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Information on EC 3.1.3.16 - protein-serine/threonine phosphatase and Organism(s) Rattus norvegicus
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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: Rattus norvegicus
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
-
-
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 2A
-
-
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
-
-
-
-
Pp4
-
-
-
-
PP5
-
-
-
-
PP6
-
-
-
-
PPT
-
-
-
-
protein phosphatase
-
-
-
-
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
fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase + H2O
? + phosphate
-
-
-
-
?
fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase + H2O
fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase + phosphate
-
heterotrimeric phosphatase 2A catalyzing the dephosphorylation of fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase
-
-
?
glycogen synthase + H2O
glycogen synthase + phosphate
-
serine-phosphorylated glycogen synthase
-
-
?
myelin basic phosphoprotein + H2O
myelin basic protein + phosphate
-
-
-
-
?
phosphophosphorylase kinase + H2O
phosphorylase kinase + phosphate
-
specific for alpha-subunit
-
-
?
phosphoproteins + H2O
proteins + phosphate
-
-
134607, 134610, 134611, 134612, 134613, 134638, 134642, 134643, 134647, 134651, 134663, 134664, 134666, 134671, 134672, 134673
-
-
?
phosphorylated 3-hydroxy 3-methylglutaryl coenzyme A reductase + H2O
3-hydroxy 3-methylglutaryl coenzyme A reductase + phosphate
-
-
-
-
?
phosphorylated acetyl-CoA carboxylase + H2O
acetyl-CoA carboxylase + phosphate
-
i.e. EC 6.4.1.2, phosphorylated
-
-
?
phosphorylated extracellular-signal-regulated kinase + H2O
extracellular-signal-regulated kinase + phosphate
-
PP2A is involved in the inactivation, but not the activation, of extracellular-signal-regulated kinase
-
-
?
phosphorylated glycogen phosphorylase + H2O
glycogen phosphorylase + phosphate
-
-
-
-
?
phosphorylated histone h1 (PKA) + H2O
histone h1 (PKA) + phosphate
-
-
-
-
?
phosphorylated histone h1 (PKC) + H2O
histone h1 (PKC) + phosphate
-
-
-
-
?
phosphorylated microtubule associated protein + H2O
microtubule associated protein + phosphate
-
-
-
-
?
phosphorylated myosin light chain 2 + H2O
myosin light chain 2 + phosphate
-
preferred target substrate for PP1 in the thick filament
-
-
?
phosphorylated phosphorylase kinase + H2O
phosphorylase kinase + phosphate
-
-
-
-
?
phosphorylated Raf + H2O
Raf + phosphate
-
Raf is dephosphorylated at Ser259
-
-
?
phosphorylated tropomyosin-related kinase A + H2O
tropomyosin-related kinase A + phosphate
-
two neuron-enriched regulatory subunits, B'beta and B'delta, recruit PP2A into a complex with tropomyosin-related kinase A to dephosphorylate the nerve growth factor receptor on Ser/Thr residues and to potentiate its intrinsic tyrosine kinase activity
-
-
?
phosphorylated troponin I + H2O
troponin I + phosphate
-
preferred target substrate for PP1 in the thin filament
-
-
?
phosphorylated troponin T + H2O
troponin T + phosphate
-
preferred target substrate for PP1 in the thin filament
-
-
?
[aquaporin-2]-serine/threonine phosphate + H2O
[aquaporin-2]-serine/threonine + phosphate
-
-
-
-
?
phospho-L-tyrosine + H2O
L-tyrosine + phosphate
-
preferred substrate
-
-
?
phosphoprotein + H2O
protein + phosphate
-
involved in the intracellular mechanism through which adrenocortical steroidogenesis is regulated, acting at a point after cAMP generation and action but proximal to the side-chain cleavage of cholesterol
-
-
?
phosphoprotein + H2O
protein + phosphate
-
involved in regulating exocytosis from the rat parotid gland via a cAMP-mediated process
-
-
?
phosphoprotein + H2O
protein + phosphate
-
control of cholesterol genesis
-
-
?
phosphorylated ERK2 + H2O
ERK2 + phosphate
-
PP2A acts as a gate-keeper of extracellular signal-regulated kinase, ERK, activity in neuronal PC12 cells, the PP2A regulatory subunits Balpha and Bdelta target the PP2A heterotrimer to dephosphorylate and inactivate ERK, silencing of B subunits leads to hyperactivation of ERK stimulated by constitutively active MEK1, overview
-
-
?
phosphorylated ERK2 + H2O
ERK2 + phosphate
-
dephosphorylation of the activation loop threonine of ERK
-
-
?
phosphorylated lamban + H2O
lamban + phosphate
-
the substrate enzyme regulates the activity of the Ca2+-ATPase pump on the sarcoplasmic reticulum and is a key regulator of both basal contractility and the heart's beta-agonist responses, overview
dephosphorylated phospholamban exhibits an inhibitory effect on SERCA2a
-
?
phosphorylated pRb protein + H2O
pRb protein + phosphate
-
ceramide prevents retinoblastoma gene product pRb protein hyperphosphorylation by PP1 activation, nerve growth factor deprivation in sympathetic neurons leads to inhibition of PP1 and hyperphosphorylation of pRb protein
-
-
?
additional information
?
-
-
ceramide-induced cell survival mechanism, overview
-
-
?
additional information
?
