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Information on EC 3.1.3.16 - protein-serine/threonine phosphatase and Organism(s) Mus musculus
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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: Mus musculus
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
-
-
-
-
PP1alpha
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 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
-
the enzyme belongs to the phosphoprotein phosphatase family
calcineurin
-
-
-
-
Pp4
-
-
-
-
PP6
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate
mechanism of PP1
-
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
phosphorylated atypical protein kinase C + H2O
atypical protein kinase C + phosphate
-
-
-
-
?
phosphorylated Cav1.2 + H2O
Cav1.2 + phosphate
-
PP2A dephosphorylates Cav1.2 at serine 1866
-
-
?
phosphorylated High mobility group box 1 protein + H2O
High mobility group box 1 protein + phosphate
-
-
-
-
?
phosphorylated myelin basic protein + H2O
myelin basic protein + phosphate
-
-
-
-
?
phosphorylated NDEL1 + H2O
NDEL1 + phosphate
-
PP4c selectively dephosphorylates NDEL1 at T219
-
-
?
phosphorylated Par-3 + H2O
Par-3 + phosphate
-
predominantly the alpha-isoform of PP1 binds phosphorylated Par-3 and specifically dephosphorylates at Ser-144 and Ser-824
-
-
?
phosphorylated phosphorylase kinase + H2O
phosphorylase kinase + phosphate
-
-
-
-
?
phosphorylated retinoblastoma protein + H2O
retinoblastoma protein + phosphate
-
-
-
-
?
phosphorylated stress-activated protein kinase + H2O
stress-activated protein kinase + phosphate
-
-
-
-
?
phosphorylated TAK1-binding protein 1 + H2O
TAK1-binding protein 1 + phosphate
-
-
-
-
?
phosphorylated transforming growth factor-beta-activated kinase 1 + H2O
transforming growth factor-beta-activated kinase 1 + phosphate
-
Thr187 in transforming growth factor-beta-activated kinase 1 is a major dephosphorylation target of PP2A, PP2A plays a pivotal role as a negative regulator of transforming growth factor-beta-activated kinase 1 activation in response to transforming growth factor-beta 1
-
-
?
SSpSLESLQTAVAEVTLNGNIPFHRPR + H2O
SSSLESLQTAVAEVTLNGNIPFHRPR + phosphate
-
-
-
-
?
[aquaporin-2]-serine/threonine phosphate + H2O
[aquaporin-2]-serine/threonine + phosphate
-
-
-
-
?
phosphorylated IkappaB kinase + H2O
IkappaB kinase + phosphate
-
PP2A positively regulates multicomponent Ikappa kinase signaling, eventhough it inhibits its activity by dephosphorylation, positive regulation requires PP2A-IKK complex formation, suppression of the complex formation attenuates IKK T loop phosphorylation and activation, PP2A inhibition attenuates TNFalpha-induced IKK degradation, overview
-
-
?
phosphorylated IkappaB kinase + H2O
IkappaB kinase + phosphate
-
formation of PP2A-IKK complexes, determination of interaction sites
-
-
?
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 myosin light chain + H2O
myosin light chain + phosphate
-
isozyme PP1delta regulates smooth muscle relaxation
-
-
?
phosphorylated myosin light chain + H2O
myosin light chain + phosphate
-
isozyme PP1delta, the reaction involves the RVxF-containing myosin phosphatase targeting subunit 1, MYPT1
-
-
?
phosphorylated p53 + H2O
p53 + phosphate
-
dephosphorylation of Ser15 by PP1, no activity with PP2A, PP1 inhibition leads to hyperphosphorylation of p53, PP1 has regulatory function
-
-
?
phosphorylated p53 + H2O
p53 + phosphate
-
dephosphorylation of Ser15 by PP1, no activity with PP2A
-
-
?
phosphorylated Raf-1 kinase + H2O
Raf 1 kinase + phosphate
-
phosphatase 2A dephosphorylates Raf-1 Ser259 in response to mitogens
-
-
?
phosphorylated Raf-1 kinase + H2O
Raf 1 kinase + phosphate
-
activation of Raf-1 by dephopshorylation at Ser259
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of diverse cellular processes and signaling pathways including embryonic development, cell proliferation, cell death, and cancer, overview, PP5 is involved in stress response negatively regulating ASK-1 dependent apoptosis and promoting tumor growth
-
-
?
additional information
?
