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Information on EC 3.1.3.16 - protein-serine/threonine phosphatase and Organism(s) Bos taurus and UniProt Accession P48452
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3.1.3.16 protein-serine/threonine phosphataseIUBMB Comments
A group of enzymes removing the serine- or threonine-bound phosphate group from a wide range of phosphoproteins, including a number of enzymes that have been phosphorylated under the action of a kinase (cf. EC 3.1.3.48 protein-tyrosine-phosphatase). The spleen enzyme also acts on phenolic phosphates and phosphamides (cf. EC 3.9.1.1, phosphoamidase).
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Word Map
- 3.1.3.16
-
cyclosporine
- phosphatases
- tacrolimus
-
rejection
-
okadaic
- mycophenolate
-
allograft
- cardiac
- steroid
-
corticosteroid
- mofetil
- rapamycin
-
nephrotoxicity
- nfat
- sirolimus
- agonist
- t-cells
- creatinine
- hypertrophy
- mapks
- glycogen
- synaptic
- mtor
-
glomerular
- pkc
- platelet
-
ca2+-dependent
- hypertension
- episode
- erk
-
atopic
- cardiomyocytes
- nephropathy
-
everolimus
- dermatitis
- myocytes
-
trough
-
hyperphosphorylation
- azathioprine
-
posttransplant
-
prophylaxis
-
allogeneic
- proteinuria
- camkii
-
post-transplantation
- graft-versus-host
- rituximab
- cyclophilins
-
biopsy-proven
- prednisone
- diagnostics
- analysis
- drug development
- medicine
The taxonomic range for the selected organisms is: Bos taurus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
calcineurin, protein phosphatase, pac-1, dusp1, dusp6, serine/threonine phosphatase, pp2ac, ppm1d, phosphoprotein phosphatase, laforin, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-hydroxy 3-methylglutaryl CoenzymeA reductase phosphatase
-
-
-
-
Aspergillus awamori acid protein phosphatase
-
-
-
-
BCKDH phosphatase
-
-
-
-
branched-chain alpha-keto acid dehydrogenase phosphatase
-
-
-
-
calcineurin
-
-
-
-
Calcineurin A1
-
-
-
-
Calcineurin A2
-
-
-
-
CaM-kinase phosphatase
-
-
-
-
CaMKPase
-
-
-
-
casein phosphatase
-
-
-
-
DRES10
-
-
-
-
Fibroblast growth factor inducible protein 13
-
-
-
-
FIN13
-
-
-
-
Flap wing protein
-
-
-
-
HMG-CoA reductase phosphatase
-
-
-
-
Magnesium-dependent calcium inhibitable phosphatase
-
-
-
-
MCPP
-
-
-
-
Microtubule star protein
-
-
-
-
phosphatase 2A
-
-
-
-
phosphatase 2B
-
-
-
-
phosphatase C-II
-
-
-
-
Phosphatase esp1
-
-
-
-
phosphatase H-II
-
-
-
-
phosphatase I
-
-
-
-
phosphatase IB
-
-
-
-
phosphatase II
-
-
-
-
phosphatase III
-
-
-
-
phosphatase IV
-
-
-
-
phosphatase SP
-
-
-
-
phosphoprotein phosphatase
-
-
-
-
phosphopyruvate dehydrogenase phosphatase
-
-
-
-
phosphospectrin phosphatase
-
-
-
-
PK-Pase
-
-
-
-
polycation modulated (PCM-) phosphatase
-
-
-
-
PP-1A
-
-
-
-
PP-1B
-
-
-
-
PP-1G
-
-
-
-
PP2A-alpha
-
-
-
-
PP2A-beta
-
-
-
-
PP2C
-
-
-
-
PP2C-alpha
-
-
-
-
PP2C-beta
-
-
-
-
PP2C-delta
-
-
-
-
PP2C-gamma
-
-
-
-
Pp4
PP5
-
-
-
-
PP6
PPEF
-
-
-
-
PPN
-
-
-
-
PPT
-
-
-
-
protein D phosphatase
-
-
-
-
protein phosphatase
-
-
-
-
Protein phosphatase 1A
-
-
-
-
Protein phosphatase 1B
-
-
-
-
Protein phosphatase 1C
-
-
-
-
Protein phosphatase magnesium-dependent 1 delta
-
-
-
-
Protein phosphatase magnesium-dependent 1 gamma
-
-
-
-
Protein phosphatase with EF calcium-binding domain
-
-
-
-
PSPase
-
-
-
-
Retinal degeneration C protein
-
-
-
-
Suppressor protein SDS21
-
-
-
-
additional information
calcineurin is a member of the Ser/Thr protein phosphatase family
Pp4
-
-
-
-
PP6
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate
mechanism of calcineurin catalysed reaction
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
protein-serine/threonine-phosphate phosphohydrolase
A group of enzymes removing the serine- or threonine-bound phosphate group from a wide range of phosphoproteins, including a number of enzymes that have been phosphorylated under the action of a kinase (cf. EC 3.1.3.48 protein-tyrosine-phosphatase). The spleen enzyme also acts on phenolic phosphates and phosphamides (cf. EC 3.9.1.1, phosphoamidase).
