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 is best curated with ATP-dependent protein folding chaperone, ATP hydrolysis, protein folding, protein stabilization, cytosol, and nucleus terms. Many additional GOA annotations describe specific client interactions, stress responses, secreted/membrane pools, neuronal contexts, or orthology-transferred phenotypes; these are retained as non-core or marked over-annotated when they are too generic or too indirect. Falcon deep research corroborates this core ATPase-driven cytosolic HSP90-alpha cycle, while treating extracellular HSP90-alpha, male-germline phenotypes, and individual client pathways as context-specific non-core biology unless a GOA annotation directly captures them.
| 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 HSP90α**, 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 HSP90α**, 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.
Proposed replacements:
protein folding chaperone complex
Supporting Evidence:
file:mouse/Hsp90aa1/Hsp90aa1-notes.md
functions as a dimer within dynamic co-chaperone/client complexes
file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
**Hsp90aa1 encodes HSP90α**, 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 eHSP90α 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 HSP90α**, 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
Hsp90α 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
Hsp90α 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 HSP90α**, 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: Replace with GO:0140662 ATP-dependent protein folding chaperone, which captures the ATP-driven Hsp90 mechanism.
Proposed replacements:
ATP-dependent protein folding chaperone
Supporting Evidence:
file:mouse/Hsp90aa1/Hsp90aa1-notes.md
GO:0051082 unfolded protein binding is not the best term for Hsp90
file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
**Hsp90aa1 encodes HSP90α**, 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 HSP90α**, 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
Hsp90α 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
Hsp90α 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 HSP90α**, 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 HSP90α**, 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 HSP90α**, a highly abundant **ATP-dependent molecular chaperone** that functions as a dimer
file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound states that orchestrate client loading, activation/maturation, and release.
|
|
GO:0044294
dendritic growth cone
|
IEA
GO_REF:0000117 |
KEEP AS NON CORE |
Summary: dendritic growth cone is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function.
Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
Supporting Evidence:
file:mouse/Hsp90aa1/Hsp90aa1-notes.md
Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations
|
|
GO:0044295
axonal growth cone
|
IEA
GO_REF:0000117 |
KEEP AS NON CORE |
Summary: axonal growth cone is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function.
Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
Supporting Evidence:
file:mouse/Hsp90aa1/Hsp90aa1-notes.md
Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations
|
|
GO:0051082
unfolded protein binding
|
IEA
GO_REF:0000002 |
MODIFY |
Summary: Unfolded protein binding is not the best description of Hsp90aa1. Hsp90 is an ATP-dependent foldase for selected clients rather than a generic unfolded-protein holdase.
Reason: Replace with GO:0140662 ATP-dependent protein folding chaperone, which captures the ATP-driven Hsp90 mechanism.
Proposed replacements:
ATP-dependent protein folding chaperone
Supporting Evidence:
file:mouse/Hsp90aa1/Hsp90aa1-notes.md
GO:0051082 unfolded protein binding is not the best term for Hsp90
file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
**Hsp90aa1 encodes HSP90α**, 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 HSP90α**, 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
Hsp90α 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 eHSP90α 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 eHSP90α into the wound bed** to promote wound repair
|
|
GO:0031396
regulation of protein ubiquitination
|
IEA
GO_REF:0000107 |
KEEP AS NON CORE |
Summary: regulation of protein ubiquitination is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function.
Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
Supporting Evidence:
file:mouse/Hsp90aa1/Hsp90aa1-notes.md
Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations
|
|
GO:0031526
brush border membrane
|
IEA
GO_REF:0000107 |
KEEP AS NON CORE |
Summary: brush border membrane is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function.
Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
Supporting Evidence:
file:mouse/Hsp90aa1/Hsp90aa1-notes.md
Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations
|
|
GO:0031625
ubiquitin protein ligase binding
|
IEA
GO_REF:0000107 |
KEEP AS NON CORE |
Summary: ubiquitin protein ligase binding is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function.
Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
Supporting Evidence:
file:mouse/Hsp90aa1/Hsp90aa1-notes.md
Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations
|
|
GO:0032273
positive regulation of protein polymerization
|
IEA
GO_REF:0000107 |
KEEP AS NON CORE |
Summary: positive regulation of protein polymerization is a peripheral or orthology-transferred Hsp90-associated annotation rather than a core Hsp90aa1 function.
Reason: The annotation is not impossible for Hsp90 biology, but the evidence is indirect or context-specific compared with the core ATP-dependent chaperone function.
Supporting Evidence:
file:mouse/Hsp90aa1/Hsp90aa1-notes.md
Many additional GOA annotations describe specific client interactions
|
|
GO:0032354
response to follicle-stimulating hormone
|
IEA
GO_REF:0000107 |
KEEP AS NON CORE |
Summary: response to follicle-stimulating hormone is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function.
Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
Supporting Evidence:
file:mouse/Hsp90aa1/Hsp90aa1-notes.md
Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations
|
|
GO:0032564
dATP binding
|
IEA
GO_REF:0000107 |
REMOVE |
Summary: dATP binding is not supported as a biologically meaningful Hsp90aa1 nucleotide-binding function.
Reason: Hsp90aa1 is an ATP-binding ATPase; automated transfer to other nucleotide-binding terms overstates the evidence.
Supporting Evidence:
file:mouse/Hsp90aa1/Hsp90aa1-notes.md
GOA terms for UTP binding, CTP binding, GTP binding, and dATP binding are not supported
|
|
GO:0032728
positive regulation of interferon-beta production
|
IEA
GO_REF:0000107 |
KEEP AS NON CORE |
Summary: positive regulation of interferon-beta production is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function.
Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
Supporting Evidence:
file:mouse/Hsp90aa1/Hsp90aa1-notes.md
Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations
|
|
GO:0032991
protein-containing complex
|
IEA
GO_REF:0000120 |
MODIFY |
Summary: Protein-containing complex is true but too generic for Hsp90aa1 chaperone complexes.
Reason: Use GO:0101031 protein folding chaperone complex for Hsp90 co-chaperone/client assemblies.
Proposed replacements:
protein folding chaperone complex
Supporting Evidence:
file:mouse/Hsp90aa1/Hsp90aa1-notes.md
functions as a dimer within dynamic co-chaperone/client complexes
file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
**Hsp90aa1 encodes HSP90α**, 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 HSP90α**, 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 HSP90α**, 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 HSP90α**, 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 HSP90α**, 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
Hsp90α knockout causes a **dramatic reduction** in the normally high steady-state level of **HIF-1α 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 eHSP90α 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 HSP90α**, 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 HSP90α**, 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 HSP90α**, 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
Hsp90α 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
Hsp90α 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
Hsp90α 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
Hsp90α 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 eHSP90α 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 eHSP90α 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 eHSP90α 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 HSP90α**, 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 eHSP90α into the wound bed** to promote wound repair
|
|
GO:0031526
brush border membrane
|
ISO
GO_REF:0000096 |
KEEP AS NON CORE |
Summary: brush border membrane is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function.
Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
Supporting Evidence:
file:mouse/Hsp90aa1/Hsp90aa1-notes.md
Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations
|
|
GO:0031625
ubiquitin protein ligase binding
|
ISO
GO_REF:0000119 |
KEEP AS NON CORE |
Summary: ubiquitin protein ligase binding is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function.
Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
Supporting Evidence:
file:mouse/Hsp90aa1/Hsp90aa1-notes.md
Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations
|
|
GO:0032564
dATP binding
|
ISO
GO_REF:0000096 |
REMOVE |
Summary: dATP binding is not supported as a biologically meaningful Hsp90aa1 nucleotide-binding function.
Reason: Hsp90aa1 is an ATP-binding ATPase; automated transfer to other nucleotide-binding terms overstates the evidence.
Supporting Evidence:
file:mouse/Hsp90aa1/Hsp90aa1-notes.md
GOA terms for UTP binding, CTP binding, GTP binding, and dATP binding are not supported
|
|
GO:0032991
protein-containing complex
|
ISO
GO_REF:0000096 |
MODIFY |
Summary: Protein-containing complex is true but too generic for Hsp90aa1 chaperone complexes.
Reason: Use GO:0101031 protein folding chaperone complex for Hsp90 co-chaperone/client assemblies.
Proposed replacements:
protein folding chaperone complex
Supporting Evidence:
file:mouse/Hsp90aa1/Hsp90aa1-notes.md
functions as a dimer within dynamic co-chaperone/client complexes
file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
**Hsp90aa1 encodes HSP90α**, a highly abundant **ATP-dependent molecular chaperone** that functions as a dimer
file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound states that orchestrate client loading, activation/maturation, and release.
|
|
GO:0032991
protein-containing complex
|
ISO
GO_REF:0000119 |
MODIFY |
Summary: Protein-containing complex is true but too generic for Hsp90aa1 chaperone complexes.
Reason: Use GO:0101031 protein folding chaperone complex for Hsp90 co-chaperone/client assemblies.
Proposed replacements:
protein folding chaperone complex
Supporting Evidence:
file:mouse/Hsp90aa1/Hsp90aa1-notes.md
functions as a dimer within dynamic co-chaperone/client complexes
file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
**Hsp90aa1 encodes HSP90α**, 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 HSP90α**, 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 HSP90α**, 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 eHSP90α 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 HSP90α**, 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
Hsp90α 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 HSP90α**, 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... |
REMOVE |
Summary: AP-3 adaptor complex binding is not supported by the cached local evidence for PMID:19010779.
Reason: 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 HSP90α**, 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
Hsp90α 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 HSP90α**, a highly abundant **ATP-dependent molecular chaperone** that functions as a dimer
file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound states that orchestrate client loading, activation/maturation, and release.
|
|
GO:0032991
protein-containing complex
|
IDA
PMID:27496612 Interaction of a Novel Chaperone PhLP2A With the Heat Shock ... |
MODIFY |
Summary: Protein-containing complex is true but too generic for Hsp90aa1 chaperone complexes.
Reason: Use GO:0101031 protein folding chaperone complex for Hsp90 co-chaperone/client assemblies.
Proposed replacements:
protein folding chaperone complex
Supporting Evidence:
file:mouse/Hsp90aa1/Hsp90aa1-notes.md
functions as a dimer within dynamic co-chaperone/client complexes
file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
**Hsp90aa1 encodes HSP90α**, 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 HSP90α**, 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-ERBα 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-ERBα 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
Hsp90α 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 HSP90α**, 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
Hsp90α 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
Hsp90α 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
Hsp90α 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
Hsp90α 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
Hsp90α 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
Hsp90α is a **cytosolic** Hsp90 isoform
|
|
GO:0030911
TPR domain binding
|
ISS
GO_REF:0000024 |
KEEP AS NON CORE |
Summary: TPR domain binding is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function.
Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
Supporting Evidence:
file:mouse/Hsp90aa1/Hsp90aa1-notes.md
Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations
|
|
GO:0006986
response to unfolded protein
|
TAS
PMID:12855682 Heat shock protein 90 as an endogenous protein enhancer of i... |
KEEP AS NON CORE |
Summary: response to unfolded protein is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function.
Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
Supporting Evidence:
file:mouse/Hsp90aa1/Hsp90aa1-notes.md
Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations
|
|
GO:0051082
unfolded protein binding
|
TAS
PMID:12855682 Heat shock protein 90 as an endogenous protein enhancer of i... |
MODIFY |
Summary: Unfolded protein binding is not the best description of Hsp90aa1. Hsp90 is an ATP-dependent foldase for selected clients rather than a generic unfolded-protein holdase.
Reason: Replace with GO:0140662 ATP-dependent protein folding chaperone, which captures the ATP-driven Hsp90 mechanism.
Proposed replacements:
ATP-dependent protein folding chaperone
Supporting Evidence:
file:mouse/Hsp90aa1/Hsp90aa1-notes.md
GO:0051082 unfolded protein binding is not the best term for Hsp90
file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
**Hsp90aa1 encodes HSP90α**, 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
Hsp90α is a **cytosolic** Hsp90 isoform
|
|
GO:0006809
nitric oxide biosynthetic process
|
TAS
PMID:12855682 Heat shock protein 90 as an endogenous protein enhancer of i... |
KEEP AS NON CORE |
Summary: nitric oxide biosynthetic process is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function.
Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
Supporting Evidence:
file:mouse/Hsp90aa1/Hsp90aa1-notes.md
Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations
|
|
GO:0030235
nitric-oxide synthase regulator activity
|
IDA
PMID:12855682 Heat shock protein 90 as an endogenous protein enhancer of i... |
KEEP AS NON CORE |
Summary: nitric-oxide synthase regulator activity is supported or plausible for a specific Hsp90aa1 client, localization, stress, or tissue context, but it is not the conserved core chaperone function.
Reason: Retain this annotation as context-specific while keeping the core review focused on ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
Supporting Evidence:
file:mouse/Hsp90aa1/Hsp90aa1-notes.md
Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations
|
|
GO:0042026
protein refolding
|
TAS
PMID:12855682 Heat shock protein 90 as an endogenous protein enhancer of i... |
MODIFY |
Summary: PMID:12855682 supports Hsp90-dependent iNOS/NO modulation, while UniProt and the Falcon synthesis support the general ATP-dependent chaperone cycle; the cited PMID does not support protein refolding specifically.
Reason: PMID:12855682 supports Hsp90-dependent modulation of iNOS/NO production, not protein refolding specifically. Replace with the core ATP-dependent protein-folding chaperone activity based on UniProt/Falcon support for the HSP90 ATPase-coupled chaperone cycle.
Proposed replacements:
ATP-dependent protein folding chaperone
Supporting Evidence:
file:mouse/Hsp90aa1/Hsp90aa1-notes.md
Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone
file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
**Hsp90aa1 encodes HSP90α**, 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.
|
The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
The UniProt entry provided (P07901) describes heat shock protein HSP 90-alpha from Mus musculus, matching the mouse gene symbol Hsp90aa1 (also referred to as Hsp90α/Hsp90a) and belonging to the cytosolic Hsp90 family. Independent mammalian isoform reviews and mouse genetics papers consistently map Hsp90α to Hsp90aa1 and distinguish it from key paralogs: Hsp90β (Hsp90ab1; constitutive; essential in early development), Grp94 (Hsp90b1; ER-resident), and TRAP1 (mitochondrial). (maiti2022cytosolichsp90isoformspecific pages 1-2, maiti2022cytosolichsp90isoformspecific pages 2-4, grad2010themolecularchaperone pages 1-2)
Hsp90aa1 encodes HSP90α, a highly abundant ATP-dependent molecular chaperone that functions as a dimer and supports proteostasis by promoting the conformational maturation/stabilization of a large set of “client” proteins, particularly signaling proteins. (oostenhawle2023organismalrolesofa pages 1-3, minari2024newinsightsinto pages 19-22)
HSP90α has the canonical Hsp90 architecture consisting of an N-terminal domain (NTD) containing the ATP-binding pocket, a middle domain (MD) involved in client interactions and ATPase regulation, and a C-terminal domain (CTD) that mediates dimerization and co-chaperone interactions (often via the C-terminal motif recognized by TPR co-chaperones). ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound states that orchestrate client loading, activation/maturation, and release. (minari2024newinsightsinto pages 19-22, wang2026targetinghsp90in pages 2-3, oostenhawle2023organismalrolesofa pages 1-3)
A useful structural depiction of the domain architecture and an integrated view of the chaperone cycle with co-chaperones is shown in the cropped figures from a recent cryoEM-focused review. (minari2024newinsightsinto media df53a9bd, minari2024newinsightsinto media 3fc408a6)
The Hsp90 system’s specificity is heavily shaped by co-chaperones:
- HOP/STI1 acts as an adaptor that can bridge Hsp70→Hsp90 client transfer (forming transfer complexes). (fedorov2025heatshockprotein pages 6-7)
- CDC37 is a kinase-directed co-chaperone that supports recruitment and maturation of a large fraction of kinase clients. (minari2024newinsightsinto pages 19-22, oostenhawle2023organismalrolesofa pages 1-3)
- AHA1 is a potent accelerator of Hsp90 ATPase activity, promoting conformational transitions and client processing. (blagg2024theroleof pages 1-2, oostenhawle2023organismalrolesofa pages 1-3)
- p23 stabilizes specific late maturation states (classically described in steroid receptor maturation complexes). (minari2024newinsightsinto pages 19-22)
Across eukaryotes, Hsp90 clients are enriched for signal transduction proteins, with prominent client classes including protein kinases and steroid/nuclear hormone receptors; recent structural work captures Hsp90 complexes with kinase and glucocorticoid receptor maturation machinery, consistent with this central role in signaling regulation rather than a narrow enzymatic substrate reaction. (minari2024newinsightsinto pages 19-22, oostenhawle2023organismalrolesofa pages 1-3)
A 2024 cryoEM-centered synthesis highlights how nucleotide state and co-chaperone binding shape Hsp90 conformations and assemblies, with structural snapshots including Hsp90:Cdc37:kinase and Hsp90:p23:glucocorticoid receptor complexes, strengthening mechanistic models of client loading and maturation. (minari2024newinsightsinto pages 19-22)
A 2023 review emphasizes that Hsp90’s functions extend beyond intracellular folding to organism-level coordination of proteostasis and stress responses, while still centering the canonical ATP-dependent cycle and the roles of Cdc37, Aha1, and p23 in regulating Hsp90 ATP hydrolysis and client processing. (oostenhawle2023organismalrolesofa pages 1-3)
A 2024 review focused on AHA1 frames it as a key ATPase accelerator whose dysregulation can promote disease states and motivates strategies to disrupt Hsp90–AHA1 interactions rather than bluntly inhibiting all Hsp90 activity. (blagg2024theroleof pages 1-2)
Hsp90α is a cytosolic Hsp90 isoform (with some functions connected to nuclear client biology via client trafficking), and is distinct from ER-localized Grp94/Hsp90b1 and mitochondrial TRAP1. (maiti2022cytosolichsp90isoformspecific pages 1-2, maiti2022cytosolichsp90isoformspecific pages 2-4)
Multiple mouse studies converge on a striking phenotype: Hsp90aa1/Hsp90α is not required for organismal viability, but is essential for male fertility.
- Hsp90aa1-null males are sterile due to a failure to produce sperm, with spermatogenesis arrest at the pachytene stage of meiosis I and progressive germ cell loss leading to seminiferous tubule depletion/azoospermia. (grad2010themolecularchaperone pages 1-2, grad2010themolecularchaperone pages 7-8)
- Pharmacologic Hsp90 inhibition during the first wave of spermatogenesis (pubertal window) can partially phenocopy aspects of this defect; one quantified observation was ~25% smaller testes than controls (n=6 treated, n=5 control; p=0.01) under a pubertal dosing regimen. (grad2010themolecularchaperone pages 7-8)
A key isoform contrast relevant to interpretation: cytosolic Hsp90β (Hsp90ab1) is described as essential for early mouse development, whereas Hsp90α is dispensable for viability but required for specific tissue function (male germline). (grad2010themolecularchaperone pages 1-2, maiti2022cytosolichsp90isoformspecific pages 8-10)
Hsp90α has a specialized role in piRNA biogenesis and germline genome defense:
- Hsp90α mutation causes a large reduction of primary and secondary piRNAs and mislocalization of MIWI2, with affected piRNA sizes reported in the ~24–32 nt range. (ichiyanagi2014hsp90αplaysan pages 1-1)
- Retrotransposon repression is perturbed at least post-transcriptionally (e.g., L1-encoded protein increase is described in the same study’s summary). (ichiyanagi2014hsp90αplaysan pages 1-2)
A mechanistically informative client relationship is the stabilization of HIF-1α:
- Hsp90α knockout causes a dramatic reduction in the normally high steady-state level of HIF-1α in testis, supporting spermatogenesis in the hypoxic testicular environment; Hsp90α also supports hypoxia-induced HIF-1α accumulation in tumor cells in that study. (tang2021heatshockprotein90alpha pages 1-2, tang2021heatshockprotein90alpha pages 6-9)
- A synthesis review likewise summarizes that Hsp90α knockout reduces HIF-1α levels in testis and connects this to spermiogenesis requirements. (maiti2022cytosolichsp90isoformspecific pages 8-10)
A distinctive and widely exploited real-world axis is secreted/extracellular HSP90α (eHSP90α):
- Keratinocytes can massively release eHSP90α into the wound bed to promote wound repair; the wound-healing activity is described as not requiring ATPase activity or dimerization, implying a noncanonical extracellular mechanism. (maiti2022cytosolichsp90isoformspecific pages 11-12, maiti2022cytosolichsp90isoformspecific pages 10-11)
- eHSP90α is implicated in tumor invasion/metastasis programs (e.g., via LRP1/CD91 signaling and protease cascades such as uPA/MMP2), and is detectable in plasma/serum as a biomarker across cancer types. (liu2024hsp90αandcell pages 5-6, maiti2022cytosolichsp90isoformspecific pages 11-12)
A major implementation of Hsp90 biology is the extensive development of inhibitors and chemical probes:
- A high-authority 2023 Nature Reviews Molecular Cell Biology resource compiles inhibitors across NTD, MD, and CTD sites and highlights co-chaperone interface disruptors (e.g., HSP90–CDC37, HSP90–HOP, HSP90–AHA1), reflecting a shift toward more selective perturbations of the Hsp90 machinery. (chiosis2023structuralandfunctional pages 1-7)
A 2024 expert analysis argues that clinical failures cannot be attributed only to “drug quality,” but reflect isoform-specific biology and dramatic tissue-to-tissue variation in Hsp90 abundance, complicating both toxicity biomarkers and maximum tolerated dose definitions. The authors report that Hsp90β depletion underlies dose-limiting toxicities, whereas Hsp90α can buffer inhibitor penetration (higher Hsp90α correlating with reduced host toxicity). (chang2024previouslyunrecognizedand pages 1-2)
A broad clinical-development synthesis describes a historical progression from pan-isoform ATPase inhibitors toward isoform-selective agents, protein–protein interaction/co-chaperone disruptors, and multi-specific strategies, reflecting expert consensus that refining selectivity is essential for therapeutic windows. (gu2025advancesinthe pages 16-16)
Hsp90 is among the most abundant proteins in cells: one review reports ~1–2% of total cellular protein in healthy cells, increasing to ~4–6% under stress (or in transformed contexts). (blagg2024theroleof pages 1-2)
Pubertal pharmacologic Hsp90 inhibition produced testes ~25% smaller than controls (n=6 treated, n=5 control; p=0.01) in one mouse study, supporting that Hsp90 activity is functionally required during spermatogenic maturation windows. (grad2010themolecularchaperone pages 7-8)
A 2024 cancer review reports that serum Hsp90α in gastric cancer achieved 52.50% sensitivity and 92.50% specificity in a cited diagnostic context, illustrating real-world diagnostic tradeoffs. (liu2024hsp90αandcell pages 5-6)
| Topic | Key points | Representative sources (with year + URL when available) |
|---|---|---|
