Hsp90aa1 encodes the inducible cytosolic Hsp90-alpha molecular chaperone, an ATP-binding and ATP-hydrolyzing protein-folding chaperone that promotes maturation, stabilization, and regulation of selected client proteins. Hsp90aa1 functions as a dimer within dynamic co-chaperone/client complexes, cycles between ATP- and ADP-bound conformations, and acts principally in the cytosol and the nucleus. The same ATPase-driven cycle underlies its wider activities: interactions with individual clients, the cytosolic stress response, a secreted extracellular HSP90-alpha pool acting at the cell surface, roles in neuronal contexts, and a male-germline requirement in mouse. These are context-specific outputs of one chaperone mechanism rather than separate core functions.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0006457 protein folding | IBA GO_REF:0000033 | ACCEPT | Summary: protein folding is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md **Hsp90aa1 encodes HSP90Ξ±**, a highly abundant **ATP-dependent molecular chaperone** that functions as a dimer file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound states that orchestrate client loading, activation/maturation, and release. |
| GO:0016887 ATP hydrolysis activity | IBA GO_REF:0000033 | ACCEPT | Summary: ATP hydrolysis activity is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md **Hsp90aa1 encodes HSP90Ξ±**, a highly abundant **ATP-dependent molecular chaperone** that functions as a dimer file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound states that orchestrate client loading, activation/maturation, and release. |
| GO:0032991 protein-containing complex | IBA GO_REF:0000033 | MODIFY | Summary: Protein-containing complex is true but too generic for Hsp90aa1 chaperone complexes. Reason: Use GO:0101031 protein folding chaperone complex for Hsp90 co-chaperone/client assemblies. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN000163629 SUPPORTS TRANSFER PTHR11528 (HSP90 family) node. Every identified seed is an HSP90 ortholog or close paralog spanning fly, worm, rodent, chicken and human, so the assertion that this protein acts within multi-subunit assemblies is soundly ancestral. Checked in the ontology: GO:0101031 is a descendant of GO:0032991 via GO:0140535, so the replacement is a parent-to-child refinement of an uninformative root-level complex term, not a change of claim. MGI:MGI:96250 Β· Hsp90aa1 SUPPORTS TRANSFER The target's own IBD seed. Mouse Hsp90aa1's own experimental annotation is one of the descendant evidences the PAINT curator used to place the IBD at PTN000163629, so its appearance in this row's WITH/FROM is expected and marks experimental grounding on the target itself. UniProtKB:P07900 Β· HSP90AA1 SUPPORTS TRANSFER Human HSP90-alpha, the target's direct ortholog; the same dimeric co-chaperone/client assemblies that GO:0101031 names. UniProtKB:P08238 Β· HSP90AB1 SUPPORTS TRANSFER Human HSP90-beta, the constitutive cytosolic paralog. A within-family paralog here, but one that forms the same class of chaperone complex, so the complex-level claim transfers. UniProtKB:P11501 Β· HSP90AA1 SUPPORTS TRANSFER Chicken HSP90-alpha, a further vertebrate ortholog seed; corroborates that the complex assertion sits above the vertebrate radiation rather than at a lineage-specific node. MGI:MGI:96247 SUPPORTS TRANSFER A further mouse PTHR11528 seed at this node. Cited by identifier only - it could not be resolved to a named gene product with the local index, so no name is asserted for it. Proposed replacements: protein folding chaperone complex Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md functions as a dimer within dynamic co-chaperone/client complexes file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md **Hsp90aa1 encodes HSP90Ξ±**, a highly abundant **ATP-dependent molecular chaperone** that functions as a dimer file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound states that orchestrate client loading, activation/maturation, and release. |
| GO:0005886 plasma membrane | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: plasma membrane is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md Keratinocytes can **massively release eHSP90Ξ± into the wound bed** to promote wound repair |
| GO:0005524 ATP binding | IBA GO_REF:0000033 | ACCEPT | Summary: ATP binding is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md **Hsp90aa1 encodes HSP90Ξ±**, a highly abundant **ATP-dependent molecular chaperone** that functions as a dimer file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound states that orchestrate client loading, activation/maturation, and release. |
| GO:0005829 cytosol | IBA GO_REF:0000033 | ACCEPT | Summary: cytosol is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md Hsp90Ξ± is a **cytosolic** Hsp90 isoform |
| GO:0005634 nucleus | IBA GO_REF:0000033 | ACCEPT | Summary: nucleus is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md Hsp90Ξ± is a **cytosolic** Hsp90 isoform |
| GO:0050821 protein stabilization | IBA GO_REF:0000033 | ACCEPT | Summary: protein stabilization is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md **Hsp90aa1 encodes HSP90Ξ±**, a highly abundant **ATP-dependent molecular chaperone** that functions as a dimer file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound states that orchestrate client loading, activation/maturation, and release. |
| GO:0034605 cellular response to heat | IBA GO_REF:0000033 | ACCEPT | Summary: cellular response to heat is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone |
| GO:0051082 unfolded protein binding | IBA GO_REF:0000033 | MODIFY | Summary: Unfolded protein binding is not the best description of Hsp90aa1. Hsp90 is an ATP-dependent foldase for selected clients rather than a generic unfolded-protein holdase. Reason: GO:0051082 is now formally obsolete, its upstream name being "obsolete unfolded protein binding". This repository records that in three tracked files, two of them machine-fetched upstream data: gocams/68b0f0d000005090/68b0f0d000005090-src.yaml:2436 and gocams/69729a3800002828/69729a3800002828-src.yaml:2717 both carry "label: obsolete unfolded protein binding", and projects/UNFOLDED_PROTEIN_BINDING.md:14 records it as checked live against QuickGO and OLS on 2026-07-25. What the local ontology snapshots carry is the pre-obsoletion label "unfolded protein binding" - cache/go/terms.csv, cache/ontologies/go.tsv (which additionally records is_obsolete False), and this gene's GOA rows - so a term-cache lookup alone will not show the obsoletion, which is why it is cited from the gocam caches instead. That project reclassifies such rows to a mechanism-specific MF term rather than leaving a generic binding term in place. Hsp90 is an ATP-dependent foldase, so GO:0140662 ATP-dependent protein folding chaperone is the term the project assigns to this class - the same replacement it records for the budding-yeast HSP90 paralogs HSP82 and HSC82, which are themselves the IBD seeds behind this very row. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: PANTHER:PTN000163527 SUPPORTS TRANSFER PTHR11528 (HSP90 family) node, and deeper than the PTN000163629 node behind the complex row - derivable from the cache rather than asserted: PTHR11528-paint.tsv gives PTN000163527's GO:0006457 row the seeds AGI_LocusCode:AT5G52640, AGI_LocusCode:AT5G56030 and UniProtKB:P0A6Z3 (E. coli HtpG) alongside its fungal and metazoan seeds, with an unconstrained taxon field, while every PTN000163629 row is stamped taxon:2759. A node carrying a bacterial seed sits above the split that a eukaryote-constrained node sits inside. The chaperone biology transfers correctly; the fault is entirely in the term. GO:0051082 is now formally obsolete (name "obsolete unfolded protein binding", carried in this repository by gocams/68b0f0d000005090/68b0f0d000005090-src.yaml:2436 and gocams/69729a3800002828/69729a3800002828-src.yaml:2717, and confirmed against QuickGO in projects/UNFOLDED_PROTEIN_BINDING.md:14), and that project reclassifies such rows to a mechanism-specific MF term rather than leaving a generic binding term in place. GO:0140662 is the value it assigns to ATP-dependent foldases. SGD:S000004798 Β· HSC82 SUPPORTS TRANSFER Budding-yeast HSC82, one of the two S. cerevisiae HSP90 paralogs (corroborated via the family index, not looked up from this MOD id). The UNFOLDED_PROTEIN_BINDING project independently reclassified HSC82's own GO:0051082 annotation to GO:0140662, so this seed's replacement term and the target's agree. SGD:S000006161 Β· HSP82 SUPPORTS TRANSFER Budding-yeast HSP82, the stress-inducible S. cerevisiae HSP90 paralog (corroborated via the family index, not looked up from this MOD id). Also reclassified to GO:0140662 by the UNFOLDED_PROTEIN_BINDING project, which is the precedent this row follows. PomBase:SPAC926.04c SUPPORTS TRANSFER A fission-yeast seed at this node, cited by identifier only because it could not be resolved to a named gene product with the local index. FB:FBgn0001233 SUPPORTS TRANSFER A Drosophila seed at this node, cited by identifier only because it could not be resolved to a named gene product with the local index. Proposed replacements: ATP-dependent protein folding chaperone Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md GO:0051082 unfolded protein binding is not the best term for Hsp90 file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md **Hsp90aa1 encodes HSP90Ξ±**, a highly abundant **ATP-dependent molecular chaperone** that functions as a dimer file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound states that orchestrate client loading, activation/maturation, and release. |
