CaMPDB: A RESOURCE FOR CALPAIN AND MODULATORY PROTEOLYSIS
David A. duVerle, Ichigaku Takigawa, Yasuko Ono, Hiroyuki Sorimachi, Hiroshi Mamitsuka
Abstract
David A. duVerle, Ichigaku Takigawa, Yasuko Ono, Hiroyuki Sorimachi, Hiroshi Mamitsuka
Abstract
While the importance of modulatory proteolysis in research has steadily increased, knowledge on this process has remained largely disorganized, with the nature and role of entities composing modulatory proteolysis still uncertain. We built CaMPDB, a resource on modulatory proteolysis, with a focus on calpain, a well-studied intracellular protease which regulates substrate functions by proteolytic processing. CaMPDB contains sequences of calpains, substrates and inhibitors as well as substrate cleavage sites, collected from the literature. Some cleavage efficiencies were evaluated by biochemical experiments and a cleavage site prediction tool is provided to assist biologists in understanding calpain-mediated cellular processes. CaMPDB is freely accessible at http://calpain.org.
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While the importance of modulatory proteolysis in research has steadily increased, knowledge on this process has remained largely disorganized, with the nature and role of entities composing modulatory proteolysis still uncertain. We built CaMPDB, a resource on modulatory proteolysis, with a focus on calpain, a well-studied intracellular protease which regulates substrate functions by proteolytic processing. CaMPDB contains sequences of calpains, substrates and inhibitors as well as substrate cleavage sites, collected from the literature. Some cleavage efficiencies were evaluated by biochemical experiments and a cleavage site prediction tool is provided to assist biologists in understanding calpain-mediated cellular processes. CaMPDB is freely accessible at http://calpain.org.
Key concepts: Proteolysis, Calpain, Cleavage (geology), Protease, Cell biology, Intracellular, Chemistry, Biochemistry