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Information on EC 3.1.3.16 - protein-serine/threonine phosphatase and Organism(s) Homo sapiens and UniProt Accession Q8N3J5

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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.3 Phosphoric-monoester hydrolases
                3.1.3.16 protein-serine/threonine phosphatase
IUBMB 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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Select one or more organisms in this record: ?
This record set is specific for:
Homo sapiens
UNIPROT: Q8N3J5
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Synonyms
calcineurin, protein phosphatase, pac-1, dusp1, dusp6, serine/threonine phosphatase, pp2ac, ppm1d, phosphoprotein phosphatase, laforin, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
PP2Ckappa
isozyme
protein phosphatase 2Ckappa
-
3-hydroxy 3-methylglutaryl CoenzymeA reductase phosphatase
-
-
-
-
Aspergillus awamori acid protein phosphatase
-
-
-
-
B56beta
-
regulatory subunit of protein phosphatase 2A
B56gamma-PP2A
-
-
B56gamma-specific protein phosphatase 2A
-
-
Balpha
-
-
BCKDH phosphatase
-
-
-
-
branched-chain alpha-keto acid dehydrogenase phosphatase
-
-
-
-
calcineurin
Calcineurin A1
-
-
-
-
Calcineurin A2
-
-
-
-
calcineurin B-like protein
-
calcium-dependent protein phosphatase 2B
-
-
CALNA
-
-
CALNB
-
-
CaM kinase phosphatase
-
-
CaM-kinase phosphatase
-
-
-
-
CaMIIKPase
-
-
CaMKPase
-
-
-
-
casein phosphatase
-
-
-
-
class I cysteine-based dual-specificity phosphatase
CN phosphatase
-
-
CNA
-
calcineurin catalytic subunit
CNAa
-
-
CNAalpha
-
-
CNAbeta
-
-
CNAgamma
-
-
DRES10
-
-
-
-
DSP
PTP domain class I DSPs differ from classical PTPs in that they can dephosphorylate phospho-Tyr, phospho-Ser and phospho-Thr residues, as well as nonproteinaceous substrates
DSP hVH5
-
-
dual specificity phosphatase
-
-
dual specificity protein phosphatase 1
-
dual specificity protein phosphatase 10
-
dual specificity protein phosphatase 26
-
dual specificity protein phosphatase 3
UniProt
dual specificity protein phosphatase 6
-
dual-specificity phosphatase 5
-
-
dual-specificity phosphatase hVH5
-
-
DUSP5
-
-
eIF2alpha phosphatase
-
Fcp1
-
-
Fibroblast growth factor inducible protein 13
-
-
-
-
FIN13
Flap wing protein
-
-
-
-
hFEM2
-
-
HMG-CoA reductase phosphatase
-
-
-
-
ILKAP
-
-
kinase associated phosphatase
-
-
Magnesium-dependent calcium inhibitable phosphatase
-
-
-
-
MCPP
-
-
-
-
Microtubule star protein
-
-
-
-
myosin light chain phosphatase
-
a specific form of PP1
NERPP-2C
-
-
PDP1
-
-
PDP2
-
-
phosphatase 2A
-
-
-
-
phosphatase 2B
-
-
-
-
phosphatase C-II
-
-
-
-
Phosphatase esp1
-
-
-
-
phosphatase H-II
-
-
-
-
phosphatase I
-
-
-
-
phosphatase IB
-
-
-
-
phosphatase II
-
-
-
-
phosphatase III
-
-
-
-
phosphatase IV
-
-
-
-
phosphatase of activated cells 1
-
phosphatase of regenerating liver
-
phosphatase PP4
-
-
phosphatase SP
-
-
-
-
phosphoglycerate mutase 5
-
phosphoprotein phosphatase
-
-
-
-
phosphopyruvate dehydrogenase phosphatase
-
-
-
-
phosphorylase phosphatase
-
phosphospectrin phosphatase
-
-
-
-
phosphothreonine/serine-specific PP
-
-
PK-Pase
-
-
-
-
polycation modulated (PCM-) phosphatase
-
-
-
-
POPX1
-
-
POPX2
-
-
PP-1A
-
-
-
-
PP-1B
-
-
-
-
PP-1G
-
-
-
-
PP-2A
-
-
PP-2B
-
-
PP-2C
-
-
PP1alpha
-
-
PP1beta
-
-
PP1c
-
protein phosphatase 1 catalytic subunit
PP1cgamma
-
-
PP1delta
-
-
PP1gamma
PP2A-alpha
-
-
-
-
PP2A-B56gamma
-
-
PP2A-beta
-
-
-
-
PP2Aalpha
-
-
PP2Abeta
-
-
PP2Ac
-
catalytic subunit of protein phosphatase 2A
PP2Acalpha
PP2Acbeta
-
-
PP2Balpha
-
-
PP2Bbeta
-
-
PP2Bgamma
-
-
PP2C epsilon
-
PP2C phosphatase
-
-
PP2C-alpha
-
-
-
-
PP2C-beta
-
-
-
-
PP2C-delta
-
-
-
-
PP2C-epsilon
-
PP2C-gamma
-
-
-
-
PP2Calpha
PP2Cbeta
PP2Cdelta
-
-
PP2Cepsilon
-
isoform
PP2Ceta
-
isoform
PP2Cgamma
PP2Cm
-
isoform
PP2CR
-
-
PP4c
-
catalytic subunit of protein phosphatase 4
PP6R1
-
regulatory subunit of protein phosphatase 6, PP6R1 acts as a scaffold with separate regions for binding to protein phosphatase 6 and to ankyrin repeat protein 28
PPEF
-
-
-
-
PPEF1
-
-
PPEF2
-
-
PPIalpha
-
-
PPM family phosphatase
-
-
PPM1D
-
-
PPM1D/Wip1
-
-
PPM1F
-
-
PPN
-
-
-
-
PPP phosphatase
-
PPP1CA
isoform
Ppp1calpha
-
-
PPP1CB
isoform
Ppp1cbeta
-
-
PPP1CC
isoform
Ppp1cgamma
-
-
PPP2CA
-
protein phosphatase 2 catalytic subunit alpha
Ppp2calpha
-
-
Ppp2cbeta
-
-
PPP3CA
-
protein phosphatase 3 catalytic subunit alpha
Ppp3calpha
-
-
Ppp3cbeta
-
-
Ppp3cgamma
-
-
PPP3R-like protein
-
PPP4
-
-
Ppp4c
-
-
Ppp5c
Ppp6c
-
-
Ppp7calpha
-
-
Ppp7cbeta
-
-
PR55gamma
-
protein phosphatase 2A subunit
PR65
-
structural core subunit of protein phosphatase 2A
protein D phosphatase
-
-
-
-
protein phosphatase
-
-
-
-
protein phosphatase 1
protein phosphatase 1-like
-
Protein phosphatase 1A
-
-
-
-
protein phosphatase 1alpha
-
-
Protein phosphatase 1B
-
-
-
-
Protein phosphatase 1C
-
-
-
-
protein phosphatase 1gamma
-
-
protein phosphatase 1L
-
protein phosphatase 2
-
-
protein phosphatase 2A
protein phosphatase 2A regulatory subunit B56alpha
-
-
protein phosphatase 2B
-
-
protein phosphatase 2C
protein phosphatase 2Cdelta
-
-
protein phosphatase 3
protein phosphatase 4
-
-
protein phosphatase 5
protein phosphatase 6
-
-
Protein phosphatase magnesium-dependent 1 delta
-
-
-
-
Protein phosphatase magnesium-dependent 1 gamma
-
-
-
-
protein phosphatase type 2A
-
-
Protein phosphatase with EF calcium-binding domain
-
-
-
-
protein phosphatase-1
-
-
protein phosphatase-2A
-
-
protein serine/threonine
-
protein serine/threonine phosphatase
protein serine/threonine phosphatase 2A
-
-
protein serine/threonine phosphatase 4
-
-
PSPase
-
-
-
-
PSTP
-
-
PTP-1B
-
-
Retinal degeneration C protein
-
-
-
-
S/T phosphatase
-
-
Ser/Thr phosphatase
-
-
Ser/Thr protein phosphatase
-
-
Ser/Thr protein phosphatase 5
serine-threonine phosphatase
-
serine-threonine protein phosphatase
-
-
serine/threonine (S/T) phosphatase
-
-
serine/threonine phosphatase
serine/threonine protein phosphatase
serine/threonine protein phosphatase 1
serine/threonine protein phosphatase 4
-
-
serine/threonine protein phosphatase type 5
-
serine/threonine protein phosphatase-5
Set-binding factor 1
-
Suppressor protein SDS21
-
-
-
-
type 1 protein phosphatase
-
-
type 2A protein phosphatase
-
-
type 2C protein phosphatase
-
-
type-1 phosphatase
-
type-2A phosphatase
-
type-2B phosphatase
-
type-I phosphatase
-
-
type-II phosphatase
-
-
wild-type p53-induced phosphatase
-
-
wound-induced protein 1
-
-
additional information
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
[a protein]-serine/threonine phosphate + H2O = [a protein]-serine/threonine + phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
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 hide
9025-75-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
?
phosphothreonine + H2O
threonine + phosphate
show the reaction diagram
-
-
-
?
4-nitrophenyl methylphosphonate + H2O
4-nitrophenol + methylphosphonate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl phosphate + H2O
4-nitrophenol + phosphate
show the reaction diagram
6,8-difluoro-4-methylumbelliferyl phosphate + H2O
6,8-difluoro-4-methylumbelliferone + phosphate
show the reaction diagram
-
-
-
-
?
a phosphoprotein + H2O
dephosphorylated protein + phosphate
show the reaction diagram
-
-
-
-
?
AAApTVA + H2O
AAATVA + phosphate
show the reaction diagram
-
-
-
?
AGPALpSPVPPV + H2O
AGPALSPVPPV + phosphate
show the reaction diagram
-
-
-
?
ALSAGpSNEYLR + H2O
ALSAGSNEYLR + phosphate
show the reaction diagram
-
-
-
?
ASQEPpSPAASA + H2O
ASQEPSPAASA + phosphate
show the reaction diagram
-
-
-
?
carrier protein-T3-phosphothreonine + H2O
carrier protein-T3-threonine + phosphate
show the reaction diagram
-
-
-
-
?
carrier protein-T4-phosphothreonine + H2O
carrier protein-T4-threonine + phosphate
show the reaction diagram
-
-
-
-
?
chicken acidic leucine-rich epidermal growth factor-like domain-containing brain protein/neuroglycan C + H2O
?
show the reaction diagram
-
the regulatory subunit of protein phosphatase 2A, B56beta, interacts with chicken acidic leucine-rich epidermal growth factor-like domain-containing brain protein/neuroglycan C (CALEB/NGC) and inhibits CALEB/NGC-mediated dendritic branching but not spine formation
-
-
?
DDApTVA + H2O
DDATVA + phosphate
show the reaction diagram
-
-
-
?
ENDpTINASL + H2O
ENDTINASL + phosphate
show the reaction diagram
-
-
-
?
ESEMEpTPSAIN + H2O
ESEMETPSAIN + phosphate
show the reaction diagram
-
-
-
?
FLRT(P)SCG + H2O
FLRTSCG + phosphate
show the reaction diagram
-
-
-
-
?
FLRTS(P)CG + H2O
FLRTSCG + phosphate
show the reaction diagram
-
-
-
-
?
FLRTT(P)CG + H2O
FLRTTCG + phosphate
show the reaction diagram
-
-
-
-
?
glycogen synthase + H2O
glycogen synthase + phosphate
show the reaction diagram
-
-
-
-
?
glycogen synthase b + H2O
glycogen synthase I + phosphate
show the reaction diagram
-
-
-
-
?
HSAPPpSPEEKD + H2O
HSAPPSPEEKD + phosphate
show the reaction diagram
-
-
-
?
myelin basic protein + H2O
? + phosphate
show the reaction diagram
-
-
-
-
?
myosin light chain phosphate + H2O
myosin light chain + phosphate
show the reaction diagram
-
myosin light chain phosphatase is a specific form of PP1
-
-
?
NFEDHpSAPPSP + H2O
NFEDHSAPPSP + phosphate
show the reaction diagram
-
-
-
?
