| Function | Co-chaperone for Hsp70 protein HSPA5/BiP that acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR). 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. Also involved in endoplasmic reticulum-associated degradation (ERAD) of misfolded proteins. Required for survival of B-cell progenitors and normal antibody production. |
| Protein Name | Dnaj Homolog Subfamily B Member 9Endoplasmic Reticulum Dna J Domain-Containing Protein 4Er-Resident Protein Erdj4Erdj4Microvascular Endothelial Differentiation Gene 1 ProteinMdg-1 |
| Database Links | Reactome: R-HSA-381038 |
| Cellular Localisation | Endoplasmic Reticulum Lumen |
| Alternative Antibody Names | Anti-Dnaj Homolog Subfamily B Member 9 antibodyAnti-Endoplasmic Reticulum Dna J Domain-Containing Protein 4 antibodyAnti-Er-Resident Protein Erdj4 antibodyAnti-Erdj4 antibodyAnti-Microvascular Endothelial Differentiation Gene 1 Protein antibodyAnti-Mdg-1 antibodyAnti-DNAJB9 antibodyAnti-MDG1 antibodyAnti-UNQ743 antibodyAnti-PRO1471 antibody |
Information sourced from Uniprot.org