| GO:0043025 neuronal cell body | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: neuronal cell body is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0043209 myelin sheath | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: myelin sheath is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0048471 perinuclear region of cytoplasm | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: perinuclear region of cytoplasm is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0005524 ATP binding | IEA GO_REF:0000120 | ACCEPT | Summary: ATP binding is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md **Hsp90aa1 encodes HSP90Ξ±**, a highly abundant **ATP-dependent molecular chaperone** that functions as a dimer file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound states that orchestrate client loading, activation/maturation, and release. |
| GO:0005634 nucleus | IEA GO_REF:0000120 | ACCEPT | Summary: nucleus is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md Hsp90Ξ± is a **cytosolic** Hsp90 isoform |
| GO:0005737 cytoplasm | IEA GO_REF:0000120 | ACCEPT | Summary: cytoplasm is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md Hsp90Ξ± is a **cytosolic** Hsp90 isoform |
| GO:0005739 mitochondrion | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: mitochondrion is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0005886 plasma membrane | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: plasma membrane is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0006457 protein folding | IEA GO_REF:0000002 | ACCEPT | Summary: protein folding is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md **Hsp90aa1 encodes HSP90Ξ±**, a highly abundant **ATP-dependent molecular chaperone** that functions as a dimer file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound states that orchestrate client loading, activation/maturation, and release. |
| GO:0016887 ATP hydrolysis activity | IEA GO_REF:0000120 | ACCEPT | Summary: ATP hydrolysis activity is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md **Hsp90aa1 encodes HSP90Ξ±**, a highly abundant **ATP-dependent molecular chaperone** that functions as a dimer file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound states that orchestrate client loading, activation/maturation, and release. |
| GO:0032880 regulation of protein localization | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: regulation of protein localization is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0042470 melanosome | IEA GO_REF:0000044 | KEEP AS NON CORE | Summary: melanosome is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0044183 protein folding chaperone | IEA GO_REF:0000117 | ACCEPT | Summary: protein folding chaperone is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md **Hsp90aa1 encodes HSP90Ξ±**, a highly abundant **ATP-dependent molecular chaperone** that functions as a dimer file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound states that orchestrate client loading, activation/maturation, and release. |
| GO:0044294 dendritic growth cone | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: dendritic growth cone is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0044295 axonal growth cone | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: axonal growth cone is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0051082 unfolded protein binding | IEA GO_REF:0000002 | MODIFY | Summary: Unfolded protein binding is not the best description of Hsp90aa1. Hsp90 is an ATP-dependent foldase for selected clients rather than a generic unfolded-protein holdase. Reason: Replace with GO:0140662 ATP-dependent protein folding chaperone, which captures the ATP-driven Hsp90 mechanism. Proposed replacements: ATP-dependent protein folding chaperone Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md GO:0051082 unfolded protein binding is not the best term for Hsp90 file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md **Hsp90aa1 encodes HSP90Ξ±**, a highly abundant **ATP-dependent molecular chaperone** that functions as a dimer file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound states that orchestrate client loading, activation/maturation, and release. |
| GO:0140662 ATP-dependent protein folding chaperone | IEA GO_REF:0000002 | ACCEPT | Summary: ATP-dependent protein folding chaperone is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md **Hsp90aa1 encodes HSP90Ξ±**, a highly abundant **ATP-dependent molecular chaperone** that functions as a dimer file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound states that orchestrate client loading, activation/maturation, and release. |
| GO:0005515 protein binding | IPI PMID:18474241 The mammalian CHORD-containing protein melusin is a stress r... | MARK AS OVER ANNOTATED | Summary: Protein binding is an uninformative physical-interaction annotation for Hsp90aa1. Reason: Hsp90 has many client and co-chaperone interactions; the useful functional call is ATP-dependent protein folding chaperone or a specific partner-binding term where justified. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md GO:0005515 protein binding is too generic for Hsp90 client or cochaperone interactions file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md Across eukaryotes, Hsp90 clients are enriched for **signal transduction proteins** file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md The Hsp90 systemβs specificity is heavily shaped by co-chaperones: |
| GO:0005515 protein binding | IPI PMID:18566586 The mammalian target of rapamycin complex 2 controls folding... | MARK AS OVER ANNOTATED | Summary: Protein binding is an uninformative physical-interaction annotation for Hsp90aa1. Reason: Hsp90 has many client and co-chaperone interactions; the useful functional call is ATP-dependent protein folding chaperone or a specific partner-binding term where justified. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md GO:0005515 protein binding is too generic for Hsp90 client or cochaperone interactions file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md Across eukaryotes, Hsp90 clients are enriched for **signal transduction proteins** file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md The Hsp90 systemβs specificity is heavily shaped by co-chaperones: |
| GO:0001764 neuron migration | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: neuron migration is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0002021 response to dietary excess | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: response to dietary excess is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0002134 UTP binding | IEA GO_REF:0000107 | REMOVE | Summary: UTP binding is not supported as a biologically meaningful Hsp90aa1 nucleotide-binding function. Reason: Hsp90aa1 is an ATP-binding ATPase; automated transfer to other nucleotide-binding terms overstates the evidence. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md GOA terms for UTP binding, CTP binding, GTP binding, and dATP binding are not supported |
| GO:0002135 CTP binding | IEA GO_REF:0000107 | REMOVE | Summary: CTP binding is not supported as a biologically meaningful Hsp90aa1 nucleotide-binding function. Reason: Hsp90aa1 is an ATP-binding ATPase; automated transfer to other nucleotide-binding terms overstates the evidence. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md GOA terms for UTP binding, CTP binding, GTP binding, and dATP binding are not supported |