NPCTEpTFTGTL + H2O
NPCTETFTGTL + phosphate
show the reaction diagram
-
-
-
?
p-nitrophenyl phosphate + H2O
p-nitrophenol + phosphate
show the reaction diagram
-
-
-
-
?
p38 MAP kinase phosphoprotein
?
show the reaction diagram
-
-
-
-
?
peptide mGluR3 + H2O
?
show the reaction diagram
-
-
-
?
phosphatidylinositol-(3,4,5)-triphosphate + H2O
?
show the reaction diagram
the enzyme displays activity towards the D3 position of the phosphoinositide second messenger phosphatidylinositol (3,4,5)-triphosphate
-
-
?
phospho-Cdk2 + H2O
Cdk6 + phosphate
show the reaction diagram
-
-
-
-
?
phospho-Cdk6 + H2O
Cdk6 + phosphate
show the reaction diagram
-
-
-
-
?
phospho-MKK + H2O
MKK + phosphate
show the reaction diagram
-
-
-
-
?
phospho-TAK1 + H2O
TAK1 + phosphate
show the reaction diagram
-
-
-
-
?
phospho-threonylpeptide + H2O
threonylpeptide + phosphate
show the reaction diagram
-
-
-
-
?
phosphocasein + H2O
casein + phosphate
show the reaction diagram
-
-
-
-
?
phosphohistone + H2O
histone + phosphate
show the reaction diagram
-
-
-
-
?
phosphoprotein + H2O
protein + phosphate
show the reaction diagram
phosphoprotein K15F + H2O
protein K15F + phosphate
show the reaction diagram
-
-
-
-
?
phosphoprotein R20A + H2O
protein R20A + phosphate
show the reaction diagram
-
-
-
-
?
phosphoprotein RII + H2O
protein RII + phosphate
show the reaction diagram
-
-
-
-
?
phosphoproteins + H2O
proteins + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylase a + H2O
?
show the reaction diagram
-
-
-
-
?
phosphorylase a + H2O
phosphorylase b + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated AD P-Tau + H2O
AD P-Tau + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated Akt protein + H2O
Akt protein + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of Akt protein
-
?
phosphorylated androgen receptor + H2O
androgen receptor + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of androgen receptor
-
?
phosphorylated AP-1/AP-2 + H2O
AP-1/AP-2 + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of AP-1/AP-2
-
?
phosphorylated APC protein + H2O
APC protein + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of APC protein
-
?
phosphorylated apoptosis signal-regulating kinase 1 + H2O
apoptosis signal-regulating kinase 1 + phosphate
show the reaction diagram
apoptosis signal-regulating kinase 1 is transiently activated by autophosphorylation at Thr845
-
-
?
phosphorylated ASK1 + H2O
ASK1 + phosphate
show the reaction diagram
-
ASK1 is inactivated by the isoform PP2Ceta
-
-
?
phosphorylated ataxia telangiectasia and Rad3-related + H2O
ataxia telangiectasia and Rad3-related + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated ataxia telangiectasia mutated kinase + H2O
ataxia telangiectasia mutated kinase + phosphate
show the reaction diagram
phosphorylated ATM and Rad 3 related kinase + H2O
ATM and Rad 3 related kinase + phosphate
show the reaction diagram
-
-
-
?
phosphorylated ATM protein + H2O
ATM protein + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of ATM protein
-
?
phosphorylated aurora A + H2O
aurora A + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of aurora A
-
?
phosphorylated axin + H2O
axin + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of axin
-
?
phosphorylated B-catenin + H2O
B-catenin + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to activation of B-catenin
-
?
phosphorylated BAD protein + H2O
BAD protein + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to activation of BAD protein
-
?
phosphorylated BAX protein + H2O
BAX protein + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to activation of BAX protein
-
?
phosphorylated BCL-2 + H2O
BCL-2 + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of BCL-2
-
?
phosphorylated Bcl2 + H2O
Bcl2 + phosphate
show the reaction diagram
-
PP2A-mediated dephosphorylation of Bcl2 promotes its direct interaction with p53 as well as a conformational change in Bcl2, PP2A directly interacts with the BH4 domain of Bcl2 as a docking site to potentially bridge PP2A to Bcl2's flexible loop domain containing the target serine 70 phosphorylation site
-
-
?
phosphorylated beta-catenin + H2O
beta-catenin + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated c-Jun N-terminal kinase + H2O
c-Jun N-terminal kinase + phosphate
show the reaction diagram
-
-
-
?
phosphorylated c-MET + H2O
c-MET + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of c-MET
-
?
phosphorylated c-Myc + H2O
c-Myc + phosphate
show the reaction diagram
phosphorylated Ca2+/calmodulin-dependent protein kinase II + H2O
Ca2+/calmodulin-dependent protein kinase II + phosphate
show the reaction diagram
phosphorylated calpain + H2O
calpain + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of calpain
-
?
phosphorylated CAM kinase IV + H2O
CAM kinase IV + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of CAM kinase IV
-
?
phosphorylated carboxypeptidase D + H2O
carboxypeptidase D + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of carboxypeptidase D
-
?
phosphorylated CAS protein + H2O
CAS protein + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of CAS protein
-
?
phosphorylated casein + H2O
casein + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated Cav1.2 + H2O
Cav1.2 + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of Cav1.2
-
?
phosphorylated Cdc25c + H2O
Cdc25c + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of Cdc25c
-
?
phosphorylated Cdc6 protein + H2O
Cdc6 protein + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to activation of Cdc6 protein
-
?
phosphorylated CFTRCXCR2 + H2O
CFTRCXCR2 + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of CFTRCXCR2
-
?
phosphorylated Chk1 + H2O
Chk1 + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated Chk1 protein + H2O
Chk1 protein + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of Chk1 protein
-
?
phosphorylated Chk2 + H2O
Chk2 + phosphate
show the reaction diagram
phosphorylated cyclin G1 + H2O
cyclin G1 + phosphate
show the reaction diagram
-
the B'alpha1 subunit of the serine/threonine protein phosphatase 2A, which binds to cyclin G1, can stabilize cyclin G1 under unstressed conditions and upon DNA damage, as well as inhibit the ability of cyclin G1 to be ubiquitinated
-
-
?
phosphorylated DARPP-32 + H2O
DARP-32 + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of DARP-32
-
?
phosphorylated deoxycytidine kinase + H2O
deoxycytidine kinase + phosphate
show the reaction diagram
-
protein phosphatase 2A negatively regulates deoxycytidine kinase activity via Ser-74 dephosphorylation
-
-
?
phosphorylated DNA-dependent protein kinase + H2O
DNA-dependent protein kinase + phosphate
show the reaction diagram
phosphorylated E-cadherin + H2O
E-cadherin + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to activation of E-cadherin
-
?
phosphorylated ERK + H2O
ERK + phosphate
show the reaction diagram
phosphorylated ERK protein + H2O
ERK protein + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of ERK protein
-
?
phosphorylated ERK-2 + H2O
ERK-2 + phosphate
show the reaction diagram
phosphorylated ERK1 + H2O
ERK1 + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated ERK2 + H2O
ERK2 + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated ERK5 + H2O
ERK5 + phosphate
show the reaction diagram
-
dephosphorylation at Thr218 and Tyr220 residues, dephosphorylation site sequences, overview
-
-
?
phosphorylated estrogen receptor A + H2O
estrogen receptor A + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of estrogen receptor A
-
?
phosphorylated glucocorticoid receptor-heat shock protein 90 + H2O
glucocorticoid receptor-heat shock protein 90 + phosphate
show the reaction diagram
-
-
-
?
phosphorylated glycogen phosphorylase a + H2O
glycogen phosphorylase a + phosphate
show the reaction diagram
phosphorylated Gp130 protein + H2O
Gp130 protein + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to activation of Gp130 protein
-
?
phosphorylated GSK3beta + H2O
GSK3beta + phosphate
show the reaction diagram
laforin dephosphorylates the inhibitory Ser9 of GSK3beta
-
-
?
phosphorylated H2AX + H2O
H2AX + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of H2AX
-
?
phosphorylated HAND-1 + H2O
HAND-1 + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of HAND-1
-
?
phosphorylated HAND-2 + H2O
HAND-2 + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of HAND-2
-
?
phosphorylated HDAC4 + H2O
HDAC4 + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of HDAC4
-
?
phosphorylated histone 2A member X + H2O
histone 2A member X + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated histone deacetylase 3 + H2O
histone deacetylase 3 + phosphate
show the reaction diagram
phosphorylated histone deacetylase 7 + H2O
histone deacetylase 7 + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated IKKB + H2O
IKKB + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of IKKB
-
?
phosphorylated IKKB protein + H2O
IKKB protein + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to activation of IKKB protein
-
?
phosphorylated ILK1 + H2O
ILK1 + phosphate
show the reaction diagram
phosphorylated INAD-protein + H2O
INAD-protein + phosphate
show the reaction diagram
-
INAD-protein is inactivation no afterpotential D-protein
-
-
?
phosphorylated JNK protein + H2O
JNK protein + phosphate
show the reaction diagram
phosphorylated JNK1 + H2O
JNK1 + phosphate
show the reaction diagram
-
dephosphorylation at Thr183 and Tyr185 residues, dephosphorylation site sequences, overview
-
-
?
phosphorylated keratin 8 + H2O
keratin 8 + phosphate
show the reaction diagram
-
dephosphorylates at phospho-Ser431
-
-
?
phosphorylated KSR protein + H2O
KSR protein + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to activation of KSR protein
-
?
phosphorylated lamban + H2O
lamban + phosphate
show the reaction diagram
phosphorylated Mdm2 protein + H2O
Mdm2 protein + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to activation of Mdm2 protein
-
?
phosphorylated MEK3 + H2O
MEK3 + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of MEK3
-
?
phosphorylated MEKK3 + H2O
MEKK3 + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of MEKK3
-
?
phosphorylated Mid1 + H2O
Mid1 + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated mitogen-activated protein kinase kinase 3 + H2O
mitogen-activated protein kinase kinase 3 + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated MKK3b + H2O
MKK3b + phosphate
show the reaction diagram
-
MKK3b is inactivated by the isoforms PP2Calpha and PP2Cbeta
-
-
?
phosphorylated MKK4 + H2O
MKK4 + phosphate
show the reaction diagram
phosphorylated MKK6b + H2O
MKK6b + phosphate
show the reaction diagram
-
MKK6b is inactivated by the isoforms PP2Calpha and PP2Cbeta
-
-
?
phosphorylated MKK7 + H2O
MKK7 + phosphate
show the reaction diagram
-
MKK7 is inactivated by the isoforms PP2Calpha and PP2Cbeta
-
-
?
phosphorylated mouse double minute 2 homologue + H2O
mouse double minute 2 homologue + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated myelin basic protein + H2O
myelin basic protein + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated myosin light chain + H2O
myosin light chain + phosphate
show the reaction diagram
phosphorylated nemo protein + H2O
nemo protein + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of nemo protein
-
?
phosphorylated occludin + H2O
occludin + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of occludin
-
?
phosphorylated P107 + H2O
P107 + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of P107
-
?
phosphorylated p38 + H2O
p38 + phosphate
show the reaction diagram
phosphorylated p38alpha + H2O
p38alpha + phosphate
show the reaction diagram
phosphorylated p53 + H2O
p53 + phosphate
show the reaction diagram
phosphorylated p53 protein + H2O
p53 protein + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to activation of p53 protein
-
?
phosphorylated p53-binding protein 1 + H2O
p53-binding protein 1 + phosphate
show the reaction diagram
-
p53-binding protein 1 is dephosphorylated at Ser25 and Ser1778
-
-
?
phosphorylated PACS-1 + H2O
PACS-1 + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of PACS-1
-
?
phosphorylated paxillin + H2O
paxillin + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of paxillin
-
?
phosphorylated peptide + H2O
peptide + phosphate
show the reaction diagram
-
PP2Cdelta prefers the dephosphorylation at diphosphorylated T(P)X(P)Y sequence compared to monophosphorylated T(P)XY sequence
-
-
?
phosphorylated period + H2O
period + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to activation of period
-
?
phosphorylated phosphorylase a + H2O
phosphorylase a + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated phosphorylase kinase + H2O
phosphorylase kinase + phosphate
show the reaction diagram
phosphorylated PIM protein + H2O
PIM protein + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of PIM protein
-
?
phosphorylated PKCbeta II + H2O
PKBbeta II + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of PKCbeta II
-
?
phosphorylated PKCdelta + H2O
PKCdelta + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of PKCdelta
-
?
phosphorylated Polo-like kinase 1 + H2O
Polo-like kinase 1 + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated protein kinase CK2alpha + H2O
protein kinase CK2alpha + phosphate
show the reaction diagram
-
-
-
?
phosphorylated protein phosphatase inhibitor-1 + H2O
protein phosphatase inhibitor-1 + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated Raf-1 kinase + H2O
Raf 1 kinase + phosphate
show the reaction diagram
phosphorylated Raf1 + H2O
Raf-1 + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated Raf1 + H2O
Raf1 + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to activation of Raf1
-
?
phosphorylated RalA + H2O
RalA + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of RalA
-
?
phosphorylated RelA + H2O
RelA + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of RelA
-
?
phosphorylated retinoblastoma protein + H2O
retinoblastoma protein + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated rhodopsin + H2O
rhodopsin + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated RNA polymerase II + H2O
RNA polymerase II + phosphate
show the reaction diagram
phosphorylated SCR protein + H2O
SCR protein + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of SCR protein
-
?
phosphorylated securin + H2O
securin + phosphate
show the reaction diagram
phosphorylated Ser/Thr protein kinase + H2O
DNA-dependent Ser/Thr protein kinase + phosphate
show the reaction diagram
-
-
-
?
phosphorylated seratonin + H2O
seratonin + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to activation of seratonin
-
?
phosphorylated serine-phosphorylated glycogen phosphorylase + H2O
glycogen phosphorylase + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated Shc protein + H2O
Shc protein + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of Shc protein
-
?
phosphorylated Sp1 + H2O
Sp1 + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to activation of Sp1
-
?
phosphorylated spliceosome-associated protein 155 + H2O
spliceosome-associated protein 155 + phosphate
show the reaction diagram
phosphorylated sprouty + H2O
sprouty + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to activation of sprouty
-
?
phosphorylated Src protein + H2O
Src protein + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of Src protein
-
?
phosphorylated stress-activated protein kinase + H2O
stress-activated protein kinase + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated Tau + H2O
Tau + phosphate
show the reaction diagram
-
the Balpha regulatory subunit of PP2A facilitates dephosphorylation of the phosphorylated Tau
-
-
?
phosphorylated tau protein + H2O
tau protein + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to activation of tau protein
-
?
phosphorylated TRAF2 + H2O
TRAF2 + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to inhibition of TRAF2
-
?
phosphorylated transforming growth factor beta-activated kinase 1 + H2O
transforming growth factor beta-activated kinase 1 + phosphate
show the reaction diagram
-
dephosphorylates Thr-187 in the TAK1 activation loop
-
-
?
phosphorylated transforming growth factor-beta-activated kinase 1 + H2O
transforming growth factor-beta-activated kinase 1 + phosphate
show the reaction diagram
-
transforming growth factor-beta-activated kinase 1 is inactivated by the isoforms PP2Cbeta and PP2Cepsilon
-
-
?
phosphorylated tumor suppressor protein p53 + H2O
tumor suppressor protein p53 + phosphate
show the reaction diagram
-
dephosphorylation at Thr55
-
-
?
phosphorylated UNG2 + H2O
UNG2 + phosphate
show the reaction diagram
-
dephosphorylation at Thr residues, identification of dephosphorylation site sequences, overview
-
-
?
phosphorylated vimentin + H2O
vimentin + phosphate
show the reaction diagram
-
-
the dephosphorylation leads to activation of vimentin
-
?
phosphospectrin + H2O
spectrin + phosphate
show the reaction diagram
-
-
-
-
?
PVARTpSPLQTP + H2O
PVARTSPLQTP + phosphate
show the reaction diagram
-
-
-
?
