguish LPS-associated and LPS-free effects. Supporting Evidence: PMID:17164250 Hsp60 specifically binds bacterial LPS PMID:17164250 both molecules synergistically enhanced IL-12p40 production in APC and IFNgamma release |
| GO:0032727 positive regulation of interferon-alpha production | IDA PMID:17164250 Synergistic and differential modulation of immune responses ... | KEEP AS NON CORE | Summary: Retain the experimentally supported extracellular immune context. Reason: PMID:17164250 directly reports Hsp60 binding to bacterial LPS and distinguishes LPS-independent IFN-alpha-linked costimulation from LPS-dependent enhancement of IL-12p40 and antigen-specific IFN-gamma. PMID:18256040 further tests endotoxin-free Hsp60. These specific positive assays support a context-dependent immune function; primary mitochondrial localization or hypothetical contamination alone is not a reason to withhold the annotation. Supporting Evidence: PMID:17164250 Hsp60 specifically binds bacterial LPS PMID:17164250 both molecules synergistically enhanced IL-12p40 production in APC and IFNgamma release |
| GO:0032729 positive regulation of type II interferon production | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Retain the experimentally supported extracellular immune context. Reason: PMID:17164250 directly reports Hsp60 binding to bacterial LPS and distinguishes LPS-independent IFN-alpha-linked costimulation from LPS-dependent enhancement of IL-12p40 and antigen-specific IFN-gamma. PMID:18256040 further tests endotoxin-free Hsp60. These specific positive assays support a context-dependent immune function; primary mitochondrial localization or hypothetical contamination alone is not a reason to withhold the annotation. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN002900230 · PTN002900230 SUPPORTS TRANSFER The vertebrate IBD includes human HSPD1 itself among experimentally supported descendants; that is target experimental grounding, not circularity. Preparation-specific studies distinguish LPS-associated and LPS-free effects. Supporting Evidence: PMID:17164250 Hsp60 specifically binds bacterial LPS PMID:17164250 both molecules synergistically enhanced IL-12p40 production in APC and IFNgamma release |
| GO:0032729 positive regulation of type II interferon production | IDA PMID:17164250 Synergistic and differential modulation of immune responses ... | KEEP AS NON CORE | Summary: Retain the experimentally supported extracellular immune context. Reason: PMID:17164250 directly reports Hsp60 binding to bacterial LPS and distinguishes LPS-independent IFN-alpha-linked costimulation from LPS-dependent enhancement of IL-12p40 and antigen-specific IFN-gamma. PMID:18256040 further tests endotoxin-free Hsp60. These specific positive assays support a context-dependent immune function; primary mitochondrial localization or hypothetical contamination alone is not a reason to withhold the annotation. Supporting Evidence: PMID:17164250 Hsp60 specifically binds bacterial LPS PMID:17164250 both molecules synergistically enhanced IL-12p40 production in APC and IFNgamma release |
| GO:0032729 positive regulation of type II interferon production | IDA PMID:17164250 Synergistic and differential modulation of immune responses ... | KEEP AS NON CORE | Summary: Retain the experimentally supported extracellular immune context. Reason: PMID:17164250 directly reports Hsp60 binding to bacterial LPS and distinguishes LPS-independent IFN-alpha-linked costimulation from LPS-dependent enhancement of IL-12p40 and antigen-specific IFN-gamma. PMID:18256040 further tests endotoxin-free Hsp60. These specific positive assays support a context-dependent immune function; primary mitochondrial localization or hypothetical contamination alone is not a reason to withhold the annotation. Supporting Evidence: PMID:17164250 Hsp60 specifically binds bacterial LPS PMID:17164250 both molecules synergistically enhanced IL-12p40 production in APC and IFNgamma release |
| GO:0032729 positive regulation of type II interferon production | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Retain the experimentally supported extracellular immune context. Reason: PMID:17164250 directly reports Hsp60 binding to bacterial LPS and distinguishes LPS-independent IFN-alpha-linked costimulation from LPS-dependent enhancement of IL-12p40 and antigen-specific IFN-gamma. PMID:18256040 further tests endotoxin-free Hsp60. These specific positive assays support a context-dependent immune function; primary mitochondrial localization or hypothetical contamination alone is not a reason to withhold the annotation. Supporting Evidence: PMID:17164250 Hsp60 specifically binds bacterial LPS PMID:17164250 both molecules synergistically enhanced IL-12p40 production in APC and IFNgamma release |
