FEATURES

FAMILY

DESCRIPTION

Also known as DJB12_HUMAN, DNAJB12. Acts as a co-chaperone with HSPA8/Hsc70; required to promote protein folding and trafficking, prevent aggregation of client proteins, and promote unfolded proteins to endoplasmic reticulum-associated degradation (ERAD) pathway (PubMed:21150129, PubMed:21148293). Acts by determining HSPA8/Hsc70's ATPase and polypeptide-binding activities (PubMed:21148293). Can also act independently of HSPA8/Hsc70: together with DNAJB14, acts as a chaperone that promotes maturation of potassium channels KCND2 and KCNH2 by stabilizing nascent channel subunits and assembling them into tetramers (PubMed:27916661). While stabilization of nascent channel proteins is dependent on HSPA8/Hsc70, the process of oligomerization of channel subunits is independent of HSPA8/Hsc70 (PubMed:27916661). When overexpressed, forms membranous structures together with DNAJB14 and HSPA8/Hsc70 within the nucleus; the role of these structures, named DJANGOs, is still unclear (PubMed:24732912)., (Microbial infection) In case of infection by polyomavirus, involved in the virus endoplasmic reticulum membrane penetration and infection (PubMed:21673190, PubMed:24675744). Homodimer and homotetramer (PubMed:27916661). Interacts (via J domain) with HSPA8/Hsc70 (PubMed:21150129, PubMed:21148293, PubMed:24732912, PubMed:27916661). Forms a multiprotein complex, at least composed of DNAJB12, DNAJB14, HSPA8/Hsc70 and SGTA; interaction with DNAJB14 and HSPA8/Hsc70 is direct (PubMed:24675744).

EXTERNAL LINKS

DNAJB12

DnaJ homolog subfamily B member 12

DNAJB12

Molecular Synopsis