Raf proto-oncogene serine/threonine protein kinase + H2O
dephosphorylated Raf proto-oncogene serine/threonine protein kinase + phosphate
show the reaction diagram
PP5 plays a role in the inactivation of Raf proto-oncogene serine/threonine protein kinase, PP5/Raf proto-oncogene serine/threonine protein kinase association occurs in response to growth factor stimulation and results in the selective dephosphorylation of Ser338, removing phosphate from this critical site that helps to maintain Raf proto-oncogene serine/threonine protein kinase activation
-
-
?
RAT(P)VA + H2O
RATVA + phosphate
show the reaction diagram
-
-
-
-
?
RGRGSpSVGGGS + H2O
RGRGSSVGGGS + phosphate
show the reaction diagram
-
-
-
?
RII peptide + H2O
? + phosphate
show the reaction diagram
-
-
-
-
?
RRApSVA + H2O
RRASVA + phosphate
show the reaction diagram
-
-
-
?
RRApTVA + H2O
RRATVA + phosphate
show the reaction diagram
RRAS(P)VA + H2O
RRASVA + phosphate
show the reaction diagram
-
synthetic substrate
-
-
?
RRAT(P)VA + H2O
RRATVA + phosphate
show the reaction diagram
-
synthetic substrate
-
-
?
SQLHIpTPGTAY + H2O
SQLHITPGTAY + phosphate
show the reaction diagram
-
-
-
?
threonine-phosphorylated lipocortin I + H2O
lipocortin I + phosphate
show the reaction diagram
-
-
-
-
?
tumor necrosis factor receptor-associated factor 6 + H2O
?
show the reaction diagram
-
PP4 negatively regulates lipopolysaccharide-induced and tumor necrosis factor receptor-associated factor 6-mediated nuclear factor-kappaB activation by inhibiting the ubiquitination of tumor necrosis factor receptor-associated factor 6, PP4 is a negative feedback regulator of lipopolysaccharide/toll-like receptor 4 pathway
-
-
?
tyrosine-phosphorylated sEGF-R + H2O
phosphorylated sEGF-R + phosphate
show the reaction diagram
-
-
-
-
?
VARKLpSAREQR + H2O
VARKLSAREQR + phosphate
show the reaction diagram
-
-
-
?
vasodilator associated phosphoprotein + H2O
vasodilator associated protein + phosphate
show the reaction diagram
-
-
-
-
?
WHLADpSPAVNG + H2O
WHLADSPAVNG + phosphate
show the reaction diagram
-
-
-
?
YLRSIpSLPVPV + H2O
YLRSISLPVPV + phosphate
show the reaction diagram
-
-
-
?
[a protein]-serine/threonine phosphate + H2O
[a protein]-serine/threonine + phosphate
show the reaction diagram
[AKT1 protein]-serine/threonine phosphate + H2O
[AKT1 protein]-serine/threonine + phosphate
show the reaction diagram
-
-
-
-
?
[elongation factor 2alpha]-serine/threonine phosphate + H2O
[elongation factor 2alpha]-serine/threonine + phosphate
show the reaction diagram
-
-
-
?
[MAP1B protein]-serine/threonine phosphate + H2O
[MAP1B protein]-serine/threonine + phosphate
show the reaction diagram
[MAP2 protein]-serine/threonine phosphate + H2O
[MAP2 protein]-serine/threonine + phosphate
show the reaction diagram
-
-
-
?
[PAK1]-serine phosphate + H2O
[PAK1]-serine + phosphate
show the reaction diagram
dephosphorylation at Ser144
-
-
?
[protein I-1]-serine/threonine phosphate + H2O
[protein I-1]-serine/threonine + phosphate
show the reaction diagram
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
show the reaction diagram
-
-
-
?
[tau protein]-serine/threonine phosphate + H2O
[tau protein]-serine/threonine + phosphate
show the reaction diagram
-
-
-
?
[tubulin]-serine/threonine phosphate + H2O
[tubulin]-serine/threonine + phosphate
show the reaction diagram
PP2A preferentially dephosphorylates unassembled tubulin
-
-
?
[VAV2]-threonine phosphate + H2O
[VAV2]-threonine + phosphate
show the reaction diagram
dephosphorylation at Thr423
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
myosin light chain phosphate + H2O
myosin light chain + phosphate
show the reaction diagram
-
myosin light chain phosphatase is a specific form of PP1
-
-
?
phospho-Cdk2 + H2O
Cdk6 + phosphate
show the reaction diagram
-
-
-
-
?
phospho-Cdk6 + H2O
Cdk6 + phosphate
show the reaction diagram
-
-
-
-
?
phospho-MKK + H2O
MKK + phosphate
show the reaction diagram
-
-
-
-
?
phospho-TAK1 + H2O
TAK1 + phosphate
show the reaction diagram
-
-
-
-
?
phosphoprotein + H2O
protein + phosphate
show the reaction diagram
phosphorylated c-Myc + H2O
c-Myc + phosphate
show the reaction diagram
phosphorylated Ca2+/calmodulin-dependent protein kinase II + H2O
Ca2+/calmodulin-dependent protein kinase II + phosphate
show the reaction diagram
-
dephosphorylation of the autophosphorylated Thr286, PPM1F negatively regulates the multifunctional Ca2+/calmodulin-dependent protein kinase II, e.g. reducing the phosphorylation of vimentin
-
-
?
phosphorylated cyclin G1 + H2O
cyclin G1 + phosphate
show the reaction diagram
-
the B'alpha1 subunit of the serine/threonine protein phosphatase 2A, which binds to cyclin G1, can stabilize cyclin G1 under unstressed conditions and upon DNA damage, as well as inhibit the ability of cyclin G1 to be ubiquitinated
-
-
?
phosphorylated DNA-dependent protein kinase + H2O
DNA-dependent protein kinase + phosphate
show the reaction diagram
-
activation of DNA-dependent protein kinase to repair DNA double strand breaks by the process of nonhomologous end joining
-
-
?
phosphorylated ERK1 + H2O
ERK1 + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated ERK2 + H2O
ERK2 + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated glycogen phosphorylase a + H2O
glycogen phosphorylase a + phosphate
show the reaction diagram
-
inactivation of the substrate enzyme, overview
-
-
?
phosphorylated histone deacetylase 3 + H2O
histone deacetylase 3 + phosphate
show the reaction diagram
phosphorylated ILK1 + H2O
ILK1 + phosphate
show the reaction diagram
-
negative regulation of Wnt signaling
-
-
?
phosphorylated lamban + H2O
lamban + phosphate
show the reaction diagram
phosphorylated myosin light chain + H2O
myosin light chain + phosphate
show the reaction diagram
phosphorylated p38 + H2O
p38 + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated p38alpha + H2O
p38alpha + phosphate
show the reaction diagram
-
mediation of a negative feedback loop of the p38 MAPK-p53 signaling pathway
-
-
?
phosphorylated p53 + H2O
p53 + phosphate
show the reaction diagram
-
dephosphorylation of Ser15 by PP1, no activity with PP2A, PP1 inhibition leads to hyperphosphorylation of p53, PP1 has regulatory function
-
-
?
phosphorylated phosphorylase kinase + H2O
phosphorylase kinase + phosphate
show the reaction diagram
-
isozyme PP1 preferentially dephosphorylates the beta-subunit of phosphorylase kinase, isozyme PP2 preferentially dephosphorylates the alpha-subunit of phosphorylase kinase
-
-
?
phosphorylated Raf-1 kinase + H2O
Raf 1 kinase + phosphate
show the reaction diagram
-
phosphatase 2A dephosphorylates Raf-1 Ser259 in response to mitogens
-
-
?
phosphorylated Raf1 + H2O
Raf-1 + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated rhodopsin + H2O
rhodopsin + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated RNA polymerase II + H2O
RNA polymerase II + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated securin + H2O
securin + phosphate
show the reaction diagram
-
-
-
-
?
phosphorylated spliceosome-associated protein 155 + H2O
spliceosome-associated protein 155 + phosphate
show the reaction diagram
-
i.e. Sap155, a U2 small nuclear ribonucleoprotein particle component. nuclear inhibitor of PP1, i.e. NIPP1, a major PP1 interactor in the vertebrate nucleus, recruits PP1 to Sap155
-
-
?
[a protein]-serine/threonine phosphate + H2O
[a protein]-serine/threonine + phosphate
show the reaction diagram
[AKT1 protein]-serine/threonine phosphate + H2O
[AKT1 protein]-serine/threonine + phosphate
show the reaction diagram
-
-
-
-
?
[elongation factor 2alpha]-serine/threonine phosphate + H2O
[elongation factor 2alpha]-serine/threonine + phosphate
show the reaction diagram
-
-
-
?
[MAP1B protein]-serine/threonine phosphate + H2O
[MAP1B protein]-serine/threonine + phosphate
show the reaction diagram
[MAP2 protein]-serine/threonine phosphate + H2O
[MAP2 protein]-serine/threonine + phosphate
show the reaction diagram
-
-
-
?
[protein I-1]-serine/threonine phosphate + H2O
[protein I-1]-serine/threonine + phosphate
show the reaction diagram
substrate is a regulatory subunit I-1 (PPP1R1A) of phosphatase PP1, dephosphorylation of I-1 at Thr35 by PP2A deactivates I-1 and thus activates enzyme PP1
-
-
?
[protein]-serine/threonine phosphate + H2O
[protein]-serine/threonine + phosphate
show the reaction diagram
-
-
-
?
[tau protein]-serine/threonine phosphate + H2O
[tau protein]-serine/threonine + phosphate
show the reaction diagram
-
-
-
?
[tubulin]-serine/threonine phosphate + H2O
[tubulin]-serine/threonine + phosphate
show the reaction diagram
PP2A preferentially dephosphorylates unassembled tubulin
-
-
?
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Calmodulin
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
dependent
Mn2+
dependent
Co2+
-
-
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1,3-bis(4-amino-2-methylquinolin-6-yl)urea
-
1-(3-bromophenyl)-6-undecyl-1,3,5-triazinane-2,4-diimine
-
2-amino-4-methyl-N-naphthalen-2-ylpentanamide
-
3-iodo-7-[(8-iodo-10-phenyl-5,10-dihydrophenazin-2-yl)amino]-5-phenylphenazin-5-ium
-
5,5',6,6',8,8'-hexahydroxy-2,2',3,3'-tetramethyl-2,2',3,3'-tetrahydro-4H,4'H-9,9'-bibenzo[g]chromene-4,4'-dione
-
6,6-dimethyl-1-[4-(4-phenylbutyl)phenyl]-1,3,5-triazinane-2,4-diimine
-
6-(3,4-dichloro-phenyl)-4-(N,N-dimethylaminoethylthio)-2-phenyl-pyrimidine
-
i.e. CN585, noncompetitively and reversibly inhibits calcineurin activity, without affecting other Ser/Thr protein phosphatases or peptidyl prolyl cis/trans isomerases. The compound shows potent immunosuppressive effects by inhibiting NFAT nuclear translocation and transactivation, cytokine production, and T cell proliferation
c(M-L-2-amino-4-phosphono-4,4-difluorobutanoate-IpYVA)
-
-
C-terminally truncated nuclear inhibitor of protein phosphatase-1
-
C-terminally truncated NIPP1 forms a hyperactive holoenzyme with PP1, rendering PP1 minimally phosphorylated on an inhibitory site
-
caffeic acid phenethyl ester
-
down-regulation of expression of PP2A catalytic subunit in cells treated with caffeic acid phenethyl ester at 48 h
calyculin
-
moderate inhibition at 0.00001 mM
calyculin A
calyculin-A
-
cantharidin
cantharidine
-
cantheridin
-
strong inhibition at 0.005 mM
Co2+
-
-
CPI-17
-
encoded by gene PPP1R14A, chromosome 19. Upon phosphorylation at Thr38, the 17 kDa PP1 inhibitor protein, CPI-17, selectively inhibits a specific form of PP1, myosin light chain phosphatase, which transduces multiple kinase signals into the phosphorylation of myosin II and other proteins. Phosphorylation of CPI-17 at Thr38 is necessary and sufficient to convert the protein into a potent MLCP inhibitor, mechanism, modeling, overview
-
creatine phosphate
-
60 mM
cyclic phosphopeptide c(M-L-2-amino-4-phosphono-4,4-difluorobutanoate-IpYVA)
-
inhibits only Wip1
cyclic phosphopeptide c(MpSIpY)
-
-
cyclic phosphopeptide c(MpSIpYV)
-
-
cyclic phosphopeptide c(MpSIpYVA)
-
inhibits only Wip1
cyclic phosphopeptide c(MpSIpYVAT)
-
-
cyclic phosphopeptide c(TDDEMpSIpYVAT)
-
-
cyclin-dependent kinase 2
-
-
-
cyclophilin
-
-
-
cyclosporin
cyclosporin A
DARPP-32
-
-
di-mu-chloro(bis[1-[(morpholin-4-yl-kappaN)methyl]naphthalen-2-olato-kappaO])dicopper
-
di-mu-chloro(bis[1-[(piperidin-1-yl-kappaN)methyl]naphthalen-2-olato kappaO])dicopper
-
dinophysistoxin-2
-
docetaxel
-
docetaxel induces the decrease in the activity of protein phosphatase 1
DSCR1
-
a calcineurin inhibitor, encoded by gene Dscr1 on chromosome 21, is elevated in Down syndrome individuals. Increased dosage of Dyrk1A, appears to act in concert with Dscr1 to suppress tumor angiogenesis by further attenuating VEGF-calcineurin-NFAT signalling in endothelial cells, mechanism, overview. DSCR1-dependent inhibition of the VEGF-calcineurin-NFAT pathway in endothelial cells as a key component of the reduced cancer incidence in Down syndrome individuals
-
EDTA
-
isozyme PP1 has low activity after depletion of Mn2+ with EDTA
endothall
-
specific inhibitor of isozyme PP2A
FK506
fostriecin
glutamate
-
inhibitor of isozyme PP2A
guanabenz
a small molecule drug that specifically inhibits translation by blocking the activity of elongation factor 2alpha (eIF2alpha) phosphatases, specifically CreP:PP1 and GADD34:PP1
human Inhibitor-3
-
possesses a putative protein phosphatase-1 binding motif, 39KKVEW43. A second interaction site, whose deletion leads to loss of inhibitory potency, is identified between residues 65-77
-
I-1