| GO:0032729 positive regulation of type II interferon production | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Retain the experimentally supported extracellular immune context. Reason: PMID:17164250 directly reports Hsp60 binding to bacterial LPS and distinguishes LPS-independent IFN-alpha-linked costimulation from LPS-dependent enhancement of IL-12p40 and antigen-specific IFN-gamma. PMID:18256040 further tests endotoxin-free Hsp60. These specific positive assays support a context-dependent immune function; primary mitochondrial localization or hypothetical contamination alone is not a reason to withhold the annotation. Supporting Evidence: PMID:17164250 Hsp60 specifically binds bacterial LPS PMID:17164250 both molecules synergistically enhanced IL-12p40 production in APC and IFNgamma release |
| GO:0032733 positive regulation of interleukin-10 production | IDA PMID:16148103 Heat shock protein 60 activates B cells via the TLR4-MyD88 p... | KEEP AS NON CORE | Summary: Retain the experimentally supported extracellular immune context. Reason: PMID:16148103 explicitly tests human HSP60 on naive mouse B cells, reports TLR4/MyD88 dependence, proliferation and IL-6/IL-10 production, and states that controls addressed LPS contamination. The responding cells are murine but the tested protein is human. The curated context is retained as non-core; the abstract supports these findings, while detailed control methods remain full-text dependent. 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. |
| GO:0032735 positive regulation of interleukin-12 production | IDA PMID:17164250 Synergistic and differential modulation of immune responses ... | KEEP AS NON CORE | Summary: Retain the experimentally supported extracellular immune context. Reason: PMID:17164250 directly reports Hsp60 binding to bacterial LPS and distinguishes LPS-independent IFN-alpha-linked costimulation from LPS-dependent enhancement of IL-12p40 and antigen-specific IFN-gamma. PMID:18256040 further tests endotoxin-free Hsp60. These specific positive assays support a context-dependent immune function; primary mitochondrial localization or hypothetical contamination alone is not a reason to withhold the annotation. Supporting Evidence: PMID:17164250 Hsp60 specifically binds bacterial LPS PMID:17164250 both molecules synergistically enhanced IL-12p40 production in APC and IFNgamma release |
| GO:0032755 positive regulation of interleukin-6 production | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Retain the experimentally supported extracellular immune context. Reason: PMID:16148103 explicitly tests human HSP60 on naive mouse B cells, reports TLR4/MyD88 dependence, proliferation and IL-6/IL-10 production, and states that controls addressed LPS contamination. The responding cells are murine but the tested protein is human. The curated context is retained as non-core; the abstract supports these findings, while detailed control methods remain full-text dependent. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN002900230 · PTN002900230 SUPPORTS TRANSFER The vertebrate IBD includes human HSPD1 itself among experimentally supported descendants; that is target experimental grounding, not circularity. Preparation-specific studies distinguish LPS-associated and LPS-free effects. 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. |
| GO:0032755 positive regulation of interleukin-6 production | IDA PMID:16148103 Heat shock protein 60 activates B cells via the TLR4-MyD88 p... | KEEP AS NON CORE | Summary: Retain the experimentally supported extracellular immune context. Reason: PMID:16148103 explicitly tests human HSP60 on naive mouse B cells, reports TLR4/MyD88 dependence, proliferation and IL-6/IL-10 production, and states that controls addressed LPS contamination. The responding cells are murine but the tested protein is human. The curated context is retained as non-core; the abstract supports these findings, while detailed control methods remain full-text dependent. 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. |
| GO:0032991 protein-containing complex | IDA PMID:21328542 ZNF703 gene amplification at 8p12 specifies luminal B breast... | KEEP AS NON CORE | Summary: Retain the detected secondary cellular compartment or assembly as non-core. Reason: Hsp60 can be detected outside its principal matrix pool, including stress-associated cytosolic, membrane and extracellular fractions. The curated observation is retained without inferring that Hsp60 is a constitutive secreted signal or a structural component of every detected vesicle. Physiological interpretation remains context-dependent. |