CAS REGISTRY NUMBER
COMMENTARY
9025-75-6
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
FYDEEVDEMY(P)REAPIDKKGNFNY(P)VEFTR + H2O
FYDEEVDEMYREAPIDKKGNFNYVEFTR + phosphate
-
-
-
-
?
phosphorylated BCKDH complex + H2O
BCKDH complex + phosphate
-
i.e. branched-chain alpha-keto acid dehydrogenase, phosphorylated
-
-
?
phosphorylated cAMP-dependent protein kinase + H2O
cAMP-dependent protein kinase + phosphate
-
phosphorylated at Ser-95
-
-
?
phosphorylated myosin light chain peptide + H2O
myosin light chain peptide + phosphate
-
KAKTTKKRPQRATSNVFS
-
-
?
phosphorylated phosphorylase kinase + H2O
phosphorylase kinase + phosphate
-
-
-
-
?
phosphorylated pyruvate dehydrogenase + H2O
pyruvate dehydrogenase + phosphate
-
-
-
-
?
synthetic peptides with phosphotyrosyl residues + H2O
synthetic peptides + phosphate
-
-
-
-
?
phosphoprotein + H2O
protein + phosphate
-
modulation of pyruvate dehydrogenase complex
-
-
?
phosphoprotein + H2O
protein + phosphate
-
phosphatase PP3 stimulates the initiation of DNA-synthesis
-
-
?
phosphoproteins + H2O
proteins + phosphate
-
-
134600, 134601, 134613, 134616, 134617, 134621, 134630, 134632, 134650, 134655, 134656, 134659, 134678
-
-
?
phosphoproteins + H2O
proteins + phosphate
-
comparison of amino acid sequence of substrates at phosphorylated sites
-
-
?
additional information
?
-
residues at 97-201 are essential for bovine retina CaN subunit A phosphatase activity
-
-
?
additional information
?
-
-
residues at 97-201 are essential for bovine retina CaN subunit A phosphatase activity
-
-
?
additional information
?
-
-
no activity on p-nitrophenyl phosphate, when assayed at pH 7.5 or at pH 10.5
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
phosphoprotein + H2O
protein + phosphate
-
modulation of pyruvate dehydrogenase complex
-
-
?
phosphoprotein + H2O
protein + phosphate
-
phosphatase PP3 stimulates the initiation of DNA-synthesis
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mn2+
additional information
-
phosphatase PP3 active in the absence of divalent cations
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
ADP
-
1.4 mM, 30°C, pH 7.5, 55% remaining activity with glycogen synthase D as substrate and 12% with phosphorylase a
AMP
-
1.4 mM, 30°C, pH 7.5, 55% remaining activity with glycogen synthase D as substrate and 10% with phosphorylase a
bovine serum albumin
-
1 mg/ml 30°C, pH 7.5, 95% remaining activity with glycogen synthase D and 92% with phosphorylase, in presence of 10 mg/ml 79% remaining activity with phosphorylase a as substrate
-
CaCl2
-
14 mM, 30°C, pH 7.5, with phosphorylase a as substrate, 50% remaining activity
cAMP
-
1 mM, 30°C, pH 7.5, 83% remaining activity with histone as substrate and 83% with phosphorylase a
citrate
-
1.4 mM, 30°C, pH 7.5, 68% remaining activity with glycogen synthase D as substrate
EDTA
-
14 mM, 30°C, pH 7.5, 23% remaining activity with glycogen synthase D as substrate and 35% with phosphorylase a
EGTA
-
14 mM, 30°C, pH 7.5, 55% remaining activity with glycogen synthase D as substrate and 83% with phosphorylase a
gelatin
-
1 mg/ml, 30°C, pH 7.5, 92% remaining activity with histone as substrate, and 31% withe phosphorylase a, in presence of 10 mg/ml 10% remaining activity with phohsphorylase a
-
histone
-
competitive when glycogen synthase D is the substrate, increases the Km-value for glycogen synthase D 4fold, but shows mixed type inhibition when phosphorylase a acts as substrate with an 1.4fold increase of Km
Inhibitor protein
-
MW 33000-36000, heat and acid stable, specific for BCKDH phosphatase
-
MgCl2
-
14 mM, 30°C, pH 7.5, with phosphorylase a as substrate, 60% remaining activity
MnCl2
-
14 mM, 30°C, pH 7.5, with phosphorylase a as substrate, 51% remaining activity
Na2HPO4
-