| GO:0002218 activation of innate immune response | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: activation of innate immune response is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0002230 positive regulation of defense response to virus by host | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: positive regulation of defense response to virus by host is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0003009 skeletal muscle contraction | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: skeletal muscle contraction is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0003729 mRNA binding | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: mRNA binding is too broad or indirect to be informative for Hsp90aa1 curation. Reason: The term does not distinguish Hsp90aa1 ATP-dependent chaperone activity from generic binding, complex membership, RNA association, or co-fractionation. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md GO:0005515 protein binding is too generic for Hsp90 client or cochaperone interactions |
| GO:0005525 GTP binding | IEA GO_REF:0000107 | REMOVE | Summary: GTP binding is not supported as a biologically meaningful Hsp90aa1 nucleotide-binding function. Reason: Hsp90aa1 is an ATP-binding ATPase; automated transfer to other nucleotide-binding terms overstates the evidence. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md GOA terms for UTP binding, CTP binding, GTP binding, and dATP binding are not supported |
| GO:0005829 cytosol | IEA GO_REF:0000120 | ACCEPT | Summary: cytosol is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md Hsp90Ξ± is a **cytosolic** Hsp90 isoform |
| GO:0009410 response to xenobiotic stimulus | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: response to xenobiotic stimulus is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0009651 response to salt stress | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: response to salt stress is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0009986 cell surface | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: cell surface is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0010592 positive regulation of lamellipodium assembly | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: positive regulation of lamellipodium assembly is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0010659 cardiac muscle cell apoptotic process | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: cardiac muscle cell apoptotic process is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0010664 negative regulation of striated muscle cell apoptotic process | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: negative regulation of striated muscle cell apoptotic process is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0016323 basolateral plasma membrane | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: basolateral plasma membrane is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0016324 apical plasma membrane | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: apical plasma membrane is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md Keratinocytes can **massively release eHSP90Ξ± into the wound bed** to promote wound repair |
| GO:0017098 sulfonylurea receptor binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: sulfonylurea receptor binding is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0019903 protein phosphatase binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: protein phosphatase binding is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0030150 protein import into mitochondrial matrix | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: protein import into mitochondrial matrix is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0030235 nitric-oxide synthase regulator activity | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: nitric-oxide synthase regulator activity is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0030911 TPR domain binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: TPR domain binding is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0031012 extracellular matrix | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: extracellular matrix is too broad or indirect to be informative for Hsp90aa1 curation. Reason: The term does not distinguish Hsp90aa1 ATP-dependent chaperone activity from generic binding, complex membership, RNA association, or co-fractionation. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md GO:0005515 protein binding is too generic for Hsp90 client or cochaperone interactions file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md Keratinocytes can **massively release eHSP90Ξ± into the wound bed** to promote wound repair |
| GO:0031396 regulation of protein ubiquitination | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: regulation of protein ubiquitination is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0031526 brush border membrane | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: brush border membrane is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0031625 ubiquitin protein ligase binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: ubiquitin protein ligase binding is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0032273 positive regulation of protein polymerization | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: positive regulation of protein polymerization is a peripheral or orthology-transferred Hsp90-associated annotation rather than a core Hsp90aa1 function. Reason: The annotation is not impossible for Hsp90 biology, but the evidence is indirect or context-specific compared with the core ATP-dependent chaperone function. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Many additional GOA annotations describe specific client interactions |
| GO:0032354 response to follicle-stimulating hormone | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: response to follicle-stimulating hormone is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0032564 dATP binding | IEA GO_REF:0000107 | REMOVE | Summary: dATP binding is not supported as a biologically meaningful Hsp90aa1 nucleotide-binding function. Reason: Hsp90aa1 is an ATP-binding ATPase; automated transfer to other nucleotide-binding terms overstates the evidence. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md GOA terms for UTP binding, CTP binding, GTP binding, and dATP binding are not supported |
| GO:0032728 positive regulation of interferon-beta production | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: positive regulation of interferon-beta production is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0032991 protein-containing complex | IEA GO_REF:0000120 | MODIFY | Summary: Protein-containing complex is true but too generic for Hsp90aa1 chaperone complexes. Reason: Use GO:0101031 protein folding chaperone complex for Hsp90 co-chaperone/client assemblies. Proposed replacements: protein folding chaperone complex Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md functions as a dimer within dynamic co-chaperone/client complexes file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md **Hsp90aa1 encodes HSP90Ξ±**, a highly abundant **ATP-dependent molecular chaperone** that functions as a dimer file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound states that orchestrate client loading, activation/maturation, and release. |
| GO:0034605 cellular response to heat | IEA GO_REF:0000120 | ACCEPT | Summary: cellular response to heat is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone |
| GO:0035900 response to isolation stress | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: response to isolation stress is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0036120 cellular response to platelet-derived growth factor stimulus | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: cellular response to platelet-derived growth factor stimulus is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0036126 sperm flagellum | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: sperm flagellum is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md **Hsp90aa1-null males are sterile** due to a failure to produce sperm |
