Calmodulin Isoform
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Target Protein
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Evidence of Interaction
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Effect of Interaction
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isoform 1
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calmodulin-dependent cyclic nucleotide phosphodiesterase (PDE)
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- biochemical evidence in Bos taurus: A peptide derived from the putative calmodulin-binding domain of PDE was show to bind to calmodulin (InfoCard)
- biochemical evidence in Bos taurus: Calmodulin stimulates phosphodiesterase activity (InfoCard)
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isoform 1
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caldesmon
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- spectroscopic evidence in Gallus gallus: Nuclear magnetic resonance studies demonstrate the ability of peptides derived from the clamodulin-binding domains fo caldesmon to bind to calmodulin (InfoCard)
- biochemical evidence in Gallus gallus: Calmodulin binding prevents the interaction of caldesmon with F-actin, removing the inhibition of the actomyosin ATPase by caldesmon (InfoCard)
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- in Gallus gallus: Calmodulin binding prevents the interaction of caldesmon with F-actin, removing the inhibition of the actomyosin ATPase by caldesmon (InfoCard)
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isoform 1
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calcineurin
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isoform 1
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erythrocyte calcium-ATPase
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- biochemical evidence in Bos taurus: Calmodulin stimulates ATPase activity, and chemical modifications of calmodulin's methionines reduced this ability (InfoCard)
- biochemical evidence in Bos taurus: Calmodulin stimulates ATPase activity (InfoCard)
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isoform 1
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adenylate cyclase
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- biochemical evidence in Bos taurus: A peptide derived from the putative calmodulin-binding domain of adenylate cyclase was shown to bind calmodulin (InfoCard)
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isoform 1
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calcium/calmodulin-dependent protein kinase II (CaMKII)
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isoform 1
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phosphorylase kinase
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isoform 1
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nicotinamide dinucleotide kinase
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- biochemical evidence in Pisum sativum: Purified NAD kinase absolutely requires calmodulin in order to function (InfoCard)
- biochemical evidence in Pisum sativum: NAD kinase is absolutely dependent on calmodulin and micromolar levels of free calcium for activity (InfoCard)
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- in Pisum sativum: NAD kinase is absolutely dependent on calmodulin and micromolar levels of free calcium for activity (InfoCard)
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isoform 1
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brush border myosin I heavy chain
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- biochemical evidence in Gallus gallus: Calmodulin immobilized on coverslips translocates actin filaments (InfoCard)
- biochemical evidence in Gallus gallus: Calmodulin functions as the light chains for this myosin, and is responsible for the calcium-dependence of the ATPase activity (InfoCard)
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- in Gallus gallus: Calmodulin functions as the light chains for this myosin, and is responsible for the calcium-dependence of the ATPase activity (InfoCard)
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isoform 1
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smooth muscle myosin light chain kinase (smMLCK)
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- biochemical evidence in Gallus gallus: A peptide derived from the putative calmodulin-binding domain of MLCK was shown to bind calmodulin (InfoCard)
- biochemical evidence in all vertebrates: Calmodulin binding stimulates kinase activity (InfoCard)
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- in all vertebrates: Calmodulin binding stimulates kinase activity (InfoCard)
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isoform 1
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skeletal muscle myosin light chain kinase (skMLCK)
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- biochemical evidence in all vertebrates: Calmodulin binding stimulates kinase activity (InfoCard)
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- in all vertebrates: Calmodulin binding stimulates kinase activity (InfoCard)
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isoform 1
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neuronal nitric oxide synthase (nNOS)
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- biochemical evidence in Bos taurus: A peptide derived from the putative calmodulin-binding domain of NOS was shown to bind calmodulin (InfoCard)
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isoform 1
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calcium/calmodulin-dependent protein kinase IV (CaMKIV)
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isoform 1
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IQGAP1
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- biochemical evidence in Homo sapiens: Affinity chromatography demonstrates that IQGAP1 binds to calmodulin-Sepharose in a calcium-dependent manner. IQGAP1 co-immunoprecipitates with calmodulin from malignant human breast epithelial cells. (InfoCard)
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isoform 1
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phosphatidylinositol 3-kinase
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- biochemical evidence in Cricetulus griseus: Affinity chromatography demonstrates that PI3-Kinase binds to calmodulin-Sepharose. PI3-Kinase co-immunoprecipitates with calmodulin from Chinese hamster ovary cells. (InfoCard)
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