Dnajb11 encodes ERdj3, an endoplasmic-reticulum DnaJ/Hsp40 co-chaperone that acts with the ER Hsp70 BiP/Hspa5 during secretory-protein folding, maturation, and quality control. Its conserved J-domain co-chaperone activity stimulates the Hsp70 ATPase cycle, while substrate-binding regions allow ERdj3 to participate in misfolded-protein recognition and ER chaperone-complex function. An interaction with APOBEC1 has been reported, but its in vivo relevance is doubtful: the observation used an N-terminally tagged construct that probably disrupted signal peptide-driven ER targeting, and APOBEC1 is nuclear.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005783 endoplasmic reticulum | IBA GO_REF:0000033 | ACCEPT | Summary: endoplasmic reticulum localization matches the ER-resident ERdj3/BiP cochaperone role. Reason: Dnajb11 is an ER luminal Hsp40 cochaperone; this localization is central to its function. Supporting Evidence: file:mouse/Dnajb11/Dnajb11-notes.md Core evidence: Dnajb11/ERdj3 is an endoplasmic reticulum DnaJ/Hsp40 co-chaperone file:mouse/Dnajb11/Dnajb11-deep-research-falcon.md DNAJB11/ERdj3 is a soluble ER-luminal Hsp40/J-domain co-chaperone for BiP/HSPA5 |
| GO:0051082 unfolded protein binding | IBA GO_REF:0000033 | MODIFY | Summary: Unfolded protein binding is not the preferred term for a DnaJ/Hsp40 co-chaperone; the supported activity is protein-folding chaperone function with BiP/Hsp70. Reason: GO:0044183 protein folding chaperone better captures ERdj3 co-chaperone activity and avoids the obsolete/vague unfolded-protein-binding term. Propagation Review Root cause: TERM SCOPING PROBLEM Failure modes: GRANULARITY MISMATCH Sources checked: MGI:MGI:1915088 · mouse Dnajb11 (the review target itself) SUPPORTS TRANSFER The target's own MGI record is the IBD seed, which marks experimental grounding on the target rather than circular support. The propagation is therefore not in question; the term is, because GO:0051082 has since been obsoleted and the repo reclassifies such rows to a mechanism-specific chaperone term. Proposed replacements: protein folding chaperone Supporting Evidence: file:mouse/Dnajb11/Dnajb11-notes.md GO:0051082 unfolded protein binding is not the preferred term for DnaJ co-chaperone activity file:mouse/Dnajb11/Dnajb11-deep-research-falcon.md DNAJB11/ERdj3 is a soluble ER-luminal Hsp40/J-domain co-chaperone for BiP/HSPA5 |
| GO:0051604 protein maturation | IBA GO_REF:0000033 | ACCEPT | Summary: protein maturation is consistent with ERdj3 acting with BiP during secretory-protein folding and maturation. Reason: Secretory-protein folding and maturation are core consequences of the ER Hsp40/BiP cochaperone cycle. Supporting Evidence: file:mouse/Dnajb11/Dnajb11-notes.md Core evidence: Dnajb11/ERdj3 is an endoplasmic reticulum DnaJ/Hsp40 co-chaperone file:mouse/Dnajb11/Dnajb11-deep-research-falcon.md DNAJB11/ERdj3 is a soluble ER-luminal Hsp40/J-domain co-chaperone for BiP/HSPA5 |
| GO:0051787 misfolded protein binding | IBA GO_REF:0000033 | ACCEPT | Summary: Misfolded protein binding is appropriate for ERdj3, which participates in recognition of incompletely folded secretory proteins as part of the ER chaperone machinery. Reason: The annotation captures substrate-recognition biology in the ER folding/quality-control system. Supporting Evidence: file:mouse/Dnajb11/Dnajb11-notes.md Core evidence: Dnajb11/ERdj3 is an endoplasmic reticulum DnaJ/Hsp40 co-chaperone file:mouse/Dnajb11/Dnajb11-deep-research-falcon.md DNAJB11/ERdj3 is a soluble ER-luminal Hsp40/J-domain co-chaperone for BiP/HSPA5 |