-
-
direct interaction between the N terminus of Rattus norvegicus adenylyl cyclase AC8 and the active catalytic subunit of PP2A activates the dephosphorylation activity
-
-
?
additional information
?
-
-
the expression of wild type PP2A catalytic subunit suppresses the MAPK kinase 3 phosphorylation
-
-
?
additional information
?
-
-
calcineurin is a Ca2+/calmodulin-dependent protein phosphatase
-
-
?
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
phosphorylated High mobility group box 1 protein + H2O
High mobility group box 1 protein + phosphate
-
-
-
-
?
phosphorylated IkappaB kinase + H2O
IkappaB kinase + phosphate
-
PP2A positively regulates multicomponent Ikappa kinase signaling, eventhough it inhibits its activity by dephosphorylation, positive regulation requires PP2A-IKK complex formation, suppression of the complex formation attenuates IKK T loop phosphorylation and activation, PP2A inhibition attenuates TNFalpha-induced IKK degradation, 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 myosin light chain + H2O
myosin light chain + phosphate
-
isozyme PP1delta regulates smooth muscle relaxation
-
-
?
phosphorylated Raf-1 kinase + H2O
Raf 1 kinase + phosphate
-
phosphatase 2A dephosphorylates Raf-1 Ser259 in response to mitogens
-
-
?
[aquaporin-2]-serine/threonine phosphate + H2O
[aquaporin-2]-serine/threonine + phosphate
-
-
-
-
?
phosphorylated p53 + H2O
p53 + phosphate
-
dephosphorylation of Ser15 by PP1, no activity with PP2A, PP1 inhibition leads to hyperphosphorylation of p53, PP1 has regulatory function
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of diverse cellular processes and signaling pathways including embryonic development, cell proliferation, cell death, and cancer, overview, PP5 is involved in stress response negatively regulating ASK-1 dependent apoptosis and promoting tumor growth
-
-
?
additional information
?
-
-
the expression of wild type PP2A catalytic subunit suppresses the MAPK kinase 3 phosphorylation
-
-
?
additional information
?
-
-
calcineurin is a Ca2+/calmodulin-dependent protein phosphatase
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
cyclosporin A
-
a specific calcineurin inhibitor, time course of inhibition in vivo, overview
DSCR1
-
a calcineurin inhibitor, encoded by gene Dscr1 on chromosome 21, is elevated in Down syndrome model mice
-
FK506
-
a specific calcineurin inhibitor, time course of inhibition in vivo, overview
protein phosphatase-1 inhibitor-1
-
the inhibitor-1 contains an RVXF motif sequence, which facilitates its interaction with PP1. On stimulation of the beta-adrenergic axis, protein kinase A phosphorylates Thr35 in inhibitor-1, resulting in PP1 inhibition and amplification of the contractile response
-
protein phosphatase-1 inhibitor-1
-
plays a role in cardiac physiology and pathophysiology, overview
-
additional information
-
DNA damage 34, i.e. gADD34, and growth arrest disturb the binding of PP1 to p53
-
additional information
-
Par-3 does not inhibit the enzymatic activity of PP1alpha
-
additional information
-
knockout of Ste20-like kinase, Mst2, reduces the expression of the catalytic subunit of PP2A, RNAi silencing of Mst2 triggers a striking proteasome-dependent decrease in the levels of the catalytic subunit of PP2A. Mst2-dependent stabilization of PP2A-C is a posttranslational process likely involving a reduction in proteasome-dependent PP2A-C degradation