| Identity / paralogs | Verified target: mouse Hsp90aa1 encodes cytosolic HSP90α, the stress-inducible Hsp90 isoform; distinct from cytosolic Hsp90β/Hsp90ab1 (constitutive, essential in early development), ER Grp94/Hsp90b1, and mitochondrial TRAP1. Cytosolic α/β share high sequence identity but differ in inducibility, tissue bias, and some client dependence. Hsp90α is reported at ~732 aa; Hsp90β at ~724 aa. (grad2010themolecularchaperone pages 1-2, maiti2022cytosolichsp90isoformspecific pages 1-2, maiti2022cytosolichsp90isoformspecific pages 2-4, chaudhury2025thehsp90βisoform pages 1-2) | Maiti & Picard 2022, Biomolecules, https://doi.org/10.3390/biom12091166 (maiti2022cytosolichsp90isoformspecific pages 1-2, maiti2022cytosolichsp90isoformspecific pages 2-4); Grad et al. 2010, PLoS ONE, https://doi.org/10.1371/journal.pone.0015770 (grad2010themolecularchaperone pages 1-2); Chaudhury et al. 2025, Med Res Rev, https://doi.org/10.1002/med.22114 (chaudhury2025thehsp90βisoform pages 1-2) |
| Domain architecture / ATPase cycle | HSP90α is a homodimeric ATP-dependent molecular chaperone with N-terminal ATP-binding domain (NTD), middle domain (MD) for client interaction/catalysis, and C-terminal dimerization domain (CTD); ATP binding promotes N-terminal closure, ATP hydrolysis drives conformational cycling and client maturation/release. The chaperone cycle includes open, closed, ADP-bound, and nucleotide-free states resolved in recent structural work. (minari2024newinsightsinto pages 19-22, oostenhawle2023organismalrolesofa pages 1-3, wang2026targetinghsp90in pages 2-3) | Minari et al. 2024, BioChem, https://doi.org/10.3390/biochem4020004 (minari2024newinsightsinto pages 19-22); van Oosten-Hawle 2023, Biomolecules, https://doi.org/10.3390/biom13020251 (oostenhawle2023organismalrolesofa pages 1-3); Wang et al. 2026, Mol Cancer, https://doi.org/10.1186/s12943-025-02559-5 (wang2026targetinghsp90in pages 2-3) |
| Key co-chaperones and roles | HOP/STI1 bridges Hsp70-to-Hsp90 client transfer; CDC37 recruits/stabilizes kinase clients; AHA1 is a major ATPase activator that accelerates conformational transitions and hydrolysis; p23 stabilizes closed/maturation complexes, especially with steroid receptors. Recent cryo-EM reviews depict these as modular regulators of client loading, activation, and release. (blagg2024theroleof pages 1-2, minari2024newinsightsinto pages 19-22, oostenhawle2023organismalrolesofa pages 1-3, fedorov2025heatshockprotein pages 6-7, chiosis2023structuralandfunctional pages 1-7) | Blagg & Catalfano 2024, Front Mol Neurosci, https://doi.org/10.3389/fnmol.2024.1509280 (blagg2024theroleof pages 1-2); Minari et al. 2024, https://doi.org/10.3390/biochem4020004 (minari2024newinsightsinto pages 19-22); van Oosten-Hawle 2023, https://doi.org/10.3390/biom13020251 (oostenhawle2023organismalrolesofa pages 1-3); Fedorov et al. 2025, Cells, https://doi.org/10.3390/cells14231837 (fedorov2025heatshockprotein pages 6-7); Chiosis et al. 2023, Nat Rev Mol Cell Biol, https://doi.org/10.1038/s41580-023-00640-9 (chiosis2023structuralandfunctional pages 1-7) |
| Client classes / pathways | HSP90α supports maturation/stability of broad signaling clients, especially protein kinases and steroid hormone receptors; representative pathway-linked clients include EGFR/HER2/BRAF, AKT/RAF/MET, and glucocorticoid receptor complexes. In mouse testis, a notable physiologic client relationship is HIF-1α stabilization by Hsp90α. Thus Hsp90aa1 functions broadly in proteostasis-linked signaling, cell survival, and developmental regulation rather than catalyzing a classic metabolic substrate reaction. (minari2024newinsightsinto pages 19-22, oostenhawle2023organismalrolesofa pages 1-3, wang2026targetinghsp90in pages 2-3, maiti2022cytosolichsp90isoformspecific pages 8-10, tang2021heatshockprotein90alpha pages 1-2) | Minari et al. 2024, https://doi.org/10.3390/biochem4020004 (minari2024newinsightsinto pages 19-22); van Oosten-Hawle 2023, https://doi.org/10.3390/biom13020251 (oostenhawle2023organismalrolesofa pages 1-3); Tang et al. 2021, Cancer Gene Ther, https://doi.org/10.1038/s41417-021-00316-6 (tang2021heatshockprotein90alpha pages 1-2); Maiti & Picard 2022, https://doi.org/10.3390/biom12091166 (maiti2022cytosolichsp90isoformspecific pages 8-10) |
| Subcellular localization, including extracellular HSP90α | Primary localization is cytosolic, with client-associated functions extending to the nucleus in some complexes; distinct family paralogs occupy ER (Grp94) and mitochondria (TRAP1). A major isoform-specific annotation is extracellular HSP90α (eHSP90α): secreted under stress/injury, acting through noncanonical extracellular signaling to promote cell migration, wound repair, invasion, angiogenesis, and ECM-remodeling programs. Wound-healing activity does not require ATPase activity or dimerization in the cited review. (maiti2022cytosolichsp90isoformspecific pages 1-2, maiti2022cytosolichsp90isoformspecific pages 11-12, maiti2022cytosolichsp90isoformspecific pages 19-21, maiti2022cytosolichsp90isoformspecific pages 10-11) | Maiti & Picard 2022, https://doi.org/10.3390/biom12091166 (maiti2022cytosolichsp90isoformspecific pages 1-2, maiti2022cytosolichsp90isoformspecific pages 11-12, maiti2022cytosolichsp90isoformspecific pages 19-21, maiti2022cytosolichsp90isoformspecific pages 10-11) |
| Mouse KO phenotypes and quantified findings | Global Hsp90aa1/Hsp90α loss is compatible with viability but causes male sterility due to failure of spermatogenesis, with arrest at/after pachytene of meiosis I and eventual azoospermia. Mechanistic mouse studies also show roles in piRNA biogenesis, MIWI2 localization, retrotransposon repression, and testicular HIF-1α stabilization. Quantified findings available in the gathered evidence: pharmacologic Hsp90 inhibition during the first wave of spermatogenesis produced testes ~25% smaller than controls (n=6 treated, n=5 control; p=0.01); Hsp90α mutant testes show a large reduction of 24–32-nt piRNAs and mislocalization of MIWI2; HIF-1α levels are described as dramatically reduced in Hsp90α-null testis. (maiti2022cytosolichsp90isoformspecific pages 8-10, tang2021heatshockprotein90alpha pages 1-2, grad2010themolecularchaperone pages 7-8, grad2010themolecularchaperone pages 1-2, ichiyanagi2014hsp90αplaysan pages 1-1) | Grad et al. 2010, https://doi.org/10.1371/journal.pone.0015770 (grad2010themolecularchaperone pages 7-8, grad2010themolecularchaperone pages 1-2); Ichiyanagi et al. 2014, Nucleic Acids Res, https://doi.org/10.1093/nar/gku881 (ichiyanagi2014hsp90αplaysan pages 1-1); Tang et al. 2021, https://doi.org/10.1038/s41417-021-00316-6 (tang2021heatshockprotein90alpha pages 1-2); Maiti & Picard 2022, https://doi.org/10.3390/biom12091166 (maiti2022cytosolichsp90isoformspecific pages 8-10) |
| Translational applications and statistics | Drug development: HSP90 is a major oncology target, but pan-HSP90 inhibitors have faced toxicity/efficacy limits; recent reviews emphasize domain-specific, co-chaperone-disrupting, and isoform-selective strategies. Reported statistics: Hsp90 constitutes ~1–2% of total protein in healthy cells and ~4–6% under stress/transformation; tumor cells average ~3–7% total Hsp90 versus ~2–3% in normal cells; since 1999 there have been ~200 monotherapy/combination HSP90 clinical trials, including at least 90 monotherapy trials, yet no FDA-approved systemic HSP90 inhibitor was noted in the cited 2024 review. In GI cancer, a 2023 systematic review identified 20 trials, with 17/20 performed before 2015. Biomarker: serum Hsp90α in gastric cancer showed 52.50% sensitivity and 92.50% specificity in the cited review. eHSP90α is also being explored as a prognostic biomarker and extracellular therapeutic target. (blagg2024theroleof pages 1-2, maiti2022cytosolichsp90isoformspecific pages 11-12, liu2024hsp90αandcell pages 5-6, chang2024previouslyunrecognizedand pages 1-2) | Blagg & Catalfano 2024, https://doi.org/10.3389/fnmol.2024.1509280 (blagg2024theroleof pages 1-2); Maiti & Picard 2022, https://doi.org/10.3390/biom12091166 (maiti2022cytosolichsp90isoformspecific pages 11-12); Liu & Qian 2024, Discover Oncology, https://doi.org/10.1007/s12672-024-01021-0 (liu2024hsp90αandcell pages 5-6); Chang et al. 2024, Cell Stress Chaperones, https://doi.org/10.1016/j.cstres.2024.08.002 (chang2024previouslyunrecognizedand pages 1-2) |
Table: This table summarizes core functional-annotation facts for mouse Hsp90aa1/HSP90α, including verified identity, mechanism, pathways, localization, mouse phenotypes, and translational relevance. It is designed as a compact evidence map for use in the final research report.
References
(maiti2022cytosolichsp90isoformspecific pages 1-2): Samarpan Maiti and Didier Picard. Cytosolic hsp90 isoform-specific functions and clinical significance. Biomolecules, 12:1166, Aug 2022. URL: https://doi.org/10.3390/biom12091166, doi:10.3390/biom12091166. This article has 83 citations.
(maiti2022cytosolichsp90isoformspecific pages 2-4): Samarpan Maiti and Didier Picard. Cytosolic hsp90 isoform-specific functions and clinical significance. Biomolecules, 12:1166, Aug 2022. URL: https://doi.org/10.3390/biom12091166, doi:10.3390/biom12091166. This article has 83 citations.
(grad2010themolecularchaperone pages 1-2): Iwona Grad, Christopher R. Cederroth, Joël Walicki, Corinne Grey, Sofia Barluenga, Nicolas Winssinger, Bernard De Massy, Serge Nef, and Didier Picard. The molecular chaperone hsp90α is required for meiotic progression of spermatocytes beyond pachytene in the mouse. PLoS ONE, 5:e15770, Dec 2010. URL: https://doi.org/10.1371/journal.pone.0015770, doi:10.1371/journal.pone.0015770. This article has 201 citations and is from a peer-reviewed journal.
(oostenhawle2023organismalrolesofa pages 1-3): Patricija van Oosten-Hawle. Organismal roles of hsp90. Biomolecules, 13:251, Jan 2023. URL: https://doi.org/10.3390/biom13020251, doi:10.3390/biom13020251. This article has 32 citations.
(minari2024newinsightsinto pages 19-22): Karine Minari, Vitor Hugo Balasco Serrão, and Júlio César Borges. New insights into hsp90 structural plasticity revealed by cryoem. BioChem, 4:62-89, Apr 2024. URL: https://doi.org/10.3390/biochem4020004, doi:10.3390/biochem4020004. This article has 7 citations.
(wang2026targetinghsp90in pages 2-3): Xueyi Wang, Ruiqing Ni, Xiaohui Wang, and Xun Li. Targeting hsp90 in cancer: advances in the development of inhibitors, mechanisms of action, and therapeutic applications. Molecular Cancer, Mar 2026. URL: https://doi.org/10.1186/s12943-025-02559-5, doi:10.1186/s12943-025-02559-5. This article has 1 citations and is from a highest quality peer-reviewed journal.
(minari2024newinsightsinto media df53a9bd): Karine Minari, Vitor Hugo Balasco Serrão, and Júlio César Borges. New insights into hsp90 structural plasticity revealed by cryoem. BioChem, 4:62-89, Apr 2024. URL: https://doi.org/10.3390/biochem4020004, doi:10.3390/biochem4020004. This article has 7 citations.
(minari2024newinsightsinto media 3fc408a6): Karine Minari, Vitor Hugo Balasco Serrão, and Júlio César Borges. New insights into hsp90 structural plasticity revealed by cryoem. BioChem, 4:62-89, Apr 2024. URL: https://doi.org/10.3390/biochem4020004, doi:10.3390/biochem4020004. This article has 7 citations.
(fedorov2025heatshockprotein pages 6-7): Viacheslav Fedorov, Andrey Kurkin, Georgii Fofanov, Vitaliya Kaneva, Anna Kondratenko, Stephanie E. Combs, and Maxim Shevtsov. Heat shock protein chaperome is a multi-faceted vector for tumor cell migratory activity, invasion, and metastasis. Cells, 14:1837, Nov 2025. URL: https://doi.org/10.3390/cells14231837, doi:10.3390/cells14231837. This article has 0 citations.
(blagg2024theroleof pages 1-2): Brian S. J. Blagg and Kevin C. Catalfano. The role of aha1 in cancer and neurodegeneration. Frontiers in Molecular Neuroscience, Dec 2024. URL: https://doi.org/10.3389/fnmol.2024.1509280, doi:10.3389/fnmol.2024.1509280. This article has 2 citations.