| GO:0005788 endoplasmic reticulum lumen | IEA GO_REF:0000044 | ACCEPT | Summary: endoplasmic reticulum lumen localization matches the ER-resident ERdj3/BiP cochaperone role. Reason: Dnajb11 is an ER luminal Hsp40 cochaperone; this localization is central to its function. Supporting Evidence: file:mouse/Dnajb11/Dnajb11-notes.md Core evidence: Dnajb11/ERdj3 is an endoplasmic reticulum DnaJ/Hsp40 co-chaperone file:mouse/Dnajb11/Dnajb11-deep-research-falcon.md DNAJB11/ERdj3 is a soluble ER-luminal Hsp40/J-domain co-chaperone for BiP/HSPA5 |
| GO:0006457 protein folding | IEA GO_REF:0000002 | ACCEPT | Summary: protein folding is consistent with ERdj3 acting with BiP during secretory-protein folding and maturation. Reason: Secretory-protein folding and maturation are core consequences of the ER Hsp40/BiP cochaperone cycle. Supporting Evidence: file:mouse/Dnajb11/Dnajb11-notes.md Core evidence: Dnajb11/ERdj3 is an endoplasmic reticulum DnaJ/Hsp40 co-chaperone file:mouse/Dnajb11/Dnajb11-deep-research-falcon.md DNAJB11/ERdj3 is a soluble ER-luminal Hsp40/J-domain co-chaperone for BiP/HSPA5 |
| GO:0051082 unfolded protein binding | IEA GO_REF:0000002 | MODIFY | Summary: Unfolded protein binding is not the preferred term for a DnaJ/Hsp40 co-chaperone; the supported activity is protein-folding chaperone function with BiP/Hsp70. Reason: GO:0044183 protein folding chaperone better captures ERdj3 co-chaperone activity and avoids the obsolete/vague unfolded-protein-binding term. Proposed replacements: protein folding chaperone Supporting Evidence: file:mouse/Dnajb11/Dnajb11-notes.md GO:0051082 unfolded protein binding is not the preferred term for DnaJ co-chaperone activity file:mouse/Dnajb11/Dnajb11-deep-research-falcon.md DNAJB11/ERdj3 is a soluble ER-luminal Hsp40/J-domain co-chaperone for BiP/HSPA5 |
| GO:0005515 protein binding | IPI PMID:21217698 Substrate discrimination of the chaperone BiP by autonomous ... | MARK AS OVER ANNOTATED | Summary: Protein binding is a generic interaction annotation for Dnajb11 and does not describe the actual molecular role. Reason: The evidence is better represented by ER protein-folding chaperone function, BiP/Hsp70 cochaperone activity, or specific context-dependent partners where reliable evidence exists. Supporting Evidence: file:mouse/Dnajb11/Dnajb11-notes.md GO:0005515 protein binding is too generic |
| GO:0005783 endoplasmic reticulum | ISO GO_REF:0000119 | ACCEPT | Summary: endoplasmic reticulum localization matches the ER-resident ERdj3/BiP cochaperone role. Reason: Dnajb11 is an ER luminal Hsp40 cochaperone; this localization is central to its function. Supporting Evidence: file:mouse/Dnajb11/Dnajb11-notes.md Core evidence: Dnajb11/ERdj3 is an endoplasmic reticulum DnaJ/Hsp40 co-chaperone file:mouse/Dnajb11/Dnajb11-deep-research-falcon.md DNAJB11/ERdj3 is a soluble ER-luminal Hsp40/J-domain co-chaperone for BiP/HSPA5 |
| GO:0032781 positive regulation of ATP-dependent activity | ISO GO_REF:0000119 | REMOVE | Summary: Positive regulation of ATP-dependent activity captures the DnaJ/Hsp40 role in stimulating the ATP-dependent Hsp70/BiP chaperone cycle. Reason: The local evidence supports direct stimulation of HSPA5/BiP ATPase activity by the DnaJ/Hsp40 co-chaperone. This source biological-process row should be removed rather than cross-aspect modified; the corresponding molecular function is captured in core_functions as GO:0001671 ATPase activator activity. Supporting Evidence: file:mouse/Dnajb11/Dnajb11-notes.md Core evidence: Dnajb11/ERdj3 is an endoplasmic reticulum DnaJ/Hsp40 co-chaperone file:mouse/Dnajb11/Dnajb11-deep-research-falcon.md DNAJB11/ERdj3 is a soluble ER-luminal Hsp40/J-domain co-chaperone for BiP/HSPA5 |
