Protein Domain : DnaJ homolog subfamily B member 2/6-like IPR043183

Type	Family
Description	DNAJB2 (also known as HSJ-1) contains an N-terminal J-domain and the C-terminal UIMs (ubiquitin (Ub)-interacting motifs)-containing domain. It binds and stimulates ATPase activity of HSP70 through its J-domain [ ]. It also binds to polyUb chains through its UIM domain and contributes to the ubiquitin-dependent proteasomal degradation of misfolded proteins [, ].DNAJB6 (also known as HSJ-2) plays an indispensable role in the organization of KRT8/KRT18 filaments. It acts as an endogenous molecular chaperone for neuronal proteins including huntingtin. DNAJB6 is able to suppress aggregation and toxicity of polyglutamine-containing, aggregation-prone proteins. It also has a stimulatory effect on the ATPase activity of HSP70 in a dose-dependent and time-dependent manner and hence acts as a co-chaperone of HSP70 [ , ]. DNAJB8 is also a suppressor of aggregation and toxicity of disease-associated polyglutamine proteins [ ].
Short Name	DNJB2/6-like