-
-
PP2A is involved in central sensitization, PP2A negatively regulates the phosphorylation of N-methyl-D-aspartate, NMDA, receptors in response to capsaicin induction in the spinal cord
-
-
?
additional information
?
-
-
PP2A modulates Akt activity, role of PP2A holoenzyme and subunits in MAPK signaling pathways, overview
-
-
?
additional information
?
-
PP5 acts as an effector in Rac GTPase signalling via interaction of its N-terminal TPR domain with Rac-GTP, PP5 inhibition results in blockage of KCNH2 channel stimulation by thyroid hormone and by Rac in pituitary cells, overview
-
-
?
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
fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase + H2O
fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase + phosphate
-
heterotrimeric phosphatase 2A catalyzing the dephosphorylation of fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase
-
-
?
phospho-L-tyrosine + H2O
L-tyrosine + phosphate
-
preferred substrate
-
-
?
phosphorylated ERK2 + H2O
ERK2 + phosphate
-
PP2A acts as a gate-keeper of extracellular signal-regulated kinase, ERK, activity in neuronal PC12 cells, the PP2A regulatory subunits Balpha and Bdelta target the PP2A heterotrimer to dephosphorylate and inactivate ERK, silencing of B subunits leads to hyperactivation of ERK stimulated by constitutively active MEK1, overview
-
-
?
phosphorylated lamban + H2O
lamban + phosphate
-
the substrate enzyme regulates the activity of the Ca2+-ATPase pump on the sarcoplasmic reticulum and is a key regulator of both basal contractility and the heart's beta-agonist responses, overview
dephosphorylated phospholamban exhibits an inhibitory effect on SERCA2a
-
?
phosphorylated pRb protein + H2O
pRb protein + phosphate
-
ceramide prevents retinoblastoma gene product pRb protein hyperphosphorylation by PP1 activation, nerve growth factor deprivation in sympathetic neurons leads to inhibition of PP1 and hyperphosphorylation of pRb protein
-
-
?
[aquaporin-2]-serine/threonine phosphate + H2O
[aquaporin-2]-serine/threonine + phosphate
-
-
-
-
?
phosphoprotein + H2O
protein + phosphate
-
involved in the intracellular mechanism through which adrenocortical steroidogenesis is regulated, acting at a point after cAMP generation and action but proximal to the side-chain cleavage of cholesterol
-
-
?
phosphoprotein + H2O
protein + phosphate
-
involved in regulating exocytosis from the rat parotid gland via a cAMP-mediated process
-
-
?
phosphoprotein + H2O
protein + phosphate
-
control of cholesterol genesis
-
-
?
additional information
?
-
-
ceramide-induced cell survival mechanism, overview
-
-
?
additional information
?
-
-
PP2A is involved in central sensitization, PP2A negatively regulates the phosphorylation of N-methyl-D-aspartate, NMDA, receptors in response to capsaicin induction in the spinal cord
-
-
?
additional information
?
-
-
PP2A modulates Akt activity, role of PP2A holoenzyme and subunits in MAPK signaling pathways, overview
-
-
?
additional information
?
-
PP5 acts as an effector in Rac GTPase signalling via interaction of its N-terminal TPR domain with Rac-GTP, PP5 inhibition results in blockage of KCNH2 channel stimulation by thyroid hormone and by Rac in pituitary cells, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Calmodulin
-
activates the enzyme with substratees phospho-L-serine and phospho-L-threonine, but not with phospho-L-tyrosine
Mg2+
Mn2+
additional information
-
heterotrimeric phosphatase 2A catalyzing the dephosphorylation of fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase is not dependent on Mg2+, Ca2+, or Mn2+
Ca2+
-
activates, synergistic with calmodulin, activation is completely inhibited by trifluoroperazine
Mg2+
when p-nitrophenyl phosphate is used as substrate 10 mM MgCl2 increases the activity, when phosphocasein is used as substrate 10 mM MgCl2 reduces the activity by 50%
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
alpha 4 protein
-
rapamycin has no effect on PP2A-C association with the inhibitor alpha 4 protein
-
FR225659
-
synthesizes by Helicomyces sp. strain 19353, inhibits PP1 and PP2A, inhibition of gluconeogenese in vivo in hepatocytes
FR253761
-
synthetic derivative of FR225659, inhibits PP1 and PP2A, inhibition of gluconeogenese in vivo in hepatocytes
FR259383
-
synthetic derivative of FR225659, inhibits PP1 and PP2A, inhibition of gluconeogenese in vivo in hepatocytes