| GO:0042220 response to cocaine | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: IEA orthology projection (GO_REF:0000107, Ensembl Compara) of a drug-response term onto a general cytosolic/nuclear molecular chaperone. There is no Hsp90aa1-specific experimental evidence that "response to cocaine" reflects a distinct biological role of this gene; any involvement would be the generic chaperoning of a client protein, not a cocaine-response function. Reason: Over-propagation by ortholog transfer onto a hub chaperone. HSP90 buffers thousands of clients, so projecting a single-species drug-response phenotype onto it adds no functional information and is not supported by direct Hsp90aa1 evidence. This mirrors the treatment of the identical IEA cocaine annotation on SMAD3 (also GO_REF:0000107), which is marked as over-annotated for the same reason. |
| GO:0042307 positive regulation of protein import into nucleus | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: positive regulation of protein import into nucleus is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0042802 identical protein binding | IEA GO_REF:0000107 | ACCEPT | Summary: identical protein binding is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md **Hsp90aa1 encodes HSP90Ξ±**, a highly abundant **ATP-dependent molecular chaperone** that functions as a dimer file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound states that orchestrate client loading, activation/maturation, and release. |
| GO:0042803 protein homodimerization activity | IEA GO_REF:0000107 | ACCEPT | Summary: protein homodimerization activity is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md **Hsp90aa1 encodes HSP90Ξ±**, a highly abundant **ATP-dependent molecular chaperone** that functions as a dimer file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound states that orchestrate client loading, activation/maturation, and release. |
| GO:0042826 histone deacetylase binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: histone deacetylase binding is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0042981 regulation of apoptotic process | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: regulation of apoptotic process is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0043025 neuronal cell body | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: neuronal cell body is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0043209 myelin sheath | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: myelin sheath is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0043627 response to estrogen | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: response to estrogen is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0044325 transmembrane transporter binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: transmembrane transporter binding is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0045732 positive regulation of protein catabolic process | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: positive regulation of protein catabolic process is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0045793 positive regulation of cell size | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: positive regulation of cell size is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0048156 tau protein binding | IEA GO_REF:0000120 | KEEP AS NON CORE | Summary: tau protein binding is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0048471 perinuclear region of cytoplasm | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: perinuclear region of cytoplasm is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0050821 protein stabilization | IEA GO_REF:0000107 | ACCEPT | Summary: protein stabilization is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md **Hsp90aa1 encodes HSP90Ξ±**, a highly abundant **ATP-dependent molecular chaperone** that functions as a dimer file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound states that orchestrate client loading, activation/maturation, and release. |
| GO:0051020 GTPase binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: GTPase binding is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0051022 Rho GDP-dissociation inhibitor binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: Rho GDP-dissociation inhibitor binding is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0051131 chaperone-mediated protein complex assembly | IEA GO_REF:0000107 | ACCEPT | Summary: chaperone-mediated protein complex assembly is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md **Hsp90aa1 encodes HSP90Ξ±**, a highly abundant **ATP-dependent molecular chaperone** that functions as a dimer file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound states that orchestrate client loading, activation/maturation, and release. |
| GO:0051604 protein maturation | IEA GO_REF:0000107 | ACCEPT | Summary: protein maturation is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone |
| GO:0060452 positive regulation of cardiac muscle contraction | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: positive regulation of cardiac muscle contraction is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0061771 response to caloric restriction | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: response to caloric restriction is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0070182 DNA polymerase binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: DNA polymerase binding is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0070301 cellular response to hydrogen peroxide | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: cellular response to hydrogen peroxide is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0071222 cellular response to lipopolysaccharide | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: cellular response to lipopolysaccharide is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0071260 cellular response to mechanical stimulus | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: cellular response to mechanical stimulus is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0071456 cellular response to hypoxia | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: cellular response to hypoxia is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md Hsp90Ξ± knockout causes a **dramatic reduction** in the normally high steady-state level of **HIF-1Ξ± in testis** |
| GO:0097110 scaffold protein binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: scaffold protein binding is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0097226 sperm mitochondrial sheath | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: sperm mitochondrial sheath is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md **Hsp90aa1-null males are sterile** due to a failure to produce sperm |
| GO:0097524 sperm plasma membrane | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: sperm plasma membrane is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md Keratinocytes can **massively release eHSP90Ξ± into the wound bed** to promote wound repair file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md **Hsp90aa1-null males are sterile** due to a failure to produce sperm |
| GO:0097718 disordered domain specific binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: disordered domain specific binding is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0098586 cellular response to virus | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: cellular response to virus is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0099072 regulation of postsynaptic membrane neurotransmitter receptor levels | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: regulation of postsynaptic membrane neurotransmitter receptor levels is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0101031 protein folding chaperone complex | IEA GO_REF:0000107 | ACCEPT | Summary: protein folding chaperone complex is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md **Hsp90aa1 encodes HSP90Ξ±**, a highly abundant **ATP-dependent molecular chaperone** that functions as a dimer file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound states that orchestrate client loading, activation/maturation, and release. |