(grad2010themolecularchaperone pages 7-8): Iwona Grad, Christopher R. Cederroth, Joël Walicki, Corinne Grey, Sofia Barluenga, Nicolas Winssinger, Bernard De Massy, Serge Nef, and Didier Picard. The molecular chaperone hsp90α is required for meiotic progression of spermatocytes beyond pachytene in the mouse. PLoS ONE, 5:e15770, Dec 2010. URL: https://doi.org/10.1371/journal.pone.0015770, doi:10.1371/journal.pone.0015770. This article has 201 citations and is from a peer-reviewed journal.
(maiti2022cytosolichsp90isoformspecific pages 8-10): Samarpan Maiti and Didier Picard. Cytosolic hsp90 isoform-specific functions and clinical significance. Biomolecules, 12:1166, Aug 2022. URL: https://doi.org/10.3390/biom12091166, doi:10.3390/biom12091166. This article has 83 citations.
(ichiyanagi2014hsp90αplaysan pages 1-1): Tomoko Ichiyanagi, Kenji Ichiyanagi, Ayako Ogawa, Satomi Kuramochi-Miyagawa, Toru Nakano, Shinichiro Chuma, Hiroyuki Sasaki, and Heiichiro Udono. Hsp90α plays an important role in pirna biogenesis and retrotransposon repression in mouse. Nucleic Acids Research, 42:11903-11911, Sep 2014. URL: https://doi.org/10.1093/nar/gku881, doi:10.1093/nar/gku881. This article has 52 citations and is from a highest quality peer-reviewed journal.
(ichiyanagi2014hsp90αplaysan pages 1-2): Tomoko Ichiyanagi, Kenji Ichiyanagi, Ayako Ogawa, Satomi Kuramochi-Miyagawa, Toru Nakano, Shinichiro Chuma, Hiroyuki Sasaki, and Heiichiro Udono. Hsp90α plays an important role in pirna biogenesis and retrotransposon repression in mouse. Nucleic Acids Research, 42:11903-11911, Sep 2014. URL: https://doi.org/10.1093/nar/gku881, doi:10.1093/nar/gku881. This article has 52 citations and is from a highest quality peer-reviewed journal.
(tang2021heatshockprotein90alpha pages 1-2): Xin Tang, Cheng Chang, Michelle Hao, Mei Chen, David T. Woodley, Axel H. Schönthal, and Wei Li. Heat shock protein-90alpha (hsp90α) stabilizes hypoxia-inducible factor-1α (hif-1α) in support of spermatogenesis and tumorigenesis. Cancer Gene Therapy, 28:1058-1070, Mar 2021. URL: https://doi.org/10.1038/s41417-021-00316-6, doi:10.1038/s41417-021-00316-6. This article has 51 citations and is from a peer-reviewed journal.
(tang2021heatshockprotein90alpha pages 6-9): Xin Tang, Cheng Chang, Michelle Hao, Mei Chen, David T. Woodley, Axel H. Schönthal, and Wei Li. Heat shock protein-90alpha (hsp90α) stabilizes hypoxia-inducible factor-1α (hif-1α) in support of spermatogenesis and tumorigenesis. Cancer Gene Therapy, 28:1058-1070, Mar 2021. URL: https://doi.org/10.1038/s41417-021-00316-6, doi:10.1038/s41417-021-00316-6. This article has 51 citations and is from a peer-reviewed journal.
(maiti2022cytosolichsp90isoformspecific pages 11-12): Samarpan Maiti and Didier Picard. Cytosolic hsp90 isoform-specific functions and clinical significance. Biomolecules, 12:1166, Aug 2022. URL: https://doi.org/10.3390/biom12091166, doi:10.3390/biom12091166. This article has 83 citations.
(maiti2022cytosolichsp90isoformspecific pages 10-11): Samarpan Maiti and Didier Picard. Cytosolic hsp90 isoform-specific functions and clinical significance. Biomolecules, 12:1166, Aug 2022. URL: https://doi.org/10.3390/biom12091166, doi:10.3390/biom12091166. This article has 83 citations.
(liu2024hsp90αandcell pages 5-6): Bin Liu and Daohai Qian. Hsp90α and cell death in cancers: a review. Discover Oncology, May 2024. URL: https://doi.org/10.1007/s12672-024-01021-0, doi:10.1007/s12672-024-01021-0. This article has 12 citations.
(chiosis2023structuralandfunctional pages 1-7): Gabriela Chiosis, Chander S. Digwal, Jane B. Trepel, and Len Neckers. Structural and functional complexity of hsp90 in cellular homeostasis and disease. Nature Reviews Molecular Cell Biology, 24:797-815, Jul 2023. URL: https://doi.org/10.1038/s41580-023-00640-9, doi:10.1038/s41580-023-00640-9. This article has 194 citations and is from a domain leading peer-reviewed journal.
(chang2024previouslyunrecognizedand pages 1-2): Cheng Chang, Xin Tang, David T. Woodley, Mei Chen, and Wei Li. Previously unrecognized and potentially consequential challenges facing hsp90 inhibitors in cancer clinical trials. Cell Stress and Chaperones, 29:642-653, Oct 2024. URL: https://doi.org/10.1016/j.cstres.2024.08.002, doi:10.1016/j.cstres.2024.08.002. This article has 9 citations and is from a peer-reviewed journal.
(gu2025advancesinthe pages 16-16): Jinying Gu, Yanyi He, Chenxi He, Qiuyue Zhang, Qifei Huang, Shangjun Bai, Ruoning Wang, Qidong You, and Lei Wang. Advances in the structures, mechanisms and targeting of molecular chaperones. Signal Transduction and Targeted Therapy, Mar 2025. URL: https://doi.org/10.1038/s41392-025-02166-2, doi:10.1038/s41392-025-02166-2. This article has 63 citations and is from a peer-reviewed journal.
(chaudhury2025thehsp90βisoform pages 1-2): Subhabrata Chaudhury, Terin D'Amico, and Brian S. J. Blagg. The hsp90β isoform: an attractive target for drug development. Medicinal Research Reviews, 45:1452-1465, Apr 2025. URL: https://doi.org/10.1002/med.22114, doi:10.1002/med.22114. This article has 11 citations and is from a domain leading peer-reviewed journal.
(maiti2022cytosolichsp90isoformspecific pages 19-21): Samarpan Maiti and Didier Picard. Cytosolic hsp90 isoform-specific functions and clinical significance. Biomolecules, 12:1166, Aug 2022. URL: https://doi.org/10.3390/biom12091166, doi:10.3390/biom12091166. This article has 83 citations.
Deep research status: just deep-research-falcon mouse Hsp90aa1 --timeout 1800 --fallback perplexity-lite completed on 2026-05-03 and created Hsp90aa1-deep-research-falcon.md. Earlier short-timeout Falcon attempts failed before the required long run was used.
Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent protein-folding chaperone. UniProt describes it as a "Molecular chaperone that promotes the maturation, structural maintenance and proper regulation of specific target proteins" and links this cycle to ATPase activity.
Falcon synthesis: The Falcon report supports the same core function: Hsp90aa1 encodes cytosolic HSP90-alpha, a dimeric ATP-dependent molecular chaperone with an N-terminal ATP-binding domain, middle client-regulatory domain, and C-terminal dimerization/co-chaperone interaction domain. It emphasizes co-chaperone-regulated maturation and stabilization of selected signaling clients rather than generic protein binding [file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md "Hsp90aa1 encodes HSP90α, 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"].
Falcon non-core context: The Falcon report also supports several context-specific annotations as non-core rather than core: extracellular HSP90-alpha in wound repair/migration programs, male germline phenotypes with spermatogenesis/piRNA effects, and HIF-1alpha client stabilization in testis [file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md "Hsp90α is a cytosolic Hsp90 isoform"; file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md "Keratinocytes can massively release eHSP90α into the wound bed"; file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md "Hsp90aa1-null males are sterile"].
ATPase evidence: UniProt lists catalytic activity "ATP + H2O = ADP + phosphate + H(+)" and notes that the Hsp90 cycle is linked to ATP binding and ATP hydrolysis. Tsc1/Aha1 experiments show cochaperone control of Hsp90 ATPase activity PMID:29127155.
Client-folding evidence: Tsc1 is described as "a new co-chaperone for Hsp90 that inhibits its ATPase activity" and the paper concludes that Tsc1 facilitates "Hsp90-mediated folding of kinase and non-kinase clients" PMID:29127155.
PhLP2A evidence: The PhLP2A study reports that "PhLP2A interacts directly with Hsp90" and that "PhLP2A forms complexes with Hsp90 which are mainly localized in the cytoplasm" PMID:27496612. This supports cytoplasmic chaperone-complex annotations.
Neuronal evidence: The neuronal-polarization study used Hsp90 inhibition and reports that "Hsp90 inhibition at different developmental stages disturbs neuronal polarity formation or axonal elongation" PMID:24286867. These annotations are context-specific and non-core because the evidence is inhibitor-based and not Hsp90aa1-isoform-specific.
Extracellular evidence: The Hectd1 study states that Hectd1 is a ubiquitin ligase substrate regulator for Hsp90 and that "Extracellular Hsp90 enhances migration of multiple cell types" PMID:22431752. Secreted or membrane-associated Hsp90 annotations should therefore be kept as non-core or marked over-annotated when the GO term implies a structural ECM location.
Nitric oxide evidence: The iNOS paper states that NO synthesis from iNOS "can be profoundly modulated by heat shock protein 90 (hsp90) through protein-protein interaction" and that Hsp90 increases iNOS activity PMID:12855682. This supports nitric-oxide-synthase regulator annotations as non-core client regulation.
Curation rule: GO:0051082 unfolded protein binding is not the best term for Hsp90; GO:0140662 ATP-dependent protein folding chaperone captures the ATP-driven Hsp90 foldase mechanism. GO:0005515 protein binding is too generic for Hsp90 client or cochaperone interactions.
Nucleotide specificity rule: Hsp90aa1 is an ATP-binding ATPase; GOA terms for UTP binding, CTP binding, GTP binding, and dATP binding are not supported as core Hsp90aa1 nucleotide-binding functions and should be removed unless direct gene-specific evidence is available.
Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations. Plasma membrane, cell surface, extracellular, neuronal growth cone, myelin, sperm, and mitochondrial annotations can be context-specific but should not be treated as the core location of cytosolic Hsp90-alpha.
id: P07901
gene_symbol: Hsp90aa1
product_type: PROTEIN
status: COMPLETE
taxon:
id: NCBITaxon:10090
label: Mus musculus
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 is best curated with ATP-dependent protein folding chaperone,
ATP hydrolysis, protein folding, protein stabilization, cytosol, and nucleus terms. Many additional
GOA annotations describe specific client interactions, stress responses, secreted/membrane pools, neuronal
contexts, or orthology-transferred phenotypes; these are retained as non-core or marked over-annotated
when they are too generic or too indirect. Falcon deep research corroborates this core ATPase-driven
cytosolic HSP90-alpha cycle, while treating extracellular HSP90-alpha, male-germline phenotypes, and
individual client pathways as context-specific non-core biology unless a GOA annotation directly captures
them.
existing_annotations:
- term:
id: GO:0006457
label: protein folding
evidence_type: IBA
original_reference_id: GO_REF:0000033
review:
summary: protein folding is consistent with the core ATP-dependent Hsp90 chaperone cycle and
principal cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1 encodes HSP90α**, a highly abundant **ATP-dependent molecular chaperone** that functions
as a dimer
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound
states that orchestrate client loading, activation/maturation, and release.
- term:
id: GO:0016887
label: ATP hydrolysis activity
evidence_type: IBA
original_reference_id: GO_REF:0000033
review:
summary: ATP hydrolysis activity is consistent with the core ATP-dependent Hsp90 chaperone cycle
and principal cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1 encodes HSP90α**, a highly abundant **ATP-dependent molecular chaperone** that functions
as a dimer
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound
states that orchestrate client loading, activation/maturation, and release.