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
butyrate induces expression of protein phosphatase when treated to the cell
-
additional information
-
association of PP2A with transforming growth factor-beta-activated kinase 1 is enhanced by transforming growth factor-beta 1 stimulation
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0005
endophilin B1t
Mus musculus
-
at 37°C, in 50 mM Tris-HCl, pH 7.5, 1 mg/ml bovine serum albumin, 1 mM MnCl2, and 0.1% beta-mercaptoethanol
-
0.00009
endothall
Mus musculus
-
in 50 mM Tris-HCl (pH 7.4), temperature not specified in the publication
0.000012
neurabin I
Mus musculus
-
at 37°C, in 50 mM Tris-HCl, pH 7.5, 1 mg/ml bovine serum albumin, 1 mM MnCl2, and 0.1% beta-mercaptoethanol
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
embryonic fibroblast cell line from GADD34-deficient mice and from wild-type mice
-
a vasopressin-responsive cell culture model of cortical collecting duct, proteomic analysis of cytoplasmic fractions from mpkCCD cells, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
malfunction
-
calcineurin inhibition by FK506 significantly enhances the phosphorylation of protein tau at Ser262, Ser198, Ser199, and/or Ser202 and Ser396, and/or Ser404, overview
malfunction
-
modest elevation in expression afforded by a single extra transgenic copy of Dscr1 is sufficient to confer significant suppression of tumor growth in mice and that such resistance is a consequence of a deficit in tumor angiogenesis arising from suppression of the calcineurin pathway. Attenuation of calcineurin activity by DSCR1 together with another chromosome 21 gene DYRK1A, may be sufficient to dramatically diminish angiogenesis
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
malfunction
-
a decrease in alpha-isoform of PP2A catalytic subunit accelerates osteoblast differentiation through the expression of bone-related genes
physiological function
-
calcineurin plays an important role in brain function and in regulation of tau phosphorylation
physiological function
-
the enzyme is involved in regulation of diverse enzyme functions via de-/activation of phosphoproteins through dephosphorylation, in the same way its inhibitor protein phosphatase-1 inhibitor-1, phosphoproteomic analysis, 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
-
overexpression of subunit PP2A Calpha reduces alkaline phosphatase activity. Osteoblast differentiation and mineralization are decreased in subunit PP2A Calpha-overexpressing cells, with reduction of bone-related genes including osterix, bone sialoprotein, and osteocalcin
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). EPM2A_MOUSE
330
0
36958
Swiss-Prot
Mitochondrion (Reliability: 4)
PHLP1_MOUSE
1687
0
182367
Swiss-Prot
other Location (Reliability: 1)
PHLP2_MOUSE
1320
0
145947
Swiss-Prot
other Location (Reliability: 5)
PP2BA_MOUSE
521
0
58644
Swiss-Prot
other Location (Reliability: 2)
PP2BB_MOUSE
525
0
59173
Swiss-Prot
other Location (Reliability: 5)
PPM1K_MOUSE
372
0
40918
Swiss-Prot
Mitochondrion (Reliability: 2)
PPM1L_MOUSE
360
0
41049
Swiss-Prot
Secretory Pathway (Reliability: 4)
PPM1M_MOUSE
462
0
51204
Swiss-Prot
Mitochondrion (Reliability: 2)
PPM1N_MOUSE
404
0
43201
Swiss-Prot
other Location (Reliability: 3)
