Threonine Tyrosine Kinase

Threonine tyrosine kinases are a class of protein kinases capable of phosphorylating both threonine and tyrosine residues on substrate proteins. This dual-specificity is relatively rare compared to the more common serine/threonine or tyrosine-only kinases. The most well-known example in this category is TTK, also known as monopolar spindle 1 (MPS1). These phosphorylation events regulate protein function, subcellular localization, interactions, and signal transduction pathways. TTK/MPS1 plays a critical role in cell cycle regulation by ensuring proper chromosome alignment during mitosis, making it a promising therapeutic target for various cancers.

ATP-dependent phosphate transfer; conformational change upon inhibitor binding; disruption of catalytic machinery