ginsenoside Rg1
from Panax ginseng roots, Rg1 alleviates left ventricular hypertrophy induced by abdominal aorta coarctation, and the protection appears to be due, at least in part, to its inhibitory effects on calcineurin and MAP kinase signaling pathways, overview
protein phosphatase-1 inhibitor-1
-
plays a role in cardiac physiology and pathophysiology, overview
-
regucalcin
-
has regulatory function in heart cytosol; the protein inhibits the enzyme in presence of EGTA or ethylene glycol and has a regulatory function for the enzyme independently of Ca2+
-
tris(2-carboxyethyl)-phosphine hydrochloride
-
phosphatase activity is decreased by 5 mM
okadaic acid
-
inhibition of heterotrimeric phosphatase 2A catalyzing the dephosphorylation of fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase
okadaic acid
-
two enzyme forms in parotid gland, one is sensitive, the other not inhibited
okadaic acid
inhibition of wild-type PP5, no inhibition of PP5 mutant 451A
okadaic acid
-
PP2A activity is dose-dependently decreased with okadaic acid with 15% inhibition at 0.05 nM, 55% inhibition at 0.5 nM, and 69% inhibition at 5 nM
additional information
-
protein phosphatase inhibitor II and cyclosporin A have no inhibitory effect on isozyme PP2A
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(5Z,8Z,14Z)-11,12-epoxyeicosatrienoic acid
-
increases activity 3fold at 0.001 mM
2-mercaptoethanol
-
phosphatase activity is increased to up to 49-62% by 3 mM
C6-ceramide
-
activates in vivo and 2-3fold in vitro, blocked by protein phosphatase inhibitor-2, i.e. I-2, ceramide prevents retinoblastoma gene product pRb hyperphosphorylation by PP1 activation
dithiothreitol
-
phosphatase activity is increased to up to 49-62% by 0.3 mM
estrogen
-
estrogen maintains the function of isozymes PP1, PP2A, and calcineurin
tris(2-carboxyethyl)-phosphine hydrochloride
-
phosphatase activity is increased to up to 49-62% by 0.3 mM
Xylulose 5-phosphate
-
activation of a heterotrimeric phosphatase 2A catalyzing the dephosphorylation of fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase
additional information
-
nerve growth factor is required for PP activation in vivo
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
134607, 134610, 134611, 134612, 134613, 134638, 134642, 134643, 134647, 134651, 134663, 134664, 134666, 134671, 134672, 134673
-
-
-
677930, 679165, 680212, 680822, 682117, 682620, 692085, 693317, 693756, 693780, 694164, 709562, 749543
-
-
regucalcin-expressing transgenic Sprague-Dawley rats and wild-type male Wistar rats
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
inner medullary collecting ducts, proteomic analysis of the cytoplasmic fraction of inner medullary collecting ducts, overview
-
reduced acitvity in diabetic animals indicates a differential regulation
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
heterotrimeric phosphatase 2A catalyzing the dephosphorylation of fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase
-
PP1 exhibits strong nuclear staining, PP2A and PP5 are more diffusely expressed
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
calcineurin participates in neuronal apoptosis, protection of neurons from apoptosis by apolipoprotein E-containing lipoproteins does not require lipoprotein uptake and involves activation of phospholipase Cgamma1 and inhibition of calcineurin
malfunction
-
perturbations in the regulation of PP1 by inhibitor-1 have been implicated in the pathogenesis of heart failure, role of PP1 and protein phosphatase-1 inhibitor-1 in the failing heart, overview
physiological function
-
type 1 protein phosphatase is a critical negative regulator of Ca2+ cycling and contractility in the cardiomyocyte. In particular, it mediates restoration of cardiac function to basal levels, after beta-adrenergic stimulation, by dephosphorylating key phospho-proteins, role of PP1 in the heart and its critical regulation by the endogenous phospho-protein I-1, overview
physiological function
-
phosphorylation of the aquaporin-2 (AQP2) water channel at four COOH-terminal serines plays a central role in the regulation of water permeability of the renal collecting duct. The level of phosphorylation at these sites is determined by a balance between phosphorylation by protein kinases and dephosphorylation by phosphatases. Serine/threonine phosphatases and aquaporin-2 regulation in renal collecting duct, overview
