Curated Information
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Home > Curated Information Page > PubMed Id: 24627475
Kang S, Xu M, Cooper EC, Hoshi N (2014) Channel-anchored protein kinase CK2 and protein phosphatase 1 reciprocally regulate KCNQ2-containing M-channels via phosphorylation of calmodulin. J Biol Chem 289, 11536-44 24627475
This page summarizes selected information from the record referenced above and curated into PhosphoSitePlus®, a comprehensive online resource for the study of protein post-translational modifications (NAR, 2015, 43:D512-20). To learn more about the scope of PhosphoSitePlus®, click here.
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T80-p - Calmodulin (rat)
Modsite: MARKMkDtDsEEEIR SwissProt Entrez-Gene
Orthologous residues
Calmodulin (human): T80‑p, Calmodulin (mouse): T80‑p, Calmodulin (rat): T80‑p, Calmodulin (chicken): T80‑p, Calmodulin (sheep): T80‑p, Calmodulin (cow): T80‑p
Characterization
Methods used to characterize site in vivo immunoprecipitation, mutation of modification site
Relevant cell lines - cell types - tissues:  CHO (fibroblast), HEK293-A (epithelial), neuron
Cellular systems studied:  cell lines, primary cultured cells
Species studied:  hamster, human
Enzymes shown to modify site in vitro
Type Enzyme
KINASE CK2A1 (human)
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
PHOSPHATASE PPP1CA (human) pharmacological inhibitor of upstream enzyme, modification site within consensus motif
KINASE CK2A1 (human) co-immunoprecipitation, pharmacological inhibitor of upstream enzyme, transfection of wild-type enzyme
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
TBB decrease
calyculin_A TBB inhibit treatment-induced decrease
TBCA decrease
calyculin_A TBCA inhibit treatment-induced decrease
Downstream Regulation
Effect of modification (function):  molecular association, regulation
Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
KCNQ4 (human) Induces pull-down assay, in vitro, co-immunoprecipitation
Comments:  T80 site is key to binding. CAM phosphorylation regulates channel trafficking and stabilizes activity-thereby regulating neuronal excitability.

S82-p - Calmodulin (rat)
Modsite: RKMkDtDsEEEIREA SwissProt Entrez-Gene
Orthologous residues
Calmodulin (human): S82‑p, Calmodulin (mouse): S82‑p, Calmodulin (rat): S82‑p, Calmodulin (chicken): S82‑p, Calmodulin (sheep): S82‑p, Calmodulin (cow): S82‑p
Characterization
Methods used to characterize site in vivo immunoprecipitation, mutation of modification site
Relevant cell lines - cell types - tissues:  CHO (fibroblast), HEK293-A (epithelial), neuron
Cellular systems studied:  cell lines, primary cultured cells
Species studied:  hamster, human
Enzymes shown to modify site in vitro
Type Enzyme
KINASE CK2A1 (human)
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE CK2A1 (human) co-immunoprecipitation, pharmacological inhibitor of upstream enzyme, transfection of wild-type enzyme
PHOSPHATASE PPP1CA (human) pharmacological inhibitor of upstream enzyme, modification site within consensus motif
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
TBB decrease
calyculin_A TBB inhibit treatment-induced decrease
TBCA decrease
calyculin_A TBCA inhibit treatment-induced decrease
Downstream Regulation
Effect of modification (function):  molecular association, regulation
Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
KCNQ4 (human) Induces pull-down assay, in vitro, co-immunoprecipitation
Comments:  T80 site is key to binding. CAM phosphorylation regulates channel trafficking and stabilizes activity-thereby regulating neuronal excitability.

S102-p - Calmodulin (rat)
Modsite: kDGNGyIsAAELRHV SwissProt Entrez-Gene
Orthologous residues
Calmodulin (human): S102‑p, Calmodulin (mouse): S102‑p, Calmodulin (rat): S102‑p, Calmodulin (chicken): S102‑p, Calmodulin (sheep): S102‑p, Calmodulin (cow): S102‑p
Characterization
Methods used to characterize site in vivo immunoprecipitation, mutation of modification site
Relevant cell lines - cell types - tissues:  CHO (fibroblast), HEK293-A (epithelial), neuron
Cellular systems studied:  cell lines, primary cultured cells
Species studied:  hamster, human
Enzymes shown to modify site in vitro
Type Enzyme
KINASE CK2A1 (human)
Upstream Regulation
Potential in vivo enzymes for site: 
Type Enzyme Evidence Notes
KINASE CK2A1 (human) co-immunoprecipitation, pharmacological inhibitor of upstream enzyme, transfection of wild-type enzyme
PHOSPHATASE PPP1CA (human) pharmacological inhibitor of upstream enzyme, modification site within consensus motif
Treatments, proteins and their effect on site modification: 
Treatments Referenced Treatments Manipulated Protein Referenced Protein Effect Notes
TBB decrease
calyculin_A TBB inhibit treatment-induced decrease
TBCA decrease
calyculin_A TBCA inhibit treatment-induced decrease
Downstream Regulation
Effect of modification (function):  molecular association, regulation
Modification regulates interactions with: 
Interacting molecule Interacting domains Effect Consequences (function) Consequences (process) Detection assays
KCNQ4 (human) Induces pull-down assay, in vitro, co-immunoprecipitation
Comments:  T80 site is key to binding. CAM phosphorylation regulates channel trafficking and stabilizes activity-thereby regulating neuronal excitability.