| GO:1902988 neurofibrillary tangle assembly | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: neurofibrillary tangle assembly is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:1905323 telomerase holoenzyme complex assembly | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: telomerase holoenzyme complex assembly is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:1990782 protein tyrosine kinase binding | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: protein tyrosine kinase binding is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0001764 neuron migration | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: neuron migration is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0002134 UTP binding | ISO GO_REF:0000096 | REMOVE | Summary: UTP binding is not supported as a biologically meaningful Hsp90aa1 nucleotide-binding function. Reason: Hsp90aa1 is an ATP-binding ATPase; automated transfer to other nucleotide-binding terms overstates the evidence. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md GOA terms for UTP binding, CTP binding, GTP binding, and dATP binding are not supported |
| GO:0002135 CTP binding | ISO GO_REF:0000096 | REMOVE | Summary: CTP binding is not supported as a biologically meaningful Hsp90aa1 nucleotide-binding function. Reason: Hsp90aa1 is an ATP-binding ATPase; automated transfer to other nucleotide-binding terms overstates the evidence. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md GOA terms for UTP binding, CTP binding, GTP binding, and dATP binding are not supported |
| GO:0003729 mRNA binding | ISO GO_REF:0000096 | MARK AS OVER ANNOTATED | Summary: mRNA binding is too broad or indirect to be informative for Hsp90aa1 curation. Reason: The term does not distinguish Hsp90aa1 ATP-dependent chaperone activity from generic binding, complex membership, RNA association, or co-fractionation. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md GO:0005515 protein binding is too generic for Hsp90 client or cochaperone interactions |
| GO:0005524 ATP binding | ISO GO_REF:0000096 | ACCEPT | Summary: ATP binding is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md **Hsp90aa1 encodes HSP90Ξ±**, a highly abundant **ATP-dependent molecular chaperone** that functions as a dimer file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound states that orchestrate client loading, activation/maturation, and release. |
| GO:0005524 ATP binding | ISO GO_REF:0000119 | ACCEPT | Summary: ATP binding is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md **Hsp90aa1 encodes HSP90Ξ±**, a highly abundant **ATP-dependent molecular chaperone** that functions as a dimer file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound states that orchestrate client loading, activation/maturation, and release. |
| GO:0005525 GTP binding | ISO GO_REF:0000096 | REMOVE | Summary: GTP binding is not supported as a biologically meaningful Hsp90aa1 nucleotide-binding function. Reason: Hsp90aa1 is an ATP-binding ATPase; automated transfer to other nucleotide-binding terms overstates the evidence. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md GOA terms for UTP binding, CTP binding, GTP binding, and dATP binding are not supported |
| GO:0005634 nucleus | ISO GO_REF:0000096 | ACCEPT | Summary: nucleus is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md Hsp90Ξ± is a **cytosolic** Hsp90 isoform |
| GO:0005737 cytoplasm | ISO GO_REF:0000096 | ACCEPT | Summary: cytoplasm is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md Hsp90Ξ± is a **cytosolic** Hsp90 isoform |
| GO:0005737 cytoplasm | ISO GO_REF:0000119 | ACCEPT | Summary: cytoplasm is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md Hsp90Ξ± is a **cytosolic** Hsp90 isoform |
| GO:0005739 mitochondrion | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: mitochondrion is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0005829 cytosol | ISO GO_REF:0000119 | ACCEPT | Summary: cytosol is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md Hsp90Ξ± is a **cytosolic** Hsp90 isoform |
| GO:0009986 cell surface | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: cell surface is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md Keratinocytes can **massively release eHSP90Ξ± into the wound bed** to promote wound repair |
| GO:0010592 positive regulation of lamellipodium assembly | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: positive regulation of lamellipodium assembly is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0010664 negative regulation of striated muscle cell apoptotic process | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: negative regulation of striated muscle cell apoptotic process is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0016323 basolateral plasma membrane | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: basolateral plasma membrane is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md Keratinocytes can **massively release eHSP90Ξ± into the wound bed** to promote wound repair |
| GO:0016324 apical plasma membrane | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: apical plasma membrane is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md Keratinocytes can **massively release eHSP90Ξ± into the wound bed** to promote wound repair |
| GO:0016887 ATP hydrolysis activity | ISO GO_REF:0000119 | ACCEPT | Summary: ATP hydrolysis activity is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md **Hsp90aa1 encodes HSP90Ξ±**, a highly abundant **ATP-dependent molecular chaperone** that functions as a dimer file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound states that orchestrate client loading, activation/maturation, and release. |
| GO:0017098 sulfonylurea receptor binding | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: sulfonylurea receptor binding is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0019903 protein phosphatase binding | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: protein phosphatase binding is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0030235 nitric-oxide synthase regulator activity | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: nitric-oxide synthase regulator activity is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0030911 TPR domain binding | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: TPR domain binding is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0031012 extracellular matrix | ISO GO_REF:0000096 | MARK AS OVER ANNOTATED | Summary: extracellular matrix is too broad or indirect to be informative for Hsp90aa1 curation. Reason: The term does not distinguish Hsp90aa1 ATP-dependent chaperone activity from generic binding, complex membership, RNA association, or co-fractionation. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md GO:0005515 protein binding is too generic for Hsp90 client or cochaperone interactions file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md Keratinocytes can **massively release eHSP90Ξ± into the wound bed** to promote wound repair |
| GO:0031526 brush border membrane | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: brush border membrane is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0031625 ubiquitin protein ligase binding | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: ubiquitin protein ligase binding is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0032564 dATP binding | ISO GO_REF:0000096 | REMOVE | Summary: dATP binding is not supported as a biologically meaningful Hsp90aa1 nucleotide-binding function. Reason: Hsp90aa1 is an ATP-binding ATPase; automated transfer to other nucleotide-binding terms overstates the evidence. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md GOA terms for UTP binding, CTP binding, GTP binding, and dATP binding are not supported |
| GO:0032991 protein-containing complex | ISO GO_REF:0000096 | MODIFY | Summary: Protein-containing complex is true but too generic for Hsp90aa1 chaperone complexes. Reason: Use GO:0101031 protein folding chaperone complex for Hsp90 co-chaperone/client assemblies. Proposed replacements: protein folding chaperone complex Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md functions as a dimer within dynamic co-chaperone/client complexes file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md **Hsp90aa1 encodes HSP90Ξ±**, a highly abundant **ATP-dependent molecular chaperone** that functions as a dimer file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound states that orchestrate client loading, activation/maturation, and release. |