| GO:0001671 ATPase activator activity | ISO GO_REF:0000119 | NEW | Summary: ERdj3/Dnajb11 is a DnaJ/Hsp40 co-chaperone that stimulates the ATPase cycle of the ER Hsp70 BiP/Hspa5. Reason: This adds the molecular-function annotation corresponding to the supported co-chaperone mechanism, instead of using a cross-aspect replacement for the removed biological-process row. Supporting Evidence: file:mouse/Dnajb11/Dnajb11-notes.md Core evidence: Dnajb11/ERdj3 is an endoplasmic reticulum DnaJ/Hsp40 co-chaperone file:mouse/Dnajb11/Dnajb11-deep-research-falcon.md DNAJB11/ERdj3 is a soluble ER-luminal Hsp40/J-domain co-chaperone for BiP/HSPA5 |
| GO:0034663 endoplasmic reticulum chaperone complex | ISO GO_REF:0000096 | ACCEPT | Summary: endoplasmic reticulum chaperone complex is consistent with Dnajb11 functioning in ER chaperone assemblies with BiP and other folding factors. Reason: The complex annotation reflects the protein folding chaperone machinery rather than an unrelated complex. Supporting Evidence: file:mouse/Dnajb11/Dnajb11-notes.md Core evidence: Dnajb11/ERdj3 is an endoplasmic reticulum DnaJ/Hsp40 co-chaperone file:mouse/Dnajb11/Dnajb11-deep-research-falcon.md DNAJB11/ERdj3 is a soluble ER-luminal Hsp40/J-domain co-chaperone for BiP/HSPA5 |
| GO:0051604 protein maturation | ISO GO_REF:0000119 | ACCEPT | Summary: protein maturation is consistent with ERdj3 acting with BiP during secretory-protein folding and maturation. Reason: Secretory-protein folding and maturation are core consequences of the ER Hsp40/BiP cochaperone cycle. Supporting Evidence: file:mouse/Dnajb11/Dnajb11-notes.md Core evidence: Dnajb11/ERdj3 is an endoplasmic reticulum DnaJ/Hsp40 co-chaperone file:mouse/Dnajb11/Dnajb11-deep-research-falcon.md DNAJB11/ERdj3 is a soluble ER-luminal Hsp40/J-domain co-chaperone for BiP/HSPA5 |
| GO:0051787 misfolded protein binding | ISO GO_REF:0000119 | ACCEPT | Summary: Misfolded protein binding is appropriate for ERdj3, which participates in recognition of incompletely folded secretory proteins as part of the ER chaperone machinery. Reason: The annotation captures substrate-recognition biology in the ER folding/quality-control system. Supporting Evidence: file:mouse/Dnajb11/Dnajb11-notes.md Core evidence: Dnajb11/ERdj3 is an endoplasmic reticulum DnaJ/Hsp40 co-chaperone file:mouse/Dnajb11/Dnajb11-deep-research-falcon.md DNAJB11/ERdj3 is a soluble ER-luminal Hsp40/J-domain co-chaperone for BiP/HSPA5 |
| GO:0101031 protein folding chaperone complex | ISO GO_REF:0000119 | ACCEPT | Summary: protein folding chaperone complex is consistent with Dnajb11 functioning in ER chaperone assemblies with BiP and other folding factors. Reason: The complex annotation reflects the protein folding chaperone machinery rather than an unrelated complex. Supporting Evidence: file:mouse/Dnajb11/Dnajb11-notes.md Core evidence: Dnajb11/ERdj3 is an endoplasmic reticulum DnaJ/Hsp40 co-chaperone file:mouse/Dnajb11/Dnajb11-deep-research-falcon.md DNAJB11/ERdj3 is a soluble ER-luminal Hsp40/J-domain co-chaperone for BiP/HSPA5 |
| GO:0005783 endoplasmic reticulum | IEA GO_REF:0000107 | ACCEPT | Summary: endoplasmic reticulum localization matches the ER-resident ERdj3/BiP cochaperone role. Reason: Dnajb11 is an ER luminal Hsp40 cochaperone; this localization is central to its function. Supporting Evidence: file:mouse/Dnajb11/Dnajb11-notes.md Core evidence: Dnajb11/ERdj3 is an endoplasmic reticulum DnaJ/Hsp40 co-chaperone file:mouse/Dnajb11/Dnajb11-deep-research-falcon.md DNAJB11/ERdj3 is a soluble ER-luminal Hsp40/J-domain co-chaperone for BiP/HSPA5 |
| GO:0034663 endoplasmic reticulum chaperone complex | IEA GO_REF:0000107 | ACCEPT | Summary: endoplasmic reticulum chaperone complex is consistent with Dnajb11 functioning in ER chaperone assemblies with BiP and other folding factors. Reason: The complex annotation reflects the protein folding chaperone machinery rather than an unrelated complex. Supporting Evidence: file:mouse/Dnajb11/Dnajb11-notes.md Core evidence: Dnajb11/ERdj3 is an endoplasmic reticulum DnaJ/Hsp40 co-chaperone file:mouse/Dnajb11/Dnajb11-deep-research-falcon.md DNAJB11/ERdj3 is a soluble ER-luminal Hsp40/J-domain co-chaperone for BiP/HSPA5 |
