DnaJ heat shock protein family member B14 (DNAJB14)

DNAJB14 is a type II transmembrane co-chaperone of the endoplasmic reticulum, part of the Hsp40 family, where its primary function is to bind Hsc70/Hsp70 and regulate their ATPase and substrate binding activities[1][3][4][5]. DNAJB14 promotes the proper folding and trafficking of client proteins, prevents aggregation of misfolded proteins, and facilitates their degradation via the ERAD pathway[1][2][3][4][5]. Together with DNAJB12, DNAJB14 also promotes maturation of specific potassium channels by stabilizing nascent channel subunits and facilitating oligomerization[2][3]. Overexpression of DNAJB14 leads to formation of specialized nuclear membrane structures (DJANGOS) and has a role in ER penetration by some viruses, such as SV40[1][3]. Disease associations (e.g., cystic fibrosis, post-vaccinal encephalitis) are reported at the genetic level but with little mechanistic data available[3]. No evidence supports direct clinical targeting or established use as a biomarker.

Other names

DnaJ homolog subfamily B member 14DNAJB14UNQ9427/PRO34683FLJ14281EGNR9427PRO34683DnaJ (Hsp40) homolog, subfamily B, member 14