DAPK3 or Death-associated protein kinase 3 (also known as ZIP) plays a role in apoptosis. DAPK3 is a nuclear serine/threonine-specific kinase that phosphorylates core histones H3 and H4, and myosine light chain in vitro. DAPK3 interacts with transcription and splicing factors as well as with pro-apoptotic protein Par-4 suggesting that it participates in multiple cellular processes. DAPK3 contains a leucine zipper structure at its C terminus and this region is responsible for binding to ATF4. The leucine zipper domain is necessary for the homodimerization of DAPK3 as well as for the activation of the kinase.