| GO:0032991 protein-containing complex | IDA PMID:23349634 A newly uncovered group of distantly related lysine methyltr... | KEEP AS NON CORE | Summary: Retain the detected secondary cellular compartment or assembly as non-core. Reason: Hsp60 can be detected outside its principal matrix pool, including stress-associated cytosolic, membrane and extracellular fractions. The curated observation is retained without inferring that Hsp60 is a constitutive secreted signal or a structural component of every detected vesicle. Physiological interpretation remains context-dependent. |
| GO:0034185 apolipoprotein binding | IPI PMID:11027668 Heat shock protein 60 is a high-affinity high-density lipopr... | KEEP AS NON CORE | Summary: Retain the source-specific interaction or host-associated effect as non-core. Reason: The curated source PMID:11027668 reports this ancillary interaction or biological context. It is not sufficient to replace ATP-dependent folding as the core function, and no generalized ligand/receptor or symbiont function is inferred beyond the reported observation. |
| 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: Retain the source-specific interaction or host-associated effect as non-core. Reason: The curated source PMID:11027668 reports this ancillary interaction or biological context. It is not sufficient to replace ATP-dependent folding as the core function, and no generalized ligand/receptor or symbiont function is inferred beyond the reported observation. |
| GO:0034514 mitochondrial unfolded protein response | IBA GO_REF:0000033 | ACCEPT | Summary: Hsp60 participates in mitochondrial protein-folding stress responses. Reason: Its chaperonin activity restores folding of nonnative proteins and supports mitochondrial proteostasis. The stress-response term is mechanistically grounded, while HSPD1 is not itself the transcriptional sensor of every unfolded-protein-response pathway. Supporting Evidence: PMID:1346131 facilitates the formation of catalytically active ribulose-bisphosphate carboxylase from an unfolded state in the presence of K+ and MgATP. |
| GO:0042026 protein refolding | IDA PMID:11050098 The importance of a mobile loop in regulating chaperonin/ co... | ACCEPT | Summary: Hsp60/Hsp10 ATP-dependent folding is established for the intact mammalian chaperonin. Reason: Purified mammalian Hsp60 with Hsp10 restores activity to unfolded substrate in an ATP-dependent reaction. This establishes folding/refolding, ATP-driven chaperoning and partner-assisted assembly. For the selected horse model, deletion of human 171–202 requires assessment of the apical-domain transition and oligomeric cycle before transferring full functional competence; conservation alone does not resolve that deletion. Supporting Evidence: PMID:1346131 facilitates the formation of catalytically active ribulose-bisphosphate carboxylase from an unfolded state in the presence of K+ and MgATP. |
| GO:0042026 protein refolding | IEA GO_REF:0000002 | ACCEPT | Summary: Hsp60/Hsp10 ATP-dependent folding is established for the intact mammalian chaperonin. Reason: Purified mammalian Hsp60 with Hsp10 restores activity to unfolded substrate in an ATP-dependent reaction. This establishes folding/refolding, ATP-driven chaperoning and partner-assisted assembly. For the selected horse model, deletion of human 171–202 requires assessment of the apical-domain transition and oligomeric cycle before transferring full functional competence; conservation alone does not resolve that deletion. Supporting Evidence: PMID:1346131 facilitates the formation of catalytically active ribulose-bisphosphate carboxylase from an unfolded state in the presence of K+ and MgATP. |
| GO:0042100 B cell proliferation | IDA PMID:16148103 Heat shock protein 60 activates B cells via the TLR4-MyD88 p... | KEEP AS NON CORE | Summary: Retain the experimentally supported extracellular immune context. Reason: PMID:16148103 explicitly tests human HSP60 on naive mouse B cells, reports TLR4/MyD88 dependence, proliferation and IL-6/IL-10 production, and states that controls addressed LPS contamination. The responding cells are murine but the tested protein is human. The curated context is retained as non-core; the abstract supports these findings, while detailed control methods remain full-text dependent. 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. |
