DNAJC1 PN Consistency Notes

• Generated: 2026-06-18
• Project: PROTEOSTASIS
• Scope: PN consistency rereview against local AIGR review and available deep-research artifacts
• UniProt: Q96KC8
• AIGR review status: COMPLETE
• Review batch: proteostasis-batch-2026-06-07b
• Batch change status: added

Source Files Checked

• AIGR review YAML: present - genes/human/DNAJC1/DNAJC1-ai-review.yaml
• AIGR review HTML: present - genes/human/DNAJC1/DNAJC1-ai-review.html
• Gene notes: present - genes/human/DNAJC1/DNAJC1-notes.md
• GOA TSV: present - genes/human/DNAJC1/DNAJC1-goa.tsv
• UniProt record: present - genes/human/DNAJC1/DNAJC1-uniprot.txt
• PN dossier: projects/PROTEOSTASIS/reports/phase1_dossiers/DNAJC1.md
• PN consistency section: projects/PROTEOSTASIS/reports/phase1_dossiers/_sections/DNAJC1.md
• PN projection report: projects/PROTEOSTASIS/reports/pn_projection/pn_projected_gene_go_summary.tsv
• PN mapping audit: projects/PROTEOSTASIS/reports/pn_mapping_audit/current_mapping_scrutiny.tsv

Deep Research Files

• No *-deep-research*.md file found in this gene directory.

AIGR Review Snapshot

• Description: DNAJC1 (MTJ1/ERdj1, human homolog HTJ1) is a single-pass type I endoplasmic reticulum (and nuclear/microsomal) membrane protein of the DNAJC subfamily of J-domain co-chaperones. Its N-terminal J domain faces the ER lumen and stimulates the ATPase activity of the ER HSP70 chaperone BiP (HSPA5), while its large cytosolic C-terminal region associates with ribosomes and modulates protein synthesis, and contains two SANT (Myb-like) domains. Through its second SANT domain it binds the serpin SERPINA3/alpha-1-antichymotrypsin and the inter-alpha-trypsin inhibitor heavy chain ITIH4, modulating their protease-inhibitory/processing behavior. DNAJC1 thereby couples the ER-membrane BiP chaperone system to translation and to regulation of secreted protease/protease-inhibitor activity.
• Existing/core annotation action counts: ACCEPT: 8; KEEP_AS_NON_CORE: 12; MARK_AS_OVER_ANNOTATED: 1

PN Consistency Summary

• 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.
• 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.

Full Consistency Review

• 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.

PN Dossier Context

• review_batch: proteostasis-batch-2026-06-07b
• review_yaml: genes/human/DNAJC1/DNAJC1-ai-review.yaml
• PN workbook rows: 1

PN row 1: ER proteostasis | Chaperone | HSP70 system | J-domain containing HSP70 cochaperone

• UniProt: Q96KC8
• In branches: ER
• PN-node mapping records (path + ancestors):
  • [type] ER proteostasis|Chaperone|HSP70 system|J-domain containing HSP70 cochaperone
    status=mapped scope=ok_for_propagation_to_go GO=[GO:0030544 Hsp70 protein binding]
    rationale: In the PN hierarchy, this type denotes J-domain cochaperones assigned to the HSP70 system. Their shared mechanistic role is direct interaction with HSP70-family chaperones, making Hsp70 protein binding the most defensible GO target in the current cache.
  • [group] ER proteostasis|Chaperone|HSP70 system
    status=no_mapping scope= GO=[]
    rationale: Reviewed as a broad PN category rather than a single GO class. The member genes span multiple activities, complexes, or contexts, so direct propagation from this node would overstate the shared biology.
  • [class] ER proteostasis|Chaperone
    status=no_mapping scope= GO=[]
    rationale: Reviewed as a broad PN category rather than a single GO class. The member genes span multiple activities, complexes, or contexts, so direct propagation from this node would overstate the shared biology.
  • [branch] ER proteostasis
    status=no_mapping scope= GO=[]
    rationale: Reviewed as a top-level PN branch. This is a systems/taxonomy umbrella, not a direct GO assertion; narrower child curations carry any propagating GO mappings.

Projected GO annotations (1)

• GO:0030544 Hsp70 protein binding | scope=ok_for_propagation_to_go | goa_status=more_specific_than_existing_goa | from=ER proteostasis|Chaperone|HSP70 system|J-domain containing HSP70 cochaperone

Note

This file is generated from the current PROTEOSTASIS phase-1 dossier and local gene-review artifacts. Edit the source review, PN mapping, or dossier rather than this generated note when correcting the underlying curation.