| GO:0051604 protein maturation | IEA GO_REF:0000107 | ACCEPT | Summary: protein maturation is consistent with ERdj3 acting with BiP during secretory-protein folding and maturation. Reason: Secretory-protein folding and maturation are core consequences of the ER Hsp40/BiP cochaperone cycle. Supporting Evidence: file:mouse/Dnajb11/Dnajb11-notes.md Core evidence: Dnajb11/ERdj3 is an endoplasmic reticulum DnaJ/Hsp40 co-chaperone file:mouse/Dnajb11/Dnajb11-deep-research-falcon.md DNAJB11/ERdj3 is a soluble ER-luminal Hsp40/J-domain co-chaperone for BiP/HSPA5 |
| GO:0051787 misfolded protein binding | IEA GO_REF:0000107 | ACCEPT | Summary: Misfolded protein binding is appropriate for ERdj3, which participates in recognition of incompletely folded secretory proteins as part of the ER chaperone machinery. Reason: The annotation captures substrate-recognition biology in the ER folding/quality-control system. Supporting Evidence: file:mouse/Dnajb11/Dnajb11-notes.md Core evidence: Dnajb11/ERdj3 is an endoplasmic reticulum DnaJ/Hsp40 co-chaperone file:mouse/Dnajb11/Dnajb11-deep-research-falcon.md DNAJB11/ERdj3 is a soluble ER-luminal Hsp40/J-domain co-chaperone for BiP/HSPA5 |
| GO:0101031 protein folding chaperone complex | IEA GO_REF:0000107 | ACCEPT | Summary: protein folding chaperone complex is consistent with Dnajb11 functioning in ER chaperone assemblies with BiP and other folding factors. Reason: The complex annotation reflects the protein folding chaperone machinery rather than an unrelated complex. Supporting Evidence: file:mouse/Dnajb11/Dnajb11-notes.md Core evidence: Dnajb11/ERdj3 is an endoplasmic reticulum DnaJ/Hsp40 co-chaperone file:mouse/Dnajb11/Dnajb11-deep-research-falcon.md DNAJB11/ERdj3 is a soluble ER-luminal Hsp40/J-domain co-chaperone for BiP/HSPA5 |
| GO:0051604 protein maturation | ISS GO_REF:0000024 | ACCEPT | Summary: protein maturation is consistent with ERdj3 acting with BiP during secretory-protein folding and maturation. Reason: Secretory-protein folding and maturation are core consequences of the ER Hsp40/BiP cochaperone cycle. Supporting Evidence: file:mouse/Dnajb11/Dnajb11-notes.md Core evidence: Dnajb11/ERdj3 is an endoplasmic reticulum DnaJ/Hsp40 co-chaperone file:mouse/Dnajb11/Dnajb11-deep-research-falcon.md DNAJB11/ERdj3 is a soluble ER-luminal Hsp40/J-domain co-chaperone for BiP/HSPA5 |
| GO:0005102 signaling receptor binding | IPI PMID:20335479 Protogenin defines a transition stage during embryonic neuro... | KEEP AS NON CORE | Summary: Signaling receptor binding is supported by the PRTG/ERdj3 neurogenesis work, but it is a context-specific extracellular signaling interaction rather than the conserved core activity. Reason: Keep the annotation because the PRTG ligand evidence is direct, but do not elevate it above the ER chaperone function. Supporting Evidence: file:mouse/Dnajb11/Dnajb11-notes.md identifies ERdj3 as a PRTG ligand |
| GO:0005615 extracellular space | IDA PMID:20335479 Protogenin defines a transition stage during embryonic neuro... | KEEP AS NON CORE | Summary: Extracellular-space detection is supported in the PRTG context, where purified ERdj3 acts outside cells, but Dnajb11 is primarily an ER luminal chaperone. Reason: This context-specific localization should be retained without making extracellular space the core localization. Supporting Evidence: file:mouse/Dnajb11/Dnajb11-notes.md Addition of purified ERdj3 protein into the P19 differentiation assay reduced neurogenesis file:mouse/Dnajb11/Dnajb11-deep-research-falcon.md stress-induced secretion |