the regulatory subunit I-1 (PPP1R1A) is a selective and potent enzyme PP1 inhibitor that facilitates crosstalk between different protein phosphatases and kinases. Protein kinase A-dependent phosphorylation of Thr35 activates I-1. As such, PKA-dependent I-1 activation and subsequent PP1 inhibition form a positive feedback loop amplifying the phosphorylation of several substrates during beta-adrenoceptor (beta-AR) stimulation. Dephosphorylation of I-1 Thr35 is mediated by enzymes PP2A and calcineurin, thereby creating additional crosstalk between different phosphatases
-
Inhibitor-1
-
inhibitor of isozyme PP1
-
Inhibitor-2
-
mesalazine
-
1 mg/ml efficiently inhibits PP2A
microcystin
-
microcystin-LR
microsystin-LR
-
N-methyl-N'-phenanthren-9-ylimidodicarbonimidic diamide
-
neurabin-I
-
IC50 for the wild-type catalytic subunit PP1alpha is 1.75 nM
-
Ni2+
-
-
nodularin
ocadaic acid
-
-
okadaic acid
p-bromotetramisole
-
PTP-1B
paclitaxel
-
paclitaxel induces decrease in activity of protein phosphatase 2 subgroups
pervanadate
-
-
phosphate
-
-
phosphocholine
-
-
phosphonothioic acid
-
phosphopeptide TDDEMpS-cyclohexylalanine-pYVAT
-
40% inhibition at 0.1 mM
phosphopeptide TDDEMpS-D-pYVAT
-
32% inhibition at 0.1 mM
phosphopeptide TDDEMpS-I-pYVAT
-
54% inhibition at 0.1 mM
phosphopeptide TDDEMpS-P-pYVAT
-
26% inhibition at 0.1 mM
phosphopeptide TDDEMpS-V-pYVAT
-
51% inhibition at 0.1 mM
pimecrolimus
protein phosphatase inhibitor II
-
specific inhibitor of isozyme PP1
-
Protein phosphatase inhibitor-1
-
protein phosphatase inhibitor-2
-
protein phosphatase-1 inhibitor-1
-
plays a role in cardiac physiology and pathophysiology, overview
-
protein phosphatase-1 inhibitor-3
-
a potent inhibitor of protein phosphatase-1 that selectively associates with PP1gamma1 and PP1alpha, but not the PP1beta isoform. It is a physiological substrate of caspase-3 harboring a putative caspase-3 cleavage site, 46DTVD49, located between the two PP1 interaction sites, which consist of a RVXF motif and an adjacent inhibitory domain, both of which are required for inhibition of PP1. Inh-3 mutant D49A is caspase-3 resistant
-
RCAN proteins
-
RCAN inhibition of CN phosphatase activity is mediated by the extreme C-terminal region
-
salubrinal
a small molecule drug that specifically inhibits translation by blocking the activity of elongation factor 2alpha (eIF2alpha) phosphatases, specifically CreP:PP1 and GADD34:PP1
sanguinarine
-
small t antigen
-
small t antigen of DNA tumor virus SV40 inhibits the phosphatase activity of the PP2A core enzyme
-
small t antigen of SV40 and polyomavirus
-
inhibits isozyme PP2A
-
small T antigen of SV40 virus
-
specifically inhibits PP2A holoenzymes with B55 or B56 regulatory subunits
-
Sodium fluoride
-
50 mM
Sodium vanadate
-
-
swine fever virus protein A238L
an African swine fever virus protein, inhibits the enzyme not by blocking its active site, but instead by binding to calcineurin substrate recognition grooves, which blocks calcineurin from binding and dephosphorylating its substrates. A238L binds calcineurin via both a PxIxIT sequence and an LxVP sequence, overview
-
tacrolimus
Tartrate
tautomycin
tetramisole
-
strong inhibition at 2 mM
Trifluorperazine
vanadate
-
at 1 mM inhibition to 60% of its activity
Zn2+
-
-
additional information
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
arachidonic acid
C2-ceramide
-
potent PP2A activator
Calmodulin
chlorogenic acid
-
PP2B but not PP1 is stimulated 4fold by 0.1 mM chlorogenic acid
docetaxel
-
docetaxel induces increase in activity of protein phosphatase 2 subgroups
ERK-2
association with ERK-2 results in catalytic activation of Pac-1
-
estrogen
-
estrogen maintains the function of PP1, PP2A, and calcineurin
heparin
-
causes dissociation to alpha1, beta1 and hence stimulation
HSP70
-
heat shock protein, activation of Ppp5 by dissociation from Hsp70
-
Hsp90
-
linoleic acid
-
increases PP2A expression rate
lipopolysaccharide
-
lipopolysaccharide stimulation induces the expression of PP4
nocodazole
-
causes loss of heat shock protein interaction and increases Ppp5 activity
nuclear inhibitor of protein phosphatase-1
-
NIPP1 directs PP1 to dephosphorylate the U2 small nuclear ribonucleoprotein particle component, spliceosome-associated protein 155, Sap155
-
paclitaxel
-
paclitaxel induces the increase in the activity of protein phosphatase 1
PTPase activator
-
PTPase activator acts like a chaperone directly affecting the activity of PP2Ac
-
RHOB GTPase
-
RAS-related small GTPase RHOB binds and activates the tumor suppressor PP2A, RHOB binds to the catalytic subunit of PP2A
-
TFIIF
-
a transcription factor that binds to the C-terminal domain
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00276
4-nitrophenyl phosphate
-
0.206
AAApTVA
at pH 7.5 and, temperature not specified in the publication
0.357
AGPALSPVPPV
at pH 7.5 and, temperature not specified in the publication
2.749
ALSAGpSNEYLR
at pH 7.5 and, temperature not specified in the publication
0.114
ASQEPpSPAASA
at pH 7.5 and, temperature not specified in the publication
0.072
DDApTVA
at pH 7.5 and, temperature not specified in the publication
0.113
ENDpTINASL
at pH 7.5 and, temperature not specified in the publication
0.036
ERK5
-
pH 7.5, 30°C, recombinant His-tagged Wip1 catalytic subunit
-
0.05
ESEMEpTPSAIN
at pH 7.5 and, temperature not specified in the publication
0.067
FLRT(P)SCG
-
-
0.71
FLRTS(P)CG
-
-
0.096
FLRTT(P)CG
-
-
0.026
HSAPPpSPEEKD
at pH 7.5 and, temperature not specified in the publication
0.023
NFEDHpSAPPSP
at pH 7.5 and, temperature not specified in the publication
0.065
NPCTEpTFTGTL
at pH 7.5 and, temperature not specified in the publication
3
p-nitrophenyl phosphate
-
-
0.0723
phosphohistone
-
-
-
0.098
PVARTpSPLQTP
at pH 7.5 and, temperature not specified in the publication
0.152
RAT(P)VA
-
-
0.656
RGRGSpSVGGGS
at pH 7.5 and, temperature not specified in the publication
1.354
RRApSVA
at pH 7.5 and, temperature not specified in the publication
0.058 - 1.954
RRApTVA
0.48
SQLHIpTPGTAY
at pH 7.5 and, temperature not specified in the publication
0.409
VARKLpSAREQR
at pH 7.5 and, temperature not specified in the publication
0.028
WHLADpSPAVNG
at pH 7.5 and, temperature not specified in the publication
0.237
YLRSIpSLPVPV
at pH 7.5 and, temperature not specified in the publication
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
13.8
4-nitrophenyl phosphate
-
1.05
AAApTVA
at pH 7.5 and, temperature not specified in the publication
1.31
AGPALpSPVPPV
at pH 7.5 and, temperature not specified in the publication
0.65
ALSAGpSNEYLR
at pH 7.5 and, temperature not specified in the publication
0.62
ASQEPpSPAASA
at pH 7.5 and, temperature not specified in the publication
1.3
DDApTVA
at pH 7.5 and, temperature not specified in the publication
1.2
ENDpTINASL
at pH 7.5 and, temperature not specified in the publication
2.4
ERK5
-
pH 7.5, 30°C, recombinant His-tagged Wip1 catalytic subunit
-
0.39
ESEMEpTPSAIN
at pH 7.5 and, temperature not specified in the publication
0.86
HSAPPpSPEEKD
at pH 7.5 and, temperature not specified in the publication
1.33
NFEDHpSAPPSP
at pH 7.5 and, temperature not specified in the publication
1.16
NPCTEpTFTGTL
at pH 7.5 and, temperature not specified in the publication
0.64
PVARTpSPLQTP
at pH 7.5 and, temperature not specified in the publication
0.03
RGRGSpSVGGGS
at pH 7.5 and, temperature not specified in the publication
0.93
RRApSVA
at pH 7.5 and, temperature not specified in the publication
0.605 - 170
RRApTVA
0.4
SQLHIpTPGTAY
at pH 7.5 and, temperature not specified in the publication
0.86
VARKLpSAREQR
at pH 7.5 and, temperature not specified in the publication
1.03
WHLADpSPAVNG
at pH 7.5 and, temperature not specified in the publication
0.48
YLRSIpSLPVPV
at pH 7.5 and, temperature not specified in the publication
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.452 - 0.532
4-nitrophenyl phosphate
5.2
AAApTVA
at pH 7.5 and, temperature not specified in the publication
3.3
AGPALpSPVPPV
at pH 7.5 and, temperature not specified in the publication
0.17
ALSAGSNEYLR
at pH 7.5 and, temperature not specified in the publication
5
ASQEPpSPAASA
at pH 7.5 and, temperature not specified in the publication
18
DDApTVA
at pH 7.5 and, temperature not specified in the publication
10.7
ENDpTINASL
at pH 7.5 and, temperature not specified in the publication
8.3
ESEMEpTPSAIN
at pH 7.5 and, temperature not specified in the publication
31.7
HSAPPpSPEEKD
at pH 7.5 and, temperature not specified in the publication
56.7
NFEDHpSAPPSP
at pH 7.5 and, temperature not specified in the publication
18.3
NPCTEpTFTGTL
at pH 7.5 and, temperature not specified in the publication
6.7
PVARTpSPLQTP
at pH 7.5 and, temperature not specified in the publication
0.03
RGRGSpSVGGGS
at pH 7.5 and, temperature not specified in the publication
0.7
RRApSVA
at pH 7.5 and, temperature not specified in the publication
0.3
RRApTVA
at pH 7.5 and, temperature not specified in the publication
0.8
SQLHIpTPGTAY
at pH 7.5 and, temperature not specified in the publication
2.17
VARKLpSAREQR
at pH 7.5 and, temperature not specified in the publication
36.7
WHLADpSPAVNG
at pH 7.5 and, temperature not specified in the publication
2
YLRSIpSLPVPV
at pH 7.5 and, temperature not specified in the publication
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0038
6-(3,4-dichloro-phenyl)-4-(N,N-dimethylaminoethylthio)-2-phenyl-pyrimidine
-
-
0.0074
cyclic phosphopeptide c(MpSIpY)
-
at 30°C and pH 7.5
0.0029
cyclic phosphopeptide c(MpSIpYV)
-
at 30°C and pH 7.5
0.0009
cyclic phosphopeptide c(MpSIpYVA)
-
at 30°C and pH 7.5
0.0252
cyclic phosphopeptide c(MpSIpYVAT)
-
at 30°CC and pH 7.5
0.035
cyclic phosphopeptide c(TDDEMpSIpYVAT)
-
at 30°C and pH 7.5
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0165
c(M-L-2-amino-4-phosphono-4,4-difluorobutanoate-IpYVA)
Homo sapiens
-
at 30°C and pH 7.5
0.0294
cyclic phosphopeptide c(MpSIpY)
Homo sapiens
-
at 30?C and pH 7.5
0.0116
cyclic phosphopeptide c(MpSIpYV)
Homo sapiens
-
at 30°C and pH 7.5
0.0037
cyclic phosphopeptide c(MpSIpYVA)
Homo sapiens
-
at 30°C and pH 7.5
0.0999
cyclic phosphopeptide c(MpSIpYVAT)
Homo sapiens
-
at 30°C and pH 7.5
0.1384
cyclic phosphopeptide c(TDDEMpSIpYVAT)
Homo sapiens
-
at 30°C and pH 7.5
0.000002 - 0.0000027
cyclosporin A
Homo sapiens
-
in fibroblasts
0.00000041
dinophysistoxin-2
Homo sapiens
at pH 8.1 and 30°C
0.00000175
neurabin-I
Homo sapiens
-
IC50 for the wild-type catalytic subunit PP1alpha is 1.75 nM
-
0.0000001 - 0.005
okadaic acid
0.000006 - 0.0000201
pimecrolimus
Homo sapiens
-
in fibroblasts
0.000025
Protein phosphatase inhibitor-1
Homo sapiens
-
i.e. I-1, specific inhibition of PP1, contains a consensus RVxF motif sequence, IC50 for the wild-type catalytic subunit PP1alpha is 25 nM
-
0.000002
protein phosphatase inhibitor-2
Homo sapiens
-
i.e. I-2, specific inhibition of PP1, contains a consensus RVxF motif sequence, IC50 for the wild-type catalytic subunit PP1alpha is 2 nM
-
0.0002
small t antigen
Homo sapiens
-
using phosphorylase a as a substrate
-
0.0000004 - 0.0000013
tacrolimus
Homo sapiens
-
in fibroblasts
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.0000008 - 0.0000017
-
T-cells from females and males, not stimulated and T-cell-stimulated
0.0038 - 0.0077
-
keratinoyctes
0.0085 - 0.0127
-
fibroblasts
0.5
-
with phosphorylase kinase as substrate
0.659
-
subunit CNAa-PP1-loop, crude cell lysate
0.665
-
subunit PP1-CNAa-loop, crude cell lysate
10.77
-
subunit PP1-CNAa-loop, after 16.2fold purification
11
-
with p-nitrophenyl phosphate as substrate
14
-
with p-nitrophenyl phosphate as substrate
16
-
with p-nitrophenyl phosphate as substrate
19
-
with p-nitrophenyl phosphate as substrate
2
-
with phosphorylase kinase as substrate
3
-
with phosphorylase kinase as substrate
3 - 8
-
with p-nitrophenylphosphate as substrate
310
-
with p-nitrophenyl phosphate as substrate
4
-
with phosphorylase kinase as substrate
40
-
with p-nitrophenyl phosphate as substrate
7.087
-
subunit CNAa-PP1-loop, after 10.8fold purification
8
-
with phosphorylase kinase as substrate
94
purified enzyme, at pH 8.1 and 30°C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10
-
with Mg2+ as activator
7.2
-
assay at
7.4
-
assay at
7.5 - 8
-
with Mg2+ as activator
7.5 - 8.5
-
with Mn2+ as activator
7.6
-
assay at
8
-
assay at
8 - 8.5
-
phosphatase PP2Calpha
additional information
-
biphasic pH-optimum at pH 7.5 and 8.5 with Mn2+ as activator
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at
23 - 30
-
assay at
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
mitochondrial precursor
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
Aalpha subunit is expressed at high levels
Manually annotated by BRENDA team
-
the enzyme activity is increased in long-term hypoxia
Manually annotated by BRENDA team
-
Pro33-isozyme positive platelets show increased MLC and ERK phosphorylation and reduced protein phosphatase activity, and vice versa in Pro33-isozyme negative platelets, overview
