Deep research: not run. In this environment falcon times out and perplexity-lite is not installed. This review uses the UniProt record and cached GOA-cited publications.
522 GOA rows (about 120 distinct terms) were reviewed term by term, so every row for a term gets the same action.
- The core is ATP-dependent chaperone activity [file:human/HSP90AA1/HSP90AA1-uniprot.txt "Undergoes a functional cycle that is linked to its ATPase activity which is essential for its chaperone activity."].
- ATPase regulation by co-chaperones [PMID:29127155 "Tsc1 is a new co-chaperone for Hsp90 that inhibits its ATPase activity"; PMID:27353360].
- Kinase client maturation PMID:27339980.
- TPR co-chaperone binding through the C-terminus PMID:9660753.
- Client/co-chaperone-specific roles kept as non-core: eNOS [PMID:9580552; PMID:11988487], telomerase, Tom70 mitochondrial import [PMID:12526792; PMID:15644312], TBK1/IRF3 antiviral signalling [PMID:20628368; PMID:25609812] and CMA PMID:25719862.
- About 25 Ensembl/ARBA rodent physiology transfers (responses to cocaine, salt, estrogen and so on) and the minor-nucleotide binding terms are marked over-annotated.
- 195 protein binding IPI rows are removed as uninformative.
- The minor locations (exosome, sperm, melanosome, growth cones and so on) are kept as non-core.
Reviewed the complete existing annotation inventory while retaining the imported fields and row counts. The focused changes distinguish AR evidence from GR/PR chaperone models; no new process annotation was manufactured from a necessity phenotype. Existing activities and client systems outside AR remain in scope. UniProt source-section metadata was derived with the normal backfill helper.
The 522-row review retains ATP-dependent folding, kinase client maturation, localization and peripheral client activities. The AR module must not infer a mandatory FKBP51-to-FKBP52 nuclear-import switch from generic steroid-receptor models: human prostate cancer cells retain AR nuclear entry after either FKBP depletion PMID:34057812. This is comparative co-chaperone evidence, not HSP90AA1-specific loss-of-function evidence. Corrected true-but-broad complex, cytoplasm and folding-chaperone terms to specific existing terms. Retained RNA binding based on covalent-UV human interactome studies [PMID:22658674; PMID:22681889], exosomal MHC-II association directly named in PMID:20458337, and tau aggregation supported by PMID:19363271. Other legacy negative judgments based only on indirectness or weak physiological relevance are now UNDECIDED where donor experiments were not resolved; this is an explicit evidence limit, not a claim that all transferred processes are false.
Reassessed all 26 generic transferred-claim UNDECIDED rows against traced rat/chicken donor publications. Four non-ATP nucleotide-binding claims and three migration/lamellipodium/negative-apoptosis claims are retained as peripheral conserved capabilities; primary nucleotide PDF includes explicit alpha/beta specificity comparison but is purified rat Hsp90, not a human assay. Cardiac apoptosis is refined to negative regulation. Muscle contraction and positive cardiac contraction are over-specific for overload-expression/cardioprotection evidence. Remaining 16 claims have individual uncertainty rationales about regulatory context, isoform resolution, stimulus definition or unavailable experiment details, not a demand for proof of falsity. Donor expression findings are not dismissed just because their evidence code is IEP. Normal publication fetches and a normal author-hosted PDF URL cache preserve the supporting source text.
All original annotation payloads were compared before/after and preserved; only reviewer assessments, source evidence, and the specified core-function location were changed.
Rows: GO:0005739 mitochondrion, IDA PMID:25609812 and IEA GO_REF:0000044 (SL-0173). No sub-compartment rows; qualifier located_in.
Checks:
- UniProt "Mitochondrion {ECO:0000269|PubMed:25609812}" [file:human/HSP90AA1/HSP90AA1-uniprot.txt], so the IEA mapping rests on the same paper as the IDA.
- PMID:25609812 (full text cached): "The clamp domain (R192) of Tom70 interacts with the C-terminal motif (EEVD) of Hsp90, thereby recruiting Hsp90/IRF3/Bax to mitochondria." Recruited pool on Sendai virus infection; no protease protection or sub-mitochondrial fractionation.
Outcome: both rows stay KEEP_AS_NON_CORE with the check recorded. Stays at root (TRAF3/BRAF precedent): no anchor, no outer-membrane assay.