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CALM1 — PHKA1

Pathways - manually collected, often from reviews:

• KEGG Calcium signaling pathway: PHKA1/PHKA2/PHKB/PHKG1/PHKG2 → CALM1/CALM2/CALM3/CALML3/CALML5/CALML6 (protein-protein, binding/association)
  
• Reactome Reaction: CALM1 → PHKA1 (direct_complex)

Text-mined interactions from Literome

Andreeva et al., Biochemistry (Mosc) 1999 : Binding of phosphorylase kinase by glycogen occurs only in the presence of Ca2+ and Mg2+ ... Binding of phosphorylase kinase by glycogen occurs only in the presence of Ca2+ and Mg2+
Zhang et al., J Biol Chem 1989 : Neither these effects nor the epinephrine stimulated increases in phosphorylation of glycogen synthase and phosphorylase kinase were attenuated by insulin
Kyriakidis et al., Biochim Biophys Acta 1988 : Ca2+- and Mg2+ dependent association of phosphorylase kinase with human erythrocyte membranes
Putkey et al., J Biol Chem 1986 : In addition, CaML16 and CaML19 do not activate phosphorylase kinase
Nikolaropoulos et al., Eur J Biochem 1985 : The gizzard phosphorylase kinase showed a high pH 6.8/8.2 activity ratio of 0.53, it was stimulated by Ca2+, inhibited up to 80 % by EGTA and it was activated about 1.9-fold by calmodulin
Furuya et al., Proc Natl Acad Sci U S A 1982 : The enzyme is also inactivated by phosphorylase kinase in the presence of Ca2+ and calmodulin ... The enzyme is also inactivated by phosphorylase kinase in the presence of Ca2+ and calmodulin
Silver et al., Mol Pharmacol 1983 : The activities of phosphorylase kinase and myosin light-chain kinase are regulated by Ca2+ binding to calmodulin
Silonova et al., Biokhimiia 1984 : There is evidence suggesting that the activation of phosphorylase kinase b by actin is not due to the presence of trace amounts of calmodulin in actin preparations : ( 1 ) Troponin I and trifluoperazine inhibit the activation of phosphorylase kinase by calmodulin but do not inhibit the activation by actin
Cohen et al., Ann N Y Acad Sci 1980 : The current evidence suggests that the regulation of phosphorylase kinase by Ca2+ in vivo is achieved through the interaction of this divalent cation with calmodulin ( the delta subunit ) and troponin C, and that the relative importance of these two calcium binding proteins depends on the state of phosphorylation of the enzyme [ FIGURE 1 ]
Gergely et al., Biochim Biophys Acta 1980 : The `` calcium dependent regulator '' or calmodulin can enhance the activity of phosphorylase kinase , increasing its affinity for Ca2+
Stokoe et al., Biochem J 1993 : The catalytic domain was most similar ( 35-40 % identity ) to calmodulin dependent protein kinases II and IV, phosphorylase kinase , putative serine kinase H1 and the C-terminal domain of MAPKAP kinase-1, which form one branch of the protein kinase phylogenetic tree
Nadeau et al., J Biol Chem 1997 : The structural effects of endogenous and exogenous Ca2+/calmodulin on phosphorylase kinase ... The structural effects of endogenous and exogenous Ca2+/calmodulin on phosphorylase kinase
Shmelev et al., Biochem Mol Biol Int 1997 : The complex formation occurs in two stages : ( i ) the formation of phosphorylase-glycogen complex controlled by ATP, ( ii ) the binding of phosphorylase kinase to the previously formed phosphorylase-glycogen complex exclusively in the presence of Ca2+ and Mg2+ ... The complex formation occurs in two stages : ( i ) the formation of phosphorylase-glycogen complex controlled by ATP, ( ii ) the binding of phosphorylase kinase to the previously formed phosphorylase-glycogen complex exclusively in the presence of Ca2+ and Mg2+