PN placement: two rows — Cytonuclear proteostasis|Chaperone|HSP70-HSP90 system integration|HSP70-HSP90 joint cochaperone|CC-TPR and PPIase domain containing and Cytonuclear proteostasis|Folding enzyme|Peptidyl-prolyl isomerases|FKBP type ; PN-node mapping: joint-cochaperone type mapped→GO:0031072 (heat shock protein binding, propagate); PPIase group/type mapped→GO:0003755 (PPIase activity, propagate; already_in_goa); subtype (mixed TPR/PPIase) no_mapping.
Consistency: Mostly consistent on the chaperone axis but a real tension on PPIase. Deep research (PMID:23737531, 35065964) and the review converge: the FKBP-like domain is a farnesyl/prenyl-binding module that does not have PPIase activity; the review REMOVEs the IEA GO:0003755 annotation. The PN row 2 / projection treat GO:0003755 as a propagatable FKBP-type activity ("already_in_goa_exact"). These directly contradict each other for AIPL1.
PN story / NEW pressure: PN projects HSP-binding (GO:0031072, more_specific_than_existing_goa). Review goes one step finer with action NEW GO:0051879 Hsp90 protein binding (verified real), backed by direct biochemistry (PMID:35065964 1:2 closed-state binding; PMID:28973376). GOA confirms no existing HSP90/heat-shock term → genuinely additive. Verdict: ADD (review's GO:0051879 ⊂ PN's GO:0031072; review is the better target).
Mapping strategy: No node change needed. The HSP-binding mapping is sound. The PPIase mapping is the problem: it is correct family-wide but wrong for AIPL1, the diverged non-catalytic member. Subtype-level no_mapping already hedges this; gene-level evidence overrides the group/type propagation.
Evidence alignment: Dossier carries no PN reference titles; review rests on AIPL1-specific primary literature (PMID:14555765, 23737531, 28973376, 35065964) — no conflict, review is better-sourced.
Verdict: Consistent on HSP90; PPIase projection over-reaches for AIPL1 (correctly REMOVE'd in review).
Recommended edits: [MAP] Flag GO:0003755 PPIase as a known false-positive for AIPL1 in the PPIase group/type mapping notes (gene-level exclusion), so the FKBP-type propagation does not re-assert PPIase activity on AIPL1.