Manually annotated by BRENDA team
-
elevated levels of PP5 protein occur in human breast cancer and suggest that PP5 over-expression may aid tumor progression
Manually annotated by BRENDA team
-
Aalpha subunit is expressed at high levels
Manually annotated by BRENDA team
-
airway epithelial cell line
Manually annotated by BRENDA team
-
Aalpha subunit is expressed at high levels
Manually annotated by BRENDA team
-
Aalpha subunit is expressed at high levels
Manually annotated by BRENDA team
-
Aalpha subunit is expressed at high levels
Manually annotated by BRENDA team
-
Aalpha subunit is expressed at high levels
Manually annotated by BRENDA team
-
the enzyme activity is increased in long-term hypoxia
Manually annotated by BRENDA team
-
PP2A is localized in the cell-cell adhesion sites between adjacent cells and associated with E-cadherin-cateinins complex in healthy human mammary epithelial HME cells
Manually annotated by BRENDA team
-
bone marrow stromal fibroblast cell line
Manually annotated by BRENDA team
-
selected from A2058 cell line
Manually annotated by BRENDA team
low expression level
Manually annotated by BRENDA team
-
Aalpha subunit is expressed at high levels
Manually annotated by BRENDA team
-
Aalpha subunit is expressed at high levels
Manually annotated by BRENDA team
-
Aalpha subunit is expressed at high levels
Manually annotated by BRENDA team
-
prostate cancer cell line
Manually annotated by BRENDA team
-
Aalpha subunit is expressed at high levels
Manually annotated by BRENDA team
-
Aalpha subunit is expressed at high levels
Manually annotated by BRENDA team
-
PTP-1B
Manually annotated by BRENDA team
-
epithelium
Manually annotated by BRENDA team
umbilical cord derived mast cell
Manually annotated by BRENDA team
-
a T-cell lymphoblastic leukemia cell line
Manually annotated by BRENDA team
-
Aalpha subunit is expressed at high levels
Manually annotated by BRENDA team
-
Aalpha subunit is expressed at high levels
Manually annotated by BRENDA team
MKP-8 is highly expressed in neuroblastoma
Manually annotated by BRENDA team
MKP-8 is highly expressed in neuroepithelioma
Manually annotated by BRENDA team
-
prostate cancer cell line
Manually annotated by BRENDA team
low enzyme expression level
Manually annotated by BRENDA team
-
Aalpha subunit is expressed at high levels, Abeta subunit is expressed at different levels
Manually annotated by BRENDA team
-
Aalpha subunit is expressed at high levels
Manually annotated by BRENDA team
-
Aalpha subunit is expressed at high levels
Manually annotated by BRENDA team
-
isozyme PP1delta
Manually annotated by BRENDA team
-
Aalpha subunit is expressed at high levels
Manually annotated by BRENDA team
-
Aalpha subunit is expressed at high levels
Manually annotated by BRENDA team
-
Aalpha subunit is expressed at high levels
Manually annotated by BRENDA team
-
Aalpha subunit is expressed at high levels
Manually annotated by BRENDA team
low enzyme expression level
Manually annotated by BRENDA team
-
Aalpha subunit is expressed at high levels
Manually annotated by BRENDA team
-
Aalpha subunit is expressed at high levels
Manually annotated by BRENDA team
-
Aalpha subunit is expressed at high levels
Manually annotated by BRENDA team
-
Aalpha subunit is expressed at high levels
Manually annotated by BRENDA team
-
Aalpha subunit is expressed at high levels
Manually annotated by BRENDA team
-
established from a primary cutaneous melanoma of radial growth phase
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
among the PP1 isoforms, PP1beta appears to be preferentially targeted to the myofilaments
Manually annotated by BRENDA team
additional information
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
PPM1K_HUMAN
372
0
40997
Swiss-Prot
Mitochondrion (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
46000
from sequence of cDNA calculated molecular weight is about 46000 kDa
66000
Trx-His-tagged recombinant enzyme
103000 - 109000
130000
-
x * 45000-50000 + x * 130000, recombinant Ppp5, SDS-PAGE
150000
-
gel filtration
155000
-
PP2A holoenzyme, X-ray crystallography
165000
-
gel filtration
170000
-
phosphatase PP2A, gel filtration
177000 - 180000
250000
-
gel filtration
28000
-
phosphatase KAP, gel filtration, SDS-PAGE
32000
34000
-
phosphatase 2A, 1 * 72000 + 1 * 63000 + 1 * 34000, SDS-PAGE
35000
36000
37000
-
protein phosphatase 1, SDS-PAGE
38500
x * 38500, calculated from amino acid sequence
440000
-
the PP6 catalytic subunit, SAPS domain subunits PP6R1 and PP6R3, and ankyrin repeat subunit ARS-A are all detected by immunoblotting, showing copurification in complexes with apparent Mr values of above 440 kDa
49000
-
gel filtration
55000
-
phosphatase PP2A, A: 1 * 63000, B: 1 * 55000, C: 1 * 60000-63000, i.e. catalytic subunit, SDS-PAGE
57000
-
1 * 57000, with fused TPR domain
60000
600000
light scattering
61000
-
recombinant catalytic subunit of calcineurin, SDS-PAGE
63000
65000
72000
-
phosphatase 2A, 1 * 72000 + 1 * 63000 + 1 * 34000, SDS-PAGE
75000
-
phosphatase PP7, calculation from amino acid sequence, SDS-PAGE
76000
-
x * 76000
90000
-
gel filtration
additional information
-
conversion of most large forms to small forms of 30000 by treatment with ethanol and freezing/thawing
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
heterodimer
heterotrimer
monomer
trimer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
methylation
-
-
phosphoprotein
proteolytic modification
-
-
side-chain modification
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method with 0.2 M MgCl2, 4.5% PEG 10000 (w/v) and 0.1 M HEPES (pH 7.5)
-
hanging drop vapour diffusion method, using 7-10% (w/v) PEG35000 and 0.1-0.15 M sodium citrate (pH 5.5)
-
in complex with nodularin-R and tautomycin, PP1:nodularin-R is crystallized in 20% (w/v) PEG 3350, 0.2 M NaI. PP1:tautomycin is crystallized in 0.1 M Tris pH 8.0, 30% (w/v) PEG 6K, 1M LiCl
phosphatase KAP
-
purified recombinant enzyme, under-oil-batch method, 21 mg/ml protein in solution is mixed with an eqal volume of crystallization buffer containing 10% w/v PEG 6000, 4% 2-methyl-2,4-pentanediol, 0.1 M Na-HEPES, pH 8.5, 3 mM DTT, under silicon oil at 14°C, cryoprotection buffer contains 13% w/v PEG 6000, 18% 2-methyl-2,4-pentanediol, 0.075 M NaHEPES, pH 8.5, X-ray diffraction structure determination and analysis at 2.9 A resolution, molecular replacement, modeling
-
purified recombinant His-tagged PP5 catalytic domain, hanging drop vapour diffusion method, 22°C, 20 mg/ml protein in 40 mM Tris, pH 7.5, is mixed with an equal volume of reservoir solution containing 45-60% 2-methyl-2,4-pentanediol, X-ray diffraction structure determination and analysis at 1.6 A resolution
single anomalous dispersion method
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C291R
-
site-directed mutagenesis, mutation of a hydrophobic surface pocket residue of subunit PP1alpha, the mutant shows reduced activity and impaired binding to protein phosphatase inhibitor-1 and protein phosphatase inhibitor-2, as well as to the neuronal regulatory subunit neurabin-I, and GM, the skeletal muscle glycogen-targeting subunit
D197K
-
the Balpha mutant shows impaired ability to facilitate the dephosphorylation of phosphorylated Tau
D88N
-
reduction of specific activity in vitro, no function in vivo
E27R
-
the Balpha mutant shows impaired ability to facilitate the dephosphorylation of phosphorylated Tau
E42A
-
site-directed mutagenesis, the mutant shows only slightly reduced sensitivity to inhibition by Inhibitor-3 compared to the wild-type enzyme
E42C
-
site-directed mutagenesis, the mutant shows only slightly reduced sensitivity to inhibition by Inhibitor-3 compared to the wild-type enzyme
E42T
-
site-directed mutagenesis, the mutant shows only slightly reduced sensitivity to inhibition by Inhibitor-3 compared to the wild-type enzyme
H118N
-
reduction of specific activity in vitro, no function in vivo
K238D
-
not inhibited by c(MpSIpYVA)
K238Q
-
not inhibited by c(MpSIpYVA)
K345E
K48E
-
the Balpha mutant shows impaired ability to facilitate the dephosphorylation of phosphorylated Tau
L289R
-
site-directed mutagenesis, mutation of a hydrophobic surface pocket residue of subunit PP1alpha, the mutant shows reduced activity and reduced sensitivity to protein phosphatase inhibitor-1 and protein phosphatase inhibitor-2, as well as to the neuronal regulatory subunit neurabin-I, and GM, the skeletal muscle glycogen-targeting subunit
M290K
-
site-directed mutagenesis, mutation of a hydrophobic surface pocket residue of subunit PP1alpha, the mutant shows reduced activity and reduced sensitivity to protein phosphatase inhibitor-1 and protein phosphatase inhibitor-2, as well as to the neuronal regulatory subunit neurabin-I, and GM, the skeletal muscle glycogen-targeting subunit
R110E
-
inhibited by c(MpSIpYVA) similar to the wild type enzyme
S19A
site-directed mutagenesis, mutant PTPN12-S19A is efficient in inhibiting EGF-induced cell migration, the mutant does not produce significant differences in PTPN12's recognition of all HER2-phospho-peptides compared to wild-type PTPN12
S19E
site-directed mutagenesis, mutant PTPN12-S19E is less efficient in inhibiting EGF-induced cell migration, the mutant does not produce significant differences in PTPN12's recognition of all HER2-phospho-peptides compared to wild-type PTPN12
S39E
site-directed mutagenesis, the mutant impairs activity of PTPN12 toward all HER2-phosphopeptide by 2-3fold compared to wild-type, mutation S39E decreases the activity of PTPN12 toward all tested HER2 pY sites in vitro, the mutation directly affected the interaction between the PTPN12 and the residues flanking the pY of the HER2 phosphorylation sites
V41D
-
site-directed mutagenesis, the mutant shows unaltered sensitivity to inhibition by Inhibitor-3 compared to the wild-type enzyme
W43A
-
site-directed mutagenesis, the mutant shows unaltered sensitivity to inhibition by Inhibitor-3 compared to the wild-type enzyme
W58A/D59A
the mutant shows markedly reduced activity compared to the wild type enzyme
W58A/D59A/W62A/D63A
the mutant shows markedly reduced activity compared to the wild type enzyme
W62A/D63A
the mutant shows markedly reduced activity compared to the wild type enzyme
Y451A
okadaic acid insensitive mutant of PP5
additional information
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ethanol
-
inhibits the enzyme at 2-5% v/v, no inactivation at 1% ethanol after 10 min
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, Tris at pH 7.2 and 0.05% (w/v) sodium azide, 2 months, no loss of activity
-80°C, 20 mM Tris-HCl, pH 7.4, 1 mM EDTA, 10% glycerol
-
-80°C, 25 mM Tris-HCl, pH 7.4, 1 mM dithiothreitol, 1 mM EDTA, 50% glycerol, recombinant alpha subunit of PP2A
-
-80°C, 50 mM Tris-HCl buffer, pH 7.4, 1 mM EDTA, 0.5 mM dithiothreitol, 0.03 M NaCl, 10% glycerol, protease inhibitor, at least 1 month
-
4-22°C, Tris-HCl and 0.05% (w/v) sodium azide, 1 month, 90% loss of activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Ni-NTA agarose column chromatography
ammonium sulfate precipitation, phenyl Sepharose column chromatography, and Q Sepharose column chromatography
-
glutathione affinity column chromatography, Source 15Q column chromatography, and Superdex 200 gel filtration
-
glutathione Sepharose column chromatography
-
immunopurification through the Xpress tag
-
microcystin-Sepharose bead chromatography and Ni-NTA bead chromatography
-
Ni-NTA column chromatography, Mono Q column chromatography, and Superdex 75 gel filtration
nickel affinity column chromatography
partial purification by DEAE column chromatography and Superose 12 gel filtration
-
phosphatase KAP
-
phosphatases I, II, III, all type 2A
-
protein A Sepharose beads chromatography
-
recombinant alpha subunit of PP2A
-
recombinant FLAG-tagged and/or HA-tagged Ppp5 from HEK-293 cells
-
recombinant FLAG-tagged PP2A subunits from HEK-293T cells by anti-FLAG immunoaffinity chromatography
-
recombinant FLAG-tagged PP4 from HEK-293T cells by anti-FLAG immunoaffinity chromatography, co-purifies with the insulin receptor substrate-4
-
recombinant His-tagged PP5 catalytic domain maltose-binding protein fusion protein from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, after cleavage of the fusion protein the His-tagged enzyme is further purified by anion exchange chromatography
recombinant N-terminally His-tagged wild-type and mutant Wip1 catalytic subunits from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant PP2Calpha
-
recombinant Ppp5 from Escherichia coli strain B834 by cation exchange, hydrophobic interaction, and nickel affinity chromatography and gel filtration