| GO:0032991 protein-containing complex | ISO GO_REF:0000119 | MODIFY | Summary: Protein-containing complex is true but too generic for Hsp90aa1 chaperone complexes. Reason: Use GO:0101031 protein folding chaperone complex for Hsp90 co-chaperone/client assemblies. Proposed replacements: protein folding chaperone complex Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md functions as a dimer within dynamic co-chaperone/client complexes file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md **Hsp90aa1 encodes HSP90Ξ±**, a highly abundant **ATP-dependent molecular chaperone** that functions as a dimer file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound states that orchestrate client loading, activation/maturation, and release. |
| GO:0036126 sperm flagellum | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: sperm flagellum is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md **Hsp90aa1-null males are sterile** due to a failure to produce sperm |
| GO:0042307 positive regulation of protein import into nucleus | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: positive regulation of protein import into nucleus is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0042802 identical protein binding | ISO GO_REF:0000119 | ACCEPT | Summary: identical protein binding is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md **Hsp90aa1 encodes HSP90Ξ±**, a highly abundant **ATP-dependent molecular chaperone** that functions as a dimer file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound states that orchestrate client loading, activation/maturation, and release. |
| GO:0042803 protein homodimerization activity | ISO GO_REF:0000119 | ACCEPT | Summary: protein homodimerization activity is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md **Hsp90aa1 encodes HSP90Ξ±**, a highly abundant **ATP-dependent molecular chaperone** that functions as a dimer file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound states that orchestrate client loading, activation/maturation, and release. |
| GO:0042826 histone deacetylase binding | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: histone deacetylase binding is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0043025 neuronal cell body | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: neuronal cell body is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0043209 myelin sheath | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: myelin sheath is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0044325 transmembrane transporter binding | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: transmembrane transporter binding is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0045793 positive regulation of cell size | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: positive regulation of cell size is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0048156 tau protein binding | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: tau protein binding is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0048156 tau protein binding | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: tau protein binding is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0048471 perinuclear region of cytoplasm | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: perinuclear region of cytoplasm is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0051020 GTPase binding | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: GTPase binding is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0051022 Rho GDP-dissociation inhibitor binding | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: Rho GDP-dissociation inhibitor binding is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0070182 DNA polymerase binding | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: DNA polymerase binding is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0097110 scaffold protein binding | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: scaffold protein binding is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0097226 sperm mitochondrial sheath | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: sperm mitochondrial sheath is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md **Hsp90aa1-null males are sterile** due to a failure to produce sperm |
| GO:0097524 sperm plasma membrane | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: sperm plasma membrane is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md Keratinocytes can **massively release eHSP90Ξ± into the wound bed** to promote wound repair file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md **Hsp90aa1-null males are sterile** due to a failure to produce sperm |
| GO:0097718 disordered domain specific binding | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: disordered domain specific binding is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0099072 regulation of postsynaptic membrane neurotransmitter receptor levels | ISO GO_REF:0000096 | KEEP AS NON CORE | Summary: regulation of postsynaptic membrane neurotransmitter receptor levels is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0101031 protein folding chaperone complex | ISO GO_REF:0000119 | ACCEPT | Summary: protein folding chaperone complex is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md **Hsp90aa1 encodes HSP90Ξ±**, a highly abundant **ATP-dependent molecular chaperone** that functions as a dimer file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound states that orchestrate client loading, activation/maturation, and release. |
| GO:0140767 enzyme-substrate adaptor activity | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: enzyme-substrate adaptor activity is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:1990782 protein tyrosine kinase binding | ISO GO_REF:0000119 | KEEP AS NON CORE | Summary: protein tyrosine kinase binding is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0005654 nucleoplasm | ISO GO_REF:0000119 | ACCEPT | Summary: nucleoplasm is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md Hsp90Ξ± is a **cytosolic** Hsp90 isoform |
| GO:0044183 protein folding chaperone | IMP PMID:24286867 Hsp90 activity is necessary to acquire a proper neuronal pol... | ACCEPT | Summary: protein folding chaperone is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md **Hsp90aa1 encodes HSP90Ξ±**, a highly abundant **ATP-dependent molecular chaperone** that functions as a dimer file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound states that orchestrate client loading, activation/maturation, and release. |
| GO:0035651 AP-3 adaptor complex binding | IDA PMID:19010779 Hermansky-Pudlak syndrome protein complexes associate with p... | UNDECIDED | Summary: Cannot be adjudicated here: PMID:19010779 is cached abstract-only. Prior observation, not a verdict: AP-3 adaptor complex binding is not supported by the cached local evidence for PMID:19010779. Reason: PMID:19010779 is cached abstract-only, so the curator's experimental evidence cannot be inspected here; per CLAUDE.md an experimental annotation is not overruled on that basis. Recorded observation, not a verdict: The cached PMID:19010779 text does not provide positive Hsp90aa1-specific evidence for AP-3 adaptor complex binding; generic cytosol/nucleus support is insufficient to retain this molecular interaction. |
| GO:0002218 activation of innate immune response | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: activation of innate immune response is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0002230 positive regulation of defense response to virus by host | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: positive regulation of defense response to virus by host is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0005739 mitochondrion | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: mitochondrion is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0032728 positive regulation of interferon-beta production | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: positive regulation of interferon-beta production is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0042981 regulation of apoptotic process | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: regulation of apoptotic process is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0098586 cellular response to virus | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: cellular response to virus is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0005515 protein binding | IPI PMID:29916806 ZMYND10 functions in a chaperone relay during axonemal dynei... | MARK AS OVER ANNOTATED | Summary: Protein binding is an uninformative physical-interaction annotation for Hsp90aa1. Reason: Hsp90 has many client and co-chaperone interactions; the useful functional call is ATP-dependent protein folding chaperone or a specific partner-binding term where justified. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md GO:0005515 protein binding is too generic for Hsp90 client or cochaperone interactions file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md Across eukaryotes, Hsp90 clients are enriched for **signal transduction proteins** file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md The Hsp90 systemβs specificity is heavily shaped by co-chaperones: |
