DNAJB2 is human HGNC:5228, UniProt P25686, also called HSJ1/HSPF3. The review preserves 41 historical source assertions and separately incorporates five newly retrieved GOA assertion triples. The current normal GOA export is used for validation; the historical export preserves the original bytes. Six historical triples absent from the current export are retained with retirement metadata, without changing their scientific assessments. The source provenance lists the exact 41-to-40-triple transition and five current additions. Review actions apply to biological claims and retain source-specific limitations.
The official UniProt record identifies P25686-3 as the displayed 324-residue HSJ1b product and P25686-2 as the 277-residue HSJ1a product. Both retain the J domain and two ubiquitin-interacting motifs. HSJ1a retains canonical residues 1–274, replaces GGR at 275–277 with DVF, and lacks residues 278–324, including the long product’s prenylated Cys321. Product identity was checked against the official individual FASTAs. This does not authenticate every older named HSJ1a expression clone as the exact modern 277-residue sequence.
The GO:0140309 definition requires prevention of aggregation plus delivery to an acceptor or location. Binding an unfolded protein alone is insufficient. GO:0042026 requires restoration of biological activity, whereas GO:0140036 combines modification-dependent recognition with an adaptor role. These distinctions separate ATPase activation, antiaggregation, functional recovery and client sorting.
| Source | Evidence inspected and interpretation | Access and construct limits |
|---|---|---|
| PMID:7957263(https://pubmed.ncbi.nlm.nih.gov/7957263/) | Both HSJ1 products stimulate mammalian-brain Hsc70 ATP hydrolysis without increasing ADP release. | Complete verified primary abstract; full original Methods unavailable. No more precise animal origin or construct endpoints inferred. |
| PMID:22219199(https://pmc.ncbi.nlm.nih.gov/articles/PMC3285371/) | Purified human HSP70, GST-controlled pull-down, NMR and phosphate-release assays support J-domain binding and ATPase activation. | Separately recovered full original; normal cache remains abstract-only. Historical HSJ1a 1–274 and isolated J-domain constructs are not the complete current 277-residue product. |
| PMID:21625540(https://doi.org/10.1371/journal.pone.0019763) | Purified UIM 206–272 binds diubiquitin by ITC/NMR. Cellular J-domain/HSP70 and UIM mutants separate Atx3 degradation from preservation of ubiquitinated Atx3. | Full original target Results and relevant Methods inspected. Co-complex association does not prove every direct interface. The historical self-product WITH/FROM pair was not resolved in this study. |
| PMID:15936278(https://doi.org/10.1016/j.cub.2005.04.058) | Primary abstract explicitly combines ubiquitinated-client binding, aggregation prevention and proteasome sorting. This supplies the delivery component for the holdase core and historical refinements. | Abstract-only; no detailed purified transport assay or construct identity is inferred. |
| PMID:28031292(https://doi.org/10.1093/hmg/ddw420) | CK2/UIM2 phosphorylation and UIM controls alter client association; human SK-N-SH imaging distinguishes HSJ1a from ER-associated HSJ1b. | Full target Results/Methods independently read. DNAJB2 is the kinase substrate. Client activity/abundance is not a refolding assay, and no new target ATPase assay was identified in the inspected Methods. |
| PMID:21231916(https://doi.org/10.1042/BJ20101247) | DNAJB2a suppresses HDQ74 and heat-induced luciferase aggregation but does not improve luciferase refolding. Figure 2C has an actual DNAJB2a experimental-localization panel, distinct from its prediction column. | Normal cache is abstract-only. The genuine HAL accepted manuscript was read using OCR because its PDF text encoding is broken; key Results and the localization panel were visually checked. Human-reference cDNA constructs were tested in HEK293/hamster O23 cells. Purified DNAJB1 assays in the same paper are not transferred to DNAJB2. |
| PMID:20889486(https://pubmed.ncbi.nlm.nih.gov/20889486/) | In human SK-N-SH cells, HSJ1a restores mutant Parkin recruitment and mitophagy-related function in a J-domain-dependent manner. | Full target Results and selected Methods inspected. Functional recovery is a cellular interpretation, not direct purified refolding kinetics; luciferase remains a negative client in the other study. |