-
recombinant subunits
-
recombinant wild-type and mutant GST-tagged enzymes from Escherichia coli by glutathione affinity chromatography
recombinant wild-type and mutant PP1alpha subunits from Escherichia coli strain BL21 performing multiple chromatographic steps including affinity chromatography on MLCR- and heparin-resins
-
recombinant wild-type and mutant PPIalpha from Escherichia coli to near homogeneity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli strain BL21
5'-UTR sequence, analysis of PP5 promoter sequence and activity
-
alpha form of PP2A expressed in Sf9 cells
-
co-overexpression of HA-tagged PP2A catalytic subunit and regulatory subunit B56alpha, with c-Myc in HEK-293 cells, overview
-
expressed in baculovirus-infected insect cells and in Escherichia coli
-
expressed in bone marrow-derived murine megakaryocytes and HEK-293 cells
-
expressed in Escherichia coli
expressed in Escherichia coli BL21 (DE3) cells with the GroEL-ES chaperone
expressed in Escherichia coli BL21 cells and hippocampal neurons of Rattus norvegicus
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli strain DH5alpha
-
expressed in Escherichia coli strains BL21(lDE3) and DH5alpha
-
expressed in fetoplacental artery endothelial cells
-
expressed in HEK-293T cells and RAW264.7 cells
-
expressed in HEK-293T cells, PP4c over-expressing cells are consistently more sensitive to UV-, cisplatin-, butyrate- and okadaic acid-induced cell death
-
expressed in HeLa and HEK-293 cells
-
expressed in insect cells
-
expressed in MDBK cells
-
expressed in Mus musculus
-
expressed in U2OS cells
-
expression in human 293 cells
-
expression in human HEK-293 cells
-
expression of FLAG-tagged PP4 in HEK-293T cells
-
expression of FLAG-tagged Ppp5 in HEK-293 cells
-
expression of N-terminally His-tagged wild-type and mutant Wip1 catalytic subunits in Escherichia coli strain BL21(DE3)
-
expression of Ppp5 in Escherichia coli strain B834
-
expression of wild-type and mutant PP1alpha subunits in Escherichia coli strain BL21
-
expression of wild-type and mutant PPIalpha in Escherichia coli
-
fusion of a C-terminal truncated PTEN (amino acids 1-378) to Mycobacterium xenopi GyrA intein, and chitin-binding domain
gene PP2C epsilon, DNA and amino acid sequence determination and analysis, mapping to chromosome 3q26.1
gene PTPN12, recombinant expression of wild-type and mutant GST-tagged enzymes in Escherichia coli
in vitro transcription and translation in rabbit reticulocyte extract or expression in Escherichia coli strain BL21 of PP2A subunits
-
isozyme PP2C epsilon, cDNA library construction, DNA and amino acid sequence determination and analysis, mapping to chromosome 3q26.1, expression in Escherichia coli strain DH5alpha
isozyme PPP3R2, DNA and amino acid sequence determination and analysis, chromosome mapping to 9q22
overexpression in insect cells with the baculovirus system
-
overexpression in Pichia pastoris KM71 and G115
-
phosphatase KAP
-
phosphatase PP2Calpha expressed in Escherichia coli
-
phosphatase PP7 expressed in SF21 insect cells
-
PP2A, DNA and amino acid sequence determination and analysis, expression of the N-terminal Ca2+/calmodulin-binding activation domain of Rattus norvegicus adenylate cyclase and the catalytic subunits of human PP2A in a yeast two-hybrid system
-
PPM1F, expression as GST-tagged enzyme, expression as HA-tagged or Myc-tagged enzyme in CHO-K1 cells
-
tetracycline-inducible, stable overexpression of FLAG-tagged PP2A subunits in HEK-293T cells
-
the catalytic subunit alpha of protein phosphatase 2A is expressed in Trichoplusia ni insect larvae
the catalytic subunit of calcineurin is expressed in Escherichia coli BL21 cells
-
the PP5 catalytic domain comprising residues 169-499 is expressed as His-tagged maltose-binding protein fusion protein containing a tobacco etch virus cleavage site in Escherichia coli strain BL21(DE3)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
both expression and activity of calcineurin A subunit are increased in paroxysmal atrial fibrillation and chronic atrial fibrillation patients
highly expressed in several human cancers (in 87.5% of primary hepatocellular carcinomas, 84% of primary lung cancers, and 81.8% of primary breast cancers)
-
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
reconstitution of PP2A from isolated subunits Aalpha, B and C
-
reconstitution of PP2A holoenzymes with recombinant subunits, overview
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
-
assembly of a biosensor system involving protein phosphatase-2A and glycogen phosphorylase a activities, method optimization, overview
diagnostics
drug development
calcineurin is the principal target of the immunosuppressive drugs, cyclosporin A and FK506/Tacrolimus, the binding of which physically prevents the recruitment of macromolecular substrates to the active site
medicine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Takeda, M.; Usui, H.; Imazu, M.; Imanoka, T.; Kinohara, N.; Tsukamoto, H.; Maeta, K.
The interaction and function of subunits in protein phosphatase 2A from pig heart and human erythrocyte
Adv. Protein Phosphatases
1
215-233
1985
Homo sapiens, Sus scrofa
-
Manually annotated by BRENDA team
Usui, H.; Imazu, M.; Maeta, K.; Tsukamoto, H.; Azuma, K.; Takeda, M.
Three distinct forms of type 2A protein phosphatase in human erythrocyte cytosol
J. Biol. Chem.
263
3752-3761
1988
Homo sapiens
Manually annotated by BRENDA team
Kamibayashi, C.; Lickteig, R.L.; Estes, R.; Walter, G.; Mumby, M.C.
Expression of a subunit of protein phosphatase 2A and characterization of its interaction with the catalytic and regulatory subunits
J. Biol. Chem.
267
21864-21872
1992
Homo sapiens
Manually annotated by BRENDA team
Marley, A.E.; Sullivan, J.E.; Carling, D.; Abbott, W.M.; Smith, G.J.; Taylor, I.W.F.; Carey, F.; Beri, R.K.
Biochemical characterization and deletion analysis of recombinant human protein phosphatase 2C
Biochem. J.
320
801-806
1996
Homo sapiens
-
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Huang, X.; Honkanen, R.E.
Molecular cloning, expression, and characterization of a novel human serine/threonine protein phosphatase PP7, that is homologous to Drosophila retinal degeneration C gene product (rdgC)
J. Biol. Chem.
273
1462-1468
1998
Homo sapiens
Manually annotated by BRENDA team
Hanlon, N.; Barford, D.
Purification and crystallization of the CDL-associated protein phosphatase KAP expressed in Escherichia coli
Protein Sci.
7
508-511
1998
Homo sapiens
Manually annotated by BRENDA team
Das, A.K.; Helps, N.R.; Cohen, P.T.; Barford, D.
Crystal structure of the protein serine/threonine phosphatase 2C at 2.0 A resolution
EMBO J.
15
6798-6809
1996
Homo sapiens
Manually annotated by BRENDA team
Barford, D.; Keller, J.C.; Flint, A.J.; Tonks, N.K.
Purification and crystallization of the catalytic domain of human protein tyrosine phosphatase 1B expressed in Escherichia coli
J. Mol. Biol.
239
726-730
1994
Homo sapiens
Manually annotated by BRENDA team
Fan, G.Y.; Maldonado, F.; Zhang, Y.; Kincaid, R.; Ellisman, M.H.; Gastinel, L.N.
In vivo calcineurin crystals formed using the baculovirus expression system
Microsc. Res. Tech.
34
77-86
1996
Homo sapiens, Neurospora crassa
Manually annotated by BRENDA team
Zhao, R.; Qi, Y.; Zhao, Z.J.
FYVE-DSP1, a dual-specificity protein phosphatase containing an FYVE domain
Biochem. Biophys. Res. Commun.
270
222-229
2000
Homo sapiens
Manually annotated by BRENDA team
Janssens, V.; Goris, J.
Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signaling
Biochem. J.
353
417-439
2001
Homo sapiens
Manually annotated by BRENDA team
Myles, T.; Schmidt, K.; Evans, D.R.H.; Cron, P.; Hemmings, B.A.
Active-site mutations impairing the catalytic function of the catalytic subunit of human protein phosphatase 2A permit baculovirus-mediated overexpression in insect cells
Biochem. J.
357
225-232
2001
Homo sapiens
Manually annotated by BRENDA team
Zhou, J.; Pham, H.T.; Ruediger, R.; Walter, G.
Characterization of the Aalpha and Abeta subunit isoforms of protein phosphatase 2A: differences in expression, subunit interaction, and evolution
Biochem. J.
369
387-398
2003
Homo sapiens
Manually annotated by BRENDA team
Swiatek, W.; Sugajska, E.; Lankiewicz, L.; Hemmings, B.A.; Zolnierowicz, S.
Biochemical characterization of recombinant subunits of type 2A protein phosphatase overexpressed in Pichia pastoris
Eur. J. Biochem.
267
5209-5216
2000
Oryctolagus cuniculus, Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Douglas, P.; Moorhead, G.B.G.; Ye, R.; Lees-Miller, S.P.
Protein phosphatases regulate DNA-dependent protein kinase activity
J. Biol. Chem.
276
18992-18998
2001
Homo sapiens
Manually annotated by BRENDA team
Hallaway, B.J.; O'Kane, D.J.
Chemiluminescence assay of serum alkaline phosphatase and phosphoprotein phosphatases
Methods Enzymol.
305
391-401
2000
Homo sapiens
Manually annotated by BRENDA team
Cheng, L.Y.; Wang, J.Z.; Gong, C.X.; Pei, J.J.; Zaidi, T.; Grundke-Iqbal, I.; Iqbal, K.
Multiple forms of phosphatase from human brain: isolation and partial characterization of affi-gel blue nonbinding phosphatase activities
Neurochem. Res.
26
425-438
2001
Homo sapiens
Manually annotated by BRENDA team
Cohen, P.T.W
Overview of protein serine/threonine phosphatases
Topics in Current Genetics (Arino, J. , Alexander, D. R. Eds. ) Springer
5
1-20
2004
Homo sapiens
-
Manually annotated by BRENDA team
Zeke, T.; Morrice, N.; Vazquez-Martin, C.; Cohen, P.T.
Human protein phosphatase 5 dissociates from heat-shock proteins and is proteolytically activated in response to arachidonic acid and the microtubule-depolymerizing drug nocodazole
Biochem. J.
385
45-56
2005
Homo sapiens
Manually annotated by BRENDA team
Yamaguchi, H.; Minopoli, G.; Demidov, O.N.; Chatterjee, D.K.; Anderson, C.W.; Durell, S.R.; Appella, E.
Substrate specificity of the human protein phosphatase 2Cdelta, Wip1
Biochemistry
44
5285-5294
2005
Homo sapiens
Manually annotated by BRENDA team
Inostroza, J.; Saenz, L.; Calaf, G.; Cabello, G.; Parra, E.
Role of the phosphatase PP4 in the activation of JNK-1 in prostate carcinoma cell lines PC-3 and LNCaP resulting in increased AP-1 and EGR-1 activity
Biol. Res.
38
163-178
2005
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Yang, J.; Roe, S.M.; Cliff, M.J.; Williams, M.A.; Ladbury, J.E.; Cohen, P.T.; Barford, D.
Molecular basis for TPR domain-mediated regulation of protein phosphatase 5
EMBO J.
24
1-10
2005
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Cohen, P.T.; Philp, A.; Vazquez-Martin, C.
Protein phosphatase 4 - from obscurity to vital functions
FEBS Lett.
579
3278-3286
2005
Arabidopsis thaliana, Saccharomyces cerevisiae, Caenorhabditis elegans, Drosophila melanogaster, Homo sapiens
Manually annotated by BRENDA team
Zhang, X.; Ozawa, Y.; Lee, H.; Wen, Y.D.; Tan, T.H.; Wadzinski, B.E.; Seto, E.
Histone deacetylase 3 (HDAC3) activity is regulated by interaction with protein serine/threonine phosphatase 4
Genes Dev.
19
827-839
2005
Homo sapiens
Manually annotated by BRENDA team
Harvey, B.P.; Banga, S.S.; Ozer, H.L.
Regulation of the multifunctional Ca2+/calmodulin-dependent protein kinase II by the PP2C phosphatase PPM1F in fibroblasts
J. Biol. Chem.
279
24889-24898
2004
Homo sapiens
Manually annotated by BRENDA team
Anderson, K.A.; Noeldner, P.K.; Reece, K.; Wadzinski, B.E.; Means, A.R.
Regulation and function of the calcium/calmodulin-dependent protein kinase IV/protein serine/threonine phosphatase 2A signaling complex
J. Biol. Chem.
279
31708-31716
2004
Homo sapiens
Manually annotated by BRENDA team
Swingle, M.R.; Honkanen, R.E.; Ciszak, E.M.
Structural basis for the catalytic activity of human serine/threonine protein phosphatase-5
J. Biol. Chem.
279
33992-33999
2004
Homo sapiens (P36873), Homo sapiens
Manually annotated by BRENDA team
Mihindukulasuriya, K.A.; Zhou, G.; Qin, J.; Tan, T.H.
Protein phosphatase 4 interacts with and down-regulates insulin receptor substrate 4 following tumor necrosis factor-alpha stimulation
J. Biol. Chem.
279
46588-46594
2004
Homo sapiens
Manually annotated by BRENDA team
Zhou, G.; Golden, T.; Aragon, I.V.; Honkanen, R.E.
Ser/Thr protein phosphatase 5 inactivates hypoxia-induced activation of an apoptosis signal-regulating kinase 1/MKK-4/JNK signaling cascade
J. Biol. Chem.
279
46595-46605
2004
Homo sapiens
Manually annotated by BRENDA team
Gibbons, J.A.; Weiser, D.C.; Shenolikar, S.
Importance of a surface hydrophobic pocket on protein phosphatase-1 catalytic subunit in recognizing cellular regulators
J. Biol. Chem.
280
15903-15911
2005
Homo sapiens
Manually annotated by BRENDA team
Vijayan, K.V.; Liu, Y.; Sun, W.; Ito, M.; Bray, P.F.
