IPR043183 matches the DNAJB6 sequence and currently maps Hsp70 protein binding; its historical unfolded-protein-binding mapping is preserved separately.

The human DNAJB6 target lies below the two imported ancestral nodes in the PTHR43948 lineage, with experimental descendant grounding for the current IBD assertions.

The human HPA target record reports supported nucleoplasm and cytosol localization without resolving the four products.

Human Mrj binds K18 and Hsp/c70 through separable regions, colocalizes with K8/18 filaments in HeLa cells, and its antibody perturbation disrupts that filament network.

MRJ is enriched in the central nervous system and suppresses polyglutamine-associated aggregation, caspase activity and toxicity in a cellular Huntington-disease model.

A BRMS1 interaction screen identifies MRJ, with controlled yeast two-hybrid and COS7 co-immunoprecipitation support for the association.

YTS membrane enrichment detects a mixture of integral and associated proteins; the membrane proteome includes nonintegral species.

DNAJB6b suppresses polyglutamine aggregation, while the historical long a construct suppresses nuclear-targeted polyglutamine despite little effect on the cytoplasmic reporter. Some detailed HDAC and acetylation mechanisms in this paper concern DNAJB8.

DNAJB6 expression partially improves relocation of aggregation-prone Parkin C289G to damaged mitochondria; stronger clearance and mitophagy experiments in the paper principally concern HSJ1a.

DNAJB6b suppresses polyglutamine and heat-induced luciferase aggregation without improving luciferase refolding in the tested cellular assays.

Proteomic analysis characterizes highly purified human sperm nuclei and provides the curated source for a DNAJB6 nuclear-detection annotation.

DNAJB6-related myopathy variants alter cellular antiaggregation, DNAJB6 is detected at human muscle Z discs, and DNAJB6b associates with BAG3, HSPB8 and STUB1 in targeted assays.

Controlled human muscle yeast two-hybrid screens identify DNAJB6 fragment interactions with MLF1 and MLF2.

The human chaperone interaction network contains DNAJB6–MLF1/MLF2 associations supported by affinity and LUMIER records.

A controlled yeast two-hybrid network identifies multiple source-specific DNAJB6 pairs, including explicitly recorded partner splice products and fragments.

Human 293T and HCT116 AP-MS networks contain the DNAJB6–MLF1 association.

The primary U2OS AP-MS network contains a DNAJB6–MLF1 edge, independently of the older interaction datasets.

The HSF1-response pathway contains HSP70 ATP-hydrolysis reactions with DNAJB6 in the co-chaperone catalyst sets.

The nucleoplasmic ATP-hydrolysis event includes a DNAJB6 2–326 entity in its HSP40 co-chaperone set.

The cytosolic ATP-hydrolysis event includes a DNAJB6 2–326 entity in its HSP40 co-chaperone set.

Mrj interacts with NFATc3 and is recovered in an NFAT-associated TNF promoter complex in rat cardiomyocytes; the assays distinguish protein recruitment from an unresolved direct Mrj–DNA contact.

Human DNAJB6 and DNAJB8 suppress polyglutamine aggregation and show client-proximity and serine-rich-region dependence; these measurements do not themselves establish productive folding or destination-specific delivery.

The DNAJB6 p.Pro96Leu myopathy variant has a dominant negative effect in the reported antiaggregation assays.

An exposed DNAJB6 J-domain binds and activates HSP70, whereas WT JD-GF and full-length WT are autoinhibited in the tested assays. Tested disease variants release this regulation, while purified DNAJB6b retains intrinsic polyglutamine antiaggregation without added HSP70.