PTEN_MOUSE
403
0
47152
Swiss-Prot
other Location (Reliability: 2)
DUS8_MOUSE
663
0
68847
Swiss-Prot
other Location (Reliability: 4)
PP2AB_MOUSE
309
0
35575
Swiss-Prot
other Location (Reliability: 1)
DUS22_MOUSE
184
0
20997
Swiss-Prot
other Location (Reliability: 3)
DUS23_MOUSE
150
0
16637
Swiss-Prot
Mitochondrion (Reliability: 5)
DUS26_MOUSE
211
0
23946
Swiss-Prot
Mitochondrion (Reliability: 2)
DUS28_MOUSE
163
0
17505
Swiss-Prot
other Location (Reliability: 4)
ILKAP_MOUSE
392
0
42774
Swiss-Prot
other Location (Reliability: 2)
PP1A_MOUSE
330
0
37540
Swiss-Prot
other Location (Reliability: 2)
PP1B_MOUSE
327
0
37187
Swiss-Prot
other Location (Reliability: 2)
SSU72_MOUSE
194
0
22517
Swiss-Prot
Mitochondrion (Reliability: 4)
CDKN3_MOUSE
211
0
23793
Swiss-Prot
other Location (Reliability: 1)
CPPED_MOUSE
312
0
35248
Swiss-Prot
Mitochondrion (Reliability: 5)
CTDP1_MOUSE
960
0
104554
Swiss-Prot
other Location (Reliability: 2)
CTDS1_MOUSE
261
0
29266
Swiss-Prot
other Location (Reliability: 2)
CTDS2_MOUSE
270
0
30546
Swiss-Prot
other Location (Reliability: 2)
CTDSL_MOUSE
276
0
31156
Swiss-Prot
other Location (Reliability: 1)
DS13A_MOUSE
188
0
20646
Swiss-Prot
other Location (Reliability: 1)
PP1G_MOUSE
323
0
36984
Swiss-Prot
other Location (Reliability: 2)
SSH1_MOUSE
1042
0
115297
Swiss-Prot
other Location (Reliability: 5)
SSH2_MOUSE
1423
0
158230
Swiss-Prot
other Location (Reliability: 5)
SSH3_MOUSE
649
0
72227
Swiss-Prot
Mitochondrion (Reliability: 4)
DS13B_MOUSE
198
1
22481
Swiss-Prot
other Location (Reliability: 5)
DUS3_MOUSE
185
0
20472
Swiss-Prot
other Location (Reliability: 1)
PLPP_MOUSE
292
0
31512
Swiss-Prot
other Location (Reliability: 3)
PPM1A_MOUSE
382
0
42433
Swiss-Prot
other Location (Reliability: 2)
PPM1B_MOUSE
390
0
42795
Swiss-Prot
other Location (Reliability: 2)
PPM1D_MOUSE
598
0
65723
Swiss-Prot
other Location (Reliability: 2)
PPP5_MOUSE
499
0
56877
Swiss-Prot
other Location (Reliability: 1)
PTPM1_MOUSE
193
0
21943
Swiss-Prot
Mitochondrion (Reliability: 5)
UBCP1_MOUSE
318
0
36837
Swiss-Prot
other Location (Reliability: 2)
DUS4_MOUSE
398
0
43372
Swiss-Prot
other Location (Reliability: 1)
DUS6_MOUSE
381
0
42408
Swiss-Prot
other Location (Reliability: 2)
DUS7_MOUSE
422
0
45220
Swiss-Prot
Mitochondrion (Reliability: 3)
EYA1_MOUSE
591
0
64324
Swiss-Prot
other Location (Reliability: 2)
PP2BC_MOUSE
513
0
58699
Swiss-Prot
Mitochondrion (Reliability: 5)
PP4C_MOUSE
307
0
35080
Swiss-Prot
other Location (Reliability: 1)
PPM1E_MOUSE
749
0
83419
Swiss-Prot
other Location (Reliability: 2)
PPM1F_MOUSE
452
0
49611
Swiss-Prot
other Location (Reliability: 2)
PPM1G_MOUSE
542
0
58728
Swiss-Prot
other Location (Reliability: 2)
PPM1H_MOUSE
513
0
56380
Swiss-Prot
other Location (Reliability: 4)
PPM1J_MOUSE
507
0
55550
Swiss-Prot
Mitochondrion (Reliability: 2)
PPTC7_MOUSE
310
0
33048
Swiss-Prot
Mitochondrion (Reliability: 4)
CC14A_MOUSE
603
0
67634
Swiss-Prot
other Location (Reliability: 2)
CC14B_MOUSE
485
1
55661
Swiss-Prot
Mitochondrion (Reliability: 2)
DUS29_MOUSE
215
0
24192
Swiss-Prot
other Location (Reliability: 2)
DUS2_MOUSE
318
0
34576
Swiss-Prot
other Location (Reliability: 5)
PGAM5_MOUSE
288
1
31994
Swiss-Prot
Secretory Pathway (Reliability: 5)
DUS10_MOUSE
483
0
52532
Swiss-Prot
other Location (Reliability: 3)
DUS12_MOUSE
339
0
37159
Swiss-Prot
other Location (Reliability: 3)
DUS14_MOUSE
198
