MELK a new member of the Snf1/AMPK family of kinases, encodes a protein with a kinase catalytic domain and a leucine zipper motif consisting of a periodic repetition of leucine residues at every seventh residue located within the N-terminal catalytic domain. This motif has been observed in myriad DNA-binding proteins and is presumed to be involved in protein-DNA interactions, and potentially protein-protein interactions. Research predicts that the gene product of MELK plays a role in the signal transduction events in the egg and early embryo. Mouse and human MELK proteins share 95% sequence identity in the kinase domain and northern blot analysis in mouse indicates that MELK expression is restricted to spermatogonia in the testis and to oocytes in the ovary.