Gene interactions and pathways from curated databases and text-mining

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CA2 — CSN2

Text-mined interactions from Literome

Hilfiker et al., J Neurochem 1999 : SyntagI, the purified, recombinant, cytoplasmic domain of rat synaptotagmin I, was an effective substrate in vitro for Ca2+/calmodulin dependent protein kinase II ( CaMKII ), protein kinase C ( PKC ), and casein kinase II ( caskII )
Kameda et al., J Mol Cell Cardiol 2006 : CSN5/Jab1 inhibits cardiac L-type Ca2+ channel activity through protein-protein interactions
Kuret et al., Biochemistry 1984 : Purified Ca2+/calmodulin dependent casein kinase activity was dependent upon Ca2+ , calmodulin, and ATP X Mg2+ or ATP X Mn2+ when measured under saturating casein concentrations
Sacks et al., Biochem Mol Biol Int 1994 : Here we demonstrate that in the presence or absence of Ca2+ , calmodulin did not significantly alter either in vitro casein kinase II activity or autophosphorylation of its beta-subunit ... In contrast, Ca2+ inhibited in a dose dependent manner both casein kinase II activity and casein kinase II-catalysed calmodulin phosphorylation
Urao et al., Mol Gen Genet 1994 : The ATCDPK2 protein expressed in Escherichia coli was found to phosphorylate casein and myelin basic protein preferentially, relative to a histone substrate, and required Ca2+ for activation
Burgoyne et al., Biochem Soc Symp 1998 : In an attempt to define control points within the secretory pathway for casein synthesis and secretion, we have examined the role of both cytosolic and intra-organelle Ca2+ in the control of casein synthesis, phosphorylation and secretion ... Experiments examining the effects of depletion of intra-organelle Ca2+ indicated that intra-organelle Ca2+ was required for maintained casein phosphorylation, but not its secretion ... Depletion of Ca2+ from the endoplasmic reticulum led to a marked inhibition of casein synthesis