0
22311
Swiss-Prot
Mitochondrion (Reliability: 5)
DUS15_MOUSE
235
0
26186
Swiss-Prot
other Location (Reliability: 3)
DUS18_MOUSE
188
0
21119
Swiss-Prot
other Location (Reliability: 5)
PP2AA_MOUSE
309
0
35608
Swiss-Prot
other Location (Reliability: 1)
PPE1_MOUSE
650
0
75058
Swiss-Prot
other Location (Reliability: 4)
DUS19_MOUSE
220
0
24181
Swiss-Prot
other Location (Reliability: 5)
DUS1_MOUSE
367
0
39370
Swiss-Prot
other Location (Reliability: 3)
DUS21_MOUSE
189
0
21509
Swiss-Prot
other Location (Reliability: 2)
FIG4_MOUSE
907
1
103447
Swiss-Prot
other Location (Reliability: 4)
PPE2_MOUSE
757
0
86645
Swiss-Prot
other Location (Reliability: 5)
CNEP1_MOUSE
244
1
28391
Swiss-Prot
Mitochondrion (Reliability: 5)
PPP6_MOUSE
305
0
35159
Swiss-Prot
other Location (Reliability: 1)
RPAP2_MOUSE
614
0
68530
Swiss-Prot
other Location (Reliability: 4)
Q8K1S9_MOUSE
452
0
48688
TrEMBL
other Location (Reliability: 5)
A0A498WGL8_MOUSE
648
0
72099
TrEMBL
Mitochondrion (Reliability: 3)
A0A494B9F4_MOUSE
138
0
16167
TrEMBL
other Location (Reliability: 2)
Q8BN07_MOUSE
285
0
32644
TrEMBL
other Location (Reliability: 1)
A0A0G2JGC1_MOUSE
273
0
31367
TrEMBL
other Location (Reliability: 2)
G3UXN0_MOUSE
265
0
29978
TrEMBL
other Location (Reliability: 1)
Q3UB30_MOUSE
381
0
42397
TrEMBL
other Location (Reliability: 2)
Q2M4K0_MOUSE
318
0
34606
TrEMBL
other Location (Reliability: 5)
A0A0R4J2A0_MOUSE
1429
0
158813
TrEMBL
other Location (Reliability: 3)
Q6ZWM8_MOUSE
323
0
36984
TrEMBL
other Location (Reliability: 2)
Q99NF7_MOUSE
477
0
52111
TrEMBL
other Location (Reliability: 2)
Q3UXV4_MOUSE
452
0
51446
TrEMBL
other Location (Reliability: 2)
E0CZ78_MOUSE
524
0
59074
TrEMBL
other Location (Reliability: 5)
Q9D5R5_MOUSE
485
0
55387
TrEMBL
Mitochondrion (Reliability: 5)
V9GXA1_MOUSE
221
0
25204
TrEMBL
other Location (Reliability: 2)
G3X8U7_MOUSE
515
0
58131
TrEMBL
other Location (Reliability: 5)
Q8VED4_MOUSE
278
0
32058
TrEMBL
other Location (Reliability: 1)
Q3V461_MOUSE
247
0
26994
TrEMBL
other Location (Reliability: 2)
A0A0N4SVL9_MOUSE
283
0
32547
TrEMBL
other Location (Reliability: 1)
A0A1W2P715_MOUSE
235
0
26572
TrEMBL
other Location (Reliability: 2)
Q1HL35_MOUSE
384
0
42253
TrEMBL
other Location (Reliability: 5)
Q3UQZ5_MOUSE
237
0
27587
TrEMBL
other Location (Reliability: 1)
Q7TNW3_MOUSE
263
0
29710
TrEMBL
Mitochondrion (Reliability: 3)
A0A286YD16_MOUSE
168
0
18702
TrEMBL
other Location (Reliability: 2)
Z4YLI2_MOUSE
316
0
35467
TrEMBL
Mitochondrion (Reliability: 4)
Q5EBQ9_MOUSE
212
0
24154
TrEMBL
other Location (Reliability: 2)
Q3UG02_MOUSE
388
0
43054
TrEMBL
other Location (Reliability: 2)
H3BKD1_MOUSE
118
0
13677
TrEMBL
other Location (Reliability: 1)
A0A0G2JFF1_MOUSE
292
0
33312
TrEMBL
other Location (Reliability: 3)
Q3UUN5_MOUSE
407
0
46893
TrEMBL
Mitochondrion (Reliability: 3)
A0A2I3BPC5_MOUSE
522
0
59730
TrEMBL
Mitochondrion (Reliability: 5)
Q546R1_MOUSE
390
0
42795
TrEMBL
other Location (Reliability: 2)
F8WHT2_MOUSE
999
0
110769
TrEMBL
Mitochondrion (Reliability: 4)
E9Q6P2_MOUSE
497
0
56098
TrEMBL
other Location (Reliability: 5)
H3BKL8_MOUSE
145
0
16013
TrEMBL
other Location (Reliability: 1)
Q3UCQ6_MOUSE
367
0
39386
TrEMBL
other Location (Reliability: 3)
Q3V2Y9_MOUSE
117
0
13232
TrEMBL
other Location (Reliability: 1)
Q3U7K1_MOUSE
323
0
37033
TrEMBL
other Location (Reliability: 2)
A0A6G6A824_MOUSE
475
0
54967