- term:
id: GO:0032991
label: protein-containing complex
evidence_type: IBA
original_reference_id: GO_REF:0000033
review:
summary: Protein-containing complex is true but too generic for Hsp90aa1 chaperone complexes.
action: MODIFY
reason: Use GO:0101031 protein folding chaperone complex for Hsp90 co-chaperone/client
assemblies.
proposed_replacement_terms:
- id: GO:0101031
label: protein folding chaperone complex
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: functions as a dimer within dynamic co-chaperone/client complexes
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1 encodes HSP90α**, a highly abundant **ATP-dependent molecular chaperone** that functions
as a dimer
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound
states that orchestrate client loading, activation/maturation, and release.
- term:
id: GO:0005886
label: plasma membrane
evidence_type: IBA
original_reference_id: GO_REF:0000033
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Keratinocytes can **massively release eHSP90α into the wound bed** to promote wound repair
- term:
id: GO:0005524
label: ATP binding
evidence_type: IBA
original_reference_id: GO_REF:0000033
review:
summary: ATP binding is consistent with the core ATP-dependent Hsp90 chaperone cycle and
principal cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1 encodes HSP90α**, a highly abundant **ATP-dependent molecular chaperone** that functions
as a dimer
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound
states that orchestrate client loading, activation/maturation, and release.
- term:
id: GO:0005829
label: cytosol
evidence_type: IBA
original_reference_id: GO_REF:0000033
review:
summary: cytosol is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal
cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Hsp90α is a **cytosolic** Hsp90 isoform
- term:
id: GO:0005634
label: nucleus
evidence_type: IBA
original_reference_id: GO_REF:0000033
review:
summary: nucleus is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal
cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Hsp90α is a **cytosolic** Hsp90 isoform
- term:
id: GO:0050821
label: protein stabilization
evidence_type: IBA
original_reference_id: GO_REF:0000033
review:
summary: protein stabilization is consistent with the core ATP-dependent Hsp90 chaperone cycle
and principal cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1 encodes HSP90α**, a highly abundant **ATP-dependent molecular chaperone** that functions
as a dimer
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound
states that orchestrate client loading, activation/maturation, and release.
- term:
id: GO:0034605
label: cellular response to heat
evidence_type: IBA
original_reference_id: GO_REF:0000033
review:
summary: cellular response to heat is consistent with the core ATP-dependent Hsp90 chaperone
cycle and principal cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- term:
id: GO:0051082
label: unfolded protein binding
evidence_type: IBA
original_reference_id: GO_REF:0000033
review:
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.
action: MODIFY
reason: Replace with GO:0140662 ATP-dependent protein folding chaperone, which captures the
ATP-driven Hsp90 mechanism.
proposed_replacement_terms:
- id: GO:0140662
label: ATP-dependent protein folding chaperone
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: GO:0051082 unfolded protein binding is not the best term for Hsp90
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1 encodes HSP90α**, a highly abundant **ATP-dependent molecular chaperone** that functions
as a dimer
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound
states that orchestrate client loading, activation/maturation, and release.
- term:
id: GO:0043025
label: neuronal cell body
evidence_type: IBA
original_reference_id: GO_REF:0000033
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0043209
label: myelin sheath
evidence_type: IBA
original_reference_id: GO_REF:0000033
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0048471
label: perinuclear region of cytoplasm
evidence_type: IBA
original_reference_id: GO_REF:0000033
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0005524
label: ATP binding
evidence_type: IEA
original_reference_id: GO_REF:0000120
review:
summary: ATP binding is consistent with the core ATP-dependent Hsp90 chaperone cycle and
principal cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1 encodes HSP90α**, a highly abundant **ATP-dependent molecular chaperone** that functions
as a dimer
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound
states that orchestrate client loading, activation/maturation, and release.
- term:
id: GO:0005634
label: nucleus
evidence_type: IEA
original_reference_id: GO_REF:0000120
review:
summary: nucleus is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal
cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Hsp90α is a **cytosolic** Hsp90 isoform
- term:
id: GO:0005737
label: cytoplasm
evidence_type: IEA
original_reference_id: GO_REF:0000120
review:
summary: cytoplasm is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal
cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Hsp90α is a **cytosolic** Hsp90 isoform
- term:
id: GO:0005739
label: mitochondrion
evidence_type: IEA
original_reference_id: GO_REF:0000120
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0005886
label: plasma membrane
evidence_type: IEA
original_reference_id: GO_REF:0000044
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0006457
label: protein folding
evidence_type: IEA
original_reference_id: GO_REF:0000002
review:
summary: protein folding is consistent with the core ATP-dependent Hsp90 chaperone cycle and
principal cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1 encodes HSP90α**, a highly abundant **ATP-dependent molecular chaperone** that functions
as a dimer
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound
states that orchestrate client loading, activation/maturation, and release.
- term:
id: GO:0016887
label: ATP hydrolysis activity
evidence_type: IEA
original_reference_id: GO_REF:0000120
review:
summary: ATP hydrolysis activity is consistent with the core ATP-dependent Hsp90 chaperone cycle
and principal cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1 encodes HSP90α**, a highly abundant **ATP-dependent molecular chaperone** that functions
as a dimer
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound
states that orchestrate client loading, activation/maturation, and release.
- term:
id: GO:0032880
label: regulation of protein localization
evidence_type: IEA
original_reference_id: GO_REF:0000117
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0042470
label: melanosome
evidence_type: IEA
original_reference_id: GO_REF:0000044
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0044183
label: protein folding chaperone
evidence_type: IEA
original_reference_id: GO_REF:0000117
review:
summary: protein folding chaperone is consistent with the core ATP-dependent Hsp90 chaperone
cycle and principal cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1 encodes HSP90α**, a highly abundant **ATP-dependent molecular chaperone** that functions
as a dimer
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound
states that orchestrate client loading, activation/maturation, and release.
- term:
id: GO:0044294
label: dendritic growth cone
evidence_type: IEA
original_reference_id: GO_REF:0000117
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0044295
label: axonal growth cone
evidence_type: IEA
original_reference_id: GO_REF:0000117
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0051082
label: unfolded protein binding
evidence_type: IEA
original_reference_id: GO_REF:0000002
review:
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.
action: MODIFY
reason: Replace with GO:0140662 ATP-dependent protein folding chaperone, which captures the
ATP-driven Hsp90 mechanism.
proposed_replacement_terms:
- id: GO:0140662
label: ATP-dependent protein folding chaperone
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: GO:0051082 unfolded protein binding is not the best term for Hsp90
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1 encodes HSP90α**, a highly abundant **ATP-dependent molecular chaperone** that functions
as a dimer
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound
states that orchestrate client loading, activation/maturation, and release.
- term:
id: GO:0140662
label: ATP-dependent protein folding chaperone
evidence_type: IEA
original_reference_id: GO_REF:0000002
review:
summary: ATP-dependent protein folding chaperone is consistent with the core ATP-dependent Hsp90
chaperone cycle and principal cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1 encodes HSP90α**, a highly abundant **ATP-dependent molecular chaperone** that functions
as a dimer
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound
states that orchestrate client loading, activation/maturation, and release.
- term:
id: GO:0005515
label: protein binding
evidence_type: IPI
original_reference_id: PMID:18474241
review:
summary: Protein binding is an uninformative physical-interaction annotation for Hsp90aa1.
action: MARK_AS_OVER_ANNOTATED
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.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: GO:0005515 protein binding is too generic for Hsp90 client or cochaperone
interactions
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Across eukaryotes, Hsp90 clients are enriched for **signal transduction proteins**
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
The Hsp90 system’s specificity is heavily shaped by co-chaperones:
- term:
id: GO:0005515
label: protein binding
evidence_type: IPI
original_reference_id: PMID:18566586
review:
summary: Protein binding is an uninformative physical-interaction annotation for Hsp90aa1.
action: MARK_AS_OVER_ANNOTATED
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.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: GO:0005515 protein binding is too generic for Hsp90 client or cochaperone
interactions
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Across eukaryotes, Hsp90 clients are enriched for **signal transduction proteins**
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
The Hsp90 system’s specificity is heavily shaped by co-chaperones:
- term:
id: GO:0001764
label: neuron migration
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0002021
label: response to dietary excess
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0002134
label: UTP binding
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
summary: UTP binding is not supported as a biologically meaningful Hsp90aa1 nucleotide-binding
function.
action: REMOVE
reason: Hsp90aa1 is an ATP-binding ATPase; automated transfer to other nucleotide-binding terms
overstates the evidence.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: GOA terms for UTP binding, CTP binding, GTP binding, and dATP binding are not
supported
- term:
id: GO:0002135
label: CTP binding
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
summary: CTP binding is not supported as a biologically meaningful Hsp90aa1 nucleotide-binding
function.
action: REMOVE
reason: Hsp90aa1 is an ATP-binding ATPase; automated transfer to other nucleotide-binding terms
overstates the evidence.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: GOA terms for UTP binding, CTP binding, GTP binding, and dATP binding are not
supported
- term:
id: GO:0002218
label: activation of innate immune response
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0002230
label: positive regulation of defense response to virus by host
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0003009
label: skeletal muscle contraction
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0003729
label: mRNA binding
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
summary: mRNA binding is too broad or indirect to be informative for Hsp90aa1 curation.
action: MARK_AS_OVER_ANNOTATED
reason: The term does not distinguish Hsp90aa1 ATP-dependent chaperone activity from generic
binding, complex membership, RNA association, or co-fractionation.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: GO:0005515 protein binding is too generic for Hsp90 client or cochaperone
interactions
- term:
id: GO:0005525
label: GTP binding
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
summary: GTP binding is not supported as a biologically meaningful Hsp90aa1 nucleotide-binding
function.
action: REMOVE
reason: Hsp90aa1 is an ATP-binding ATPase; automated transfer to other nucleotide-binding terms
overstates the evidence.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: GOA terms for UTP binding, CTP binding, GTP binding, and dATP binding are not
supported
- term:
id: GO:0005829
label: cytosol
evidence_type: IEA
original_reference_id: GO_REF:0000120
review:
summary: cytosol is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal
cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Hsp90α is a **cytosolic** Hsp90 isoform
- term:
id: GO:0009410
label: response to xenobiotic stimulus
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0009651
label: response to salt stress
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0009986
label: cell surface
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0010592
label: positive regulation of lamellipodium assembly
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0010659
label: cardiac muscle cell apoptotic process
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0010664
label: negative regulation of striated muscle cell apoptotic process
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0016323
label: basolateral plasma membrane
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0016324
label: apical plasma membrane
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Keratinocytes can **massively release eHSP90α into the wound bed** to promote wound repair
- term:
id: GO:0017098
label: sulfonylurea receptor binding
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0019903
label: protein phosphatase binding
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0030150
label: protein import into mitochondrial matrix
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0030235
label: nitric-oxide synthase regulator activity
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0030911
label: TPR domain binding
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0031012
label: extracellular matrix
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
summary: extracellular matrix is too broad or indirect to be informative for Hsp90aa1 curation.
action: MARK_AS_OVER_ANNOTATED
reason: The term does not distinguish Hsp90aa1 ATP-dependent chaperone activity from generic
binding, complex membership, RNA association, or co-fractionation.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: GO:0005515 protein binding is too generic for Hsp90 client or cochaperone
interactions
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Keratinocytes can **massively release eHSP90α into the wound bed** to promote wound repair
- term:
id: GO:0031396
label: regulation of protein ubiquitination
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0031526
label: brush border membrane
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0031625
label: ubiquitin protein ligase binding
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0032273
label: positive regulation of protein polymerization
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
summary: positive regulation of protein polymerization is a peripheral or orthology-transferred
Hsp90-associated annotation rather than a core Hsp90aa1 function.
action: KEEP_AS_NON_CORE
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.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: Many additional GOA annotations describe specific client interactions
- term:
id: GO:0032354
label: response to follicle-stimulating hormone
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0032564
label: dATP binding
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
summary: dATP binding is not supported as a biologically meaningful Hsp90aa1 nucleotide-binding
function.
action: REMOVE
reason: Hsp90aa1 is an ATP-binding ATPase; automated transfer to other nucleotide-binding terms
overstates the evidence.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: GOA terms for UTP binding, CTP binding, GTP binding, and dATP binding are not
supported
- term:
id: GO:0032728
label: positive regulation of interferon-beta production
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0032991
label: protein-containing complex
evidence_type: IEA
original_reference_id: GO_REF:0000120
review:
summary: Protein-containing complex is true but too generic for Hsp90aa1 chaperone complexes.
action: MODIFY
reason: Use GO:0101031 protein folding chaperone complex for Hsp90 co-chaperone/client
assemblies.
proposed_replacement_terms:
- id: GO:0101031
label: protein folding chaperone complex
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: functions as a dimer within dynamic co-chaperone/client complexes
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1 encodes HSP90α**, a highly abundant **ATP-dependent molecular chaperone** that functions
as a dimer
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound
states that orchestrate client loading, activation/maturation, and release.
