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Proteins/UNIPROT:Q9UBS3
Co-chaperone for Hsp70 protein HSPA5/BiP that acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR) (By similarity). J domain-containing co-chaperones stimulate the ATPase activity of Hsp70 proteins and are required for efficient substrate recognition by Hsp70 proteins. In the unstressed endoplasmic reticulum, interacts with the luminal region of ERN1/IRE1 and selectively recruits HSPA5/BiP: HSPA5/BiP disrupts the dimerization of the active ERN1/IRE1 luminal region, thereby inactivating ERN1/IRE1 (By similarity). Also involved in endoplasmic reticulum-associated degradation (ERAD) of misfolded proteins. Required for survival of B-cell progenitors and normal antibody production (By similarity)..
Function from UniProtKB (Q9UBS3), read 2026-09-23. CC BY 4.0.
Curated compounds routed: 0
98 statements
98 statements · 4 reference databases · Subject: DNAJB9 · Sources: gene ontology, Hetionet, Reactome, WikiPathways
6 names
Resolves to: DNAJB9