| GO:0042110 T cell activation | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Retain the experimentally supported extracellular immune context. Reason: PMID:15371451 compares low-endotoxin recombinant human Hsp60 with Hsp60 expressed in eukaryotic cells. It separates endotoxin-dependent macrophage TNF induction from retained antigen-specific T-cell costimulation. This direct experimental distinction supports the T-cell annotation and contradicts leaving it unresolved solely because contamination is hypothetically possible. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN002900230 · PTN002900230 SUPPORTS TRANSFER The vertebrate IBD includes human HSPD1 itself among experimentally supported descendants; that is target experimental grounding, not circularity. Preparation-specific studies distinguish LPS-associated and LPS-free effects. Supporting Evidence: PMID:15371451 the Hsp60-mediated enhancement of antigen-specific T cell activation does not correlate with endotoxin contamination. |
| GO:0042110 T cell activation | IDA PMID:15371451 Lipopolysaccharide-free heat shock protein 60 activates T ce... | KEEP AS NON CORE | Summary: Retain the experimentally supported extracellular immune context. Reason: PMID:15371451 compares low-endotoxin recombinant human Hsp60 with Hsp60 expressed in eukaryotic cells. It separates endotoxin-dependent macrophage TNF induction from retained antigen-specific T-cell costimulation. This direct experimental distinction supports the T-cell annotation and contradicts leaving it unresolved solely because contamination is hypothetically possible. Supporting Evidence: PMID:15371451 the Hsp60-mediated enhancement of antigen-specific T cell activation does not correlate with endotoxin contamination. |
| GO:0042110 T cell activation | IDA PMID:17164250 Synergistic and differential modulation of immune responses ... | KEEP AS NON CORE | Summary: Retain the experimentally supported extracellular immune context. Reason: PMID:17164250 directly reports Hsp60 binding to bacterial LPS and distinguishes LPS-independent IFN-alpha-linked costimulation from LPS-dependent enhancement of IL-12p40 and antigen-specific IFN-gamma. PMID:18256040 further tests endotoxin-free Hsp60. These specific positive assays support a context-dependent immune function; primary mitochondrial localization or hypothetical contamination alone is not a reason to withhold the annotation. Supporting Evidence: PMID:17164250 Hsp60 specifically binds bacterial LPS PMID:17164250 both molecules synergistically enhanced IL-12p40 production in APC and IFNgamma release |
| GO:0042110 T cell activation | IDA PMID:18256040 Hsp60-mediated T cell stimulation is independent of TLR4 and... | KEEP AS NON CORE | Summary: Retain the experimentally supported extracellular immune context. Reason: PMID:18256040 explicitly examines endotoxin-free Hsp60 and reports IFN-alpha-linked T-cell costimulation independent of TLR4/MyD88 and IL-12. Retain the specific costimulatory effect as non-core, distinguishing it from the LPS-associated signaling route rather than treating the two as interchangeable. Supporting Evidence: PMID:18256040 LPS-free Hsp60 enhances IFN alpha expression in APC |
| GO:0042113 B cell activation | IDA PMID:16148103 Heat shock protein 60 activates B cells via the TLR4-MyD88 p... | KEEP AS NON CORE | Summary: Retain the experimentally supported extracellular immune context. Reason: PMID:16148103 explicitly tests human HSP60 on naive mouse B cells, reports TLR4/MyD88 dependence, proliferation and IL-6/IL-10 production, and states that controls addressed LPS contamination. The responding cells are murine but the tested protein is human. The curated context is retained as non-core; the abstract supports these findings, while detailed control methods remain full-text dependent. 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. |
| GO:0043032 positive regulation of macrophage activation | IDA PMID:17164250 Synergistic and differential modulation of immune responses ... | KEEP AS NON CORE | Summary: Retain the experimentally supported extracellular immune context. Reason: PMID:17164250 directly reports Hsp60 binding to bacterial LPS and distinguishes LPS-independent IFN-alpha-linked costimulation from LPS-dependent enhancement of IL-12p40 and antigen-specific IFN-gamma. PMID:18256040 further tests endotoxin-free Hsp60. These specific positive assays support a context-dependent immune function; primary mitochondrial localization or hypothetical contamination alone is not a reason to withhold the annotation. Supporting Evidence: PMID:17164250 Hsp60 specifically binds bacterial LPS PMID:17164250 both molecules synergistically enhanced IL-12p40 production in APC and IFNgamma release |