- term:
id: GO:0034605
label: cellular response to heat
evidence_type: IEA
original_reference_id: GO_REF:0000120
review:
summary: cellular response to heat is consistent with the core ATP-dependent Hsp90 chaperone
cycle and principal cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- term:
id: GO:0035900
label: response to isolation stress
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0036120
label: cellular response to platelet-derived growth factor stimulus
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0036126
label: sperm flagellum
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1-null males are sterile** due to a failure to produce sperm
- term:
id: GO:0042220
label: response to cocaine
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: MARK_AS_OVER_ANNOTATED
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.
- term:
id: GO:0042307
label: positive regulation of protein import into nucleus
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0042802
label: identical protein binding
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
summary: identical protein binding is consistent with the core ATP-dependent Hsp90 chaperone
cycle and principal cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1 encodes HSP90α**, a highly abundant **ATP-dependent molecular chaperone** that functions
as a dimer
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound
states that orchestrate client loading, activation/maturation, and release.
- term:
id: GO:0042803
label: protein homodimerization activity
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
summary: protein homodimerization activity is consistent with the core ATP-dependent Hsp90
chaperone cycle and principal cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1 encodes HSP90α**, a highly abundant **ATP-dependent molecular chaperone** that functions
as a dimer
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound
states that orchestrate client loading, activation/maturation, and release.
- term:
id: GO:0042826
label: histone deacetylase binding
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0042981
label: regulation of apoptotic process
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0043025
label: neuronal cell body
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0043209
label: myelin sheath
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0043627
label: response to estrogen
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0044325
label: transmembrane transporter binding
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0045732
label: positive regulation of protein catabolic process
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0045793
label: positive regulation of cell size
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0048156
label: tau protein binding
evidence_type: IEA
original_reference_id: GO_REF:0000120
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0048471
label: perinuclear region of cytoplasm
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0050821
label: protein stabilization
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
summary: protein stabilization is consistent with the core ATP-dependent Hsp90 chaperone cycle
and principal cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1 encodes HSP90α**, a highly abundant **ATP-dependent molecular chaperone** that functions
as a dimer
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound
states that orchestrate client loading, activation/maturation, and release.
- term:
id: GO:0051020
label: GTPase binding
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0051022
label: Rho GDP-dissociation inhibitor binding
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0051131
label: chaperone-mediated protein complex assembly
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
summary: chaperone-mediated protein complex assembly is consistent with the core ATP-dependent
Hsp90 chaperone cycle and principal cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1 encodes HSP90α**, a highly abundant **ATP-dependent molecular chaperone** that functions
as a dimer
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound
states that orchestrate client loading, activation/maturation, and release.
- term:
id: GO:0051604
label: protein maturation
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
summary: protein maturation is consistent with the core ATP-dependent Hsp90 chaperone cycle and
principal cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- term:
id: GO:0060452
label: positive regulation of cardiac muscle contraction
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0061771
label: response to caloric restriction
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0070182
label: DNA polymerase binding
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0070301
label: cellular response to hydrogen peroxide
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0071222
label: cellular response to lipopolysaccharide
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0071260
label: cellular response to mechanical stimulus
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0071456
label: cellular response to hypoxia
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Hsp90α knockout causes a **dramatic reduction** in the normally high steady-state level of **HIF-1α
in testis**
- term:
id: GO:0097110
label: scaffold protein binding
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0097226
label: sperm mitochondrial sheath
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1-null males are sterile** due to a failure to produce sperm
- term:
id: GO:0097524
label: sperm plasma membrane
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Keratinocytes can **massively release eHSP90α into the wound bed** to promote wound repair
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1-null males are sterile** due to a failure to produce sperm
- term:
id: GO:0097718
label: disordered domain specific binding
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0098586
label: cellular response to virus
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0099072
label: regulation of postsynaptic membrane neurotransmitter receptor levels
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0101031
label: protein folding chaperone complex
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
summary: protein folding chaperone complex is consistent with the core ATP-dependent Hsp90
chaperone cycle and principal cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1 encodes HSP90α**, a highly abundant **ATP-dependent molecular chaperone** that functions
as a dimer
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound
states that orchestrate client loading, activation/maturation, and release.
- term:
id: GO:1902988
label: neurofibrillary tangle assembly
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:1905323
label: telomerase holoenzyme complex assembly
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:1990782
label: protein tyrosine kinase binding
evidence_type: IEA
original_reference_id: GO_REF:0000107
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0001764
label: neuron migration
evidence_type: ISO
original_reference_id: GO_REF:0000096
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0002134
label: UTP binding
evidence_type: ISO
original_reference_id: GO_REF:0000096
review:
summary: UTP binding is not supported as a biologically meaningful Hsp90aa1 nucleotide-binding
function.
action: REMOVE
reason: Hsp90aa1 is an ATP-binding ATPase; automated transfer to other nucleotide-binding terms
overstates the evidence.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: GOA terms for UTP binding, CTP binding, GTP binding, and dATP binding are not
supported
- term:
id: GO:0002135
label: CTP binding
evidence_type: ISO
original_reference_id: GO_REF:0000096
review:
summary: CTP binding is not supported as a biologically meaningful Hsp90aa1 nucleotide-binding
function.
action: REMOVE
reason: Hsp90aa1 is an ATP-binding ATPase; automated transfer to other nucleotide-binding terms
overstates the evidence.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: GOA terms for UTP binding, CTP binding, GTP binding, and dATP binding are not
supported
- term:
id: GO:0003729
label: mRNA binding
evidence_type: ISO
original_reference_id: GO_REF:0000096
review:
summary: mRNA binding is too broad or indirect to be informative for Hsp90aa1 curation.
action: MARK_AS_OVER_ANNOTATED
reason: The term does not distinguish Hsp90aa1 ATP-dependent chaperone activity from generic
binding, complex membership, RNA association, or co-fractionation.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: GO:0005515 protein binding is too generic for Hsp90 client or cochaperone
interactions
- term:
id: GO:0005524
label: ATP binding
evidence_type: ISO
original_reference_id: GO_REF:0000096
review:
summary: ATP binding is consistent with the core ATP-dependent Hsp90 chaperone cycle and
principal cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1 encodes HSP90α**, a highly abundant **ATP-dependent molecular chaperone** that functions
as a dimer
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound
states that orchestrate client loading, activation/maturation, and release.
- term:
id: GO:0005524
label: ATP binding
evidence_type: ISO
original_reference_id: GO_REF:0000119
review:
summary: ATP binding is consistent with the core ATP-dependent Hsp90 chaperone cycle and
principal cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1 encodes HSP90α**, a highly abundant **ATP-dependent molecular chaperone** that functions
as a dimer
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound
states that orchestrate client loading, activation/maturation, and release.
- term:
id: GO:0005525
label: GTP binding
evidence_type: ISO
original_reference_id: GO_REF:0000096
review:
summary: GTP binding is not supported as a biologically meaningful Hsp90aa1 nucleotide-binding
function.
action: REMOVE
reason: Hsp90aa1 is an ATP-binding ATPase; automated transfer to other nucleotide-binding terms
overstates the evidence.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: GOA terms for UTP binding, CTP binding, GTP binding, and dATP binding are not
supported
- term:
id: GO:0005634
label: nucleus
evidence_type: ISO
original_reference_id: GO_REF:0000096
review:
summary: nucleus is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal
cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Hsp90α is a **cytosolic** Hsp90 isoform
- term:
id: GO:0005737
label: cytoplasm
evidence_type: ISO
original_reference_id: GO_REF:0000096
review:
summary: cytoplasm is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal
cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Hsp90α is a **cytosolic** Hsp90 isoform
- term:
id: GO:0005737
label: cytoplasm
evidence_type: ISO
original_reference_id: GO_REF:0000119
review:
summary: cytoplasm is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal
cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Hsp90α is a **cytosolic** Hsp90 isoform
- term:
id: GO:0005739
label: mitochondrion
evidence_type: ISO
original_reference_id: GO_REF:0000119
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0005829
label: cytosol
evidence_type: ISO
original_reference_id: GO_REF:0000119
review:
summary: cytosol is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal
cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Hsp90α is a **cytosolic** Hsp90 isoform
- term:
id: GO:0009986
label: cell surface
evidence_type: ISO
original_reference_id: GO_REF:0000096
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Keratinocytes can **massively release eHSP90α into the wound bed** to promote wound repair
- term:
id: GO:0010592
label: positive regulation of lamellipodium assembly
evidence_type: ISO
original_reference_id: GO_REF:0000096
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0010664
label: negative regulation of striated muscle cell apoptotic process
evidence_type: ISO
original_reference_id: GO_REF:0000096
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0016323
label: basolateral plasma membrane
evidence_type: ISO
original_reference_id: GO_REF:0000096
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Keratinocytes can **massively release eHSP90α into the wound bed** to promote wound repair
- term:
id: GO:0016324
label: apical plasma membrane
evidence_type: ISO
original_reference_id: GO_REF:0000096
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Keratinocytes can **massively release eHSP90α into the wound bed** to promote wound repair
- term:
id: GO:0016887
label: ATP hydrolysis activity
evidence_type: ISO
original_reference_id: GO_REF:0000119
review:
summary: ATP hydrolysis activity is consistent with the core ATP-dependent Hsp90 chaperone cycle
and principal cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1 encodes HSP90α**, a highly abundant **ATP-dependent molecular chaperone** that functions
as a dimer
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound
states that orchestrate client loading, activation/maturation, and release.
- term:
id: GO:0017098
label: sulfonylurea receptor binding
evidence_type: ISO
original_reference_id: GO_REF:0000096
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0019903
label: protein phosphatase binding
evidence_type: ISO
original_reference_id: GO_REF:0000096
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0030235
label: nitric-oxide synthase regulator activity
evidence_type: ISO
original_reference_id: GO_REF:0000119
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0030911
label: TPR domain binding
evidence_type: ISO
original_reference_id: GO_REF:0000119
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0031012
label: extracellular matrix
evidence_type: ISO
original_reference_id: GO_REF:0000096
review:
summary: extracellular matrix is too broad or indirect to be informative for Hsp90aa1 curation.
action: MARK_AS_OVER_ANNOTATED
reason: The term does not distinguish Hsp90aa1 ATP-dependent chaperone activity from generic
binding, complex membership, RNA association, or co-fractionation.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: GO:0005515 protein binding is too generic for Hsp90 client or cochaperone
interactions
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Keratinocytes can **massively release eHSP90α into the wound bed** to promote wound repair
- term:
id: GO:0031526
label: brush border membrane
evidence_type: ISO
original_reference_id: GO_REF:0000096
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0031625
label: ubiquitin protein ligase binding
evidence_type: ISO
original_reference_id: GO_REF:0000119
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0032564
label: dATP binding
evidence_type: ISO
original_reference_id: GO_REF:0000096
review:
summary: dATP binding is not supported as a biologically meaningful Hsp90aa1 nucleotide-binding
function.
action: REMOVE
reason: Hsp90aa1 is an ATP-binding ATPase; automated transfer to other nucleotide-binding terms
overstates the evidence.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: GOA terms for UTP binding, CTP binding, GTP binding, and dATP binding are not
supported
- term:
id: GO:0032991
label: protein-containing complex
evidence_type: ISO
original_reference_id: GO_REF:0000096
review:
summary: Protein-containing complex is true but too generic for Hsp90aa1 chaperone complexes.
action: MODIFY
reason: Use GO:0101031 protein folding chaperone complex for Hsp90 co-chaperone/client
assemblies.
proposed_replacement_terms:
- id: GO:0101031
label: protein folding chaperone complex
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: functions as a dimer within dynamic co-chaperone/client complexes
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1 encodes HSP90α**, a highly abundant **ATP-dependent molecular chaperone** that functions
as a dimer
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound
states that orchestrate client loading, activation/maturation, and release.
