## DNAJC1
- **UniProt:** Q96KC8 (MTJ1/ERdj1/HTJ1) · **batch:** proteostasis-batch-2026-06-07b · **review status:** COMPLETE
- **PN placement:** `ER proteostasis|Chaperone|HSP70 system|J-domain containing HSP70 cochaperone` (branch ER) ; **PN-node mapping:** type=mapped, scope=ok_for_propagation_to_go, GO:0030544 Hsp70 protein binding (parents no_mapping)
- **Consistency:** Consistent on the chaperone axis. Notes/YAML describe a single-pass type-I ER-membrane J-protein whose lumenal J domain stimulates BiP/HSPA5 ATPase (GO:0001671 TAS PMID:14668352, ACCEPT/core) and binds BiP (GO:0051087 IEA, ACCEPT). PN "J-domain HSP70 cochaperone" type fits. The review adds two non-chaperone facets PN does not capture (ribosome-associated translation modulation; SANT2-mediated serpin/protease regulation — GO:0045861, GO:0050708) — these are extra, not contradictory.
- **PN story / NEW pressure:** PN's HSP70-binding claim is captured (GO:0001671 ATPase activator + GO:0051087 chaperone binding, both ACCEPT/core). PN-projected GO:0030544 (verified real) is narrower than GO:0051087 — defensible specialization since DNAJC1 has TAS evidence its J domain stimulates BiP. No NEW GO term needed for proteostasis. Verdict: already captured.
- **Mapping strategy:** GO:0030544 mapping is appropriate and does not over-reach — DNAJC1 has direct (TAS) BiP-ATPase-stimulation evidence, a genuine HSP70-cochaperone MF (not an over-broad holdase/unfolded-protein-binding claim). Note the partner is ER HSP70 BiP, consistent with "Hsp70 protein binding."
- **Evidence alignment:** Core PMID:14668352 (J-domain→BiP ATPase; SANT2-serpin) and PMID:16271702 (ITIH4) carry the function; PN supplies path context. No conflict; review's many HT-interactome PMIDs (CFTR, RMND1, etc.) are non-core and absent from PN.
- **Verdict:** CONSISTENT — GO:0030544 a sound narrower specialization of the verified J-domain→BiP ATPase-stimulating MF; node mapping correct.