DnaJ/HSP40 Homolog Subfamily C, Member 28 (DNAJC28)

DnaJ/Hsp40 proteins have been preserved throughout evolution and are important for protein translation, folding, unfolding, translocation, and degradation, primarily by stimulating the ATPase activity of chaperone proteins, Hsp70s. Because the ATP hydrolysis is essential for the activity of Hsp70s, DnaJ/Hsp40 proteins actually determine the activity of Hsp70s by stabilizing their interaction with substrate proteins. DnaJ/Hsp40 proteins all contain the J domain through which they bind to Hsp70s and can be categorized into three groups, depending on the presence of other domains. DNAJC28 contains 1 J domain. Expressed in the fetal and adult brain, testis, uterus, spleen and liver. May have a role in protein folding or as a chaperone.