Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3-hydroxy 3-methylglutaryl CoenzymeA reductase phosphatase
-
-
-
-
Aspergillus awamori acid protein phosphatase
-
-
-
-
BCKDH phosphatase
-
-
-
-
branched-chain alpha-keto acid dehydrogenase phosphatase
-
-
-
-
CaM-kinase phosphatase
-
-
-
-
casein phosphatase
-
-
-
-
Fibroblast growth factor inducible protein 13
-
-
-
-
Flap wing protein
-
-
-
-
general phosphoprotein phosphatase
-
-
glycogen synthase phosphatase
-
-
HMG-CoA reductase phosphatase
-
-
-
-
Magnesium-dependent calcium inhibitable phosphatase
-
-
-
-
Microtubule star protein
-
-
-
-
phosphoprotein phosphatase
-
-
-
-
phosphopyruvate dehydrogenase phosphatase
-
-
-
-
phosphospectrin phosphatase
-
-
-
-
polycation modulated (PCM-) phosphatase
-
-
-
-
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
-
-
-
-
protein serine/threonine phosphatase
-
Retinal degeneration C protein
-
-
-
-
serine/threonine protein phosphatase
-
Suppressor protein SDS21
-
-
-
-
additional information
calcineurin is a member of the Ser/Thr protein phosphatase family
calcineurin
-
-
-
-
PP3
-
-
Pp4
-
-
-
-
PP6
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
-
-
-
?
alpha-naphthyl phosphate + H2O
alpha-naphthol + phosphate
-
-
-
-
?
beta-naphthyl phosphate + H2O
beta-naphthol + phosphate
-
-
-
-
?
cAMP dependent protein kinase + H2O
?
-
-
-
-
?
DLDVPIPGRFDRRVS(P)VAAE + H2O
DLDVPIPGRFDRRVSVAAE + phosphate
-
-
-
-
?
DLDVPIPGRFDRRVY(P)VAAE + H2O
DLDVPIPGRFDRRVYVAAE + phosphate
-
-
-
-
?
DRRVS(P)VAAE + H2O
DRRVSVAAE + phosphate
-
-
-
-
?
DRVY(P)IHPFHL + H2O
DRVYIHPFHL + phosphate
-
-
-
-
?
FDRRVS(P)VAAE + H2O
FDRRVSVAAE + phosphate
-
-
-
-
?
fluorotyrosine phosphate + H2O
fluorotyrosine + phosphate
-
-
-
-
?
FYDEEVDEMY(P)REAPIDKKGNFNY(P)VEFTR + H2O
FYDEEVDEMYREAPIDKKGNFNYVEFTR + phosphate
-
-
-
-
?
glycogen synthase D + H2O
glycogen synthase I + phosphate
histone + H2O
histone + phosphate
-
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
-
-
-
-
?
phospho-D,L-tyrosine + H2O
D,L-tyrosine + phosphate
-
-
-
-
?
phospho-L-tyrosine + H2O
L-tyrosine + phosphate
-
-
-
-
?
phosphoangiotensin + H2O
angiotensin + phosphate
-
phosphorylated at Tyr
-
-
?
phosphocasein + H2O
casein + phosphate
-
-
-
-
?
phosphohistone + H2O
histone + phosphate
-
-
-
-
?
phosphomyosin light chain + H2O
myosin light chain + phosphate
-
-
-
-
?
phosphoprotein + H2O
protein + phosphate
phosphoproteins + H2O
proteins + phosphate
phosphorylase a + H2O
phosphorylase b + 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 casein (PKA) + H2O
casein (PKA) + phosphate
-
-
-
-
?
phosphorylated histone + H2O
histone + phosphate
phosphorylated histone h1 (PKA) + H2O
histone h1 (PKA) + phosphate
-
-
-
-
?
phosphorylated histone h1 (PKC) + H2O
histone h1 (PKC) + phosphate
-
-
-
-
?
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
-
-
-
-
?
phosphorylated troponin + H2O
troponin + phosphate
-
-
-
-
?
PIPGRFDRRVS(P)VAAE + H2O
PIPGRFDRRVSVAAE + phosphate
-
-
-
-
?
synthetic peptides with phosphotyrosyl residues + H2O
synthetic peptides + phosphate
-
-
-
-
?
tetrafluorotyrosine phosphate + H2O
tetrafluorotyrosine + phosphate
-
-
-
-
?
additional information
?
-
glycogen synthase D + H2O
glycogen synthase I + phosphate
-
-
-
-
?
glycogen synthase D + H2O
glycogen synthase I + phosphate
-
-
-
-
r
phosphoprotein + H2O
protein + phosphate
-
-
-
-
?
phosphoprotein + H2O
protein + 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
-
-
?
phosphorylase a + H2O
phosphorylase b + phosphate
-
-
-
-
?
phosphorylase a + H2O
phosphorylase b + phosphate
-
-
-
-
r
phosphorylated histone + H2O
histone + phosphate
-
-
-
-
?
phosphorylated histone + H2O
histone + phosphate
-
-
-
?
additional information
?
