CaBP

Targets of Calmodulin

Proteins and small molecules whose interaction with calmodulin is thought to be biologically relevent are included in this table.

Calmodulin Isoform
Target Protein
Evidence of Interaction
Effect of Interaction
isoform 1
calmodulin-dependent cyclic nucleotide phosphodiesterase
(PDE)
  • 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)


isoform 1
caldesmon
  • 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)

  • in Gallus gallus: Calmodulin binding prevents the interaction of caldesmon with F-actin, removing the inhibition of the actomyosin ATPase by caldesmon (InfoCard)

isoform 1
calcineurin


isoform 1
erythrocyte calcium-ATPase
  • 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)


isoform 1
adenylate cyclase
  • biochemical evidence in Bos taurus: A peptide derived from the putative calmodulin-binding domain of adenylate cyclase was shown to bind calmodulin (InfoCard)


    isoform 1
    calcium/calmodulin-dependent protein kinase II
    (CaMKII)


    isoform 1
    phosphorylase kinase


      isoform 1
      nicotinamide dinucleotide kinase
      • 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)

      • in Pisum sativum: NAD kinase is absolutely dependent on calmodulin and micromolar levels of free calcium for activity (InfoCard)

      isoform 1
      brush border myosin I heavy chain
      • 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)

      • in Gallus gallus: Calmodulin functions as the light chains for this myosin, and is responsible for the calcium-dependence of the ATPase activity (InfoCard)

      isoform 1
      smooth muscle myosin light chain kinase
      (smMLCK)
      • 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)

      • in all vertebrates: Calmodulin binding stimulates kinase activity (InfoCard)

      isoform 1
      skeletal muscle myosin light chain kinase
      (skMLCK)
      • biochemical evidence in all vertebrates: Calmodulin binding stimulates kinase activity (InfoCard)

      • in all vertebrates: Calmodulin binding stimulates kinase activity (InfoCard)

      isoform 1
      neuronal nitric oxide synthase
      (nNOS)
      • biochemical evidence in Bos taurus: A peptide derived from the putative calmodulin-binding domain of NOS was shown to bind calmodulin (InfoCard)


        isoform 1
        calcium/calmodulin-dependent protein kinase IV
        (CaMKIV)


          isoform 1
          IQGAP1
          • 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)


          isoform 1
          phosphatidylinositol 3-kinase
          • 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)