Cancer is the second leading cause of death worldwide, with 27.5 million new cases projected by 2040. Disruptions in cell cycle control cause DNA errors to accumulate during cell growth, mak-ing proteins that regulate cell cycle progression crucial targets for cancer therapy. NIMA-related kinases (NEKs) are involved in regulating the cell cycle and checkpoints in humans. Among these, NEK10 is the most divergent member and has been associated with both cancer and ciliopathies. Despite its biological significance and distinctive domain architecture, structural details of NEK10 remain unknown. To address this gap, we modeled the complete structure of the NEK10 protein. Our analysis revealed a catalytic domain flanked by two coiled-coil domains, armadil-lo-type repeats, an ATP binding site, two putative UBA domains and a PEST sequence. Further-more, we mapped a comprehensive interactome of NEK10, uncovering previously unknown in-teractions with the cancer-related proteins MAP3K1 and HSPB1. MAP3K1, a serine/threonine kinase and E3 ubiquitin ligase frequently mutated in cancers, interacts with NEK10 via its scaf-fold regions. The interaction with HSPB1, a chaperone associated with poor cancer prognosis is mediated by NEK10’s armadillo repeats. Our findings underscore a connection of NEK10 with ciliogenesis and cancer, suggesting its important role in cancer development and progression.