The Receptor Interacting Protein (RIP) kinase family comprises seven threonine/serine and tyrosine kinases (RIP1 - 7), that are involved in various biological processes, including innate immunity, inflammation and regulation of cell death. They are characterized by a homologous kinase domain, but have distinct non-kinase regions, which are key to the specific function of each RIP kinase. RIP1-5 all have a N-terminal kinase domain, while RIP6 and RIP7 (also known as LRRK1 and LRRK2, respectively) contain multiple and diverse domain structures, including a leucine-rich repeat region, in addition to the kinase domain.
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