| GO:0042802 identical protein binding | IPI PMID:12885400 Identification of the nuclear receptor CAR:HSP90 complex in ... | ACCEPT | Summary: identical protein binding is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md **Hsp90aa1 encodes HSP90Ξ±**, a highly abundant **ATP-dependent molecular chaperone** that functions as a dimer file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound states that orchestrate client loading, activation/maturation, and release. |
| GO:0005737 cytoplasm | IDA PMID:27496612 Interaction of a Novel Chaperone PhLP2A With the Heat Shock ... | ACCEPT | Summary: cytoplasm is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md Hsp90Ξ± is a **cytosolic** Hsp90 isoform |
| GO:0006457 protein folding | IMP PMID:27496612 Interaction of a Novel Chaperone PhLP2A With the Heat Shock ... | ACCEPT | Summary: protein folding is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md **Hsp90aa1 encodes HSP90Ξ±**, a highly abundant **ATP-dependent molecular chaperone** that functions as a dimer file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound states that orchestrate client loading, activation/maturation, and release. |
| GO:0032991 protein-containing complex | IDA PMID:27496612 Interaction of a Novel Chaperone PhLP2A With the Heat Shock ... | MODIFY | Summary: Protein-containing complex is true but too generic for Hsp90aa1 chaperone complexes. Reason: Use GO:0101031 protein folding chaperone complex for Hsp90 co-chaperone/client assemblies. Proposed replacements: protein folding chaperone complex Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md functions as a dimer within dynamic co-chaperone/client complexes file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md **Hsp90aa1 encodes HSP90Ξ±**, a highly abundant **ATP-dependent molecular chaperone** that functions as a dimer file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound states that orchestrate client loading, activation/maturation, and release. |
| GO:0034605 cellular response to heat | IMP PMID:27496612 Interaction of a Novel Chaperone PhLP2A With the Heat Shock ... | ACCEPT | Summary: cellular response to heat is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone |
| GO:0044183 protein folding chaperone | IMP PMID:27496612 Interaction of a Novel Chaperone PhLP2A With the Heat Shock ... | ACCEPT | Summary: protein folding chaperone is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md **Hsp90aa1 encodes HSP90Ξ±**, a highly abundant **ATP-dependent molecular chaperone** that functions as a dimer file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound states that orchestrate client loading, activation/maturation, and release. |
| GO:0005515 protein binding | IPI PMID:27686098 REV-ERBΞ± influences the stability and nuclear localization o... | MARK AS OVER ANNOTATED | Summary: Protein binding is an uninformative physical-interaction annotation for Hsp90aa1. Reason: Hsp90 has many client and co-chaperone interactions; the useful functional call is ATP-dependent protein folding chaperone or a specific partner-binding term where justified. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md GO:0005515 protein binding is too generic for Hsp90 client or cochaperone interactions file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md Across eukaryotes, Hsp90 clients are enriched for **signal transduction proteins** file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md The Hsp90 systemβs specificity is heavily shaped by co-chaperones: |
| GO:0005737 cytoplasm | IDA PMID:27686098 REV-ERBΞ± influences the stability and nuclear localization o... | ACCEPT | Summary: cytoplasm is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md Hsp90Ξ± is a **cytosolic** Hsp90 isoform |
| GO:0005515 protein binding | IPI PMID:29127155 Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facil... | MARK AS OVER ANNOTATED | Summary: Protein binding is an uninformative physical-interaction annotation for Hsp90aa1. Reason: Hsp90 has many client and co-chaperone interactions; the useful functional call is ATP-dependent protein folding chaperone or a specific partner-binding term where justified. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md GO:0005515 protein binding is too generic for Hsp90 client or cochaperone interactions file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md Across eukaryotes, Hsp90 clients are enriched for **signal transduction proteins** file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md The Hsp90 systemβs specificity is heavily shaped by co-chaperones: |
| GO:0032880 regulation of protein localization | IMP PMID:24286867 Hsp90 activity is necessary to acquire a proper neuronal pol... | KEEP AS NON CORE | Summary: regulation of protein localization is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0043025 neuronal cell body | IDA PMID:24286867 Hsp90 activity is necessary to acquire a proper neuronal pol... | KEEP AS NON CORE | Summary: neuronal cell body is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0044294 dendritic growth cone | IDA PMID:24286867 Hsp90 activity is necessary to acquire a proper neuronal pol... | KEEP AS NON CORE | Summary: dendritic growth cone is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0044295 axonal growth cone | IDA PMID:24286867 Hsp90 activity is necessary to acquire a proper neuronal pol... | KEEP AS NON CORE | Summary: axonal growth cone is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0048471 perinuclear region of cytoplasm | IDA PMID:24286867 Hsp90 activity is necessary to acquire a proper neuronal pol... | KEEP AS NON CORE | Summary: perinuclear region of cytoplasm is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0005524 ATP binding | ISS GO_REF:0000024 | ACCEPT | Summary: ATP binding is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md **Hsp90aa1 encodes HSP90Ξ±**, a highly abundant **ATP-dependent molecular chaperone** that functions as a dimer file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound states that orchestrate client loading, activation/maturation, and release. |
| GO:0046677 response to antibiotic | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: response to antibiotic is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0005515 protein binding | IPI PMID:23184943 Dynamic nucleotide-dependent interactions of cysteine- and h... | MARK AS OVER ANNOTATED | Summary: Protein binding is an uninformative physical-interaction annotation for Hsp90aa1. Reason: Hsp90 has many client and co-chaperone interactions; the useful functional call is ATP-dependent protein folding chaperone or a specific partner-binding term where justified. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md GO:0005515 protein binding is too generic for Hsp90 client or cochaperone interactions file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md Across eukaryotes, Hsp90 clients are enriched for **signal transduction proteins** file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md The Hsp90 systemβs specificity is heavily shaped by co-chaperones: |
| GO:0005634 nucleus | ISS GO_REF:0000024 | ACCEPT | Summary: nucleus is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md Hsp90Ξ± is a **cytosolic** Hsp90 isoform |
| GO:0005737 cytoplasm | ISS GO_REF:0000024 | ACCEPT | Summary: cytoplasm is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md Hsp90Ξ± is a **cytosolic** Hsp90 isoform |
| GO:0009408 response to heat | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: response to heat is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0009409 response to cold | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: response to cold is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0005515 protein binding | IPI PMID:22431752 Hectd1 regulates intracellular localization and secretion of... | MARK AS OVER ANNOTATED | Summary: Protein binding is an uninformative physical-interaction annotation for Hsp90aa1. Reason: Hsp90 has many client and co-chaperone interactions; the useful functional call is ATP-dependent protein folding chaperone or a specific partner-binding term where justified. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md GO:0005515 protein binding is too generic for Hsp90 client or cochaperone interactions file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md Across eukaryotes, Hsp90 clients are enriched for **signal transduction proteins** file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md The Hsp90 systemβs specificity is heavily shaped by co-chaperones: |