14 mM, 30°C, pH 7.5, no activity with glycogen synthase D as substrate, remaining activity 79% with histone as substrate, and 64% with phosphorylase a as substrate
Na2P2O7
-
14 mM, 30°C, pH 7.5, remaining activity 6% with glycogen synthase D as substrate, 15% with histone as substrate, and 8% with phosphorylase a as substrate
Na2SO4
-
14 mM, 30°C, pH 7.5, remaining activity 53% with glycogen synthase D as substrate and 32% with phosphorylase a as substrate
NaCl
-
14 mM, 30°C, pH 7.5, with phosphorylase a as substrate, 83% remaining activity
NaF
-
14 mM, 30°C, pH 7.5, remaining activity 31% with glycogen synthase D as substrate, 67% with histone as substrate, and 37% with phosphorylase a as substrate
NaHCO3
-
14 mM, 30°C, pH 7.5, remaining activity 49% with glycogen synthase D as substrate, 79% with histone as substrate, and 64% with phosphorylase a as substrate
NaNO3
-
14 mM, 30°C, pH 7.5, remaining activity 70% with glycogen synthase D as substrate, 83% with histone as substrate, and 78% with phosphorylase a as substrate
phosphorylase a
-
mixed type inhibitor with glycogen synthase d as substrate, increases Km 2fold with only small decearse in vmax
rabbit liver glycogen
-
1 mg/ml 30°C, pH 7.5, 88% remaining activity with glycogen synthase D and 37% remaining activity with 10 mg/ml inhibitor
-
UDP
-
1.4 mM, 30°C, pH 7.5, 52% remaining activity with glycogen synthase D as substrate and 20% with phosphorylase a
UMP
-
1.4 mM, 30°C, pH 7.5, 58% remaining activity with glycogen synthase D as substrate and 16% with phosphorylase a
UTP
-
1.4 mM, 30°C, pH 7.5, 44% remaining activity with glycogen synthase D as substrate and 21% with phosphorylase a
ATP
-
1.4 mM, 30°C, pH 7.5, 47% remaining activity with glycogen synthase D as substrate and 15% with phosphorylase a
phosphate
-
competitive inhibition to C-subunit and AC-dimer, noncompetitive inhibition to AC-R2
additional information
the residues at 407-456 also have an inhibitory effect on CaN A phosphatase activity in addition to the previously known autoinhibitory domain at 457-480
-
additional information
-
the residues at 407-456 also have an inhibitory effect on CaN A phosphatase activity in addition to the previously known autoinhibitory domain at 457-480
-
additional information
-
study of effects of D-glucose 6-phosphate on inhibitory compounds
-
additional information
-
study of effects of MgCl2 in presence of AMP, ADP, ATP, UMP, UDP, UTP, or citrate
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
bovine serum albumin
-
10 mg/ml, 30°C, pH 7.5, 112% relative activity with histone as substrate
-
CaCl2
-
14 mM, 30°C, pH 7.5, relative activity 126% with glycogen synthase D as substrate and 232% with histone as substrate compared to no addition
cAMP
-
1 mM, 30°C, pH 7.5, 115% relative activity with glycogen synthase D as substrate
D-glucosamine 6-phosphate
-
1.4 mM, 30°C, pH7.5, relative activity 109% with glycogen synthase D as substrate, 117% with histone as substrate, and 102% with phosphorylase a as substrate compared to no addition
D-glucose
-
1.4 mM, 30°C, pH7.5, relative activity 109% with glycogen synthase D as substrate, 101% with histone as substrate, and 106% with phosphorylase a as substrate compared to no addition
D-glucose 6-phosphate
-
1.4 mM, 30°C, pH 7.5, 109% relative activity with phosphorylase a as substrate
gelatin
-
1 mg/ml, 30°C, pH 7.5, 128% relative activity with glycogen synthase D as substrate, with 10 mg/ml 110% relative activity
-
MgCl2
-
14 mM, 30°C, pH 7.5, relative activity 256% with glycogen synthase D as substrate and 238% with histone as substrate compared to no addition
MnCl2
-
14 mM, 30°C, pH 7.5, relative activity 361% with glycogen synthase D as substrate and 280% with histone as substrate compared to no addition
Na2SO4
-
14 mM, 30°C, pH 7.5, relative activity 152% with histone as substrate compared to no addition
NaCl
-