The Pro33 isoform of integrin beta3 enhances outside-in signaling in human platelets by regulating the activation of serine/threonine phosphatases
J. Biol. Chem.
280
21756-21762
2005
Homo sapiens
Manually annotated by BRENDA team
Thelin, W.R.; Kesimer, M.; Tarran, R.; Kreda, S.M.; Grubb, B.R.; Sheehan, J.K.; Stutts, M.J.; Milgram, S.L.
The cystic fibrosis transmembrane conductance regulator is regulated by a direct interaction with the protein phosphatase 2A
J. Biol. Chem.
280
41512-41520
2005
Homo sapiens
Manually annotated by BRENDA team
Adams, D.G.; Coffee, R.L., Jr.; Zhang, H.; Pelech, S.; Strack, S.; Wadzinski, B.E.
Positive regulation of Raf1-MEK1/2-ERK1/2 signaling by protein serine/threonine phosphatase 2A holoenzymes
J. Biol. Chem.
280
42644-42654
2005
Homo sapiens
Manually annotated by BRENDA team
Takahashi, K.; Nakajima, E.; Suzuki, K.
Involvement of protein phosphatase 2A in the maintenance of E-cadherin-mediated cell-cell adhesion through recruitment of IQGAP1
J. Cell. Physiol.
206
814-820
2006
Homo sapiens
Manually annotated by BRENDA team
Jin, F.; Ji, C.; Liu, L.; Dai, J.; Gu, S.; Sun, X.; Xie, Y.; Mao, Y.
Molecular cloning and characterization of a novel human protein phosphatase 2C cDNA (PP2C epsilon)
Mol. Biol. Rep.
31
197-202
2004
Homo sapiens (Q5SGD2), Homo sapiens
Manually annotated by BRENDA team
Liu, L.; Zhang, J.; Yuan, J.; Dang, Y.; Yang, C.; Chen, X.; Xu, J.; Yu, L.
Characterization of a human regulatory subunit of protein phosphatase 3 gene (PPP3RL) expressed specifically in testis
Mol. Biol. Rep.
32
41-45
2005
Homo sapiens (Q96LZ3), Homo sapiens
Manually annotated by BRENDA team
Arnold, H.K.; Sears, R.C.
Protein phosphatase 2A regulatory subunit B56alpha associates with c-myc and negatively regulates c-myc accumulation
Mol. Cell. Biol.
26
2832-2844
2006
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Chung, H.Y.; Cha, B.; Kim, H.
Inhibition of serine-threonine protein phosphatases in monocyte chemoattractant protein-1 expression in Helicobacter pylori-stimulated gastric epithelial cells
Ann. N. Y. Acad. Sci.
1095
220-227
2007
Homo sapiens
Manually annotated by BRENDA team
Escargueil, A.E.; Larsen, A.K.
Mitosis-specific MPM-2 phosphorylation of DNA topoisomerase IIalpha is regulated directly by protein phosphatase 2A
Biochem. J.
403
235-242
2007
Homo sapiens
Manually annotated by BRENDA team
Karlsson, M.; Mandl, M.; Keyse, S.M.
Spatio-temporal regulation of mitogen-activated protein kinase (MAPK) signalling by protein phosphatases
Biochem. Soc. Trans.
34
842-845
2006
Homo sapiens
Manually annotated by BRENDA team
Codreanu, S.G.; Adams, D.G.; Dawson, E.S.; Wadzinski, B.E.; Liebler, D.C.
Inhibition of protein phosphatase 2A activity by selective electrophile alkylation damage
Biochemistry
45
10020-10029
2006
Homo sapiens
Manually annotated by BRENDA team
Yamaguchi, H.; Durell, S.R.; Feng, H.; Bai, Y.; Anderson, C.W.; Appella, E.
Development of a substrate-based cyclic phosphopeptide inhibitor of protein phosphatase 2Cdelta, Wip1
Biochemistry
45
13193-13202
2006
Homo sapiens
Manually annotated by BRENDA team
Xie, X.J.; Xue, C.Z.; Huang, W.; Yu, D.Y.; Wei, Q.
The beta12-beta13 loop is a key regulatory element for the activity and properties of the catalytic domain of protein phosphatase 1 and 2B
Biol. Chem.
387
1461-1467
2006
Homo sapiens
Manually annotated by BRENDA team
Kochinyan, S.; Sun, L.; Ghosh, I.; Barshevsky, T.; Xu, J.; Xu, M.Q.
Use of intein-mediated phosphoprotein arrays to study substrate specificity of protein phosphatases
Biotechniques
42
63-69
2007
Oryctolagus cuniculus, Homo sapiens
Manually annotated by BRENDA team
Miglietta, A.; Bozzo, F.; Gabriel, L.; Bocca, C.; Canuto, R.A.
Extracellular signal-regulated kinase 1/2 and protein phosphatase 2A are involved in the antiproliferative activity of conjugated linoleic acid in MCF-7 cells
Br. J. Nutr.
96
22-27
2006
Homo sapiens
Manually annotated by BRENDA team
Bos, C.L.; Diks, S.H.; Hardwick, J.C.; Walburg, K.V.; Peppelenbosch, M.P.; Richel, D.J.
Protein phosphatase 2A is required for mesalazine-dependent inhibition of Wnt/beta-catenin pathway activity
Carcinogenesis
27
2371-2382
2006
Homo sapiens
Manually annotated by BRENDA team
Avci, C.B.; Sahin, F.; Gunduz, C.; Selvi, N.; Aydin, H.H.; Oktem, G.; Topcuoglu, N.; Saydam, G.
Protein phosphatase 2A (PP2A) has a potential role in CAPE-induced apoptosis of CCRF-CEM cells via effecting human telomerase reverse transcriptase activity
Hematology
12
519-525
2007
Homo sapiens
Manually annotated by BRENDA team
Dai, J.; Zhang, J.; Sun, Y.; Wu, Q.; Sun, L.; Ji, C.; Gu, S.; Feng, C.; Xie, Y.; Mao, Y.
Characterization of a novel human protein phosphatase 2C family member, PP2Ckappa
Int. J. Mol. Med.
17
1117-1123
2006
Homo sapiens (Q8N3J5), Homo sapiens
Manually annotated by BRENDA team
Kajino, T.; Ren, H.; Iemura, S.; Natsume, T.; Stefansson, B.; Brautigan, D.L.; Matsumoto, K.; Ninomiya-Tsuji, J.
Protein phosphatase 6 down-regulates TAK1 kinase activation in the IL-1 signaling pathway
J. Biol. Chem.
281
39891-39896
2006
Homo sapiens
Manually annotated by BRENDA team
Kitatani, K.; Idkowiak-Baldys, J.; Hannun, Y.A.
Mechanism of inhibition of sequestration of protein kinase C alpha/betaII by ceramide. Roles of ceramide-activated protein phosphatases and phosphorylation/dephosphorylation of protein kinase C alpha/betaII on threonine 638/641
J. Biol. Chem.
282
20647-20656
2007
Homo sapiens
Manually annotated by BRENDA team
Jang, Y.J.; Ji, J.H.; Choi, Y.C.; Ryu, C.J.; Ko, S.Y.
Regulation of Polo-like kinase 1 by DNA damage in mitosis. Inhibition of mitotic PLK-1 by protein phosphatase 2A
J. Biol. Chem.
282
2473-2482
2007
Homo sapiens
Manually annotated by BRENDA team
Ricotta, D.; Hansen, J.; Preiss, C.; Teichert, D.; Hoening, S.
Characterization of a protein phosphatase 2A holoenzyme (PP2A) that dephosphorylates the clathrin adaptors AP-1 and AP-2
J. Biol. Chem.
283
5510-551
2008
Homo sapiens
Manually annotated by BRENDA team
Tao, G.Z.; Toivola, D.M.; Zhou, Q.; Strnad, P.; Xu, B.; Michie, S.A.; Omary, M.B.
Protein phosphatase-2A associates with and dephosphorylates keratin 8 after hyposmotic stress in a site- and cell-specific manner
J. Cell Sci.
119
1425-1432
2006
Homo sapiens
Manually annotated by BRENDA team
Rogers, J.P.; Beuscher, A.E.; Flajolet, M.; McAvoy, T.; Nairn, A.C.; Olson, A.J.; Greengard, P.
Discovery of protein phosphatase 2C inhibitors by virtual screening
J. Med. Chem.
49
1658-1667
2006
Homo sapiens (P35813)
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Prickett, T.D.; Brautigan, D.L.
Cytokine activation of p38 mitogen-activated protein kinase and apoptosis is opposed by alpha-4 targeting of protein phosphatase 2A for site-specific dephosphorylation of MEK3
Mol. Cell. Biol.
27
4217-4227
2007
Homo sapiens
Manually annotated by BRENDA team
Shouse, G.P.; Cai, X.; Liu, X.
Serine 15 phosphorylation of p53 directs its interaction with B56gamma and the tumor suppressor activity of B56gamma-specific protein phosphatase 2A
Mol. Cell. Biol.
28
448-456
2008
Homo sapiens
Manually annotated by BRENDA team
Chen, Y.; Xu, Y.; Bao, Q.; Xing, Y.; Li, Z.; Lin, Z.; Stock, J.B.; Jeffrey, P.D.; Shi, Y.
Structural and biochemical insights into the regulation of protein phosphatase 2A by small t antigen of SV40
Nat. Struct. Mol. Biol.
14
527-534
2007
Homo sapiens
Manually annotated by BRENDA team
Cho, U.S.; Xu, W.
Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme
Nature
445
53-57
2007
Homo sapiens
Manually annotated by BRENDA team
Eichhorn, P.J.; Creyghton, M.P.; Wilhelmsen, K.; van Dam, H.; Bernards, R.
A RNA interference screen identifies the protein phosphatase 2A subunit PR55gamma as a stress-sensitive inhibitor of c-SRC
PLoS Genet.
3
e218
2007
Homo sapiens
Manually annotated by BRENDA team
Kuroda, F.; Moss, J.; Vaughan, M.
Regulation of brefeldin A-inhibited guanine nucleotide-exchange protein 1 (BIG1) and BIG2 activity via PKA and protein phosphatase 1gamma
Proc. Natl. Acad. Sci. USA
104
3201-3206
2007
Homo sapiens
Manually annotated by BRENDA team
Shah, B.H.; Catt, K.J.
Protein phosphatase 5 as a negative key regulator of Raf-1 activation
Trends Endocrinol. Metab.
17
382-384
2006
Homo sapiens
Manually annotated by BRENDA team
Stefansson, B.; Ohama, T.; Daugherty, A.E.; Brautigan, D.L.
Protein phosphatase 6 regulatory subunits composed of ankyrin repeat domains
Biochemistry
47
1442-1451
2008
Homo sapiens
Manually annotated by BRENDA team
Golden, T.; Aragon, I.V.; Rutland, B.; Tucker, J.A.; Shevde, L.A.; Samant, R.S.; Zhou, G.; Amable, L.; Skarra, D.; Honkanen, R.E.
Elevated levels of Ser/Thr protein phosphatase 5 (PP5) in human breast cancer
Biochim. Biophys. Acta
1782
259-270
2008
Homo sapiens
Manually annotated by BRENDA team
Mourtada-Maarabouni, M.; Williams, G.T.
Protein phosphatase 4 regulates apoptosis, proliferation and mutation rate of human cells
Biochim. Biophys. Acta
1783
1490-1502
2008
Homo sapiens
Manually annotated by BRENDA team
Eichhorn, P.J.; Creyghton, M.P.; Bernards, R.
Protein phosphatase 2A regulatory subunits and cancer
Biochim. Biophys. Acta
1795
1-15
2009
Homo sapiens
Manually annotated by BRENDA team
Wang, K.; Song, Y.; Chen, D.B.; Zheng, J.
Protein phosphatase 3 differentially modulates vascular endothelial growth factor- and fibroblast growth factor 2-stimulated cell proliferation and signaling in ovine fetoplacental artery endothelial cells
Biol. Reprod.
79
704-710
2008
Homo sapiens
Manually annotated by BRENDA team
Deng, X.; Gao, F.; May, W.S.
Protein phosphatase 2A inactivates Bcl2s antiapoptotic function by dephosphorylation and up-regulation of Bcl2-p53 binding
Blood
113
422-428
2009
Homo sapiens
Manually annotated by BRENDA team
Golden, T.; Swingle, M.; Honkanen, R.E.
The role of serine/threonine protein phosphatase type 5 (PP5) in the regulation of stress-induced signaling networks and cancer
Cancer Metastasis Rev.
27
169-178
2008
Homo sapiens (P53041), Homo sapiens
Manually annotated by BRENDA team
Lu, G.; Wang, Y.
Functional diversity of mammalian type 2C protein phosphatase isoforms: new tales from an old family
Clin. Exp. Pharmacol. Physiol.
35
107-112
2008
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Brandt, N.; Franke, K.; Johannes, S.; Buck, F.; Harder, S.; Hassel, B.; Nitsch, R.; Schumacher, S.
B56beta, a regulatory subunit of protein phosphatase 2A, interacts with CALEB/NGC and inhibits CALEB/NGC-mediated dendritic branching
FASEB J.
22
2521-2533
2008
Homo sapiens
Manually annotated by BRENDA team
Pulido, R.; Hooft van Huijsduijnen, R.
Protein tyrosine phosphatases: dual-specificity phosphatases in health and disease
FEBS J.
275
848-866
2008
Homo sapiens (O95248), Homo sapiens (O95278), Homo sapiens (P28562), Homo sapiens (P60484), Homo sapiens (Q05923), Homo sapiens (Q16828), Homo sapiens (Q93096), Homo sapiens (Q9BV47), Homo sapiens (Q9Y6W6)
Manually annotated by BRENDA team
Chen, L.; Dong, W.; Zou, T.; Ouyang, L.; He, G.; Liu, Y.; Qi, Y.
Protein phosphatase 4 negatively regulates LPS cascade by inhibiting ubiquitination of TRAF6
FEBS Lett.
582
2843-2849
2008
Homo sapiens
Manually annotated by BRENDA team
Sahin, F.; Celik, H.A.; Aydin, H.H.; Oktem, G.; Omay, S.B.; Saydam, G.