TrEMBL
other Location (Reliability: 5)
A0A494BB72_MOUSE
242
0
27263
TrEMBL
Mitochondrion (Reliability: 4)
Q3U8W0_MOUSE
330
0
37526
TrEMBL
other Location (Reliability: 2)
Q7TNL7_MOUSE
452
0
48658
TrEMBL
other Location (Reliability: 5)
Q9DA25_MOUSE
263
0
29735
TrEMBL
Mitochondrion (Reliability: 3)
Q3U786_MOUSE
381
0
42457
TrEMBL
other Location (Reliability: 2)
Q3UNF2_MOUSE
307
0
35080
TrEMBL
other Location (Reliability: 1)
Q0VF80_MOUSE
397
0
43314
TrEMBL
other Location (Reliability: 2)
A0A6B9EQU3_MOUSE
534
0
60276
TrEMBL
other Location (Reliability: 5)
Q5I0X8_MOUSE
261
0
29266
TrEMBL
other Location (Reliability: 2)
A0A0G2JDU8_MOUSE
82
0
9700
TrEMBL
other Location (Reliability: 2)
Q3U0S4_MOUSE
960
0
104524
TrEMBL
other Location (Reliability: 2)
Q5BKS2_MOUSE
476
0
52024
TrEMBL
other Location (Reliability: 2)
Q80XK0_MOUSE
538
0
61440
TrEMBL
Mitochondrion (Reliability: 4)
V9GXH4_MOUSE
248
0
27875
TrEMBL
other Location (Reliability: 1)
Q3U8K3_MOUSE
367
0
39370
TrEMBL
other Location (Reliability: 3)
Q3TYF5_MOUSE
329
0
37125
TrEMBL
Mitochondrion (Reliability: 5)
B1AQF4_MOUSE
210
0
23223
TrEMBL
other Location (Reliability: 3)
F7BX26_MOUSE
476
0
54317
TrEMBL
other Location (Reliability: 1)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
36000
-
1 * 65000 + 1 * 36000 + 1 * ?, the heterotrimer consists of a 36000 Da catalytic C subunit, a 65000 Da structural A subunit, and a regulatory B subunit PP2AB
65000
-
1 * 65000 + 1 * 36000 + 1 * ?, the heterotrimer consists of a 36000 Da catalytic C subunit, a 65000 Da structural A subunit, and a regulatory B subunit PP2AB
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
heterotrimer
-
1 * 65000 + 1 * 36000 + 1 * ?, the heterotrimer consists of a 36000 Da catalytic C subunit, a 65000 Da structural A subunit, and a regulatory B subunit PP2AB
trimer
-
PP2A is a trimeric enzyme composed of a dimeric core consisting of a structural A subunit, a catalytic C subunit and a variable B subunit that confers targeting specificity
additional information
-
the enzymes are monomers or heterodimers, the different serine/threonine protein phosphatases are formed by different catalytic subunits forming the different isozymes
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
carboxymethylation
-
PP2AC undergoes at least three different posttranslational modifications: phosphorylation of Tyr-307, carboxymethylation of Leu-309, and phosphorylation of unidentified threonine residues
phosphoprotein
-
PP2AC undergoes at least three different posttranslational modifications: phosphorylation of Tyr-307, carboxymethylation of Leu-309, and phosphorylation of unidentified threonine residues
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
L309Q
additional information
-
PP2A Calpha subunit knockout mice show early embryonic death
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
DEAE cellulose column chromatography, Sephadex G-200 gel filtration, and Shim-pack Diol 300 gel filtration
-
there is no reliable method of separating native PP1c isoforms directly from testis without contamination
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
PP1alpha N-terminally tagged with a monomeric variant of red fluorescent protein is expressed in MDCKII cells
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Johnson, T.R.; Biggs, J.R.; Winbourn, S.E.; Kraft, A.S.
