Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Gene Ontology annotation based on curation of immunofluorescence data
Combined Automated Annotation using Multiple IEA Methods
Falcon deep research synthesis for AHSA1
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AHSA1/AHA1 is a cytosolic HSP90 co-chaperone and the most potent known stimulator of HSP90 ATP hydrolysis, with recent work defining ICD, NxNNWHW, and RKxK motif contributions.
"AHSA1 (also called AHA1) encodes a conserved HSP90 co-chaperone that is the most potent known stimulator of HSP90 ATP hydrolysis."
Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1.
Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone.
A yeast 2-hybrid analysis of human GTP cyclohydrolase I protein interactions.
Large-scale proteomics and phosphoproteomics of urinary exosomes.
A proteomic investigation of ligand-dependent HSP90 complexes reveals CHORDC1 as a novel ADP-dependent HSP90-interacting protein.
CHIP participates in protein triage decisions by preferentially ubiquitinating Hsp70-bound substrates.
A quantitative chaperone interaction network reveals the architecture of cellular protein homeostasis pathways.
E-cadherin interactome complexity and robustness resolved by quantitative proteomics.
Middle domain of human Hsp90 isoforms differentially binds Aha1 in human cells and alters Hsp90 activity in yeast.
The FNIP co-chaperones decelerate the Hsp90 chaperone cycle and enhance drug binding.
Tumor suppressor Tsc1 is a new Hsp90 co-chaperone that facilitates folding of kinase and non-kinase clients.
Structure and pro-toxic mechanism of the human Hsp90/PPIase/Tau complex.
Aha1 Exhibits Distinctive Dynamics Behavior and Chaperone-Like Activity.
OpenCell: Endogenous tagging for the cartography of human cellular organization.
Human Aha1's N-terminal extension confers it holdase activity in vitro.
Recruitment of Ahsa1 to Hsp90 is regulated by a conserved peptide that inhibits ATPase stimulation.
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AHSA1 contains a metazoan-specific intrinsic chaperone domain (ICD, aa ~1-20) that dampens ATPase stimulation by interfering with NxNNWHW function and controls regulated recruitment to HSP90
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NxNNWHW and RKxK are conserved motifs central to AHSA1 ATPase stimulatory function; RKxK stabilizes the HSP90 catalytic loop to facilitate ATP hydrolysis
Aha1 regulates Hsp90's conformation and function in a stoichiometry-dependent way.
HSP90 and Aha1 modulate microRNA maturation through promoting the folding of Dicer1.
AHSA1 is a promising therapeutic target for cellular proliferation and proteasome inhibitor resistance in multiple myeloma.
The role of Aha1 in cancer and neurodegeneration.
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Review framing Aha1 dysregulation as a driver of disease phenotypes in cancer, cystic fibrosis, and neurodegeneration via HSP90 proteostasis network imbalance
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HSP90/Aha1 protein-protein interaction interface proposed as a therapeutic target with potential to spare essential baseline HSP90 functions
Structural and functional complexity of HSP90 in cellular homeostasis and disease.