| GO:0050768 negative regulation of neurogenesis | ISO PMID:20335479 Protogenin defines a transition stage during embryonic neuro... | KEEP AS NON CORE | Summary: Negative regulation of neurogenesis is supported by the PRTG/ERdj3 perturbation study but is downstream and context-specific. Reason: The annotation reflects a developmental outcome of extracellular ERdj3/PRTG signaling, not the conserved molecular function of the gene. Supporting Evidence: file:mouse/Dnajb11/Dnajb11-notes.md reduced neurogenesis |
| GO:0050768 negative regulation of neurogenesis | IMP PMID:20335479 Protogenin defines a transition stage during embryonic neuro... | KEEP AS NON CORE | Summary: Negative regulation of neurogenesis is supported by the PRTG/ERdj3 perturbation study but is downstream and context-specific. Reason: The annotation reflects a developmental outcome of extracellular ERdj3/PRTG signaling, not the conserved molecular function of the gene. Supporting Evidence: file:mouse/Dnajb11/Dnajb11-notes.md reduced neurogenesis |
| GO:0050768 negative regulation of neurogenesis | IPI PMID:20335479 Protogenin defines a transition stage during embryonic neuro... | KEEP AS NON CORE | Summary: Negative regulation of neurogenesis is supported by the PRTG/ERdj3 perturbation study but is downstream and context-specific. Reason: The annotation reflects a developmental outcome of extracellular ERdj3/PRTG signaling, not the conserved molecular function of the gene. Supporting Evidence: file:mouse/Dnajb11/Dnajb11-notes.md reduced neurogenesis |
| GO:0005634 nucleus | IDA PMID:11584023 A DnaJ protein, apobec-1-binding protein-2, modulates apolip... | UNDECIDED | Summary: Cannot be adjudicated here: PMID:11584023 is cached abstract-only. Prior observation, not a verdict: The PMID:11584023 nuclear localization came from an N-terminal GFP-tagged construct that UniProt cautions likely disrupted ER targeting. Reason: PMID:11584023 is cached abstract-only, so the curator's experimental evidence cannot be inspected here; per CLAUDE.md an experimental annotation is not overruled on that basis. Recorded observation, not a verdict: The reported nucleus localization is not reliable evidence for endogenous Dnajb11 localization because the tag likely affected signal peptide-driven ER targeting. Supporting Evidence: file:mouse/Dnajb11/Dnajb11-uniprot.txt PubMed:11584023 reported a cytosolic, as well as nuclear subcellular location. This result was obtained using an N-terminally GFP-tagged construct which most probably affected signal peptide-driven targeting to the ER. |
| GO:0005737 cytoplasm | IDA PMID:11584023 A DnaJ protein, apobec-1-binding protein-2, modulates apolip... | UNDECIDED | Summary: Cannot be adjudicated here: PMID:11584023 is cached abstract-only. Prior observation, not a verdict: The PMID:11584023 cytoplasmic localization came from an N-terminal GFP-tagged construct that UniProt cautions likely disrupted ER targeting. Reason: PMID:11584023 is cached abstract-only, so the curator's experimental evidence cannot be inspected here; per CLAUDE.md an experimental annotation is not overruled on that basis. Recorded observation, not a verdict: The reported cytoplasm localization is not reliable evidence for endogenous Dnajb11 localization because the tag likely affected signal peptide-driven ER targeting. Supporting Evidence: file:mouse/Dnajb11/Dnajb11-uniprot.txt PubMed:11584023 reported a cytosolic, as well as nuclear subcellular location. This result was obtained using an N-terminally GFP-tagged construct which most probably affected signal peptide-driven targeting to the ER. |
| GO:0005634 nucleus | ISO GO_REF:0000008 | REMOVE | Summary: The APOBEC1-associated nuclear localization is undermined by UniProt's caution that the N-terminal GFP tag likely disrupted ER targeting. Reason: Do not retain this transferred nucleus annotation because the underlying localization evidence is likely artifactual for endogenous Dnajb11. Supporting Evidence: file:mouse/Dnajb11/Dnajb11-uniprot.txt As a consequence, the in vivo revelance of the observed interaction with APOBEC1, a nuclear protein, is dubious. |
