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Literature summary extracted from

  • Klee, C.B.; Krinks, M.H.; Manalan, A.S.; Draetta, G.F.; Newton, D.L.
    Control of calcineurin protein phosphatase activity (1985), Adv. Protein Phosphatases, 1, 135-146.
No PubMed abstract available

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.1.3.16 Co2+
-
 Mammalia
3.1.3.16 Co2+
-
 Oryctolagus cuniculus
3.1.3.16 Mg2+
-
 Mammalia
3.1.3.16 Mg2+
-
 Oryctolagus cuniculus
3.1.3.16 Ni2+ activation Mammalia
3.1.3.16 Ni2+ activation Oryctolagus cuniculus
3.1.3.16 Zn2+
-
 Mammalia

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.1.3.16 80000 90000 phosphatase 2B, i.e. calcineurin, sedimentation equilibrium centrifugation Mammalia
3.1.3.16 80000 90000 phosphatase 2B, i.e. calcineurin, sedimentation equilibrium centrifugation Oryctolagus cuniculus

Organism

EC Number Organism UniProt Comment Textmining
3.1.3.16 Mammalia
-
-
-
3.1.3.16 Oryctolagus cuniculus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
3.1.3.16 brain
-
 Mammalia
-
3.1.3.16 brain
-
 Oryctolagus cuniculus
-
3.1.3.16 additional information
-
 Mammalia
-
3.1.3.16 additional information
-
 Oryctolagus cuniculus
-
3.1.3.16 skeletal muscle
-
 Oryctolagus cuniculus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.3.16 phosphoproteins + H2O
-
 Oryctolagus cuniculus proteins + phosphate
-
 ?
3.1.3.16 phosphoproteins + H2O most of the substrates are phosphorylated by cAMP and cGMP dependent protein kinases, other substrates are phosphorylated by calmodulin dependent multiprotein kinase Mammalia proteins + phosphate
-
 ?

Subunits

EC Number Subunits Comment Organism
3.1.3.16 dimer
-
 Mammalia

Cofactor

EC Number Cofactor Comment Organism Structure
3.1.3.16 Calmodulin activation, dependent on Ca2+ Mammalia
3.1.3.16 Calmodulin activation, dependent on Ca2+ Oryctolagus cuniculus