-
-
no activity on p-nitrophenyl phosphate, when assayed at pH 7.5 or at pH 10.5
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
3-hydroxy-3-methylglutaryl CoA
-
-
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
-
Ca2+
-
degree of inhibition depends on concentration of Mg2+
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
-
guanosine 5'-(beta,gamma-imido)triphosphate
-
-
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
myosin light chain hydroxy peptide
-
competitive inhibition
-
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
Nucleoside mono-, di-, and triphosphates
-
e.g. GTP, GDP, ATP, ADP
-
phosphorylase a
-
mixed type inhibitor with glycogen synthase d as substrate, increases Km 2fold with only small decearse in vmax
protamine
-
inhibition of phosphatase PP3
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
-
-
ATP
-
1.4 mM, 30°C, pH 7.5, 47% remaining activity with glycogen synthase D as substrate and 15% with phosphorylase a
microcystin-LR
-
inhibition of phosphatase PP3
okadaic acid
-
inhibition of phosphatase PP3
okadaic acid
-
no inhibition of phosphatase PP2C
phosphate
-
-
phosphate
-
competitive inhibition to C-subunit and AC-dimer, noncompetitive inhibition to AC-R2
additional information
-
study of effects of D-glucose 6-phosphate on inhibitory compounds; study of effects of MgCl2 in presence of AMP, ADP, ATP, UMP, UDP, UTP, or citrate
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ADP
-
1.4 mM, 30°C, pH 7.5, 104% relative activity with histone as substrate
AMP
-
1.4 mM, 30°C, pH 7.5, 102% relative activity with histone as substrate
ATP
-
1.4 mM, 30°C, pH 7.5, 107% relative activity with histone as substrate
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
EDTA
-
14 mM, 30°C, pH 7.5, 175% relative activity with histone as substrate
EGTA
-
14 mM, 30°C, pH 7.5, 127% relative activity with histone 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
-
Inhibitor-2
-
stimulation of phosphatase PP3
-
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
-
UMP
-
1.4 mM, 30°C, pH 7.5, 102% relative activity with histone as substrate
UTP
-
1.4 mM, 30°C, pH 7.5, 108% relative activity with histone as substrate
additional information
-
regulated by phosphorylation, phosphatase 2B
-
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DUS10_BOVIN
482
0
52389
Swiss-Prot
other Location (Reliability: 3)
PP2BA_BOVIN
521
0
58672
Swiss-Prot
other Location (Reliability: 2)
PPM1K_BOVIN
372
0
41151
Swiss-Prot
Mitochondrion (Reliability: 1)
PPM1L_BOVIN
360
0
41042
Swiss-Prot
Secretory Pathway (Reliability: 4)
PP2AB_BOVIN
309
0
35561
Swiss-Prot
other Location (Reliability: 1)
SSU72_BOVIN
194
0
22588
Swiss-Prot
Mitochondrion (Reliability: 4)
DUS26_BOVIN
211
0
23767
Swiss-Prot
Mitochondrion (Reliability: 2)
DUS29_BOVIN
219
0
24984
Swiss-Prot
other Location (Reliability: 1)
ILKAP_BOVIN
370
0
40622
Swiss-Prot
other Location (Reliability: 1)
PP1A_BOVIN
330
0
37512
Swiss-Prot
other Location (Reliability: 2)
PP1B_BOVIN
327
0
37187
Swiss-Prot
other Location (Reliability: 2)
CPPED_BOVIN
313
0
35410
Swiss-Prot
Mitochondrion (Reliability: 4)
PP1G_BOVIN
323
0
36984
Swiss-Prot
other Location (Reliability: 2)
PLPP_BOVIN
296
0
31749
Swiss-Prot
other Location (Reliability: 4)
PPM1A_BOVIN
382
0
42530
Swiss-Prot
other Location (Reliability: 2)
PPM1B_BOVIN
484
0
53431
Swiss-Prot