The interaction between taxoids and serine/threonine protein phosphatase activities during taxan-induced apoptosis of HL 60 leukemic cells
Hematology
13
215-223
2008
Homo sapiens
Manually annotated by BRENDA team
Xie, X.J.; Huang, W.; Xue, C.Z.; Wei, Q.
The nonconserved N-terminus of protein phosphatase 2B confers its properties to protein phosphatase 1
IUBMB Life
61
178-183
2009
Homo sapiens
Manually annotated by BRENDA team
McWhirter, C.; Lund, E.A.; Tanifum, E.A.; Feng, G.; Sheikh, Q.I.; Hengge, A.C.; Williams, N.H.
Mechanistic study of protein phosphatase-1 (PP1), a catalytically promiscuous enzyme
J. Am. Chem. Soc.
130
13673-13682
2008
Homo sapiens
Manually annotated by BRENDA team
Gushiken, F.C.; Patel, V.; Liu, Y.; Pradhan, S.; Bergeron, A.L.; Peng, Y.; Vijayan, K.V.
Protein phosphatase 2A negatively regulates integrin alpha(IIb)beta(3) signaling
J. Biol. Chem.
283
12862-12869
2008
Homo sapiens
Manually annotated by BRENDA team
Kang, Y.; Lee, J.H.; Hoan, N.N.; Sohn, H.M.; Chang, I.Y.; You, H.J.
Protein phosphatase 5 regulates the function of 53BP1 after NCS-induced DNA damage
J. Biol. Chem.
284
9845-9853
2009
Homo sapiens
Manually annotated by BRENDA team
Kelker, M.S.; Page, R.; Peti, W.
Crystal structures of protein phosphatase-1 bound to nodularin-R and tautomycin: a novel scaffold for structure-based drug design of serine/threonine phosphatase inhibitors
J. Mol. Biol.
385
11-21
2009
Homo sapiens (P62136)
Manually annotated by BRENDA team
Wang, N.; Leung, H.T.; Pak, W.L.; Carl, Y.T.; Wadzinski, B.E.; Shieh, B.H.
Role of protein phosphatase 2A in regulating the visual signaling in Drosophila
J. Neurosci.
28
1444-1451
2008
Drosophila melanogaster, Homo sapiens
Manually annotated by BRENDA team
Xu, Y.; Chen, Y.; Zhang, P.; Jeffrey, P.D.; Shi, Y.
Structure of a protein phosphatase 2A holoenzyme: insights into B55-mediated Tau dephosphorylation
Mol. Cell
31
873-885
2008
Homo sapiens
Manually annotated by BRENDA team
Li, H.; Okamoto, K.; Peart, M.J.; Prives, C.
Lysine-independent turnover of cyclin G1 can be stabilized by Balpha subunits of protein phosphatase 2A
Mol. Cell. Biol.
29
919-928
2009
Homo sapiens
Manually annotated by BRENDA team
Martin, M.; Potente, M.; Janssens, V.; Vertommen, D.; Twizere, J.C.; Rider, M.H.; Goris, J.; Dimmeler, S.; Kettmann, R.; Dequiedt, F.
Protein phosphatase 2A controls the activity of histone deacetylase 7 during T cell apoptosis and angiogenesis
Proc. Natl. Acad. Sci. USA
105
4727-4732
2008
Homo sapiens
Manually annotated by BRENDA team
Wang, B.; Zhang, P.; Wei, Q.
Recent progress on the structure of Ser/Thr protein phosphatases
Sci. China C Life Sci.
51
487-494
2008
Homo sapiens
Manually annotated by BRENDA team
Huang, H.S.; Lee, E.Y.
Protein phosphatase-1 inhibitor-3 is an in vivo target of caspase-3 and participates in the apoptotic response
J. Biol. Chem.
283
18135-18146
2008
Homo sapiens
Manually annotated by BRENDA team
Ryan, K.; Khleborodova, A.; Pan, J.; Ryan, X.P.
Small molecule activators of pre-mRNA 3 cleavage
RNA
15
483-492
2009
Homo sapiens
Manually annotated by BRENDA team
Volpe, G.; Cotroneo, E.; Moscone, D.; Croci, L.; Cozzi, L.; Ciccaglioni, G.; Palleschi, G.
A bienzyme electrochemical probe for flow injection analysis of okadaic acid based on protein phosphatase-2A inhibition: an optimization study
Anal. Biochem.
385
50-56
2009
Homo sapiens
Manually annotated by BRENDA team
Fortwendel, J.R.; Juvvadi, P.R.; Pinchai, N.; Perfect, B.Z.; Alspaugh, J.A.; Perfect, J.R.; Steinbach, W.J.
Differential effects of inhibiting chitin and 1,3-{beta}-D-glucan synthesis in ras and calcineurin mutants of Aspergillus fumigatus
Antimicrob. Agents Chemother.
53
476-482
2009
Homo sapiens
Manually annotated by BRENDA team
Thaci, D.; Salgo, R.
Malignancy concerns of topical calcineurin inhibitors for atopic dermatitis: facts and controversies
Clin. Dermatol.
28
52-56
2010
Homo sapiens
Manually annotated by BRENDA team
Chen, G.; Zhou, X.; Nicolaou, P.; Rodriguez, P.; Song, G.; Mitton, B.; Pathak, A.; Zachariah, A.; Fan, G.C.; Dorn, G.W.; Kranias, E.G.
A human polymorphism of protein phosphatase-1 inhibitor-1 is associated with attenuated contractile response of cardiomyocytes to beta-adrenergic stimulation
FASEB J.
22
1790-1796
2008
Homo sapiens
Manually annotated by BRENDA team
Juhasz, T.; Matta, C.; Veress, G.; Nagy, G.; Szijgyarto, Z.; Molnar, Z.; Fodor, J.; Zakany, R.; Gergely, P.
Inhibition of calcineurin by cyclosporine A exerts multiple effects on human melanoma cell lines HT168 and WM35
Int. J. Oncol.
34
995-1003
2009
Homo sapiens
Manually annotated by BRENDA team
Tanuma, N.; Kim, S.E.; Beullens, M.; Tsubaki, Y.; Mitsuhashi, S.; Nomura, M.; Kawamura, T.; Isono, K.; Koseki, H.; Sato, M.; Bollen, M.; Kikuchi, K.; Shima, H.
Nuclear inhibitor of protein phosphatase-1 (NIPP1) directs protein phosphatase-1 (PP1) to dephosphorylate the U2 small nuclear ribonucleoprotein particle (snRNP) component, spliceosome-associated protein 155 (Sap155)
J. Biol. Chem.
283
35805-35814
2008
Homo sapiens
Manually annotated by BRENDA team
Eto, M.
Regulation of cellular protein phosphatase-1 (PP1) by phosphorylation of the CPI-17 family, C-kinase-activated PP1 inhibitors
J. Biol. Chem.
284
35273-35277
2009
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Erdmann, F.; Weiwad, M.; Kilka, S.; Karanik, M.; Paetzel, M.; Baumgrass, R.; Liebscher, J.; Fischer, G.
The novel calcineurin inhibitor CN585 has potent immunosuppressive properties in stimulated human T cells
J. Biol. Chem.
285
1888-1898
2010
Homo sapiens
Manually annotated by BRENDA team
Smit, N.P.; Van Rossum, H.H.; Romijn, F.P.; Sellar, K.J.; Breetveld, M.; Gibbs, S.; Van Pelt, J.
Calcineurin activity and inhibition in skin and (epi)dermal cell cultures
J. Invest. Dermatol.
128
1686-1690
2008
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Tumlin, J.A.; Roberts, B.R.; Kokko, K.E.; El Minshawy, O.; Gooch, J.L.
T-cell receptor-stimulated calcineurin activity is inhibited in isolated T cells from transplant patients
J. Pharmacol. Exp. Ther.
330
602-607
2009
Homo sapiens
Manually annotated by BRENDA team
Nagane, Y.; Suzuki, S.; Suzuki, N.; Utsugisawa, K.
Factors associated with response to calcineurin inhibitors in myasthenia gravis
Muscle Nerve
41
212-218
2010
Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Baczkowska, T.; Durlik, M.
Calcineurin inhibitor sparing immunosuppressive regimens in kidney allograft recipients
Pol. Arch. Med. Wewn.
119
318-325
2009
Homo sapiens
Manually annotated by BRENDA team
Martinez-Martinez, S.; Genesca, L.; Rodriguez, A.; Raya, A.; Salichs, E.; Were, F.; Lopez-Maderuelo, M.D.; Redondo, J.M.; de la Luna, S.
The RCAN carboxyl end mediates calcineurin docking-dependent inhibition via a site that dictates binding to substrates and regulators
Proc. Natl. Acad. Sci. USA
106
6117-6122
2009
Homo sapiens
Manually annotated by BRENDA team
Rubiolo, J.A.; Lopez-Alonso, H.; Alfonso, A.; Vega, F.V.; Vieytes, M.R.; Botana, L.M.
Characterization and activity determination of the human protein phosphatase 2A catalytic subunit alpha expressed in insect larvae
Appl. Biochem. Biotechnol.
167
918-928
2012
Homo sapiens (P67775)
Manually annotated by BRENDA team
De Wever, V.; Nasa, I.; Chamousset, D.; Lloyd, D.; Nimick, M.; Xu, H.; Trinkle-Mulcahy, L.; Moorhead, G.B.
The human mitotic kinesin KIF18A binds protein phosphatase 1 (PP1) through a highly conserved docking motif
Biochem. Biophys. Res. Commun.
453
432-437
2014
Homo sapiens
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
Peti, W.; Nairn, A.C.; Page, R.
Structural basis for protein phosphatase 1 regulation and specificity
FEBS J.
280
596-611
2013
Homo sapiens (P62136)
Manually annotated by BRENDA team
Sents, W.; Ivanova, E.; Lambrecht, C.; Haesen, D.; Janssens, V.
The biogenesis of active protein phosphatase 2A holoenzymes: a tightly regulated process creating phosphatase specificity
FEBS J.
280
644-661
2013
Homo sapiens
Manually annotated by BRENDA team
Amsailale, R.; Beyaert, M.; Smal, C.; Janssens, V.; Van Den Neste, E.; Bontemps, F.
Protein phosphatase 2A regulates deoxycytidine kinase activity via Ser-74 dephosphorylation
FEBS Lett.
588
727-732
2014
Homo sapiens
Manually annotated by BRENDA team
Kasa, A.; Czikora, I.; Verin, A.D.; Gergely, P.; Csortos, C.
Protein phosphatase 2A activity is required for functional adherent junctions in endothelial cells
Microvasc. Res.
89
86-94
2013
Homo sapiens
Manually annotated by BRENDA team
Gregorio, L.K.; Esteves, S.L.; Fardilha, M.
Protein phosphatase 1 catalytic isoforms: specificity toward interacting proteins
Transl. Res.
164
366-391
2014
Homo sapiens (P36873), Homo sapiens (P62136), Homo sapiens (P62140)
Manually annotated by BRENDA team
Wilkins, J.; McConnell, C.; Tipton, P.; Hannink, M.
A conserved motif mediates both multimer formation and allosteric activation of phosphoglycerate mutase 5
J. Biol. Chem.
289
25137-25148
2014
Homo sapiens (Q96HS1)
Manually annotated by BRENDA team
Hengge, A.C.
Kinetic isotope effects in the characterization of catalysis by protein tyrosine phosphatases
Biochim. Biophys. Acta
1854
1768-1775
2015
Homo sapiens (P51452)
Manually annotated by BRENDA team
Peti, W.; Page, R.
Strategies to make protein serine/threonine (PP1, calcineurin) and tyrosine phosphatases (PTP1B) druggable Achieving specificity by targeting substrate and regulatory protein interaction sites
Bioorg. Med. Chem.
23
2781-2785
2015
Homo sapiens (P62136), Homo sapiens (Q08209)
Manually annotated by BRENDA team
Zhi, X.; Zhang, H.; He, C.; Wei, Y.; Bian, L.; Li, G.
Serine/threonine protein phosphatase-5 accelerates cell growth and migration in human glioma
Cell. Mol. Neurobiol.
35
669-677
2015
Homo sapiens (P53041), Homo sapiens
Manually annotated by BRENDA team
Li, H.; Yang, D.; Ning, S.; Xu, Y.; Yang, F.; Yin, R.; Feng, T.; Han, S.; Guo, L.; Zhang, P.; Qu, W.; Guo, R.; Song, C.; Xiao, P.; Zhou, C.; Xu, Z.; Sun, J.P.; Yu, X.
Switching of the substrate specificity of protein tyrosine phosphatase N12 by cyclin-dependent kinase 2 phosphorylation orchestrating 2 oncogenic pathways
FASEB J.
32
73-82
2018
Homo sapiens (Q05209)
Manually annotated by BRENDA team
Chen, Z.; Dempsey, D.R.; Thomas, S.N.; Hayward, D.; Bolduc, D.M.; Cole, P.A.
Molecular features of phosphatase and tensin homolog (PTEN) regulation by C-terminal phosphorylation
J. Biol. Chem.
291
14160-14169
2016
Homo sapiens (P60484)
Manually annotated by BRENDA team
Heijman, J.; Ghezelbash, S.; Wehrens, X.H.T.; Dobrev, D.
Serine/threonine phosphatases in atrial fibrillation
J. Mol. Cell. Cardiol.
103
110-120
2017
Homo sapiens (P62136), Homo sapiens (P67775), Homo sapiens (Q08209)
Manually annotated by BRENDA team
Hoffman, A.; Taleski, G.; Sontag, E.
The protein serine/threonine phosphatases PP2A, PP1 and calcineurin A triple threat in the regulation of the neuronal cytoskeleton
Mol. Cell. Neurosci.
84
119-131
2017
Homo sapiens (P62136), Homo sapiens (P67775), Homo sapiens (Q08209)
Manually annotated by BRENDA team
Calvayrac, O.; Pradines, A.; Favre, G.
RHOB expression controls the activity of serine/threonine protein phosphatase PP2A to modulate mesenchymal phenotype and invasion in non-small cell lung cancers
Small GTPases
9
339-344
2018
Homo sapiens
Manually annotated by BRENDA team