| GO:0043066 negative regulation of apoptotic process | IMP PMID:18086682 Hsp60 regulation of tumor cell apoptosis. | KEEP AS NON CORE | Summary: Retain the context-dependent cytosolic/apoptotic interaction or effect as non-core. Reason: PMID:18086682 directly identifies Hsp60-associated survivin and an Hsp60-p53 complex in tumor cells. Acute Hsp60 loss destabilizes mitochondrial survivin and promotes p53/Bax-dependent apoptosis. This supports the specific binding, stabilization or survival context as ancillary to mitochondrial folding. Supporting Evidence: PMID:18086682 Hsp60 orchestrates a broad cell survival program centered on stabilization of mitochondrial survivin and restraining of p53 function |
| 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: Retain the source-specific interaction or host-associated effect as non-core. Reason: The curated source PMID:20633027 reports this ancillary interaction or biological context. It is not sufficient to replace ATP-dependent folding as the core function, and no generalized ligand/receptor or symbiont function is inferred beyond the reported observation. |
| GO:0045041 protein import into mitochondrial intermembrane space | IBA GO_REF:0000033 | UNDECIDED | Summary: Conflicting source experiments leave the intermembrane-space import inference unresolved. Reason: The cached PAINT IBD at PTN000143510 is seeded by yeast HSP60/SGD:S000004249. PMID:1347713 proposes that matrix Hsp60 holds cytochrome b2 unfolded for export to the intermembrane space, whereas PMID:7911803 finds cytochrome-b2-presequence fusion proteins sorted by stop transfer without Hsp60 exposure. These substrate/route-specific results require adjudication and human conservation evidence. Neither matrix localization nor a single yeast source settles the claim. A neutral focused OpenScientist report is queued. Propagation Review Root cause: UNRESOLVED Sources checked: PANTHER:PTN000143510 · 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 the protein interacts with hsp60, which arrests its folding prior to export. PMID:7911803 the attached passenger protein is never exposed to hsp60. |
| GO:0046696 lipopolysaccharide receptor complex | IDA PMID:17164250 Synergistic and differential modulation of immune responses ... | UNDECIDED | Summary: LPS binding and receptor colocalization do not alone resolve stable receptor-complex membership. Reason: PMID:17164250 supports direct LPS binding, APC-surface association and colocalization with CD14. Those observations resolve the binding/immune-activity rows but the retrieved abstract does not independently establish the composition or stability of GO:0046696. Retain uncertainty specific to complex membership rather than a blanket contamination objection. Supporting Evidence: PMID:17164250 Hsp60 bound to the cell surface of APC colocalizes with the LPS co-receptor CD14 |
| GO:0048291 isotype switching to IgG isotypes | IDA PMID:16148103 Heat shock protein 60 activates B cells via the TLR4-MyD88 p... | UNDECIDED | Summary: The isotype-switching assay requires the full B-cell study. Reason: PMID:16148103 supports human-Hsp60-induced B-cell proliferation, cytokine production and TLR4/MyD88 dependence, but the retrieved abstract does not describe the IgG-isotype-switching experiment. Preserve the experimental annotation as unresolved rather than inferring its absence from the abstract. |
| GO:0050821 protein stabilization | IMP PMID:18086682 Hsp60 regulation of tumor cell apoptosis. | KEEP AS NON CORE | Summary: Retain the context-dependent cytosolic/apoptotic interaction or effect as non-core. Reason: PMID:18086682 directly identifies Hsp60-associated survivin and an Hsp60-p53 complex in tumor cells. Acute Hsp60 loss destabilizes mitochondrial survivin and promotes p53/Bax-dependent apoptosis. This supports the specific binding, stabilization or survival context as ancillary to mitochondrial folding. Supporting Evidence: PMID:18086682 Hsp60 orchestrates a broad cell survival program centered on stabilization of mitochondrial survivin and restraining of p53 function |
| GO:0050821 protein stabilization | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Retain the context-dependent cytosolic/apoptotic interaction or effect as non-core. Reason: The primary apoptosis study demonstrates cytosolic Hsp60 accumulation with either pro-death or pro-survival effects depending on the inducer and caspase-3 interaction. Opposite apoptotic-direction annotations need not conflict when contexts differ. These secondary roles do not replace the matrix folding function. Supporting Evidence: PMID:17823127 the cytosolically accumulated HSP60 possesses either pro-survival or pro-death functions, which involves differential interactions with caspase-3. |