other Location (Reliability: 2)
UBCP1_BOVIN
318
0
36805
Swiss-Prot
other Location (Reliability: 2)
DUS6_BOVIN
381
0
42307
Swiss-Prot
other Location (Reliability: 2)
PP4C_BOVIN
307
0
35080
Swiss-Prot
other Location (Reliability: 1)
PPM1G_BOVIN
543
0
58607
Swiss-Prot
other Location (Reliability: 3)
DUS14_BOVIN
198
0
22237
Swiss-Prot
Mitochondrion (Reliability: 5)
DUS18_BOVIN
188
0
21028
Swiss-Prot
Mitochondrion (Reliability: 3)
PP2AA_BOVIN
309
0
35594
Swiss-Prot
other Location (Reliability: 1)
CNEP1_BOVIN
244
1
28393
Swiss-Prot
Mitochondrion (Reliability: 5)
RPAP2_BOVIN
608
0
68698
Swiss-Prot
Mitochondrion (Reliability: 4)
A6H703_BOVIN
525
0
59097
TrEMBL
other Location (Reliability: 5)
E1BBD9_BOVIN
195
0
22653
TrEMBL
Mitochondrion (Reliability: 3)
A0A3Q1M4S8_BOVIN
352
0
38153
TrEMBL
other Location (Reliability: 3)
F1MM08_BOVIN
394
0
42968
TrEMBL
other Location (Reliability: 1)
A0A3Q1MPJ7_BOVIN
351
0
39267
TrEMBL
Mitochondrion (Reliability: 3)
A0A3Q1M7P6_BOVIN
562
0
63397
TrEMBL
Mitochondrion (Reliability: 3)
Q2T9T8_BOVIN
198
0
22357
TrEMBL
Mitochondrion (Reliability: 5)
A5D7T5_BOVIN
512
0
58180
TrEMBL
other Location (Reliability: 5)
E1BDE3_BOVIN
260
0
29121
TrEMBL
other Location (Reliability: 2)
A0A3Q1MG50_BOVIN
464
0
50944
TrEMBL
other Location (Reliability: 1)
A0A3Q1MPV2_BOVIN
566
0
63883
TrEMBL
Mitochondrion (Reliability: 3)
Q58D70_BOVIN
309
0
35580
TrEMBL
other Location (Reliability: 1)
A0A3Q1LQB7_BOVIN
221
0
25585
TrEMBL
Mitochondrion (Reliability: 4)
A0A3Q1LQS6_BOVIN
557
0
62837
TrEMBL
Mitochondrion (Reliability: 3)
A0A3Q1NK59_BOVIN
243
0
28021
TrEMBL
other Location (Reliability: 3)
A9ZTK8_BOVIN
123
0
14355
TrEMBL
other Location (Reliability: 2)
A0A3Q1M5Y8_BOVIN
250
0
27989
TrEMBL
Secretory Pathway (Reliability: 3)
F1ME76_BOVIN
198
0
22341
TrEMBL
Mitochondrion (Reliability: 5)
F1MG88_BOVIN
354
0
39401
TrEMBL
Mitochondrion (Reliability: 5)
A0A3Q1MWS0_BOVIN
932
0
101041
TrEMBL
other Location (Reliability: 2)
A0A3Q1MYZ2_BOVIN
276
0
30961
TrEMBL
other Location (Reliability: 1)
Q2KJE3_BOVIN
367
0
39528
TrEMBL
other Location (Reliability: 3)
F1MP34_BOVIN
314
0
34118
TrEMBL
other Location (Reliability: 3)
E1BIZ2_BOVIN
1031
0
113100
TrEMBL
other Location (Reliability: 5)
A0A3Q1LPR7_BOVIN
988
0
108532
TrEMBL
Mitochondrion (Reliability: 3)
F1MI99_BOVIN
367
0
39544
TrEMBL
other Location (Reliability: 3)
A0A3Q1MTH2_BOVIN
499
0
56485
TrEMBL
other Location (Reliability: 2)
A0A3Q1LM41_BOVIN
84
0
9640
TrEMBL
other Location (Reliability: 1)
Q0V8L5_BOVIN
430
0
49319
TrEMBL
other Location (Reliability: 1)
A0A3Q1MHT1_BOVIN
524
0
59209
TrEMBL
other Location (Reliability: 2)
Q2T9T7_BOVIN
203
0
22555
TrEMBL
other Location (Reliability: 1)
A6QQH5_BOVIN
146
0
16456
TrEMBL
other Location (Reliability: 1)
A0A3Q1M0B7_BOVIN
489
0
55793
TrEMBL
Mitochondrion (Reliability: 5)
A6QPK9_BOVIN
112
0
11836
TrEMBL
other Location (Reliability: 3)
G3N3B3_BOVIN
422
0
44975
TrEMBL
other Location (Reliability: 2)
A6QLS1_BOVIN
368
0
40561
TrEMBL
other Location (Reliability: 2)
A0A3Q1MJE6_BOVIN
321
0
36570
TrEMBL
Mitochondrion (Reliability: 5)
F1MQM7_BOVIN
457
0
49663
TrEMBL
Mitochondrion (Reliability: 3)
E1BPN5_BOVIN
1409
0
155824
TrEMBL
other Location (Reliability: 3)
A0A3Q1MKH1_BOVIN
577
0
65336
TrEMBL
other Location (Reliability: 4)
A7YY43_BOVIN
185
0
20504
TrEMBL
other Location (Reliability: 1)
Q32PC4_BOVIN
167
0
18659
TrEMBL
other Location (Reliability: 1)