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). CPPED_RAT
312
0
35261
Swiss-Prot
Mitochondrion (Reliability: 4)
EPM2A_RAT
331
0
37144
Swiss-Prot
Mitochondrion (Reliability: 4)
PHLP1_RAT
1696
0
183364
Swiss-Prot
other Location (Reliability: 2)
PP2BA_RAT
521
0
58644
Swiss-Prot
other Location (Reliability: 2)
PP2BB_RAT
525
0
59113
Swiss-Prot
other Location (Reliability: 5)
PP2AA_RAT
309
0
35608
Swiss-Prot
other Location (Reliability: 1)
PP2AB_RAT
309
0
35575
Swiss-Prot
other Location (Reliability: 1)
DUS26_RAT
211
0
23947
Swiss-Prot
Mitochondrion (Reliability: 2)
ILKAP_RAT
392
0
42744
Swiss-Prot
other Location (Reliability: 2)
PP1A_RAT
330
0
37512
Swiss-Prot
other Location (Reliability: 2)
PP1B_RAT
327
0
37187
Swiss-Prot
other Location (Reliability: 2)
SSU72_RAT
194
0
22544
Swiss-Prot
Mitochondrion (Reliability: 4)
CDKN3_RAT
212
0
23774
Swiss-Prot
other Location (Reliability: 1)
CNEP1_RAT
244
1
28391
Swiss-Prot
Mitochondrion (Reliability: 5)
PP1G_RAT
323
0
36984
Swiss-Prot
other Location (Reliability: 2)
SSH3_RAT
652
0
72071
Swiss-Prot
Mitochondrion (Reliability: 3)
PLPP_RAT
309
0
33115
Swiss-Prot
other Location (Reliability: 3)
PPM1A_RAT
382
0
42417
Swiss-Prot
other Location (Reliability: 2)
PPM1B_RAT
390
0
42889
Swiss-Prot
other Location (Reliability: 2)
PPP5_RAT
499
0
56917
Swiss-Prot
other Location (Reliability: 1)
PTPM1_RAT
193
0
21886
Swiss-Prot
Secretory Pathway (Reliability: 5)
UBCP1_RAT
318
0
36867
Swiss-Prot
other Location (Reliability: 2)
DUS4_RAT
395
0
43187
Swiss-Prot
other Location (Reliability: 2)
DUS5_RAT
384
0
42094
Swiss-Prot
Mitochondrion (Reliability: 5)
DUS6_RAT
381
0
42319
Swiss-Prot
other Location (Reliability: 2)
DUS7_RAT
419
0
45067
Swiss-Prot
Mitochondrion (Reliability: 4)
PP4C_RAT
307
0
35068
Swiss-Prot
other Location (Reliability: 1)
PPM1E_RAT
750
0
83439
Swiss-Prot
other Location (Reliability: 2)
PPM1F_RAT
450
0
49165
Swiss-Prot
other Location (Reliability: 2)
PPM1G_RAT
542
0
58743
Swiss-Prot
other Location (Reliability: 2)
PPM1H_RAT
513
0
56380
Swiss-Prot
other Location (Reliability: 4)
PPM1J_RAT
504
0
55211
Swiss-Prot
Mitochondrion (Reliability: 3)
DUS29_RAT
215
0
24073
Swiss-Prot
other Location (Reliability: 2)
PGAM5_RAT
288
1
32060
Swiss-Prot
Secretory Pathway (Reliability: 5)
DUS12_RAT
339
0
37196
Swiss-Prot
other Location (Reliability: 2)
DUS15_RAT
236
0
26309
Swiss-Prot
other Location (Reliability: 3)
PPE1_RAT
640
0
73966
Swiss-Prot
Mitochondrion (Reliability: 5)
DUS18_RAT
204
0
22754
Swiss-Prot
other Location (Reliability: 4)
DUS1_RAT
367
0
39541
Swiss-Prot
other Location (Reliability: 3)
PPP6_RAT
305
0
35159
Swiss-Prot
other Location (Reliability: 1)
RPAP2_RAT
609
0
67892
Swiss-Prot
other Location (Reliability: 5)
F1M4Q5_RAT
1430
0
159264
TrEMBL
other Location (Reliability: 2)
M0R4W4_RAT
276
0
31224
TrEMBL
other Location (Reliability: 1)
M0R5X1_RAT
273
0
30742
TrEMBL
other Location (Reliability: 2)
A0A8I6G7H2_RAT
553
0
61476
TrEMBL
other Location (Reliability: 5)
A0A8I5ZQT7_RAT
582
0
64879
TrEMBL
other Location (Reliability: 5)
A0A0G2K9N1_RAT
342
0
38345
TrEMBL
Mitochondrion (Reliability: 5)
A0A8I6AF61_RAT
212
0
23287
TrEMBL
other Location (Reliability: 2)
A0A0G2K820_RAT
496
0
56675
TrEMBL
Mitochondrion (Reliability: 5)
Q6AYZ4_RAT
337
0
38504
TrEMBL
other Location (Reliability: 2)
B2RYA2_RAT
263
0
29802
TrEMBL
Mitochondrion (Reliability: 5)
O54857_RAT
403
0
47118
TrEMBL
other Location (Reliability: 2)
A0A8I6ACZ1_RAT
258
0
28914
TrEMBL
other Location (Reliability: 4)
F1LNH9_RAT
625
0
72302
TrEMBL
Mitochondrion (Reliability: 2)
F1LR78_RAT
657
0
72641
TrEMBL
Mitochondrion (Reliability: 3)
A0A8I6ATT8_RAT
1423
0
158552
TrEMBL
other Location (Reliability: 5)
A0A0G2K0J7_RAT
1030
0
113330
TrEMBL
Mitochondrion (Reliability: 5)
A0A8I5ZJA1_RAT
312
0
35786
TrEMBL
Secretory Pathway (Reliability: 4)
D4A520_RAT
307
0
32847
TrEMBL
Mitochondrion (Reliability: 5)
A0A8I5Y7T7_RAT
521
0
58588
TrEMBL
other Location (Reliability: 3)
E2CWF0_RAT
515
0
58833
TrEMBL
Mitochondrion (Reliability: 5)
A0A0H2UHE5_RAT
472
0
53465
TrEMBL
Mitochondrion (Reliability: 4)
A0A8I6ABP0_RAT
325
0
37022
TrEMBL
Secretory Pathway (Reliability: 4)
A0A8I5ZZ39_RAT
286
0
32823
TrEMBL
other Location (Reliability: 1)
A0A0G2K7C6_RAT
372
0
40999
TrEMBL
other Location (Reliability: 2)
G3V7L2_RAT
395
0
43173
TrEMBL
