DnaJ/HSP40 Homolog Subfamily B, Member 14 (DNAJB14)

The DnaJ family, one of the largest of all the chaperone families, has evolved with diverse cellular localization and functions. DnaJ heat-shock induced proteins are derived from the bacterium Escherichia coli and are under the control of the htpR regulatory protein. DnaJ proteins play a critical role in the HSP 70 chaperone machine by interacting with HSP 70 to stimulate ATP hydrolysis. Members of this family contain cysteine-rich regions that are composed of zinc fingers that form a peptide-binding domain responsible for chaperone function. DnaJ family members are important mediators of proteolysis and are involved in the regulation of protein degradation, exocytosis and endocytosis. DnaJB14 is a 379 amino acid single-pass membrane protein containing one J domain and is thought to act as a co-chaperone. DnaJB14 exists as two alternatively spliced isoforms.