In this study we identified snapin as an interaction partner of the CK1 isoform delta (CK1δ) in the yeast two-hybrid system and localized the interacting domains of both proteins. The interaction of CK1δ with snapin was confirmed by co-immunoprecipitation. Snapin was phosphorylated by CK1δ in vitro. Both proteins localized in close proximity in the perinuclear region, wherein snapin was found to associate with membranes of the Golgi apparatus. The identification of snapin as a new substrate of CK1δ points towards a possible function for CK1δ in modulating snapin specific functions.