| GO:0050870 positive regulation of T cell activation | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Retain the experimentally supported extracellular immune context. Reason: PMID:17164250 directly reports Hsp60 binding to bacterial LPS and distinguishes LPS-independent IFN-alpha-linked costimulation from LPS-dependent enhancement of IL-12p40 and antigen-specific IFN-gamma. PMID:18256040 further tests endotoxin-free Hsp60. These specific positive assays support a context-dependent immune function; primary mitochondrial localization or hypothetical contamination alone is not a reason to withhold the annotation. Propagation Review Root cause: NO FAILURE NON CORE Sources checked: PANTHER:PTN002900230 · PTN002900230 SUPPORTS TRANSFER The vertebrate IBD includes human HSPD1 itself among experimentally supported descendants; that is target experimental grounding, not circularity. Preparation-specific studies distinguish LPS-associated and LPS-free effects. Supporting Evidence: PMID:17164250 Hsp60 specifically binds bacterial LPS PMID:17164250 both molecules synergistically enhanced IL-12p40 production in APC and IFNgamma release |
| 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: Retain the experimentally supported extracellular immune context. Reason: PMID:16148103 explicitly tests human HSP60 on naive mouse B cells, reports TLR4/MyD88 dependence, proliferation and IL-6/IL-10 production, and states that controls addressed LPS contamination. The responding cells are murine but the tested protein is human. The curated context is retained as non-core; the abstract supports these findings, while detailed control methods remain full-text dependent. 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. |
| GO:0050870 positive regulation of T cell activation | IDA PMID:17164250 Synergistic and differential modulation of immune responses ... | KEEP AS NON CORE | Summary: Retain the experimentally supported extracellular immune context. Reason: PMID:17164250 directly reports Hsp60 binding to bacterial LPS and distinguishes LPS-independent IFN-alpha-linked costimulation from LPS-dependent enhancement of IL-12p40 and antigen-specific IFN-gamma. PMID:18256040 further tests endotoxin-free Hsp60. These specific positive assays support a context-dependent immune function; primary mitochondrial localization or hypothetical contamination alone is not a reason to withhold the annotation. Supporting Evidence: PMID:17164250 Hsp60 specifically binds bacterial LPS PMID:17164250 both molecules synergistically enhanced IL-12p40 production in APC and IFNgamma release |
| GO:0050870 positive regulation of T cell activation | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Retain the experimentally supported extracellular immune context. Reason: PMID:17164250 directly reports Hsp60 binding to bacterial LPS and distinguishes LPS-independent IFN-alpha-linked costimulation from LPS-dependent enhancement of IL-12p40 and antigen-specific IFN-gamma. PMID:18256040 further tests endotoxin-free Hsp60. These specific positive assays support a context-dependent immune function; primary mitochondrial localization or hypothetical contamination alone is not a reason to withhold the annotation. Supporting Evidence: PMID:17164250 Hsp60 specifically binds bacterial LPS PMID:17164250 both molecules synergistically enhanced IL-12p40 production in APC and IFNgamma release |
| GO:0050870 positive regulation of T cell activation | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: Retain the experimentally supported extracellular immune context. Reason: PMID:17164250 directly reports Hsp60 binding to bacterial LPS and distinguishes LPS-independent IFN-alpha-linked costimulation from LPS-dependent enhancement of IL-12p40 and antigen-specific IFN-gamma. PMID:18256040 further tests endotoxin-free Hsp60. These specific positive assays support a context-dependent immune function; primary mitochondrial localization or hypothetical contamination alone is not a reason to withhold the annotation. Supporting Evidence: PMID:17164250 Hsp60 specifically binds bacterial LPS PMID:17164250 both molecules synergistically enhanced IL-12p40 production in APC and IFNgamma release |
| GO:0051087 protein-folding chaperone binding | IBA GO_REF:0000033 | ACCEPT | Summary: Hsp60/Hsp10 ATP-dependent folding is established for the intact mammalian chaperonin. Reason: Purified mammalian Hsp60 with Hsp10 restores activity to unfolded substrate in an ATP-dependent reaction. This establishes folding/refolding, ATP-driven chaperoning and partner-assisted assembly. For the selected horse model, deletion of human 171–202 requires assessment of the apical-domain transition and oligomeric cycle before transferring full functional competence; conservation alone does not resolve that deletion. Supporting Evidence: PMID:1346131 facilitates the formation of catalytically active ribulose-bisphosphate carboxylase from an unfolded state in the presence of K+ and MgATP. |
