UniProt functional annotation for Q9UBS3



	UniProt functional annotation for Q9UBS3

UniProt code: Q9UBS3.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: 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). {ECO:0000250|UniProtKB:G3H0N9, ECO:0000250|UniProtKB:Q9QYI6, ECO:0000269|PubMed:18400946}.

Subunit: Interacts with HSPA5/BiP; interaction is direct (By similarity). Interacts with ERN1/IRE1 (via the luminal region) (By similarity). Interacts with DERL1 (By similarity). {ECO:0000250|UniProtKB:G3H0N9, ECO:0000250|UniProtKB:Q9QYI6}.

Subcellular location: Endoplasmic reticulum lumen {ECO:0000250|UniProtKB:Q9QYI6}.

Tissue specificity: Widely expressed. Expressed at highest level in the liver, placenta and kidney (PubMed:11836248). {ECO:0000269|PubMed:11836248}.

Domain: The J domain stimulates the ATPase activity of HSPA5/BiP, while the divergent targeting domain is required for efficient substrate recognition by HSPA5/BiP. The divergent targeting domain specifically recognizes and binds to aggregation-prone sequences. {ECO:0000250|UniProtKB:Q9QYI6}.

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		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). {ECO:0000250\|UniProtKB:G3H0N9, ECO:0000250\|UniProtKB:Q9QYI6, ECO:0000269\|PubMed:18400946}.


Subunit:		Interacts with HSPA5/BiP; interaction is direct (By similarity). Interacts with ERN1/IRE1 (via the luminal region) (By similarity). Interacts with DERL1 (By similarity). {ECO:0000250\|UniProtKB:G3H0N9, ECO:0000250\|UniProtKB:Q9QYI6}.
Subcellular location:		Endoplasmic reticulum lumen {ECO:0000250\|UniProtKB:Q9QYI6}.
Tissue specificity:		Widely expressed. Expressed at highest level in the liver, placenta and kidney (PubMed:11836248). {ECO:0000269\|PubMed:11836248}.
Domain:		The J domain stimulates the ATPase activity of HSPA5/BiP, while the divergent targeting domain is required for efficient substrate recognition by HSPA5/BiP. The divergent targeting domain specifically recognizes and binds to aggregation-prone sequences. {ECO:0000250\|UniProtKB:Q9QYI6}.