other Location (Reliability: 2)
G3V9L3_RAT
211
0
23115
TrEMBL
other Location (Reliability: 2)
A0A8I5ZJ60_RAT
308
0
35231
TrEMBL
other Location (Reliability: 2)
D3ZP99_RAT
403
0
43249
TrEMBL
other Location (Reliability: 3)
F7EXD6_RAT
316
0
35585
TrEMBL
Mitochondrion (Reliability: 3)
M0RBM2_RAT
326
0
36449
TrEMBL
other Location (Reliability: 2)
A0A0G2JVK2_RAT
332
0
37703
TrEMBL
other Location (Reliability: 2)
A0A8I5ZX24_RAT
328
0
37311
TrEMBL
other Location (Reliability: 3)
F1LWM1_RAT
1032
0
114523
TrEMBL
Mitochondrion (Reliability: 5)
A0A8I6AAD3_RAT
534
0
60276
TrEMBL
other Location (Reliability: 5)
A0A0G2K3I9_RAT
145
0
15970
TrEMBL
other Location (Reliability: 1)
A0A8I6G515_RAT
304
0
34224
TrEMBL
other Location (Reliability: 1)
A0A0G2K7T5_RAT
498
0
56552
TrEMBL
other Location (Reliability: 1)
Q5XIN2_RAT
198
1
22499
TrEMBL
other Location (Reliability: 3)
A0A8I5ZS45_RAT
594
0
67045
TrEMBL
other Location (Reliability: 1)
A0A8I6A2G7_RAT
997
0
110373
TrEMBL
Mitochondrion (Reliability: 4)
F6Z8N5_RAT
248
0
27941
TrEMBL
other Location (Reliability: 1)
A0A8I6G995_RAT
935
0
103021
TrEMBL
Mitochondrion (Reliability: 5)
Q64538_RAT
479
0
54718
TrEMBL
other Location (Reliability: 1)
A0A8I5ZS34_RAT
261
0
29348
TrEMBL
other Location (Reliability: 1)
Q68G16_RAT
499
0
56903
TrEMBL
other Location (Reliability: 1)
Q2YDV1_RAT
414
0
44780
TrEMBL
other Location (Reliability: 5)
Q5M863_RAT
318
0
34520
TrEMBL
other Location (Reliability: 5)
A0A8I6A8I8_RAT
450
0
51371
TrEMBL
other Location (Reliability: 2)
A0A8I6B0P9_RAT
1053
0
116307
TrEMBL
Mitochondrion (Reliability: 5)
Q6AYJ0_RAT
506
0
57801
TrEMBL
Mitochondrion (Reliability: 5)
E2CWF2_RAT
262
0
30121
TrEMBL
Mitochondrion (Reliability: 5)
A0A8I6GLZ4_RAT
515
0
58131
TrEMBL
other Location (Reliability: 5)
A0A8I6AGT7_RAT
168
0
18741
TrEMBL
other Location (Reliability: 2)
D3ZRE9_RAT
188
0
20579
TrEMBL
other Location (Reliability: 1)
A0A8I6ABY8_RAT
576
0
64244
TrEMBL
other Location (Reliability: 5)
A0A8I6A2X6_RAT
498
0
56526
TrEMBL
other Location (Reliability: 1)
B5DFF7_RAT
185
0
20468
TrEMBL
other Location (Reliability: 1)
A0A8I5ZL24_RAT
595
0
66315
TrEMBL
other Location (Reliability: 5)
B1WC24_RAT
261
0
29294
TrEMBL
other Location (Reliability: 1)
E2CWF1_RAT
483
0
55179
TrEMBL
Mitochondrion (Reliability: 5)
A0A8I6AIB0_RAT
1018
0
112468
TrEMBL
other Location (Reliability: 5)
A0A8I6A1E7_RAT
484
0
53942
TrEMBL
other Location (Reliability: 2)
A0A8I5ZK68_RAT
283
0
32547
TrEMBL
other Location (Reliability: 1)
Q99ND8_RAT
465
0
51010
TrEMBL
other Location (Reliability: 2)
A0A8I6ACH2_RAT
311
0
35576
TrEMBL
other Location (Reliability: 5)
A0A8I6AU71_RAT
414
0
48501
TrEMBL
other Location (Reliability: 3)
Q642F2_RAT
393
0
43533
TrEMBL
other Location (Reliability: 2)
Q4V8L2_RAT
99
0
11015
TrEMBL
other Location (Reliability: 2)
A0A0H2UHC8_RAT
318
0
36859
TrEMBL
other Location (Reliability: 2)
D3ZN69_RAT
754
0
86546
TrEMBL
other Location (Reliability: 5)
G3V8M5_RAT
307
0
35080
TrEMBL
other Location (Reliability: 1)
A0A8I6B3D3_RAT
664
0
76420
TrEMBL
other Location (Reliability: 2)
A0A8I6GLU2_RAT
505
0
57746
TrEMBL
Secretory Pathway (Reliability: 1)
A0A0G2JYS8_RAT
317
0
36025
TrEMBL
other Location (Reliability: 2)
A0A0G2JYA4_RAT
309
0
35523
TrEMBL
other Location (Reliability: 1)
A0A8I5ZM93_RAT
495
0
56378
TrEMBL
other Location (Reliability: 1)
A0A0G2K7Q5_RAT
484
0
53134
TrEMBL
other Location (Reliability: 5)
Q63683_RAT
367
0
39616
TrEMBL
other Location (Reliability: 3)
A0A8J8XJJ2_RAT
502
0
57321
TrEMBL
other Location (Reliability: 3)
A0A8I6AFB1_RAT
586
0
65281
TrEMBL
other Location (Reliability: 5)
F1LPJ5_RAT
384
0
42130
TrEMBL
Mitochondrion (Reliability: 5)
A0A8I5ZV44_RAT
259
0
29308
TrEMBL
Mitochondrion (Reliability: 4)
A0A8I5ZSW1_RAT
332
0
38064
TrEMBL
other Location (Reliability: 5)
A0A8I6GE87_RAT
265
0
30046
TrEMBL
other Location (Reliability: 1)
CANB1_RAT
170
0
19300
Swiss-Prot
other Location (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
150000
-
heterotrimeric phosphatase 2A catalyzing the dephosphorylation of fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase, gel filtration
150000 - 165000
-
gel filtration, calculation from Stokes' radius and sucrose density gradient centrifugation
177000 - 180000
-
calculation from Stokes' radius and sucrose density gradient centrifugation
19000
-
1 * 61000 + 1 * 19000, calcineurin A, catalytic subunit + calcineurin B, Ca2+-binding subunit
35000
