MELK(Maternal embryonic leucine zipper kinase) also known as KIAA0175, HPK38 is a member of the Snf1/AMPK family of kinases, characterized by a kinase catalytic domain and a distinctive leucine zipper motif that consists of periodic repetition of leucine residues at every seventh position within the N-terminal catalytic domain. This structural motif is significant as leucine zippers are often found in various DNA-binding proteins, suggesting involvement in crucial protein-DNA and protein-protein interactions. MELK plays a key role in signal transduction events during egg and early embryo stages of development. Mouse and human MELK proteins share 95% sequence identity in the kinase domain, demonstrating high conservation.