| GO:0051087 protein-folding chaperone binding | IPI PMID:10205158 Presence of a pre-apoptotic complex of pro-caspase-3, Hsp60 ... | ACCEPT | Summary: Hsp60/Hsp10 ATP-dependent folding is established for the intact mammalian chaperonin. Reason: Purified mammalian Hsp60 with Hsp10 restores activity to unfolded substrate in an ATP-dependent reaction. This establishes folding/refolding, ATP-driven chaperoning and partner-assisted assembly. For the selected horse model, deletion of human 171–202 requires assessment of the apical-domain transition and oligomeric cycle before transferring full functional competence; conservation alone does not resolve that deletion. Supporting Evidence: PMID:1346131 facilitates the formation of catalytically active ribulose-bisphosphate carboxylase from an unfolded state in the presence of K+ and MgATP. |
| GO:0051131 chaperone-mediated protein complex assembly | ISS GO_REF:0000024 | ACCEPT | Summary: Hsp60/Hsp10 ATP-dependent folding is established for the intact mammalian chaperonin. Reason: Purified mammalian Hsp60 with Hsp10 restores activity to unfolded substrate in an ATP-dependent reaction. This establishes folding/refolding, ATP-driven chaperoning and partner-assisted assembly. For the selected horse model, deletion of human 171–202 requires assessment of the apical-domain transition and oligomeric cycle before transferring full functional competence; conservation alone does not resolve that deletion. Supporting Evidence: PMID:1346131 facilitates the formation of catalytically active ribulose-bisphosphate carboxylase from an unfolded state in the presence of K+ and MgATP. |
| GO:0051604 protein maturation | ISS GO_REF:0000024 | ACCEPT | Summary: Hsp60/Hsp10 ATP-dependent folding is established for the intact mammalian chaperonin. Reason: Purified mammalian Hsp60 with Hsp10 restores activity to unfolded substrate in an ATP-dependent reaction. This establishes folding/refolding, ATP-driven chaperoning and partner-assisted assembly. For the selected horse model, deletion of human 171–202 requires assessment of the apical-domain transition and oligomeric cycle before transferring full functional competence; conservation alone does not resolve that deletion. Supporting Evidence: PMID:1346131 facilitates the formation of catalytically active ribulose-bisphosphate carboxylase from an unfolded state in the presence of K+ and MgATP. |
| 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: Retain the source-specific interaction or host-associated effect as non-core. Reason: The curated source PMID:20507888 reports this ancillary interaction or biological context. It is not sufficient to replace ATP-dependent folding as the core function, and no generalized ligand/receptor or symbiont function is inferred beyond the reported observation. |
| GO:0070062 extracellular exosome | HDA PMID:19056867 Large-scale proteomics and phosphoproteomics of urinary exos... | KEEP AS NON CORE | Summary: Retain the detected secondary cellular compartment or assembly as non-core. Reason: Hsp60 can be detected outside its principal matrix pool, including stress-associated cytosolic, membrane and extracellular fractions. The curated observation is retained without inferring that Hsp60 is a constitutive secreted signal or a structural component of every detected vesicle. Physiological interpretation remains context-dependent. |
| GO:0070062 extracellular exosome | HDA PMID:20458337 MHC class II-associated proteins in B-cell exosomes and pote... | KEEP AS NON CORE | Summary: Retain the detected secondary cellular compartment or assembly as non-core. Reason: Hsp60 can be detected outside its principal matrix pool, including stress-associated cytosolic, membrane and extracellular fractions. The curated observation is retained without inferring that Hsp60 is a constitutive secreted signal or a structural component of every detected vesicle. Physiological interpretation remains context-dependent. |
| GO:0070062 extracellular exosome | IDA PMID:21276792 Morphologic and proteomic characterization of exosomes relea... | KEEP AS NON CORE | Summary: Retain the detected secondary cellular compartment or assembly as non-core. Reason: Hsp60 can be detected outside its principal matrix pool, including stress-associated cytosolic, membrane and extracellular fractions. The curated observation is retained without inferring that Hsp60 is a constitutive secreted signal or a structural component of every detected vesicle. Physiological interpretation remains context-dependent. |
