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Significance Protein kinases are exceptionally important and effective targets in human diseases, but a significant proportion of the human kinome remains uncharacterized and consequently unexplored as potential therapeutic targets. Here, we describe a kinase not annotated in the original human kinome, C19orf35/PEAK3, which shares structural similarities with PEAK1/Sgk269 and Pragmin/SgK223 pseudokinases. Our work reveals the cellular pool of PEAK3 binding partners and focuses on cellular phenotypes resulting from the PEAK3-dependent inhibition of CrkII, an adaptor protein that controls cell migration. Most importantly, we investigate how the structure and dimerization of the PEAK3 pseudokinase domain regulates its behavior, which highlights potential avenues for pharmacological regulation of PEAK3 function.

PEAK3/C19orf35 pseudokinase, a new NFK3 kinase family member, inhibits CrkII through dimerization