36000
37000
-
x * 36000, catalytic subunit of PP1, SDS-PAGE, x * 37000, catalytic subunit of PP2A, SDS-PAGE, x * 60000, regulatory subunit of PP2A, SDS-PAGE
45000
52000
-
1 * 65000 + 1 * 52000 + 1 * 36000, heterotrimeric phosphatase 2A catalyzing the dephosphorylation of fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase
60000
-
x * 36000, catalytic subunit of PP1, SDS-PAGE, x * 37000, catalytic subunit of PP2A, SDS-PAGE, x * 60000, regulatory subunit of PP2A, SDS-PAGE
61000
-
1 * 61000 + 1 * 19000, calcineurin A, catalytic subunit + calcineurin B, Ca2+-binding subunit
65000
-
1 * 65000 + 1 * 52000 + 1 * 36000, heterotrimeric phosphatase 2A catalyzing the dephosphorylation of fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase
36000
-
1 * 65000 + 1 * 52000 + 1 * 36000, heterotrimeric phosphatase 2A catalyzing the dephosphorylation of fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase
36000
-
x * 36000, catalytic subunit of PP1, SDS-PAGE, x * 37000, catalytic subunit of PP2A, SDS-PAGE, x * 60000, regulatory subunit of PP2A, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
heterotrimer
trimer
additional information
?
-
x * 36000, catalytic subunit of PP1, SDS-PAGE, x * 37000, catalytic subunit of PP2A, SDS-PAGE, x * 60000, regulatory subunit of PP2A, SDS-PAGE
dimer
-
1 * 61000 + 1 * 19000, calcineurin A, catalytic subunit + calcineurin B, Ca2+-binding subunit
trimer
-
1 * 65000 + 1 * 52000 + 1 * 36000, heterotrimeric phosphatase 2A catalyzing the dephosphorylation of fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase
additional information
PP5 contains an unique tetratricopeptide repeat TPR-containing N-termiinal regulatory domain, PP5-Rac-GTP docking and structure modeling using crystal structure PDB code 1A17
additional information
-
the enzyme is located in a multimeric phosphorylation complex in giant neurons
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with inhibitor-2 using the sitting drop vapour diffusion method with 100 mM Tris-HCl, pH 7.5, 300 mM potassium acetate, 12% (w/v) polyethylene glycol 3350, or with 100 mM Tris-HCl, pH 8.6, 150 mM sodium citrate, and 20% (w/v) polyethylene glycol 3350
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
construction of regucalcin-expressing transgenic Sprague-Dawley rats showing reduced protein phosphatase activity in the heart cytosol, overview
additional information
-
construction of transgenic rats expressing the inhibitory protein regucalcin in the heart muscle cell cytosol leading to reduced enzyme activity and abolishing the activating effect of Ca2+, overview
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
heterotrimeric phosphatase 2A catalyzing the dephosphorylation of fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase
-
nickel-nitrilotriacetic acid chromatography and Superdex G75 gel filtration
-
recombinant FLAG-tagged PP2A from COS-M6 cells by immunoaffinity chromatography
-
separation of isozyme subunits by latex bead-immobilized-inhibitor affinity chromatography using FR225659, FR23761, and FR259383
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
abdominal aorta coarctation induces increases in calcineurin expression
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
PP2A inhibition may offer a new therapeutic approach to the treatment of diseases caused by cerebral ischemia
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Hegardt, F.G.
Regulation of rat liver HMG-CoA reductase by reductase kinase and the cytosolic and microsomal protein phosphatases
Adv. Protein Phosphatases
3
1-30
1986
Rattus norvegicus
-
Miyamoto, E.; Goto, S.; Yamamoto, H.; Fukuyama, K.; Matsukado, Y.
Endogenous substrates and distribution of calcineurin in rat brain
Adv. Protein Phosphatases
3
187-200
1986
Rattus norvegicus
-
Witters, L.A.
Protein kinases and phosphatases active on acetyl-CoA carboxylase
Adv. Protein Phosphatases
3
201-224
1986
Rattus norvegicus
-
Thampy, K.G.; Wakil, S.J.
The role of protein phosphorylation in the regulation of acetyl-CoA carboxylase
Adv. Protein Phosphatases
3
257-270
1986
Rattus norvegicus
-
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
-
Shenolikar, S.; Ingebritsen, T.S.
Protein (serine and threonine) phosphate phosphatases
Methods Enzymol.
107
102-129
1984
Oryctolagus cuniculus, Mammalia, Meleagris gallopavo, Rattus norvegicus
Tamura, S.; Tsuiki, S.
