## CANX
- **UniProt:** P27824 · **batch:** proteostasis-batch-2026-06-06 · **review status:** COMPLETE (exhaustive; ~90 annotations reviewed, notes present)
- **PN placement:** `ER proteostasis|Glycoproteostasis|N-glycosylation system|Lectin chaperone` ; **PN-node mapping:** type (Lectin chaperone)→no_mapping; group (N-glycosylation system)→GO:0006487 protein N-linked glycosylation (mapped/ok_for_propagation); class/branch→no_mapping.
- **Consistency:** Internally consistent on biology — review, notes, and PN all describe calnexin as the membrane-bound lectin chaperone of the CNX/CRT cycle binding monoglucosylated N-glycans. BUT the PROJECTED GO term is inconsistent with calnexin's molecular role (see below).
- **PN story / NEW pressure:** GO:0006487 is VERIFIED real but its definition is "a process in which a carbohydrate unit is ADDED to a protein via the N4 atom of asparagine" — i.e. the catalytic glycan-transfer step (OST machinery). Calnexin RECOGNIZES/BINDS the already-installed glycan; it does not perform N-glycosylation. The review correctly captures the true function as GO:0030246 carbohydrate binding, GO:0044183 protein folding chaperone, GO:0034975 protein folding in ER, GO:0036503 ERAD. GO:0006487 is absent from CANX GOA (confirmed). Conclude: OVER-REACHES — projecting GO:0006487 to a lectin chaperone is a category error from a mixed "N-glycosylation system" container node; do NOT add.
- **Mapping strategy:** The group node "N-glycosylation system" lumps the OST/glycan-installing/processing enzymes with the lectin chaperones that read the glycan; a single GO:0006487 mapping over-annotates the lectin-chaperone members (CANX, CALR). Recommend the lectin-chaperone TYPE node carry a binding/chaperone mapping (e.g. GO:0030246 carbohydrate binding or GO:0006457/GO:0036503) rather than inheriting the enzymatic process term.
- **Evidence alignment:** PN node carries no reference titles; review is heavily evidenced (PMID:22314232 palmitoyl-translocon, PMID:8136357 cloning/Ca2+, PMID:35948544/Reactome MHC-I, many IDA ER-localization). No citation conflict, but no shared evidence supports the N-glycosylation-process claim.
- **Verdict:** OVER-REACHES — projected GO:0006487 mis-assigns an enzymatic process to a lectin chaperone; reject for CANX (true function already captured). **Recommended edits:** [MAP] do not propagate GO:0006487 to CANX; re-map the "Lectin chaperone" type node to a binding/chaperone term (e.g. GO:0030246 carbohydrate binding / GO:0036503 ERAD pathway).