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Caenorhabditis elegans MPS1 is a single transmembrane helical auxiliary subunit that co localizes with the voltage gated Ugg Prezzi Bassi potassium channel KVS1 in the nematode nervous system. MPS 1 shares high homology with KCNE (potassium voltage gated channel subfamily E member) auxiliary subunits, and its cytosolic domain was reported to have a serine/threonine kinase activity that modulates KVS1 channel function via phosphorylation. In this study, NMR spectroscopy indicated that the full length and truncated MPS 1 cytosolic domain (134 256) in the Prezzo Ugg New York presence or absence of n dodecylphosphocholine detergent micelles adopted a highly flexible random coil secondary structure. In contrast, protein kinases usually adopt a stable folded conformation in order to implement substrate recognition and phosphoryl transfer. The highly flexible random coil secondary structure suggests that MPS 1 in the free state is unstructured but may require a substrate or binding partner to adopt stable structure required for serine/threonine kinase activity.