Regulation of dual-specificity phosphatases M3/6 and hVH5 by phorbol esters. Analysis of a delta-like domain
J. Biol. Chem.
275
31755-31762
2000
Homo sapiens, Mus musculus
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
Gallego, M.; Virshup, D.M.
Protein serine/threonine phosphatases: life, death, and sleeping
Curr. Opin. Cell Biol.
17
197-202
2005
Drosophila melanogaster, Lingulodinium polyedra, Homo sapiens, Mus musculus, Neurospora crassa
Haneda, M.; Kojima, E.; Nishikimi, A.; Hasegawa, T.; Nakashima, I.; Isobe, K.
Protein phosphatase 1, but not protein phosphatase 2A, dephosphorylates DNA-damaging stress-induced phospho-serine 15 of p53
FEBS Lett.
567
171-174
2004
Homo sapiens, Mus musculus
Kray, A.E.; Carter, R.S.; Pennington, K.N.; Gomez, R.J.; Sanders, L.E.; Llanes, J.M.; Khan, W.N.; Ballard, D.W.; Wadzinski, B.E.
Positive regulation of IkappaB kinase signaling by protein serine/threonine phosphatase 2A
J. Biol. Chem.
280
35974-35982
2005
Mus musculus, Mus musculus C57BL6
Crossthwaite, A.J.; Ciruela, A.; Rayner, T.F.; Cooper, D.M.
A direct interaction between the N terminus of adenylyl cyclase AC8 and the catalytic subunit of protein phosphatase 2A
Mol. Pharmacol.
69
608-617
2006
Homo sapiens, Mus musculus
Hrabchak, C.; Henderson, H.; Varmuza, S.
A testis specific isoform of endophilin B1, endophilin B1t, interacts specifically with protein phosphatase-1c gamma2 in mouse testis and is abnormally expressed in PP1c gamma null mice
Biochemistry
46
4635-4644
2007
Mus musculus
Belakavadi, M.; Prabhakar, B.T.; Salimath, B.P.
Purification and characterization of butyrate-induced protein phosphatase involved in apoptosis of Ehrlich ascites tumor cells
Biochim. Biophys. Acta
1770
39-47
2007
Mus musculus
Toole, B.J.; Cohen, P.T.
The skeletal muscle-specific glycogen-targeted protein phosphatase 1 plays a major role in the regulation of glycogen metabolism by adrenaline in vivo
Cell. Signal.
19
1044-1055
2007
Mus musculus
Liu, C.W.; Wang, R.H.; Berndt, N.
Protein phosphatase 1alpha activity prevents oncogenic transformation
Mol. Carcinog.
45
648-656
2006
Homo sapiens, Mus musculus
Shmueli, A.; Gdalyahu, A.; Sapoznik, S.; Sapir, T.; Tsukada, M.; Reiner, O.
Site-specific dephosphorylation of doublecortin (DCX) by protein phosphatase 1 (PP1)
Mol. Cell. Neurosci.