A0A3Q1NKG4_BOVIN
286
0
32404
TrEMBL
other Location (Reliability: 5)
A0A3Q1MH19_BOVIN
290
0
33058
TrEMBL
other Location (Reliability: 1)
A0A3Q1NGM8_BOVIN
324
0
36906
TrEMBL
other Location (Reliability: 4)
A6QLP9_BOVIN
649
0
71168
TrEMBL
Mitochondrion (Reliability: 3)
F6S044_BOVIN
112
0
11654
TrEMBL
other Location (Reliability: 2)
F1N6B7_BOVIN
498
0
56495
TrEMBL
other Location (Reliability: 2)
F1N719_BOVIN
499
0
56882
TrEMBL
other Location (Reliability: 1)
E1BAB2_BOVIN
194
0
22530
TrEMBL
Mitochondrion (Reliability: 5)
Q2KJ43_BOVIN
271
0
30706
TrEMBL
other Location (Reliability: 2)
Q0V8M3_BOVIN
432
0
49505
TrEMBL
other Location (Reliability: 1)
A0A3Q1N170_BOVIN
311
0
35548
TrEMBL
other Location (Reliability: 2)
Q7M2R6_BOVIN
114
0
12606
TrEMBL
other Location (Reliability: 2)
E1B9Y5_BOVIN
753
0
86399
TrEMBL
Mitochondrion (Reliability: 5)
Q7M2L6_BOVIN
33
0
3998
TrEMBL
other Location (Reliability: 1)
A0A3Q1MWP5_BOVIN
489
1
55433
TrEMBL
Secretory Pathway (Reliability: 1)
A0A3Q1MBU1_BOVIN
425
0
47124
TrEMBL
other Location (Reliability: 2)
A0A3Q1LZG0_BOVIN
563
0
63668
TrEMBL
other Location (Reliability: 4)
A0A3Q1MLW0_BOVIN
337
0
38548
TrEMBL
other Location (Reliability: 2)
Q2KIC7_BOVIN
305
0
35144
TrEMBL
other Location (Reliability: 1)
A0A3Q1M091_BOVIN
434
0
47675
TrEMBL
other Location (Reliability: 1)
A0A3Q1MCX5_BOVIN
609
1
68959
TrEMBL
Mitochondrion (Reliability: 3)
A0A3Q1N2B0_BOVIN
1402
0
155067
TrEMBL
other Location (Reliability: 5)
F1MI92_BOVIN
649
0
71188
TrEMBL
Mitochondrion (Reliability: 3)
A0A3Q1MWQ3_BOVIN
1429
0
157970
TrEMBL
Mitochondrion (Reliability: 5)
A0A3Q1M4S3_BOVIN
527
0
59281
TrEMBL
other Location (Reliability: 2)
A0A3Q1NIY5_BOVIN
608
0
68697
TrEMBL
Mitochondrion (Reliability: 3)
A0A3Q1LM49_BOVIN
454
0
51568
TrEMBL
other Location (Reliability: 5)
A0A3Q1NG49_BOVIN
577
0
64913
TrEMBL
Mitochondrion (Reliability: 3)
F1MBQ1_BOVIN
658
0
75965
TrEMBL
other Location (Reliability: 1)
E1BEW5_BOVIN
307
0
32817
TrEMBL
Mitochondrion (Reliability: 5)
F1MEZ2_BOVIN
380
0
41589
TrEMBL
Mitochondrion (Reliability: 3)
CANB1_BOVIN
170
0
19300
Swiss-Prot
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
brenda
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
-
brenda
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
-
brenda
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
-
brenda
Reed, L.J.; Damuni, Z.
Mitochondrial protein phosphatases
Adv. Protein Phosphatases
4
59-76
1987
Bos taurus
-
brenda
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
brenda
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
-
brenda
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
-
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
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
brenda
Price, N.E.; Mumby, M.C.
Effects of regulatory subunits on the kinetics of protein phosphatase 2A
Biochemistry
39
11312-11318
2000
Bos taurus
brenda
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
brenda
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
brenda
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
brenda
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
brenda
Zhang, M.; Yogesha, S.D.; Mayfield, J.E.; Gill, G.N.; Zhang, Y.
Viewing serine/threonine protein phosphatases through the eyes of drug designers
FEBS J.
280
4739-4760
2013
Homo sapiens (P36873), Bos taurus (P48452)
brenda