14 mM, 30°C, pH 7.5, relative activity 102% with glycogen synthase D as substrate and 108% with histone as substrate compared to no addition
rabbit liver glycogen
-
1 mg/ml, 30°C, pH 7.5, 119% relative activity with histone as substrate
-
additional information
-
study of effects of D-glucose 6-phosphate on activating compounds
-
additional information
-
study of effects of MgCl2 in presence of AMP, ADP, ATP, UMP, UDP, UTP, or citrate
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
kinetics with glycogen synthase D, phosphorylase a, and histone in presence of no, 10, 35, and 100 mM MgCl2, expressed as concentrations of [32P] phosphate
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5
-
isoelectric focusing, pH-range 3-10, phosphatase activities cannot be separated on the basis of isoelectric properties of the enzyme
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PP2BA_BOVIN
521
0
58672
Swiss-Prot
other Location (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
18000
1 * 60000, subunit A, + 2 * 18000, subunit B, retina isozyme CaN A and B subunits, SDS-PAGE
60000
1 * 60000, subunit A, + 2 * 18000, subunit B, retina isozyme CaN A and B subunits, SDS-PAGE
80000 - 90000
-
phosphatase 2B, i.e. calcineurin, sedimentation equilibrium centrifugation
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterotrimer
1 * 60000, subunit A, + 2 * 18000, subunit B, retina isozyme CaN A and B subunits, SDS-PAGE
dimer
dimer
-
calcineurin B: 19200, Ca2+ binding, 35% homology with bovine brain calmodulin
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
-
methylation of the C-terminus of the catalytic subunit controls the formation of heterotrimeric holoenzymes by increasing the binding of regulatory B subunits
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 50 mM imidazole chloride buffer, pH 7.3, 1 mM EDTA, 1 mM benzamidine, 0.1 mM phenylmethanesulfonyl fluoride, 1 mM dithiothreitol, 1.4 M NaCl, 10% glycerol, 8 months
-
4°C, or -20°C, or -70°C, half-life 24 h, inactivation is not prevented by addition of glycerol, bovine serum albumin, divalent cations or SH-reagents
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged isozymes from Escherichia coli strain M13 by nickel affinity chromatography to near homogeneity
150fold purified, ratio of activities with glycogen synthase D, phosphorylase a, and histone as substrates are unchanged during purification, final enzyme preparation is also active on phosphorylase kinase and casein, no activity on p-nitrophenyl phosphate, when assayed at pH 7.5 or at pH 10.5
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cDNA sequence determination and analysis, a 10 amino acid, residues ATVEAIEADE, deletion before the autoinhibitory domain is observed in bovine retina CaN A compared to bovine brain CaN A, sequence comparisona, expression of His-tagged isozymes in Escherichia coli strain M13(pREP4) using expression vector pQE9
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nakai, C.; Thomas, J.A.
Substrate specificity of glycogen synthase phosphatase from bovine heart: action on phosphorylase a and histone
Biochem. Biophys. Res. Commun.
52
530-536
1973
Bos taurus
Blumenthal, D.K.; Chan, C.P.; Takio, K.; Gallis, B.; Hansen, R.S.; Krebs, E.G.
Substrate specificity of calmodulin-dependent protein phosphatases
Adv. Protein Phosphatases
1
163-174
1985
Bos taurus
-
Simonelli, P.F.; Li, H.G.
Regulation of calmodulin-dependent phosphoprotein phosphatase (calcineurin) by synergistic action of Ca(II), calmodulin, and Mg(II) or transition metal ions
Adv. Protein Phosphatases
1
175-190
1985
Bos taurus
-
Mumby, M.
The structure and function of cardiac protein phosphatases
Adv. Protein Phosphatases
3
301-326
1986
Bos taurus, Canis lupus familiaris, Oryctolagus cuniculus, Mammalia, Rattus norvegicus, Sus scrofa
-
Reed, L.J.; Damuni, Z.