- term:
id: GO:0032991
label: protein-containing complex
evidence_type: ISO
original_reference_id: GO_REF:0000119
review:
summary: Protein-containing complex is true but too generic for Hsp90aa1 chaperone complexes.
action: MODIFY
reason: Use GO:0101031 protein folding chaperone complex for Hsp90 co-chaperone/client
assemblies.
proposed_replacement_terms:
- id: GO:0101031
label: protein folding chaperone complex
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: functions as a dimer within dynamic co-chaperone/client complexes
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1 encodes HSP90α**, a highly abundant **ATP-dependent molecular chaperone** that functions
as a dimer
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound
states that orchestrate client loading, activation/maturation, and release.
- term:
id: GO:0036126
label: sperm flagellum
evidence_type: ISO
original_reference_id: GO_REF:0000096
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1-null males are sterile** due to a failure to produce sperm
- term:
id: GO:0042307
label: positive regulation of protein import into nucleus
evidence_type: ISO
original_reference_id: GO_REF:0000096
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0042802
label: identical protein binding
evidence_type: ISO
original_reference_id: GO_REF:0000119
review:
summary: identical protein binding is consistent with the core ATP-dependent Hsp90 chaperone
cycle and principal cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1 encodes HSP90α**, a highly abundant **ATP-dependent molecular chaperone** that functions
as a dimer
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound
states that orchestrate client loading, activation/maturation, and release.
- term:
id: GO:0042803
label: protein homodimerization activity
evidence_type: ISO
original_reference_id: GO_REF:0000119
review:
summary: protein homodimerization activity is consistent with the core ATP-dependent Hsp90
chaperone cycle and principal cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1 encodes HSP90α**, a highly abundant **ATP-dependent molecular chaperone** that functions
as a dimer
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound
states that orchestrate client loading, activation/maturation, and release.
- term:
id: GO:0042826
label: histone deacetylase binding
evidence_type: ISO
original_reference_id: GO_REF:0000119
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0043025
label: neuronal cell body
evidence_type: ISO
original_reference_id: GO_REF:0000096
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0043209
label: myelin sheath
evidence_type: ISO
original_reference_id: GO_REF:0000096
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0044325
label: transmembrane transporter binding
evidence_type: ISO
original_reference_id: GO_REF:0000096
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0045793
label: positive regulation of cell size
evidence_type: ISO
original_reference_id: GO_REF:0000096
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0048156
label: tau protein binding
evidence_type: ISO
original_reference_id: GO_REF:0000096
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0048156
label: tau protein binding
evidence_type: ISO
original_reference_id: GO_REF:0000119
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0048471
label: perinuclear region of cytoplasm
evidence_type: ISO
original_reference_id: GO_REF:0000096
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0051020
label: GTPase binding
evidence_type: ISO
original_reference_id: GO_REF:0000119
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0051022
label: Rho GDP-dissociation inhibitor binding
evidence_type: ISO
original_reference_id: GO_REF:0000096
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0070182
label: DNA polymerase binding
evidence_type: ISO
original_reference_id: GO_REF:0000119
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0097110
label: scaffold protein binding
evidence_type: ISO
original_reference_id: GO_REF:0000119
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0097226
label: sperm mitochondrial sheath
evidence_type: ISO
original_reference_id: GO_REF:0000096
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1-null males are sterile** due to a failure to produce sperm
- term:
id: GO:0097524
label: sperm plasma membrane
evidence_type: ISO
original_reference_id: GO_REF:0000096
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Keratinocytes can **massively release eHSP90α into the wound bed** to promote wound repair
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1-null males are sterile** due to a failure to produce sperm
- term:
id: GO:0097718
label: disordered domain specific binding
evidence_type: ISO
original_reference_id: GO_REF:0000119
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0099072
label: regulation of postsynaptic membrane neurotransmitter receptor levels
evidence_type: ISO
original_reference_id: GO_REF:0000096
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0101031
label: protein folding chaperone complex
evidence_type: ISO
original_reference_id: GO_REF:0000119
review:
summary: protein folding chaperone complex is consistent with the core ATP-dependent Hsp90
chaperone cycle and principal cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1 encodes HSP90α**, a highly abundant **ATP-dependent molecular chaperone** that functions
as a dimer
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound
states that orchestrate client loading, activation/maturation, and release.
- term:
id: GO:0140767
label: enzyme-substrate adaptor activity
evidence_type: ISO
original_reference_id: GO_REF:0000119
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:1990782
label: protein tyrosine kinase binding
evidence_type: ISO
original_reference_id: GO_REF:0000119
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0005654
label: nucleoplasm
evidence_type: ISO
original_reference_id: GO_REF:0000119
review:
summary: nucleoplasm is consistent with the core ATP-dependent Hsp90 chaperone cycle and
principal cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Hsp90α is a **cytosolic** Hsp90 isoform
- term:
id: GO:0044183
label: protein folding chaperone
evidence_type: IMP
original_reference_id: PMID:24286867
review:
summary: protein folding chaperone is consistent with the core ATP-dependent Hsp90 chaperone
cycle and principal cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1 encodes HSP90α**, a highly abundant **ATP-dependent molecular chaperone** that functions
as a dimer
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound
states that orchestrate client loading, activation/maturation, and release.
- term:
id: GO:0035651
label: AP-3 adaptor complex binding
evidence_type: IDA
original_reference_id: PMID:19010779
review:
summary: AP-3 adaptor complex binding is not supported by the cached local evidence for
PMID:19010779.
action: REMOVE
reason: 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.
- term:
id: GO:0002218
label: activation of innate immune response
evidence_type: ISS
original_reference_id: GO_REF:0000024
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0002230
label: positive regulation of defense response to virus by host
evidence_type: ISS
original_reference_id: GO_REF:0000024
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0005739
label: mitochondrion
evidence_type: ISS
original_reference_id: GO_REF:0000024
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0032728
label: positive regulation of interferon-beta production
evidence_type: ISS
original_reference_id: GO_REF:0000024
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0042981
label: regulation of apoptotic process
evidence_type: ISS
original_reference_id: GO_REF:0000024
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0098586
label: cellular response to virus
evidence_type: ISS
original_reference_id: GO_REF:0000024
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0005515
label: protein binding
evidence_type: IPI
original_reference_id: PMID:29916806
review:
summary: Protein binding is an uninformative physical-interaction annotation for Hsp90aa1.
action: MARK_AS_OVER_ANNOTATED
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.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: GO:0005515 protein binding is too generic for Hsp90 client or cochaperone
interactions
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Across eukaryotes, Hsp90 clients are enriched for **signal transduction proteins**
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
The Hsp90 system’s specificity is heavily shaped by co-chaperones:
- term:
id: GO:0042802
label: identical protein binding
evidence_type: IPI
original_reference_id: PMID:12885400
review:
summary: identical protein binding is consistent with the core ATP-dependent Hsp90 chaperone
cycle and principal cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1 encodes HSP90α**, a highly abundant **ATP-dependent molecular chaperone** that functions
as a dimer
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound
states that orchestrate client loading, activation/maturation, and release.
- term:
id: GO:0005737
label: cytoplasm
evidence_type: IDA
original_reference_id: PMID:27496612
review:
summary: cytoplasm is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal
cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Hsp90α is a **cytosolic** Hsp90 isoform
- term:
id: GO:0006457
label: protein folding
evidence_type: IMP
original_reference_id: PMID:27496612
review:
summary: protein folding is consistent with the core ATP-dependent Hsp90 chaperone cycle and
principal cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1 encodes HSP90α**, a highly abundant **ATP-dependent molecular chaperone** that functions
as a dimer
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound
states that orchestrate client loading, activation/maturation, and release.
- term:
id: GO:0032991
label: protein-containing complex
evidence_type: IDA
original_reference_id: PMID:27496612
review:
summary: Protein-containing complex is true but too generic for Hsp90aa1 chaperone complexes.
action: MODIFY
reason: Use GO:0101031 protein folding chaperone complex for Hsp90 co-chaperone/client
assemblies.
proposed_replacement_terms:
- id: GO:0101031
label: protein folding chaperone complex
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: functions as a dimer within dynamic co-chaperone/client complexes
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1 encodes HSP90α**, a highly abundant **ATP-dependent molecular chaperone** that functions
as a dimer
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound
states that orchestrate client loading, activation/maturation, and release.
- term:
id: GO:0034605
label: cellular response to heat
evidence_type: IMP
original_reference_id: PMID:27496612
review:
summary: cellular response to heat is consistent with the core ATP-dependent Hsp90 chaperone
cycle and principal cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- term:
id: GO:0044183
label: protein folding chaperone
evidence_type: IMP
original_reference_id: PMID:27496612
review:
summary: protein folding chaperone is consistent with the core ATP-dependent Hsp90 chaperone
cycle and principal cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1 encodes HSP90α**, a highly abundant **ATP-dependent molecular chaperone** that functions
as a dimer
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound
states that orchestrate client loading, activation/maturation, and release.
- term:
id: GO:0005515
label: protein binding
evidence_type: IPI
original_reference_id: PMID:27686098
review:
summary: Protein binding is an uninformative physical-interaction annotation for Hsp90aa1.
action: MARK_AS_OVER_ANNOTATED
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.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: GO:0005515 protein binding is too generic for Hsp90 client or cochaperone
interactions
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Across eukaryotes, Hsp90 clients are enriched for **signal transduction proteins**
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
The Hsp90 system’s specificity is heavily shaped by co-chaperones:
- term:
id: GO:0005737
label: cytoplasm
evidence_type: IDA
original_reference_id: PMID:27686098
review:
summary: cytoplasm is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal
cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Hsp90α is a **cytosolic** Hsp90 isoform
- term:
id: GO:0005515
label: protein binding
evidence_type: IPI
original_reference_id: PMID:29127155
review:
summary: Protein binding is an uninformative physical-interaction annotation for Hsp90aa1.
action: MARK_AS_OVER_ANNOTATED
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.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: GO:0005515 protein binding is too generic for Hsp90 client or cochaperone
interactions
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Across eukaryotes, Hsp90 clients are enriched for **signal transduction proteins**
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
The Hsp90 system’s specificity is heavily shaped by co-chaperones:
- term:
id: GO:0032880
label: regulation of protein localization
evidence_type: IMP
original_reference_id: PMID:24286867
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0043025
label: neuronal cell body
evidence_type: IDA
original_reference_id: PMID:24286867
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0044294
label: dendritic growth cone
evidence_type: IDA
original_reference_id: PMID:24286867
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0044295
label: axonal growth cone
evidence_type: IDA
original_reference_id: PMID:24286867
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0048471
label: perinuclear region of cytoplasm
evidence_type: IDA
original_reference_id: PMID:24286867
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0005524
label: ATP binding
evidence_type: ISS
original_reference_id: GO_REF:0000024
review:
summary: ATP binding is consistent with the core ATP-dependent Hsp90 chaperone cycle and
principal cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1 encodes HSP90α**, a highly abundant **ATP-dependent molecular chaperone** that functions
as a dimer
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound
states that orchestrate client loading, activation/maturation, and release.
