DNAJB9

DnaJ homolog subfamily B member 9

223 amino acids

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 (PubMed:18400946). 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).

25.518 kDa

MATPQSIFIFAICILMITELILASKSYYDILGVPKSASERQIKKAFHKLAMKYHPDKNKSPDAEAKFREIAEAYETLSDANRRKEYDTLGHSAFTSGKGQRGSGSSFEQSFNFNFDDLFKDFGFFGQNQNTGSKKRFENHFQTRQDGGSSRQRHHFQEFSFGGGLFDDMFEDMEKMFSFSGFDSTNQHTVQTENRFHGSSKHCRTVTQRRGNMVTTYTDCSGQ

DNAJB9

DnaJ homolog subfamily B member 9

223 amino acids

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 (By similarity). 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).

25.605 kDa

MATPQSIFIFAICILMITELILASKSYYDILGVPKSASERQIKKAFHKLAMKYHPDKNKSPDAEAKFREIAEAYETLSDANRRKEYDTLGHSAFTNGKGQRGSGSSFEQSFNFNFDDLFKDFGFFGQNQNTRSKKHFENHFQTRPDGGSSRQRHHFQEFSFGGGLFDDMFEDMEKMFSFSGFDPTSRHTVQTENRFHGSSKHCRTVTQRRGNMVTTYTDCSGQ

DNAJB9

DnaJ homolog subfamily B member 9

222 amino acids

Co-chaperone for Hsp70 protein HSPA5/BiP that acts as a key repressor of the ERN1/IRE1-mediated unfolded protein response (UPR) (PubMed:29198525). J domain-containing co-chaperones stimulate the ATPase activity of Hsp70 proteins and are required for efficient substrate recognition by Hsp70 proteins (PubMed:29198525). 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 (PubMed:29198525). Also involved in endoplasmic reticulum-associated degradation (ERAD) of misfolded proteins (By similarity). Required for survival of B-cell progenitors and normal antibody production (By similarity).

25.646 kDa

MATPQSVFVFAICILMITELILASKSYYDILGVPKSASERQIKKAFHKLAMKYHPDKNKSPDAEAKFREIAEAYETLSDAHRRKEYDTVGHTAFTNGKGQRGSGSPFEQSFNFNFDDLFKDFNLFGQNQNTRSKKHFENHFQTHQDGSNRQRHHFQEFSFGGGLFDDMFEDMEKMFSFSGFDTTNRHTVQTENRFHGSSKHCRTVTQRRGNMVTTYTDCSGQ

Dnajb9

DnaJ homolog subfamily B member 9

222 amino acids

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 (PubMed:11836248). 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 (PubMed:22267725). Required for survival of B-cell progenitors and normal antibody production (PubMed:25222125).

25.616 kDa

MATPQSVFVFAICILMITELILASKSYYDILGVPKSASERQIKKAFHKLAMKYHPDKNKSPDAEAKFREIAEAYETLSDANSRKEYDTIGHSAFTNGKGQRGNGSPFEQSFNFNFDDLFKDFNFFGQNQNTRSKKHFENHFHTRQDGSSRQRHHFQEFSFGGGLFDDMFEDMEKMFSFSGFDTTNRHTVQTENRFHGSSKHCRTVTQRRGNMVTTYTDCSGQ

Dnajb9

DnaJ homolog subfamily B member 9

222 amino acids

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 (By similarity). 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).

25.717 kDa

MATPQSVFVFAICILMITELILASKNYYDILGVPKSASERQIKKAFHKLAMKYHPDKNKSPDAEAKFREIAEAYETLSDANRRKEYDIIGHSAFTNGKGQRSNGSPFEQSFNFNFDDLFKDFNLFGQNQNTRSKKHFENHFQTRQDGSSRQRHHFQEFSFGGGLFDDMFEDMEKMFSFSGFDSTNRRTVQTENRFHGSSKHCRTVTQRRGNMVTTYTDCSGQ