Purification and subunit structure of rat-liver phosphoprotein phosphatase, whose molecular weight is 260000 by gel filtration (phosphatase IB)
Eur. J. Biochem.
111
217-224
1980
Rattus norvegicus
Tamura, S.; Kikuchi, H.; Kikuchi, K.; Hiraga, A.; Tsuiki, S.
Purification and subunit structure of a high-molecular-weight phosphoprotein phosphatase (phosphatase II) from rat liver
Eur. J. Biochem.
104
347-355
1980
Rattus norvegicus
Titanji, V.P.K.
Purification and properties of a phosphoprotein phosphatase from rat liver
Biochim. Biophys. Acta
481
140-151
1977
Rattus norvegicus
Begum, N.; Sussman, E.; Draznin, B.
Differential effects of diabetes on adipocyte and liver phosphotyrosine and phosphosereine phosphatase activities
Diabetes
40
1620-1629
1991
Gallus gallus, Rattus norvegicus, Sus scrofa
Haddy, A.; Rusnak, F.
Overexpression and characterization of a recombinant form of rat calcineurin A
Biochem. Biophys. Res. Commun.
200
1221-1229
1994
Rattus norvegicus
Nishimura, M.; Uyeda, K.
Purification and characterization of a novel xylulose 5-phosphate-activated protein phosphatase catalyzing dephosphorylation of fructose-6-phosphate,2-kinase:fructose-2,6-bisphosphatase
J. Biol. Chem.
270
26341-26346
1995
Rattus norvegicus
Yokoyama, N.; Kobayashi, T.; Tamura, S.; Sugiya, H.
Purification and characterization of protein phosphatase 2C in rat parotid acinar cells: two forms of Mg2+-avtivated histone phosphatase and phosphorylation by cAMP-dependent protein kinase
Arch. Biochem. Biophys.
331
1-8
1996
Rattus norvegicus
Nagase, T.; Murakami, T.; Nozaki, H.; Inoue, R.; Nishito, Y.; Tanabe, O.; Usui, H.; Takeda, M.
Tissue and subcellular distributions, and characterization of rat brain protein phosphatase 2A containing a 72-kDa delta/B subunit
J. Biochem.
122
178-187
1997
Homo sapiens, Rattus norvegicus
Oh, J.S.; Hwang, I.S.; Choi, M.U.
Purification and characterization of protein phosphatase 2C from rat liver
J. Biochem. Mol. Biol.
30
222-228
1997
Rattus norvegicus
-
Sayed, S.B.; Whitehouse, B.J.; Jones, P.M.
Phosphoserine/threonine phosphatases in the rat adrenal cortex: a role in the control of steroidogenesis?
J. Endocrinol.
154
449-458
1997
Rattus norvegicus
Bahl, R.; Bradley, K.C.; Thompson, K.J.; Swain, R.A.; Rossie, S.; Meisel, R.L.
Localization of protein Ser/Thr phosphatase 5 in rat brain
Brain Res. Mol. Brain Res.
90
101-109
2001
Rattus norvegicus
de la Fuente van Bentem, S.; Vossen, J.H.; Vermeer, J.E.; de Vroomen, M.J.; Gadella, T.W., Jr.; Haring, M.A.; Cornelissen, B.J.
The subcellular localization of plant protein phosphatase 5 isoforms is determined by alternative splicing
Plant Physiol.
133
702-712
2003
Rattus norvegicus (P53042), Solanum lycopersicum (Q84K11), Solanum lycopersicum
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
Chinkers, M.
PP5: the TPR phosphatase
Topics in Current Genetics (Arino, J. , Alexander, D. R. Eds. ) Springer
5
107-130
2004
Drosophila melanogaster, Neurospora crassa, Plasmodium falciparum, Rattus norvegicus, Trypanosoma brucei
-
Plummer, G.; Perreault, K.R.; Holmes, C.F.; Posse De Chaves, E.I.
Activation of serine/threonine protein phosphatase-1 is required for ceramide-induced survival of sympathetic neurons
Biochem. J.
385
685-693
2005
Rattus norvegicus
Zhang, X.; Wu, J.; Lei, Y.; Fang, L.; Willis, W.D.
Protein phosphatase modulates the phosphorylation of spinal cord NMDA receptors in rats following intradermal injection of capsaicin
Brain Res. Mol. Brain Res.
138
264-272
2005
Rattus norvegicus
Ichikawa, E.; Tsurusaki, Y.; Yamaguchi, M.
Suppressive effect of regucalcin on protein phosphatase activity in the heart cytosol of normal and regucalcin transgenic rats
Int. J. Mol. Med.
13
289-293
2004
Rattus norvegicus
Hatori, H.; Zenkoh, T.; Kobayashi, M.; Ohtsu, Y.; Shigematsu, N.; Setoi, H.; Hino, M.; Handa, H.
FR225659-binding proteins: identification as serine/threonine protein phosphatase PP1 and PP2A using high-performance affinity beads
J. Antibiot.
57
456-461
2004
Rattus norvegicus
Van Kanegan, M.J.; Adams, D.G.; Wadzinski, B.E.; Strack, S.
