Hsp90aa1

UniProt ID: P07901
Organism: Mus musculus
Review Status: COMPLETE
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Gene Description

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.

Existing Annotations Review

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.
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.
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.
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 system’s 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 system’s 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.
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.
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.
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 system’s 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.
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 system’s 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 system’s 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 system’s 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 system’s 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 system’s 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 system’s 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.
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 system’s 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.
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.

Core Functions

Hsp90aa1 is an ATP-dependent protein-folding chaperone that uses ATP binding and hydrolysis to mature and stabilize selected client proteins in cytosolic and nuclear chaperone complexes.

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-notes.md
    Tsc1 facilitates "Hsp90-mediated folding of kinase and non-kinase clients"
  • 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.
  • file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
    Hsp90Ξ± is a **cytosolic** Hsp90 isoform
  • file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
    Across eukaryotes, Hsp90 clients are enriched for **signal transduction proteins**

References

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Deep Research

Falcon

(Hsp90aa1-deep-research-falcon.md)

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πŸ“š Additional Documentation

Notes

(Hsp90aa1-notes.md)

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