| PMID:24023695(https://pubmed.ncbi.nlm.nih.gov/24023695/) | Human HSJ1a in mutant-SOD1 mice and cell assays changes aggregation, ubiquitination and turnover; client association and domain mutants are informative. | Full target Results and selected Methods inspected. Neither decreased aggregation nor improved animal outcome alone establishes restored SOD1 catalytic activity. |
| PMID:12754272(https://doi.org/10.1074/jbc.M212349200) | The primary abstract establishes geranylgeranylation-dependent HSJ1b targeting to the cytosolic ER face and altered rhodopsin processing/inclusions. | Legacy cache explicitly marks abstract-only; publisher attempts did not recover full Methods. Nuclear/cytosolic assertions are additionally supported by independently inspected localization sources. |
| PMID:9553041(https://pmc.ncbi.nlm.nih.gov/articles/PMC316709/) | A human 78-residue HSJ1 J domain can supply Hsp70 recruitment in WT1 fusion constructs, with HPD and WT1 DNA-binding controls. | Full original Methods/Results inspected. This is genuine HSJ1-domain evidence, but the construct-dependent growth phenotype does not establish native DNAJB2 growth control. |
| PMID:1599432(https://pmc.ncbi.nlm.nih.gov/articles/PMC1132662/) | Human cDNA cloning, expression and sequence analysis establish neuronal enrichment and splice forms. The discussion treats function prospectively. | Normal cache remains abstract-only. Original scanned pages 470,474 and475 were visually inspected; no unfolded-client perturbation assay is claimed. Constitutive expression does not refute the response term. |
The second core now explicitly uses GO:0140309 for the combined antiaggregation-and-delivery function. The live GO:0140036 annotation still records modification-dependent recognition and adaptor activity, which supplies one mechanism of that coupled unit. No third core, NEW annotation row or contributes_to molecular-function qualifier is required. The five historical holdase replacement recommendations remain reviewable on their retired source rows.
The two core activities describe a coordinated system rather than a universal outcome. The J domain can promote degradation while UIM-dependent preservation retards it for the same Atx3 client. HSJ1b overexpression can enhance rhodopsin inclusions in its ER context. Neither effect invalidates antiaggregation in the separately demonstrated systems.
PMID:25036637(https://pmc.ncbi.nlm.nih.gov/articles/PMC4104544/) supplies LUMIER Methods and the literal human MLF1–DNAJB2 record EBI-9364639 / IM-22301-375: Renilla-tagged MLF1 and FLAG-tagged DNAJB2 in HEK293T cells. PMID:33961781(https://pmc.ncbi.nlm.nih.gov/articles/PMC8165030/) supplies the HCT116 AP-MS record EBI-54862867 / IM-29278-19149: tagged MLF1 bait and DNAJB2 prey, with spoke expansion. Both pairs’ sequence/taxon identifiers match the current canonical proteins. These are positive lysate associations, not purified direct-contact measurements. MLF1’s tentative transcription-factor designation does not justify a more specific binding activity from these experiments. The independently recovered original Methods are distinct from the partial normal cache extractions.
The PMID:21625540 annotation’s WITH/FROM is P25686-2. Its exact self-association assay remains unresolved; current IntAct and MINT records did not supply it. The verified primary abstract of the inherited DNAJB2a extension study independently reports wild-type and mutant polydisperse oligomers. This supports retention of gene-level association while leaving original-pair attribution and oligomer stoichiometry open.
The HPA DNAJB2 record and its official XML report enhanced-reliability nuclear-membrane ICC/IF localization in A-431, U-251MG and U2OS, with an siRNA validation record. The record was read; image pixels were not independently scored, and no splice-product identity is inferred from the antibody signal.
Positive binding is preserved under the project’s explicit policy. Genericity is not a reason to remove an experimentally positive association. Specific refinements require the actual partner and activity context.