| GO:0005737 cytoplasm | ISO GO_REF:0000008 | REMOVE | Summary: The APOBEC1-associated cytoplasmic localization is undermined by UniProt's caution that the N-terminal GFP tag likely disrupted ER targeting. Reason: Do not retain this transferred cytoplasm annotation because the underlying localization evidence is likely artifactual for endogenous Dnajb11. Supporting Evidence: file:mouse/Dnajb11/Dnajb11-uniprot.txt As a consequence, the in vivo revelance of the observed interaction with APOBEC1, a nuclear protein, is dubious. |
| GO:0016556 mRNA modification | ISO GO_REF:0000008 | REMOVE | Summary: The APOBEC1/mRNA-editing role from PMID:11584023 is undermined by UniProt's caution that the construct likely disrupted ER targeting, making the in vivo relevance of the observed APOBEC1 interaction dubious. Reason: The endogenous protein is an ER-luminal BiP co-chaperone, and local evidence does not support retaining an APOBEC1-dependent mRNA-editing role. Supporting Evidence: file:mouse/Dnajb11/Dnajb11-uniprot.txt As a consequence, the in vivo revelance of the observed interaction with APOBEC1, a nuclear protein, is dubious. |
| GO:0051082 unfolded protein binding | IDA PMID:11584023 A DnaJ protein, apobec-1-binding protein-2, modulates apolip... | MODIFY | Summary: Unfolded protein binding is not the preferred term for a DnaJ/Hsp40 co-chaperone; the supported activity is protein-folding chaperone function with BiP/Hsp70. Reason: GO:0044183 protein folding chaperone better captures ERdj3 co-chaperone activity and avoids the obsolete/vague unfolded-protein-binding term. Proposed replacements: protein folding chaperone Supporting Evidence: file:mouse/Dnajb11/Dnajb11-notes.md GO:0051082 unfolded protein binding is not the preferred term for DnaJ co-chaperone activity file:mouse/Dnajb11/Dnajb11-deep-research-falcon.md DNAJB11/ERdj3 is a soluble ER-luminal Hsp40/J-domain co-chaperone for BiP/HSPA5 |
| GO:0005515 protein binding | IPI PMID:11584023 A DnaJ protein, apobec-1-binding protein-2, modulates apolip... | REMOVE | Summary: Protein binding is a generic interaction annotation for Dnajb11 and does not describe the actual molecular role. Reason: The evidence is better represented by ER protein-folding chaperone function and BiP/Hsp70 cochaperone activity; UniProt cautions that the in vivo relevance of the APOBEC1 interaction observed in PMID:11584023 is dubious. Supporting Evidence: file:mouse/Dnajb11/Dnajb11-notes.md GO:0005515 protein binding is too generic |
| GO:0016556 mRNA modification | IDA PMID:11584023 A DnaJ protein, apobec-1-binding protein-2, modulates apolip... | UNDECIDED | Summary: Cannot be adjudicated here: PMID:11584023 is cached abstract-only. Prior observation, not a verdict: The APOBEC1/mRNA-editing role from PMID:11584023 is undermined by UniProt's caution that the construct likely disrupted ER targeting, making the in vivo relevance of the observed APOBEC1 interaction dubious. Reason: PMID:11584023 is cached abstract-only, so the curator's experimental evidence cannot be inspected here; per CLAUDE.md an experimental annotation is not overruled on that basis. Recorded observation, not a verdict: The endogenous protein is an ER-luminal BiP co-chaperone, and local evidence does not support retaining an APOBEC1-dependent mRNA-editing role. Supporting Evidence: file:mouse/Dnajb11/Dnajb11-uniprot.txt As a consequence, the in vivo revelance of the observed interaction with APOBEC1, a nuclear protein, is dubious. |
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