| GO:0043209 myelin sheath | HDA PMID:17634366 Proteolipid protein is required for transport of sirtuin 2 i... | KEEP AS NON CORE | Summary: myelin sheath is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0005829 cytosol | IDA PMID:17923681 Mammalian Sir2 homolog SIRT3 regulates global mitochondrial ... | ACCEPT | Summary: cytosol is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md Hsp90Ξ± is a **cytosolic** Hsp90 isoform |
| GO:0005829 cytosol | TAS Reactome:R-MMU-9646345 | ACCEPT | Summary: cytosol is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md Hsp90Ξ± is a **cytosolic** Hsp90 isoform |
| GO:0005829 cytosol | TAS Reactome:R-MMU-9646359 | ACCEPT | Summary: cytosol is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md Hsp90Ξ± is a **cytosolic** Hsp90 isoform |
| GO:0005515 protein binding | IPI PMID:23055941 RAB-like 2 has an essential role in male fertility, sperm in... | MARK AS OVER ANNOTATED | Summary: Protein binding is an uninformative physical-interaction annotation for Hsp90aa1. Reason: Hsp90 has many client and co-chaperone interactions; the useful functional call is ATP-dependent protein folding chaperone or a specific partner-binding term where justified. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md GO:0005515 protein binding is too generic for Hsp90 client or cochaperone interactions file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md Across eukaryotes, Hsp90 clients are enriched for **signal transduction proteins** file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md The Hsp90 systemβs specificity is heavily shaped by co-chaperones: |
| GO:0005515 protein binding | IPI PMID:12885400 Identification of the nuclear receptor CAR:HSP90 complex in ... | MARK AS OVER ANNOTATED | Summary: Protein binding is an uninformative physical-interaction annotation for Hsp90aa1. Reason: Hsp90 has many client and co-chaperone interactions; the useful functional call is ATP-dependent protein folding chaperone or a specific partner-binding term where justified. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md GO:0005515 protein binding is too generic for Hsp90 client or cochaperone interactions file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md Across eukaryotes, Hsp90 clients are enriched for **signal transduction proteins** file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md The Hsp90 systemβs specificity is heavily shaped by co-chaperones: |
| GO:0005737 cytoplasm | IDA PMID:17908927 A role for AGL ubiquitination in the glycogen storage disord... | ACCEPT | Summary: cytoplasm is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md Hsp90Ξ± is a **cytosolic** Hsp90 isoform |
| GO:0030911 TPR domain binding | ISS GO_REF:0000024 | KEEP AS NON CORE | Summary: TPR domain binding is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0006986 response to unfolded protein | TAS PMID:12855682 Heat shock protein 90 as an endogenous protein enhancer of i... | KEEP AS NON CORE | Summary: response to unfolded protein is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0051082 unfolded protein binding | TAS PMID:12855682 Heat shock protein 90 as an endogenous protein enhancer of i... | MODIFY | Summary: Unfolded protein binding is not the best description of Hsp90aa1. Hsp90 is an ATP-dependent foldase for selected clients rather than a generic unfolded-protein holdase. Reason: Replace with GO:0140662 ATP-dependent protein folding chaperone, which captures the ATP-driven Hsp90 mechanism. Proposed replacements: ATP-dependent protein folding chaperone Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md GO:0051082 unfolded protein binding is not the best term for Hsp90 file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md **Hsp90aa1 encodes HSP90Ξ±**, a highly abundant **ATP-dependent molecular chaperone** that functions as a dimer file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound states that orchestrate client loading, activation/maturation, and release. |
| GO:0005515 protein binding | IPI PMID:12855682 Heat shock protein 90 as an endogenous protein enhancer of i... | MARK AS OVER ANNOTATED | Summary: Protein binding is an uninformative physical-interaction annotation for Hsp90aa1. Reason: Hsp90 has many client and co-chaperone interactions; the useful functional call is ATP-dependent protein folding chaperone or a specific partner-binding term where justified. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md GO:0005515 protein binding is too generic for Hsp90 client or cochaperone interactions file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md Across eukaryotes, Hsp90 clients are enriched for **signal transduction proteins** file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md The Hsp90 systemβs specificity is heavily shaped by co-chaperones: |
| GO:0005829 cytosol | TAS PMID:12855682 Heat shock protein 90 as an endogenous protein enhancer of i... | ACCEPT | Summary: cytosol is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal cytosolic/nuclear localization. Reason: This term captures a central molecular activity, process, complex, or main localization of Hsp90aa1. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md Hsp90Ξ± is a **cytosolic** Hsp90 isoform |
| GO:0006809 nitric oxide biosynthetic process | TAS PMID:12855682 Heat shock protein 90 as an endogenous protein enhancer of i... | KEEP AS NON CORE | Summary: nitric oxide biosynthetic process is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0030235 nitric-oxide synthase regulator activity | IDA PMID:12855682 Heat shock protein 90 as an endogenous protein enhancer of i... | KEEP AS NON CORE | Summary: nitric-oxide synthase regulator activity is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0042026 protein refolding | TAS PMID:12855682 Heat shock protein 90 as an endogenous protein enhancer of i... | MODIFY | Summary: PMID:12855682 supports Hsp90-dependent iNOS/NO modulation, while UniProt and the Falcon synthesis support the general ATP-dependent chaperone cycle; the cited PMID does not support protein refolding specifically. Reason: PMID:12855682 supports Hsp90-dependent modulation of iNOS/NO production, not protein refolding specifically. Replace with the core ATP-dependent protein-folding chaperone activity based on UniProt/Falcon support for the HSP90 ATPase-coupled chaperone cycle. Proposed replacements: ATP-dependent protein folding chaperone Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md **Hsp90aa1 encodes HSP90Ξ±**, a highly abundant **ATP-dependent molecular chaperone** that functions as a dimer file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound states that orchestrate client loading, activation/maturation, and release. |
| GO:0045429 positive regulation of nitric oxide biosynthetic process | IDA PMID:12855682 Heat shock protein 90 as an endogenous protein enhancer of i... | KEEP AS NON CORE | Summary: positive regulation of nitric oxide biosynthetic process is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function. Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes. Supporting Evidence: file:mouse/Hsp90aa1/Hsp90aa1-notes.md Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations |
| GO:0045585 positive regulation of cytotoxic T cell differentiation | TAS PMID:12855682 Heat shock protein 90 as an endogenous protein enhancer of i... | REMOVE | Summary: Positive regulation of cytotoxic T cell differentiation is not supported by PMID:12855682, which addresses iNOS-mediated nitric oxide production and cytotoxicity. Reason: PMID:12855682 supports iNOS-mediated nitric oxide production and cytotoxicity, not cytotoxic T-cell differentiation. Generic Hsp90 location/function evidence does not support retaining this BP annotation. |
Loading supporting contentβ¦
Download this section (compressed HTML)Loading supporting contentβ¦
Download this section (compressed HTML)Loading supporting contentβ¦
Download this section (compressed HTML)Loading supporting contentβ¦
Download this section (compressed HTML)