| GO:0097225 sperm midpiece | IMP PMID:32791035 Bi-allelic Loss-of-function Variants in CFAP58 Cause Flagell... | KEEP AS NON CORE | Summary: Retain the detected secondary cellular compartment or assembly as non-core. Reason: Hsp60 can be detected outside its principal matrix pool, including stress-associated cytosolic, membrane and extracellular fractions. The curated observation is retained without inferring that Hsp60 is a constitutive secreted signal or a structural component of every detected vesicle. Physiological interpretation remains context-dependent. |
| GO:0140494 migrasome | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Retain the detected secondary cellular compartment or assembly as non-core. Reason: Hsp60 can be detected outside its principal matrix pool, including stress-associated cytosolic, membrane and extracellular fractions. The curated observation is retained without inferring that Hsp60 is a constitutive secreted signal or a structural component of every detected vesicle. Physiological interpretation remains context-dependent. |
| GO:0140608 cysteine-type endopeptidase activator activity | IDA PMID:17823127 Cytosolic accumulation of HSP60 during apoptosis with or wit... | KEEP AS NON CORE | Summary: Retain the context-dependent cytosolic/apoptotic interaction or effect as non-core. Reason: The primary apoptosis study demonstrates cytosolic Hsp60 accumulation with either pro-death or pro-survival effects depending on the inducer and caspase-3 interaction. Opposite apoptotic-direction annotations need not conflict when contexts differ. These secondary roles do not replace the matrix folding function. Supporting Evidence: PMID:17823127 the cytosolically accumulated HSP60 possesses either pro-survival or pro-death functions, which involves differential interactions with caspase-3. |
| GO:0140662 ATP-dependent protein folding chaperone | IDA PMID:1346131 Mammalian mitochondrial chaperonin 60 functions as a single ... | ACCEPT | Summary: Hsp60/Hsp10 ATP-dependent folding is established for the intact mammalian chaperonin. Reason: Purified mammalian Hsp60 with Hsp10 restores activity to unfolded substrate in an ATP-dependent reaction. This establishes folding/refolding, ATP-driven chaperoning and partner-assisted assembly. For the selected horse model, deletion of human 171–202 requires assessment of the apical-domain transition and oligomeric cycle before transferring full functional competence; conservation alone does not resolve that deletion. Supporting Evidence: PMID:1346131 facilitates the formation of catalytically active ribulose-bisphosphate carboxylase from an unfolded state in the presence of K+ and MgATP. |
| GO:0140662 ATP-dependent protein folding chaperone | IEA GO_REF:0000002 | ACCEPT | Summary: Hsp60/Hsp10 ATP-dependent folding is established for the intact mammalian chaperonin. Reason: Purified mammalian Hsp60 with Hsp10 restores activity to unfolded substrate in an ATP-dependent reaction. This establishes folding/refolding, ATP-driven chaperoning and partner-assisted assembly. For the selected horse model, deletion of human 171–202 requires assessment of the apical-domain transition and oligomeric cycle before transferring full functional competence; conservation alone does not resolve that deletion. Supporting Evidence: PMID:1346131 facilitates the formation of catalytically active ribulose-bisphosphate carboxylase from an unfolded state in the presence of K+ and MgATP. |
| 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: Retain the context-dependent cytosolic/apoptotic interaction or effect as non-core. Reason: The primary apoptosis study demonstrates cytosolic Hsp60 accumulation with either pro-death or pro-survival effects depending on the inducer and caspase-3 interaction. Opposite apoptotic-direction annotations need not conflict when contexts differ. These secondary roles do not replace the matrix folding function. Supporting Evidence: PMID:17823127 the cytosolically accumulated HSP60 possesses either pro-survival or pro-death functions, which involves differential interactions with caspase-3. |
| 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: Retain the context-dependent cytosolic/apoptotic interaction or effect as non-core. Reason: The primary apoptosis study demonstrates cytosolic Hsp60 accumulation with either pro-death or pro-survival effects depending on the inducer and caspase-3 interaction. Opposite apoptotic-direction annotations need not conflict when contexts differ. These secondary roles do not replace the matrix folding function. Supporting Evidence: PMID:17823127 the cytosolically accumulated HSP60 possesses either pro-survival or pro-death functions, which involves differential interactions with caspase-3. |
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