Acts as a general chaperone in regulated exocytosis (By similarity). Acts as a co-chaperone for the SNARE protein SNAP-25 (By similarity). Involved in the calcium-mediated control of a late stage of exocytosis (By similarity). May have an important role in presynaptic function. May be involved in calcium-dependent neurotransmitter release at nerve endings (By similarity). Oligomers (PubMed:27452402). Homodimer (By similarity). Interacts with the chaperone complex consisting of HSC70 and SGTA (By similarity). Interacts with ZDHHC13 (via ANK repeats) (By similarity). Interacts with ZDHHC17 (via ANK repeats) (PubMed:28882895). Interacts with SYT1, SYT5 and SYT7, and with SYT9, forming a complex with SNAP25 (By similarity). The association with membranes is regulated by palmitoylation (By similarity). Identified by mass spectrometry in melanosome fractions from stage I to stage IV (PubMed:17081065). Expressed in pancreas, kidney, skeletal muscle, liver, lung, placenta, brain and heart. Ser-10 phosphorylation induces an order-to-disorder transition triggering the interaction with Lys-58 (PubMed:27452402). This conformational switch modulates DNAJC5's cellular functions by reducing binding to syntaxin and synaptogamin without altering HSC70 interactions (PubMed:27452402). Palmitoylated. Could be palmitoylated by DHHC3, DHHC7, DHHC15 and DHHC17. Palmitoylation occurs probably in the cysteine-rich domain and regulates DNAJC5 membrane attachment. The disease is caused by variants affecting the gene represented in this entry. Upon phosphorylation, Ser-10 interacts with Lys-58, a highly conserved residue in DnaJ proteins that is also a ubiquitination site in DNAJC5.