- term:
id: GO:0046677
label: response to antibiotic
evidence_type: ISS
original_reference_id: GO_REF:0000024
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0005515
label: protein binding
evidence_type: IPI
original_reference_id: PMID:23184943
review:
summary: Protein binding is an uninformative physical-interaction annotation for Hsp90aa1.
action: MARK_AS_OVER_ANNOTATED
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.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: GO:0005515 protein binding is too generic for Hsp90 client or cochaperone
interactions
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Across eukaryotes, Hsp90 clients are enriched for **signal transduction proteins**
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
The Hsp90 system’s specificity is heavily shaped by co-chaperones:
- term:
id: GO:0005634
label: nucleus
evidence_type: ISS
original_reference_id: GO_REF:0000024
review:
summary: nucleus is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal
cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Hsp90α is a **cytosolic** Hsp90 isoform
- term:
id: GO:0005737
label: cytoplasm
evidence_type: ISS
original_reference_id: GO_REF:0000024
review:
summary: cytoplasm is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal
cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Hsp90α is a **cytosolic** Hsp90 isoform
- term:
id: GO:0009408
label: response to heat
evidence_type: ISS
original_reference_id: GO_REF:0000024
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0009409
label: response to cold
evidence_type: ISS
original_reference_id: GO_REF:0000024
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0005515
label: protein binding
evidence_type: IPI
original_reference_id: PMID:22431752
review:
summary: Protein binding is an uninformative physical-interaction annotation for Hsp90aa1.
action: MARK_AS_OVER_ANNOTATED
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.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: GO:0005515 protein binding is too generic for Hsp90 client or cochaperone
interactions
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Across eukaryotes, Hsp90 clients are enriched for **signal transduction proteins**
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
The Hsp90 system’s specificity is heavily shaped by co-chaperones:
- term:
id: GO:0043209
label: myelin sheath
evidence_type: HDA
original_reference_id: PMID:17634366
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0005829
label: cytosol
evidence_type: IDA
original_reference_id: PMID:17923681
review:
summary: cytosol is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal
cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Hsp90α is a **cytosolic** Hsp90 isoform
- term:
id: GO:0005829
label: cytosol
evidence_type: TAS
original_reference_id: Reactome:R-MMU-9646345
review:
summary: cytosol is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal
cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Hsp90α is a **cytosolic** Hsp90 isoform
- term:
id: GO:0005829
label: cytosol
evidence_type: TAS
original_reference_id: Reactome:R-MMU-9646359
review:
summary: cytosol is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal
cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Hsp90α is a **cytosolic** Hsp90 isoform
- term:
id: GO:0005515
label: protein binding
evidence_type: IPI
original_reference_id: PMID:23055941
review:
summary: Protein binding is an uninformative physical-interaction annotation for Hsp90aa1.
action: MARK_AS_OVER_ANNOTATED
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.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: GO:0005515 protein binding is too generic for Hsp90 client or cochaperone
interactions
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Across eukaryotes, Hsp90 clients are enriched for **signal transduction proteins**
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
The Hsp90 system’s specificity is heavily shaped by co-chaperones:
- term:
id: GO:0005515
label: protein binding
evidence_type: IPI
original_reference_id: PMID:12885400
review:
summary: Protein binding is an uninformative physical-interaction annotation for Hsp90aa1.
action: MARK_AS_OVER_ANNOTATED
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.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: GO:0005515 protein binding is too generic for Hsp90 client or cochaperone
interactions
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Across eukaryotes, Hsp90 clients are enriched for **signal transduction proteins**
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
The Hsp90 system’s specificity is heavily shaped by co-chaperones:
- term:
id: GO:0005737
label: cytoplasm
evidence_type: IDA
original_reference_id: PMID:17908927
review:
summary: cytoplasm is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal
cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Hsp90α is a **cytosolic** Hsp90 isoform
- term:
id: GO:0030911
label: TPR domain binding
evidence_type: ISS
original_reference_id: GO_REF:0000024
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0006986
label: response to unfolded protein
evidence_type: TAS
original_reference_id: PMID:12855682
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0051082
label: unfolded protein binding
evidence_type: TAS
original_reference_id: PMID:12855682
review:
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.
action: MODIFY
reason: Replace with GO:0140662 ATP-dependent protein folding chaperone, which captures the
ATP-driven Hsp90 mechanism.
proposed_replacement_terms:
- id: GO:0140662
label: ATP-dependent protein folding chaperone
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: GO:0051082 unfolded protein binding is not the best term for Hsp90
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1 encodes HSP90α**, a highly abundant **ATP-dependent molecular chaperone** that functions
as a dimer
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound
states that orchestrate client loading, activation/maturation, and release.
- term:
id: GO:0005515
label: protein binding
evidence_type: IPI
original_reference_id: PMID:12855682
review:
summary: Protein binding is an uninformative physical-interaction annotation for Hsp90aa1.
action: MARK_AS_OVER_ANNOTATED
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.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: GO:0005515 protein binding is too generic for Hsp90 client or cochaperone
interactions
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Across eukaryotes, Hsp90 clients are enriched for **signal transduction proteins**
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
The Hsp90 system’s specificity is heavily shaped by co-chaperones:
- term:
id: GO:0005829
label: cytosol
evidence_type: TAS
original_reference_id: PMID:12855682
review:
summary: cytosol is consistent with the core ATP-dependent Hsp90 chaperone cycle and principal
cytosolic/nuclear localization.
action: ACCEPT
reason: This term captures a central molecular activity, process, complex, or main localization
of Hsp90aa1.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Hsp90α is a **cytosolic** Hsp90 isoform
- term:
id: GO:0006809
label: nitric oxide biosynthetic process
evidence_type: TAS
original_reference_id: PMID:12855682
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0030235
label: nitric-oxide synthase regulator activity
evidence_type: IDA
original_reference_id: PMID:12855682
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0042026
label: protein refolding
evidence_type: TAS
original_reference_id: PMID:12855682
review:
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.
action: MODIFY
reason: PMID:12855682 supports Hsp90-dependent modulation of iNOS/NO production, not
protein refolding specifically. Replace with the core ATP-dependent protein-folding
chaperone activity based on UniProt/Falcon support for the HSP90 ATPase-coupled
chaperone cycle.
proposed_replacement_terms:
- id: GO:0140662
label: ATP-dependent protein folding chaperone
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1 encodes HSP90α**, a highly abundant **ATP-dependent molecular chaperone** that functions
as a dimer
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound
states that orchestrate client loading, activation/maturation, and release.
- term:
id: GO:0045429
label: positive regulation of nitric oxide biosynthetic process
evidence_type: IDA
original_reference_id: PMID:12855682
review:
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.
action: KEEP_AS_NON_CORE
reason: Retain this annotation as context-specific while keeping the core review focused on
ATP-dependent chaperone activity and cytosolic/nuclear chaperone complexes.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core location rule: Cytosol/cytoplasm and nucleus are core Hsp90aa1 locations'
- term:
id: GO:0045585
label: positive regulation of cytotoxic T cell differentiation
evidence_type: TAS
original_reference_id: PMID:12855682
review:
summary: Positive regulation of cytotoxic T cell differentiation is not supported by
PMID:12855682, which addresses iNOS-mediated nitric oxide production and cytotoxicity.
action: REMOVE
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.
references:
- id: GO_REF:0000002
title: Gene Ontology annotation through association of InterPro records with GO terms
findings: []
- id: GO_REF:0000024
title: Manual transfer of experimentally-verified manual GO annotation data to orthologs by
curator judgment of sequence similarity
findings: []
- id: GO_REF:0000033
title: Annotation inferences using phylogenetic trees
findings: []
- id: GO_REF:0000044
title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary
mapping, accompanied by conservative changes to GO terms applied by UniProt
findings: []
- id: GO_REF:0000096
title: Automated transfer of experimentally-verified manual GO annotation data to mouse-rat
orthologs
findings: []
- id: GO_REF:0000107
title: Automatic transfer of experimentally verified manual GO annotation data to orthologs using
Ensembl Compara
findings: []
- id: GO_REF:0000117
title: Electronic Gene Ontology annotations created by ARBA machine learning models
findings: []
- id: GO_REF:0000119
title: Automated transfer of experimentally-verified manual GO annotation data to mouse-human
orthologs
findings: []
- id: GO_REF:0000120
title: Combined Automated Annotation using Multiple IEA Methods
findings: []
- id: PMID:12855682
title: Heat shock protein 90 as an endogenous protein enhancer of inducible nitric-oxide synthase.
findings: []
- id: PMID:12885400
title: Identification of the nuclear receptor CAR:HSP90 complex in mouse liver and recruitment of
protein phosphatase 2A in response to phenobarbital.
findings: []
- id: PMID:17634366
title: Proteolipid protein is required for transport of sirtuin 2 into CNS myelin.
findings: []
- id: PMID:17908927
title: A role for AGL ubiquitination in the glycogen storage disorders of Lafora and Cori's
disease.
findings: []
- id: PMID:17923681
title: Mammalian Sir2 homolog SIRT3 regulates global mitochondrial lysine acetylation.
findings: []
- id: PMID:18474241
title: The mammalian CHORD-containing protein melusin is a stress response protein interacting
with Hsp90 and Sgt1.
findings: []
- id: PMID:18566586
title: The mammalian target of rapamycin complex 2 controls folding and stability of Akt and
protein kinase C.
findings: []
- id: PMID:19010779
title: Hermansky-Pudlak syndrome protein complexes associate with phosphatidylinositol 4-kinase
type II alpha in neuronal and non-neuronal cells.
findings: []
- id: PMID:22431752
title: Hectd1 regulates intracellular localization and secretion of Hsp90 to control cellular
behavior of the cranial mesenchyme.
findings: []
- id: PMID:23055941
title: RAB-like 2 has an essential role in male fertility, sperm intra-flagellar transport, and
tail assembly.
findings: []
- id: PMID:23184943
title: Dynamic nucleotide-dependent interactions of cysteine- and histidine-rich domain
(CHORD)-containing Hsp90 cochaperones Chp-1 and melusin with cochaperones PP5 and Sgt1.
findings: []
- id: PMID:24286867
title: Hsp90 activity is necessary to acquire a proper neuronal polarization.
findings: []
- id: PMID:27496612
title: Interaction of a Novel Chaperone PhLP2A With the Heat Shock Protein Hsp90.
findings: []
- id: PMID:27686098
title: REV-ERBα influences the stability and nuclear localization of the glucocorticoid receptor.
findings: []
- id: PMID:29127155
title: Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facilitates folding of kinase and
non-kinase clients.
findings: []
- id: PMID:29916806
title: ZMYND10 functions in a chaperone relay during axonemal dynein assembly.
findings: []
- id: Reactome:R-MMU-9646345
title: Ubiquitin binds Vcp:Hdac6:Hsp90:Hsf1
findings: []
- id: Reactome:R-MMU-9646359
title: PolyUb-Misfolded Proteins:Hdac6 dissociate from complex
findings: []
- id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
title: Hsp90aa1 curator notes
findings: []
- id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
title: Hsp90aa1 Falcon deep research report
findings:
- statement: Hsp90aa1 encodes cytosolic HSP90-alpha, a dimeric ATP-dependent molecular chaperone.
supporting_text: >-
**Hsp90aa1 encodes HSP90α**, a highly abundant **ATP-dependent molecular chaperone** that functions
as a dimer
- statement: ATP binding and hydrolysis drive the HSP90-alpha chaperone cycle for client loading
and maturation.
supporting_text: >-
ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound
states that orchestrate client loading, activation/maturation, and release.
- statement: HSP90-alpha is primarily cytosolic, with non-core extracellular and male-germline
contexts.
supporting_text: >-
Hsp90α is a **cytosolic** Hsp90 isoform
core_functions:
- description: 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.
supported_by:
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: 'Core evidence: Hsp90aa1 is the inducible cytosolic/nuclear Hsp90-alpha ATP-dependent
protein-folding chaperone'
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-notes.md
supporting_text: Tsc1 facilitates "Hsp90-mediated folding of kinase and non-kinase clients"
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
**Hsp90aa1 encodes HSP90α**, a highly abundant **ATP-dependent molecular chaperone** that functions
as a dimer
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
ATP binding and hydrolysis drive a conformational cycle through open/closed and nucleotide-bound
states that orchestrate client loading, activation/maturation, and release.
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Hsp90α is a **cytosolic** Hsp90 isoform
- reference_id: file:mouse/Hsp90aa1/Hsp90aa1-deep-research-falcon.md
supporting_text: >-
Across eukaryotes, Hsp90 clients are enriched for **signal transduction proteins**
molecular_function:
id: GO:0140662
label: ATP-dependent protein folding chaperone
directly_involved_in:
- id: GO:0006457
label: protein folding
- id: GO:0050821
label: protein stabilization
- id: GO:0051131
label: chaperone-mediated protein complex assembly
locations:
- id: GO:0005829
label: cytosol
- id: GO:0005634
label: nucleus
in_complex:
id: GO:0101031
label: protein folding chaperone complex
proposed_new_terms: []
suggested_questions: []
suggested_experiments: []