Gene interactions and pathways from curated databases and text-mining

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CALM3 — SYN2

Text-mined interactions from Literome

Cohen et al., Proc Natl Acad Sci U S A 1990 : In the presence of Ca2+/CaM , synapsin I was phosphorylated
Steiner et al., J Biol Chem 1987 : The binding of synapsin with the neurofilament subunit is specific since this binding interaction is saturable, with a 1 : 1 stoichiometry, the binding involves only certain proteolytically derived domains of synapsin, and is therefore not a simple electrostatic interaction between the basic domains of synapsin and the acidic regions in the neurofilament subunit, and Ca2+/calmodulin dependent phosphorylation of synapsin inhibits this interaction
Bartelt et al., Biochem J 1986 : In the presence of Ca2+ and calmodulin , phosphorylation of smooth-muscle myosin light chain and brain synapsin and autophosphorylation of a Mr-50,000 protein were observed