Mitochondrial protein phosphatases
Adv. Protein Phosphatases
4
59-76
1987
Bos taurus
-
Damuni, Z.; Reed, L.J.
Purification and characterization of a divalent cation-independent, spermine-stimulated protein phosphatase from bovine kidney mitochondria
J. Biol. Chem.
262
5133-5138
1987
Bos taurus
Martin, B.L.; Graves, D.J.
The chemical mechanism of calcineurin: A model for phosphotyrosyl protein phosphatases
Adv. Protein Phosphatases
4
95-125
1987
Bos taurus
-
Stone, S.R.; Hofsteenge, J.; Hemmings, B.A.
The primary structure of the catalytic subunit of phosphatase 2A as determined by molecular cloning: conservation of sequence between species and existence of isotypes
Adv. Protein Phosphatases
4
375-389
1987
Bos taurus, Oryctolagus cuniculus, Sus scrofa
-
Green, D.D.; Yang, S.; Mumby, M.C.
Molecular cloning and sequence analysis of the catalytic subunit of bovine type 2A protein phosphatase
Proc. Natl. Acad. Sci. USA
84
4880-4884
1987
Bos taurus
Merat, D.L.; Cheung, W.Y.
Calmodulin-dependent protein phosphatase: isolation of subunits and reconstitution to holoenzyme
Methods Enzymol.
139
79-87
1987
Bos taurus
Chernoff, J.; Seels, M.A.; Li, H.C.
Characterization of phosphotyrosyl-protein phosphatase activity associated with calcineurin
Biochem. Biophys. Res. Commun.
121
141-148
1984
Bos taurus
Damuni, Z.; Reed, L.J.
Purification and properties of the catalytic subunit of the branched-chain alpha-keto acid dehydrogenase phosphatase from bovine kidney mitochondria
J. Biol. Chem.
262
5129-5132
1987
Bos taurus
King, M.M.; Huang, C.Y.
The calmodulin-dependent activation and deactivation of the phosphoprotein phosphatase, calcineurin, and the effect of nucleotides, pyrophosphate, and divalent metal ions. Identification of calcineurin as a Zn and Fe metalloenzyme
J. Biol. Chem.
259
8847-8856
1984
Bos taurus
Honkanen, R.E.; Zwiller, J.; Daily, S.L.; Khatra, B.S.; Dukelow, M.; Boynton, A.L.
Identification, purification, and characterization of a novel serine/threonine protein phosphatase from bovine brain
J. Biol. Chem.
266
6614-6619
1991
Bos taurus
Klumpp, S.; Selke, D.; Fischer, D.; Baumann, A.; Muller, F.; Thanos, S.
Protein phosphatase type-2C isozymes present in vertebrate retinae: purification, characterization, and localization in photoreceptors
J. Neurosci. Res.
51
328-338
1998
Bos taurus
Price, N.E.; Mumby, M.C.
Effects of regulatory subunits on the kinetics of protein phosphatase 2A
Biochemistry
39
11312-11318
2000
Bos taurus
Tolstykh, T.; Lee, J.; Vafai, S.; Stock, J.B.
Carboxyl methylation regulates phosphoprotein phosphatase 2A by controlling the association of regulatory B subunits
EMBO J.
19
5682-5691
2000
Bos taurus
Nakai, C.; Thomas, J.A.
Properties of a phosphoprotein phosphatase from bovine heart with activity on glycogen synthase, phosphorylase, and histone
J. Biol. Chem.
249
6459-6467
1974
Bos taurus
Kloeker, S.; Reed, R.; McConnell, J.L.; Chang, D.; Tran, K.; Westphal, R.S.; Law, B.K.; Colbran, R.J.; Kamoun, M.; Campbell, K.S.; Wadzinski, B.E.
Parallel purification of three catalytic subunits of the protein serine/threonine phosphatase 2A family (PP2A(C), PP4(C), and PP6(C)) and analysis of the interaction of PP2A(C) with alpha4 protein
Protein Expr. Purif.
31
19-33
2003
Bos taurus, Mus musculus, Rattus norvegicus
Zuo, Y.; Selvakumar, P.; Sharma, R.K.
Molecular cloning and biochemical characterization of bovine retina calcineurin
Mol. Cell. Biochem.
333
73-82
2010
Bos taurus (P48452), Bos taurus
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