Distinct protein phosphatase 2A heterotrimers modulate growth factor signaling to extracellular signal-regulated kinases and Akt
J. Biol. Chem.
280
36029-36036
2005
Rattus norvegicus
Gentile, S.; Darden, T.; Erxleben, C.; Romeo, C.; Russo, A.; Martin, N.; Rossie, S.; Armstrong, D.L.
Rac GTPase signaling through the PP5 protein phosphatase
Proc. Natl. Acad. Sci. USA
103
5202-5206
2006
Rattus norvegicus (P53042)
El-Armouche, A.; Bednorz, A.; Pamminger, T.; Ditz, D.; Didie, M.; Dobrev, D.; Eschenhagen, T.
Role of calcineurin and protein phosphatase-2A in the regulation of phosphatase inhibitor-1 in cardiac myocytes
Biochem. Biophys. Res. Commun.
346
700-706
2006
Rattus norvegicus
Meiselbach, H.; Sticht, H.; Enz, R.
Structural analysis of the protein phosphatase 1 docking motif: molecular description of binding specificities identifies interacting proteins
Chem. Biol.
13
49-59
2006
Rattus norvegicus
Jideama, N.M.; Crawford, B.H.; Hussain, A.K.; Raynor, R.L.
Dephosphorylation specificities of protein phosphatase for cardiac troponin I, troponin T, and sites within troponin T
Int. J. Biol. Sci.
2
1-9
2006
Rattus norvegicus
Hurley, T.D.; Yang, J.; Zhang, L.; Goodwin, K.D.; Zou, Q.; Cortese, M.; Dunker, A.K.; DePaoli-Roach, A.A.
Structural basis for regulation of protein phosphatase 1 by inhibitor-2
J. Biol. Chem.
282
28874-28883
2007
Rattus norvegicus
Foley, T.D.; Petro, L.A.; Stredny, C.M.; Coppa, T.M.
Oxidative inhibition of protein phosphatase 2A activity: role of catalytic subunit disulfides
Neurochem. Res.
32
1957-1964
2007
Rattus norvegicus
Dimitropoulou, C.; West, L.; Field, M.B.; White, R.E.; Reddy, L.M.; Falck, J.R.; Imig, J.D.
Protein phosphatase 2A and Ca2+-activated K+ channels contribute to 11,12-epoxyeicosatrienoic acid analog mediated mesenteric arterial relaxation
Prostaglandins Other Lipid Mediat.
83
50-61
2007
Rattus norvegicus
Yi, K.D.; Simpkins, J.W.
Protein phosphatase 1, protein phosphatase 2A, and calcineurin play a role in estrogen-mediated neuroprotection
Endocrinology
149
5235-5243
2008
Homo sapiens, Rattus norvegicus
Yoo, S.J.; Jimenez, R.H.; Sanders, J.A.; Boylan, J.M.; Brautigan, D.L.; Gruppuso, P.A.
The alpha4-containing form of protein phosphatase 2A in liver and hepatic cells
J. Cell. Biochem.
105
290-300
2008
Mus musculus, Rattus norvegicus
Wilkerson, J.E.; Satriotomo, I.; Baker-Herman, T.L.; Watters, J.J.; Mitchell, G.S.
Okadaic acid-sensitive protein phosphatases constrain phrenic long-term facilitation after sustained hypoxia
J. Neurosci.
28
2949-2958
2008
Rattus norvegicus
Zhao, J.; Wu, H.W.; Chen, Y.J.; Tian, H.P.; Li, L.X.; Han, X.; Guo, J.
Protein phosphatase 2A-negative regulation of the protective signaling pathway of Ca2+/CaM-dependent ERK activation in cerebral ischemia
J. Neurosci. Res.
86
2733-2745
2008
Rattus norvegicus
Van Kanegan, M.J.; Strack, S.
The protein phosphatase 2A regulatory subunits B'beta and B'delta mediate sustained TrkA neurotrophin receptor autophosphorylation and neuronal differentiation
Mol. Cell. Biol.
29
662-674
2009
Rattus norvegicus
Deng, J.; Lv, X.T.; Wu, Q.; Huang, X.N.
Ginsenoside Rg(1) inhibits rat left ventricular hypertrophy induced by abdominal aorta coarctation: involvement of calcineurin and mitogen-activated protein kinase signalings
Eur. J. Pharmacol.
608
42-47
2009
Rattus norvegicus (P63329)
Hayashi, H.; Campenot, R.B.; Vance, D.E.; Vance, J.E.
Protection of neurons from apoptosis by apolipoprotein E-containing lipoproteins does not require lipoprotein uptake and involves activation of phospholipase Cgamma1 and inhibition of calcineurin
J. Biol. Chem.
284
29605-29613
2009
Rattus norvegicus
Nicolaou, P.; Hajjar, R.J.; Kranias, E.G.
Role of protein phosphatase-1 inhibitor-1 in cardiac physiology and pathophysiology
J. Mol. Cell. Cardiol.
47
365-371
2009
Cavia porcellus, Homo sapiens, Mus musculus, Rattus norvegicus
LeMaire, S.; Raghuram, V.; Grady, C.R.; Pickering, C.M.; Chou, C.-L.; Umejiego, E.N.; Knepper, M.A.
Serine/threonine phosphatases and aquaporin-2 regulation in renal collecting duct
Am. J. Physiol. Renal. Physiol.
312
F84-F95
2017
Mus musculus, Rattus norvegicus, Rattus norvegicus Sprague-Dawley
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