32
15-26
2006
Mus musculus
Kim, S.I.; Kwak, J.H.; Wang, L.; Choi, M.E.
Protein phosphatase 2A is a negative regulator of transforming growth factor-beta1-induced TAK1 activation in mesangial cells
J. Biol. Chem.
283
10753-10763
2008
Mus musculus
Toyo-oka, K.; Mori, D.; Yano, Y.; Shiota, M.; Iwao, H.; Goto, H.; Inagaki, M.; Hiraiwa, N.; Muramatsu, M.; Wynshaw-Boris, A.; Yoshiki, A.; Hirotsune, S.
Protein phosphatase 4 catalytic subunit regulates Cdk1 activity and microtubule organization via NDEL1 dephosphorylation
J. Cell Biol.
180
1133-1147
2008
Mus musculus
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
Traweger, A.; Wiggin, G.; Taylor, L.; Tate, S.A.; Metalnikov, P.; Pawson, T.
Protein phosphatase 1 regulates the phosphorylation state of the polarity scaffold Par-3
Proc. Natl. Acad. Sci. USA
105
10402-10407
2008
Mus musculus
Luo, J.; Ma, J.; Yu, D.Y.; Bu, F.; Zhang, W.; Tu, L.H.; Wei, Q.
Infusion of FK506, a specific inhibitor of calcineurin, induces potent tau hyperphosphorylation in mouse brain
Brain Res. Bull.
76
464-468
2008
Mus musculus
Nicolaou, P.; Rodriguez, P.; Ren, X.; Zhou, X.; Qian, J.; Sadayappan, S.; Mitton, B.; Pathak, A.; Robbins, J.; Hajjar, R.J.; Jones, K.; Kranias, E.G.
Inducible expression of active protein phosphatase-1 inhibitor-1 enhances basal cardiac function and protects against ischemia/reperfusion injury
Circ. Res.
104
1012-1020
2009
Mus musculus
Kilili, G.K.; Kyriakis, J.M.
Mammalian Ste20-like kinase (Mst2) indirectly supports Raf-1/ERK pathway activity via maintenance of protein phosphatase-2A catalytic subunit levels and consequent suppression of inhibitory Raf-1 phosphorylation
J. Biol. Chem.
285
15076-15087
2010
Homo sapiens, Mus musculus
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
Baek, K.H.; Zaslavsky, A.; Lynch, R.C.; Britt, C.; Okada, Y.; Siarey, R.J.; Lensch, M.W.; Park, I.H.; Yoon, S.S.; Minami, T.; Korenberg, J.R.; Folkman, J.; Daley, G.Q.; Aird, W.C.; Galdzicki, Z.; Ryeom, S.
Downs syndrome suppression of tumour growth and the role of the calcineurin inhibitor DSCR1
Nature
459
1126-1130
2009
Homo sapiens, Mus musculus
Shi, J.; Gu, P.; Zhu, Z.; Liu, J.; Chen, Z.; Sun, X.; Chen, W.; Gao, X.; Zhang, Z.
Protein phosphatase 2A effectively modulates basal L-type Ca2+ current by dephosphorylating Cav1.2 at serine 1866 in mouse cardiac myocytes
Biochem. Biophys. Res. Commun.
418
792-798
2012
Mus musculus
Haeseleer, F.; Sokal, I.; Gregory, F.D.; Lee, A.
Protein phosphatase 2A dephosphorylates CaBP4 and regulates CaBP4 function
Invest. Ophthalmol. Vis. Sci.
54
1214-1226
2013
Mus musculus
Taira, J.; Kida, Y.; Kuwano, K.; Higashimoto, Y.
Protein phosphatase 2A dephosphorylates phosphoserines in nucleocytoplasmic shuttling and secretion of high mobility group box 1
J. Biochem.
154
299-308
2013
Mus musculus
Okamura, H.; Yoshida, K.; Yang, D.; Haneji, T.
Protein phosphatase 2A Calpha regulates osteoblast differentiation and the expressions of bone sialoprotein and osteocalcin via osterix transcription factor
J. Cell. Physiol.
228
1031-1037
2013
Mus musculus
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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