The recovered PTHR45168 topology places human P25686 at PTN002554731, descending from PTN002376289. Four current IBD assertions at that ancestor cover cytosol, ATPase activation, Hsp70 binding and protein refolding, with target P25686 experimental evidence. Target self-inclusion is legitimate descendant grounding. The historical obsolete GO:0051082 IBD no longer occurs in the current download; its source assertion is still retained, and this difference is not presented as a target-specific functional loss.
The actual InterPro2GO mapping contains IPR043183 → GO:0030544. The official DNAJB2 record carries this signature. The historical unfolded-protein-binding mapping is preserved as historical source data, despite its absence from the current mapping file.
The actual rules ARBA00087599, ARBA00088077 and ARBA00026971 contain matching branches for FunFam 1.10.287.110:FF:000021, with applicable Haplorrhini/Homo taxonomic conditions where present. Their selected zero-based condition-set indices are 1, 7 and 928 respectively. The matched outputs are anti-inclusion assembly, folding-chaperone binding and cytoplasm. Direct target evidence independently supports the biological interpretation; broad terms are refined rather than treated as failed propagation.
The inherited neuromuscular-chaperone review, distal-myopathy review, J-protein review, DNAJB2a extension study and fibroblast heat-shock study retain their original reference identities. Their identifiers, titles and complete abstracts were independently verified. Full Methods were not read for these five contextual references. The fibroblast chemical response is not a clinical efficacy claim, and therapeutic doses are omitted from the biological description.
All existing publication caches and the authentic Falcon report remain unchanged. Both GOA versions preserve their original bytes: the current export occupies the standard path and the historical export is archived. The inherited UniProt file also remains unchanged. Cache flags describe those files, not whether a separate accepted manuscript or original scan was accessible. The YAML’s four short literal primary anchors occur once each; other support is reference-only with the source and assay limits recorded above.
The normal cache flags are unchanged. The following locators make the actual additional source scope explicit; they do not upgrade an abstract cache or claim that every experiment was inspected.
| Source | Public original locator | Actual relevant scope |
|---|---|---|
| PMID:9553041 | PMC316709, Results subsection on substituting the HSJ1 Hsp70-binding domain for the WT1 amino terminus; Figures 6–7 and corresponding plasmid Methods | The full original identifies the human HSJ1 J-domain chimera, Hsp70-binding mutation and WT1 DNA-binding controls. The abstract corroborates the chimera result, but does not replace these inspected construct details. |
| PMID:22219199 | PMC3285371, Experimental Procedures for construct preparation, recombinant purification and the malachite-green phosphate-release assay | Historical HSJ1a residues 1–274 and J-domain fragments were used with human HSP70; neither full-length natural-product equivalence nor intrinsic HSJ1 ATPase activity is inferred. |
| PMID:21231916 | HAL accepted manuscript, PDF page 10 target Results and PDF page 23 Figure 2C, with the Figure 2 caption | Broken PDF text encoding required OCR; the decisive target result and experimental-localization panel were visually checked against the original. DNAJB2a suppresses aggregation without improving the tested luciferase-refolding response. |
| PMID:1599432 | PMC1132662 original scanned article, printed pages 470, 474 and 475 | Original scans were visually read for human cloning, expression, splice-form and prospective-function scope; no unfolded-client perturbation assay is claimed. |
| PMID:12754272 | Verified primary abstract | Abstract-only. The unsuccessful publisher routes did not produce a full-original claim. |
The inherited contextual DOIs and authentic provider report remain identified as context rather than being given artificial primary-evidence citations. The source guide supplies public locators and assay context; the core is supported by the primary references.
The two GOA versions and the provenance record document a specific source transition. The standard DNAJB2-goa.tsv is the validation input regenerated by normal fetches; the dated QuickGO snapshot records the fixed export retrieved on 2026-10-17 at 20:10:55 UTC. The prior-main snapshot records the earlier export as archived during this review; its date is not an inferred original retrieval date. The YAML provenance retains the source-transition data and records the new locations. The archived previous export and computed transition record make retirement decisions inspectable without altering source objects. Their preservation is intentional; they are not separate competing databases and are not individually refreshed.